|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
827-1576 |
0e+00 |
|
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various eukaryotic acetyl-CoA carboxylases, N-terminal to the catalytic domain (pfam01039). This enzyme (EC:6.4.1.2) is involved in the synthesis of long-chain fatty acids, as it catalyzes the rate-limiting step in this process.
Pssm-ID: 462429 Cd Length: 718 Bit Score: 1014.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 827 LDNPSKVQQAELHTGSLPRIQSTALRGEKLHRVFHYVLDNLVNVMNGYCLpdpffSSKVKDWVERLMKTLRDPSLPLLEL 906
Cdd:pfam08326 2 LDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELPYLEW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 907 QDIMTSVSGRIPPNVEKSIKKEMAQYASNitsvLCQFPSQQIANILDSHAATLNRKSEREVFFMNTQSIVQLVQRYRSGI 986
Cdd:pfam08326 77 QEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 987 RGHMKAVVMDLLRQYLRVETQFQ--NGHYDKCVFALREENKSDMNTVLNYIFSHAQVTKKNLLVTMLIDQLCGR---DPT 1061
Cdd:pfam08326 153 KGHEYSVFASLLEEYYDVEKLFSggNVREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNcpnVSN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1062 LTDELLNILTELTQLSKTTNAKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGH--------QFCIENLQKLILS 1133
Cdd:pfam08326 233 VAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKELIDS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1134 ETSIFDVLPNFFYHSNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRMSFSSnl 1213
Cdd:pfam08326 313 KYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPIVSWQFQLPSSHSSEFGSPLSPSSDSSP-- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1214 nhyGMTHVASVSD-VLLDNSFTPPCQRMGGMVSFRTFEDFVRIFDEVMGCFSDSPPQSPTFPEaghtslydedkvpRDEP 1292
Cdd:pfam08326 391 ---PFKRIASVSDlSYLVNKSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEPEESGESNS-------------SDEP 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1293 IHILNVAIKTDCDIE-DDRLAAMFREFTQQNKATLVDHGIRRLTFLVAQKDfrkqvnyevdrrfhREFPKFFTFRARDKF 1371
Cdd:pfam08326 455 INVLNVAIRDAEGSDsDEELLERLEEILKENKEELLAAGVRRITFIIGRKD--------------GQYPKYFTFRGPDNY 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1372 EEDRIYRHLEPALAFQLELNRMRNFDLTAIPCANHKMHLYLGAAKVEVgtevTDYRFFVRAIIRHSDLVTKEASFEYLQN 1451
Cdd:pfam08326 521 EEDPIIRHIEPALAFQLELGRLSNFDIKPVPTENRQIHLYEAVGKENP----TDKRFFVRAIIRPGRLRDDIPTAEYLIS 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1452 EGERLLLEAMDELEVAfNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYGSRLWKLRVLQAELKINIRLTPTGK 1531
Cdd:pfam08326 597 EAERLLNDILDALEVA-SIGNSNSDLNHIFLNFVPVFNVDPEDVEEAVGGFLERFGKRLWRLRVTQAEIRIIIRDPETGP 675
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 767994502 1532 AIPIRLFLTNESGYYLDISLYKEVTDSRtAQIMFQAYGdKQGPLH 1576
Cdd:pfam08326 676 PIPLRLVITNVSGYVVKVELYREVKDDK-GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1676-2224 |
0e+00 |
|
Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.
Pssm-ID: 426008 [Multi-domain] Cd Length: 491 Bit Score: 615.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1676 PEYPEGRDIIVIGNDITYRIGSFGPQEDLLFLRASELARAEgIPRIYVSANSGARIGLAEEIRHMFHVAWVDPEDPYKGY 1755
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1756 RylyLTPQDYKRVSAlnsvhcehvedeGESRYKITDIIGKEEGIGPENLRGSGMIAGESSLAYNEIITISLVTCRAIGIG 1835
Cdd:pfam01039 80 K---ILRAMEIAIKT------------GLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1836 AYLVRLGQRTIQVEN-SHLILTGAGALNKVLGrEVYTSNNQLGGIQIMHNNGVTHCTVCDDFEGVFTVLHWLSYMPKSVH 1914
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1915 S---SVPLLNSKDPIDR---IIEFVPT--KTPYDPRWMLAGRphptqkgqwlsgfFDYGSFSEIMQPWAQTVVVGRARLG 1986
Cdd:pfam01039 224 NnrePVPIVPTKDPPDRdapLVSIVPDdpKKPYDVREVIAGI-------------VDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1987 GIPVGVVAVETRtvelsipadpanldseakiiQQAGqVWFPDSAFKTYQAIKDFNREGLPLMVFANWRGFSGGMKDMYDQ 2066
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 2067 VLKFGAYIVDGLRECCQPVLVYIPPqaELRGGSWVVIDSSINPRHMeMYADRESRGSVLEPEGTVEIKFRRKDLVKTMRR 2146
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRG 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767994502 2147 VDPvyihlaerlgtpelstaeRKELENKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVISDILDWKTSRtFFYW 2224
Cdd:pfam01039 427 KDL------------------AATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPR-FFPW 485
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
125-634 |
3.48e-139 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 443.69 E-value: 3.48e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 125 IEKVLIANNGIAAVKCMRSIRrwsyEMfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIA 204
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 205 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 284
Cdd:COG4770 71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 285 ilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IFVMRLAK 360
Cdd:COG4770 135 ----------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREAKaafGDDrVYLEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 361 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 440
Cdd:COG4770 205 RPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 441 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRmmygvspwgdspidfedsahvpcPRGHVIAARITS 519
Cdd:COG4770 285 YFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLpFTQEDIK-----------------------LRGHAIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 520 ENPDEGFKPSSGTVQELNFRsnknvwGYFSVAAAGGLHE------FADSQFGHCFSWGENREEAISNMVVALKELSIRGd 593
Cdd:COG4770 342 EDPARGFLPSPGTITRLRPP------GGPGVRVDSGVYEgyeippYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG- 414
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 767994502 594 FRTTVEYLIKLLETESFQMNRIDTGWLDRLIAEKVQAERPD 634
Cdd:COG4770 415 VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
125-630 |
2.46e-116 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 377.22 E-value: 2.46e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 125 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIA 204
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 205 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPwsGSglrvdwqendfskr 284
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVP--GS-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 285 ilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSPIFVM-RLAK 360
Cdd:PRK08591 135 ----------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPGVYMeKYLE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 361 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 440
Cdd:PRK08591 205 NPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 441 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmygvspwgdspidfedsahvpcpRGHVIAARITS 519
Cdd:PRK08591 285 YFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLsIKQEDIVF-----------------------RGHAIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 520 ENPDEGFKPSSGTVQelnfrsnknvwGYFsvaAAGGLH--------------EFADSQFGHCFSWGENREEAISNMVVAL 585
Cdd:PRK08591 342 EDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipPYYDSMIGKLIVHGETREEAIARMKRAL 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 767994502 586 KELSIRGdFRTTVEYLIKLLETESFQMNRIDTGWLDRLIAEKVQA 630
Cdd:PRK08591 408 SEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
125-626 |
2.39e-105 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 345.59 E-value: 2.39e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 125 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIA 204
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACK---------ELGIKTVAVHSTAD--RDALHVLLADEAVCIGPAPSAKSYLNIPNIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 205 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 284
Cdd:TIGR00514 71 EITGADAIHPGYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 285 ilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IFVMRLAK 360
Cdd:TIGR00514 135 ----------DGLVEDEEENVRIAKRIGYPVIIKATAGGGGRGMRVVREPDELVKSISMTRAEAKaafGNDgVYIEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 361 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 440
Cdd:TIGR00514 205 NPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 441 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLyrikdirmmygvsPWGDSPIDFedsahvpcpRGHVIAARITSE 520
Cdd:TIGR00514 285 YFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL-------------SLKQEDVVV---------RGHAIECRINAE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 521 NPDEGFKPSSGTVQE------LNFRSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 594
Cdd:TIGR00514 343 DPIKTFLPSPGRITRylppggPGVRWDSHVYSGYTVPP------YYDSMIGKLITYGKTREVAIARMKRALSEFIIDG-I 415
|
490 500 510
....*....|....*....|....*....|..
gi 767994502 595 RTTVEYLIKLLETESFQMNRIDTGWLDRLIAE 626
Cdd:TIGR00514 416 KTTIPFHQRILEDENFQHGGTNIHYLEKKLGM 447
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
286-477 |
1.16e-61 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 210.24 E-value: 1.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 286 LNVPQELYEKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSP----IFVMRLAKQ 361
Cdd:pfam02786 12 AGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSLKG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 362 SRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQD-GSF 440
Cdd:pfam02786 92 PKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFsGEY 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 767994502 441 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL 477
Cdd:pfam02786 172 YFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
515-621 |
1.58e-32 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 214878 [Multi-domain] Cd Length: 107 Bit Score: 122.91 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 515 ARITSENPDEGFKPSSGTVQELNFRSNKNVwgYFSVAAAGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 592
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 767994502 593 dFRTTVEYLIKLLETESFQMNRIDTGWLD 621
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1663-1994 |
2.20e-19 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 94.32 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1663 EIGM-VAWKMTFKSPEYP-----------EGRDIIVIGNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVSANSGAR 1730
Cdd:COG4799 51 ELGAlAGHRMYDDDDRVPgdgvvtgigtvDGRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGAR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1731 IGLAEEIRHMFhvawvdpedpykgyrylyltpqdykrvsalnsvhcehvedeGESRYKitdiigkeegigpeNLRGSGMI 1810
Cdd:COG4799 131 LQEGVESFAGY-----------------------------------------GRIFYR--------------NARSSGGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1811 AgesslayneiiTISLVTCRAIGIGAYLVRLGQRTIQVE-NSHLILTGAGALNKVLGREVytSNNQLGGIQiMHN--NGV 1887
Cdd:COG4799 156 P-----------QISVIMGPCAAGGAYSPALSDFVIMVKgTSQMFLGGPPVVKAATGEEV--TAEELGGAD-VHArvSGV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1888 THCTVCDDFEGVFTVLHWLSYMPKSVHSSVPLLNSKDP---IDRIIEFVPT--KTPYDPRWMLAGrphptqkgqwlsgFF 1962
Cdd:COG4799 222 ADYLAEDEEEALALARRLLSYLPSNNLEDPPRAEPAPPardPEELYGIVPEdpRKPYDMREVIAR-------------LV 288
|
330 340 350
....*....|....*....|....*....|..
gi 767994502 1963 DYGSFSEIMQPWAQTVVVGRARLGGIPVGVVA 1994
Cdd:COG4799 289 DGGSFFEFKPLYGPNIVTGFARIDGRPVGIVA 320
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
760-825 |
1.90e-17 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 78.80 E-value: 1.90e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767994502 760 VMRSPSAGKLI-----QYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVKRP-GAALDPGCVLAKM 825
Cdd:pfam00364 2 EIKSPMIGESVregvvEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
762-825 |
2.53e-14 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 69.37 E-value: 2.53e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767994502 762 RSPSAGKLIQYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVK-RPGAALDPGCVLAKM 825
Cdd:cd06850 3 TAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
1822-2075 |
4.76e-04 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 45.18 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1822 ITISLVTCRAiGiGAYLVRLGQRTIQV-ENSHLILTGAGALNKVLGREVytSNNQLGGIQImhnngvtHCT---VCDDF- 1896
Cdd:PLN02820 209 IALVLGSCTA-G-GAYVPAMADESVIVkGNGTIFLAGPPLVKAATGEEV--SAEDLGGADV-------HCKvsgVSDHFa 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1897 ----------EGVFTVLHWLSYMPKSVHSSVPLLNSKDPIDRIIEF---VPT--KTPYDPRWMLAGrphptqkgqwlsgF 1961
Cdd:PLN02820 278 qdelhalaigRNIVKNLHLAAKQGMENTLGSKNPEYKEPLYDVKELrgiVPAdhKQSFDVRSVIAR-------------I 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1962 FDYGSFSEIMQPWAQTVVVGRARLGGIPVGVVAvetrtvelsipadpanldseakiiqqAGQVWFPDSAFKTYQAIKDFN 2041
Cdd:PLN02820 345 VDGSEFDEFKKNYGTTLVTGFARIYGQPVGIIG--------------------------NNGILFTESALKGAHFIELCA 398
|
250 260 270
....*....|....*....|....*....|....
gi 767994502 2042 REGLPLMVFANWRGFSGGMKDMYDQVLKFGAYIV 2075
Cdd:PLN02820 399 QRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMV 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ACC_central |
pfam08326 |
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various ... |
827-1576 |
0e+00 |
|
Acetyl-CoA carboxylase, central region; The region featured in this family is found in various eukaryotic acetyl-CoA carboxylases, N-terminal to the catalytic domain (pfam01039). This enzyme (EC:6.4.1.2) is involved in the synthesis of long-chain fatty acids, as it catalyzes the rate-limiting step in this process.
Pssm-ID: 462429 Cd Length: 718 Bit Score: 1014.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 827 LDNPSKVQQAELHTGSLPRIQSTALRGEKLHRVFHYVLDNLVNVMNGYCLpdpffSSKVKDWVERLMKTLRDPSLPLLEL 906
Cdd:pfam08326 2 LDDPSRVKHAQPFEGQLPELGPPTVVGNKPHQRFAALLNILENILAGYDN-----QVIMNETLKDLIEVLRDPELPYLEW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 907 QDIMTSVSGRIPPNVEKSIKKEMAQYASNitsvLCQFPSQQIANILDSHAATLNRKSEREVFFMNTQSIVQLVQRYRSGI 986
Cdd:pfam08326 77 QEQLSALSGRIPAKLEASLRQLVERAHSR----SAEFPAKQLRKILDKFLAELVLKADRDLFEATLAPLVDLVERYRNGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 987 RGHMKAVVMDLLRQYLRVETQFQ--NGHYDKCVFALREENKSDMNTVLNYIFSHAQVTKKNLLVTMLIDQLCGR---DPT 1061
Cdd:pfam08326 153 KGHEYSVFASLLEEYYDVEKLFSggNVREEDVILKLRDENKDDLDKVVDIVLSHSRVSSKNKLILALLDHYRPNcpnVSN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1062 LTDELLNILTELTQLSKTTNAKVALRARQVLIASHLPSYELRHNQVESIFLSAIDMYGH--------QFCIENLQKLILS 1133
Cdd:pfam08326 233 VAKELRPVLKKLAELESRETAKVALKAREVLIQCALPSLEERKNQMEHILKSSVVESGYgesgwkhrEPSLEVLKELIDS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1134 ETSIFDVLPNFFYHSNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRMSFSSnl 1213
Cdd:pfam08326 313 KYTVFDVLPPFFYHSDPWVSLAALEVYVRRAYRAYSLKSIQYHEGEDSPPIVSWQFQLPSSHSSEFGSPLSPSSDSSP-- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1214 nhyGMTHVASVSD-VLLDNSFTPPCQRMGGMVSFRTFEDFVRIFDEVMGCFSDSPPQSPTFPEaghtslydedkvpRDEP 1292
Cdd:pfam08326 391 ---PFKRIASVSDlSYLVNKSEDEPLRTGAMVAFKSLDDLEEALPRALEEFPSEPEESGESNS-------------SDEP 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1293 IHILNVAIKTDCDIE-DDRLAAMFREFTQQNKATLVDHGIRRLTFLVAQKDfrkqvnyevdrrfhREFPKFFTFRARDKF 1371
Cdd:pfam08326 455 INVLNVAIRDAEGSDsDEELLERLEEILKENKEELLAAGVRRITFIIGRKD--------------GQYPKYFTFRGPDNY 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1372 EEDRIYRHLEPALAFQLELNRMRNFDLTAIPCANHKMHLYLGAAKVEVgtevTDYRFFVRAIIRHSDLVTKEASFEYLQN 1451
Cdd:pfam08326 521 EEDPIIRHIEPALAFQLELGRLSNFDIKPVPTENRQIHLYEAVGKENP----TDKRFFVRAIIRPGRLRDDIPTAEYLIS 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1452 EGERLLLEAMDELEVAfNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYGSRLWKLRVLQAELKINIRLTPTGK 1531
Cdd:pfam08326 597 EAERLLNDILDALEVA-SIGNSNSDLNHIFLNFVPVFNVDPEDVEEAVGGFLERFGKRLWRLRVTQAEIRIIIRDPETGP 675
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 767994502 1532 AIPIRLFLTNESGYYLDISLYKEVTDSRtAQIMFQAYGdKQGPLH 1576
Cdd:pfam08326 676 PIPLRLVITNVSGYVVKVELYREVKDDK-GEWVFKSIG-KPGPMH 718
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
1676-2224 |
0e+00 |
|
Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.
Pssm-ID: 426008 [Multi-domain] Cd Length: 491 Bit Score: 615.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1676 PEYPEGRDIIVIGNDITYRIGSFGPQEDLLFLRASELARAEgIPRIYVSANSGARIGLAEEIRHMFHVAWVDPEDPYKGY 1755
Cdd:pfam01039 1 PEHPRGKLTARERIDLLLDPGSFGELEDLFFHRATEFGRKR-IPRDGVVTGSGAVIGRAVEVVAQDFTVFGGSLGPAKGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1756 RylyLTPQDYKRVSAlnsvhcehvedeGESRYKITDIIGKEEGIGPENLRGSGMIAGESSLAYNEIITISLVTCRAIGIG 1835
Cdd:pfam01039 80 K---ILRAMEIAIKT------------GLPLIGINDSGGARIQEGVENLRGSGKIFGRNSLASGVIPQISLIMGPCAGGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1836 AYLVRLGQRTIQVEN-SHLILTGAGALNKVLGrEVYTSNNQLGGIQIMHNNGVTHCTVCDDFEGVFTVLHWLSYMPKSVH 1914
Cdd:pfam01039 145 AYLPALGDFVIMVEGtSPMFLTGPPVIKKVTG-EEVTSEELGGATQHMTISGVSHLTALDDEDALELIRKWLSYLPKPAP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1915 S---SVPLLNSKDPIDR---IIEFVPT--KTPYDPRWMLAGRphptqkgqwlsgfFDYGSFSEIMQPWAQTVVVGRARLG 1986
Cdd:pfam01039 224 NnrePVPIVPTKDPPDRdapLVSIVPDdpKKPYDVREVIAGI-------------VDEGEFFEIKPGYAKTVVTGFARLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1987 GIPVGVVAVETRtvelsipadpanldseakiiQQAGqVWFPDSAFKTYQAIKDFNREGLPLMVFANWRGFSGGMKDMYDQ 2066
Cdd:pfam01039 291 GIPVGVVANQPR--------------------VGAG-VLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 2067 VLKFGAYIVDGLRECCQPVLVYIPPqaELRGGSWVVIDSSINPRHMeMYADRESRGSVLEPEGTVEIKFRRKDLVKTMRR 2146
Cdd:pfam01039 350 ILKHGAKLLYALAEATVPKITVIPR--KAYGGAYVVMDSKINGADI-NFAWPTARIAVMGPEGAVEIKFRKEKAAAEMRG 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767994502 2147 VDPvyihlaerlgtpelstaeRKELENKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVISDILDWKTSRtFFYW 2224
Cdd:pfam01039 427 KDL------------------AATRKQKIAEYEEELSPPYVAAARGFADAVIDPGRTRAKLVIALAALWTKPR-FFPW 485
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
125-634 |
3.48e-139 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 443.69 E-value: 3.48e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 125 IEKVLIANNGIAAVKCMRSIRrwsyEMfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIA 204
Cdd:COG4770 2 FKKVLIANRGEIAVRIIRTCR----EL-----GIRTVAVYSDAD--RDALHVRLADEAVCIGPAPAAESYLNIDAIIAAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 205 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 284
Cdd:COG4770 71 KATGADAIHPGYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 285 ilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IFVMRLAK 360
Cdd:COG4770 135 ----------DGPVQDAEEALAIAEEIGYPVLIKASAGGGGKGMRVVRSEEELEEAFESARREAKaafGDDrVYLEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 361 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 440
Cdd:COG4770 205 RPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIEEAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVDADGNF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 441 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRmmygvspwgdspidfedsahvpcPRGHVIAARITS 519
Cdd:COG4770 285 YFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGEPLpFTQEDIK-----------------------LRGHAIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 520 ENPDEGFKPSSGTVQELNFRsnknvwGYFSVAAAGGLHE------FADSQFGHCFSWGENREEAISNMVVALKELSIRGd 593
Cdd:COG4770 342 EDPARGFLPSPGTITRLRPP------GGPGVRVDSGVYEgyeippYYDSMIAKLIVWGPDREEAIARMRRALAEFVIEG- 414
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 767994502 594 FRTTVEYLIKLLETESFQMNRIDTGWLDRLIAEKVQAERPD 634
Cdd:COG4770 415 VKTNIPFLRALLAHPDFRAGDVDTGFIERELAELLAAAAPE 455
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
125-630 |
2.46e-116 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 377.22 E-value: 2.46e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 125 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIA 204
Cdd:PRK08591 2 FDKILIANRGEIALRIIRACK---------ELGIKTVAVHSTAD--RDALHVQLADEAVCIGPAPSKKSYLNIPAIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 205 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPwsGSglrvdwqendfskr 284
Cdd:PRK08591 71 EITGADAIHPGYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVP--GS-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 285 ilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSPIFVM-RLAK 360
Cdd:PRK08591 135 ----------DGPVDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKaafGNPGVYMeKYLE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 361 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 440
Cdd:PRK08591 205 NPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLEEAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGEF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 441 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmygvspwgdspidfedsahvpcpRGHVIAARITS 519
Cdd:PRK08591 285 YFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGEPLsIKQEDIVF-----------------------RGHAIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 520 ENPDEGFKPSSGTVQelnfrsnknvwGYFsvaAAGGLH--------------EFADSQFGHCFSWGENREEAISNMVVAL 585
Cdd:PRK08591 342 EDPAKNFMPSPGKIT-----------RYH---PPGGPGvrvdsavytgytipPYYDSMIGKLIVHGETREEAIARMKRAL 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 767994502 586 KELSIRGdFRTTVEYLIKLLETESFQMNRIDTGWLDRLIAEKVQA 630
Cdd:PRK08591 408 SEFVIDG-IKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQEEK 451
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
126-629 |
6.03e-107 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 352.36 E-value: 6.03e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 126 EKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIAK 205
Cdd:PRK08654 3 KKILIANRGEIAIRVMRACR---------ELGIKTVAVYSEAD--KNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 206 RIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSGlrvdwqendfskri 285
Cdd:PRK08654 72 KAGADAIHPGYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEG-------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 286 lnvpqelyekgyVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLF---RQVQAEVPGSP-IFVMRLAKQ 361
Cdd:PRK08654 138 ------------IEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIestQSIAQSAFGDStVFIEKYLEK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 362 SRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSqDGSFY 441
Cdd:PRK08654 206 PRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS-NGNFY 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 442 FLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmygvspwgdspidfedsahvpcpRGHVIAARITSE 520
Cdd:PRK08654 285 FLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGEELsFKQEDITI-----------------------RGHAIECRINAE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 521 NPDEGFKPSSGTVQelnfrsnknvwGYFSVAAAG-----GLH------EFADSQFGHCFSWGENREEAISNMVVALKELS 589
Cdd:PRK08654 342 DPLNDFAPSPGKIK-----------RYRSPGGPGvrvdsGVHmgyeipPYYDSMISKLIVWGRTREEAIARMRRALYEYV 410
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 767994502 590 IRGdFRTTVEYLIKLLETESFQMNRIDTGWLD--RLIAEKVQ 629
Cdd:PRK08654 411 IVG-VKTNIPFHKAVMENENFVRGNLHTHFIEeeTTILEEMK 451
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
125-626 |
2.39e-105 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 345.59 E-value: 2.39e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 125 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIA 204
Cdd:TIGR00514 2 LDKILIANRGEIALRILRACK---------ELGIKTVAVHSTAD--RDALHVLLADEAVCIGPAPSAKSYLNIPNIISAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 205 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 284
Cdd:TIGR00514 71 EITGADAIHPGYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 285 ilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IFVMRLAK 360
Cdd:TIGR00514 135 ----------DGLVEDEEENVRIAKRIGYPVIIKATAGGGGRGMRVVREPDELVKSISMTRAEAKaafGNDgVYIEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 361 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 440
Cdd:TIGR00514 205 NPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLEEAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGEF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 441 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLyrikdirmmygvsPWGDSPIDFedsahvpcpRGHVIAARITSE 520
Cdd:TIGR00514 285 YFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGEPL-------------SLKQEDVVV---------RGHAIECRINAE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 521 NPDEGFKPSSGTVQE------LNFRSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 594
Cdd:TIGR00514 343 DPIKTFLPSPGRITRylppggPGVRWDSHVYSGYTVPP------YYDSMIGKLITYGKTREVAIARMKRALSEFIIDG-I 415
|
490 500 510
....*....|....*....|....*....|..
gi 767994502 595 RTTVEYLIKLLETESFQMNRIDTGWLDRLIAE 626
Cdd:TIGR00514 416 KTTIPFHQRILEDENFQHGGTNIHYLEKKLGM 447
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
123-621 |
4.55e-105 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 366.39 E-value: 4.55e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 123 KVIEKVLIANNGIAAVKCMRSIrrwsyemfrNERAIRFVVMVTPED------LKANAEYIkmadhyVPVPGGPNNNnYAN 196
Cdd:PRK12999 3 KKIKKVLVANRGEIAIRIFRAA---------TELGIRTVAIYSEEDklslhrFKADEAYL------IGEGKHPVRA-YLD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 197 VELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSGlrvdw 276
Cdd:PRK12999 67 IDEIIRVAKQAGVDAIHPGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGP----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 277 qendfskrilnvpqelyekgyVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP- 352
Cdd:PRK12999 142 ---------------------IDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKaafGNDe 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 353 IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEY 432
Cdd:PRK12999 201 VYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVVEIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEF 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 433 LYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLyrikdirmmygvspwgDSPIDFEDSAHVPCPRGHV 512
Cdd:PRK12999 281 LVDADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGATL----------------HDLEIGIPSQEDIRLRGYA 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 513 IAARITSENPDEGFKPSSGTVQElnFRSNknvwGYFSV------AAAGGlhEFA---DSQFGHCFSWGENREEAISNMVV 583
Cdd:PRK12999 345 IQCRITTEDPANNFMPDTGRITA--YRSP----GGFGVrldggnAFAGA--EITpyyDSLLVKLTAWGRTFEQAVARMRR 416
|
490 500 510
....*....|....*....|....*....|....*...
gi 767994502 584 ALKELSIRGdFRTTVEYLIKLLETESFQMNRIDTGWLD 621
Cdd:PRK12999 417 ALREFRIRG-VKTNIPFLENVLKHPDFRAGDYTTSFID 453
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
125-622 |
8.40e-105 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 343.93 E-value: 8.40e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 125 IEKVLIANNGIAAVKCMRSIRRWsyemfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIA 204
Cdd:PRK06111 2 FQKVLIANRGEIAVRIIRTCQKL---------GIRTVAIYSEAD--RDALHVKMADEAYLIGGPRVQESYLNLEKIIEIA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 205 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSGSGLrvdwqendfskr 284
Cdd:PRK06111 71 KKTGAEAIHPGYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNL------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 285 ilnvpqelyekgyvKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IFVMRLAK 360
Cdd:PRK06111 139 --------------EDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKAFESNKKRAAnffGNGeMYIEKYIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 361 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 440
Cdd:PRK06111 205 DPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIEEAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVDEQKNF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 441 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmygvspwgdspidfedsahvpcpRGHVIAARITS 519
Cdd:PRK06111 285 YFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLsFTQDDIKR-----------------------SGHAIEVRIYA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 520 ENPDEgFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTVE 599
Cdd:PRK06111 342 EDPKT-FFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEAISRLHDALEELKVEG-IKTNIP 419
|
490 500
....*....|....*....|...
gi 767994502 600 YLIKLLETESFQMNRIDTGWLDR 622
Cdd:PRK06111 420 LLLQVLEDPVFKAGGYTTGFLTK 442
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
123-621 |
2.50e-100 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 352.07 E-value: 2.50e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 123 KVIEKVLIANNG-IAavkcmrsIRrwsyeMFR--NERAIRFVVMVTPED------LKANAEY-IKMADHyvPVpggpnnN 192
Cdd:COG1038 2 KKIKKVLVANRGeIA-------IR-----VFRaaTELGIRTVAIYSEEDryslhrFKADEAYlIGEGKG--PV------D 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 193 NYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPwsGSgl 272
Cdd:COG1038 62 AYLDIEEIIRVAKEKGVDAIHPGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIP--GT-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 273 rvdwqendfskrilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP--- 349
Cdd:COG1038 138 ----------------------EGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKaaf 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 350 GSP-IFVMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAG 428
Cdd:COG1038 196 GDDeVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVVEIAPAPNLDEELREAICEAAVKLAKAVGYVNAG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 429 TVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLyrikdirmmygvspwGDSPIDFEDSAHVPCp 508
Cdd:COG1038 276 TVEFLVDDDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEGYSL---------------DDPEIGIPSQEDIRL- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 509 RGHVIAARITSENPDEGFKPSSGTVQElnFRSnknvwgyfsvaaAGGlhefadsqFG------HCFS------------- 569
Cdd:COG1038 340 NGYAIQCRITTEDPANNFMPDTGRITA--YRS------------AGG--------FGirldggNAYTgavitpyydsllv 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 767994502 570 ----WGENREEAISNMVVALKELSIRGdFRTTVEYLIKLLETESFQMNRIDTGWLD 621
Cdd:COG1038 398 kvtaWGRTFEEAIRKMRRALREFRIRG-VKTNIPFLENVLNHPDFLAGECTTSFID 452
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
125-622 |
1.00e-96 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 320.54 E-value: 1.00e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 125 IEKVLIANNGIAAVKCMRSIRrwsyEMfrNERAIrfVVMVTPEDlkaNAEYIKMADHYVPVPGGPNNNNYANVELILDIA 204
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQ----EM--GKEAI--AIYSTADK---DALYLKYADAKICIGGAKSSESYLNIPAIISAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 205 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 284
Cdd:PRK08462 73 EIFEADAIFPGYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGS---------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 285 ilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGS----PIFVMRLAK 360
Cdd:PRK08462 137 ----------DGALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEALSAfgdgTMYMEKFIN 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 361 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 440
Cdd:PRK08462 207 NPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEESPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDF 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 441 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLYRIKDIRMmygvspwgdspidfedsahvpcpRGHVIAARITSE 520
Cdd:PRK08462 287 YFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSQESIKL-----------------------KGHAIECRITAE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 521 NPdEGFKPSSGTVQEL------NFRSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 594
Cdd:PRK08462 344 DP-KKFYPSPGKITKWiapggrNVRMDSHAYAGYVVPP------YYDSMIGKLIVWGEDRNRAIAKMKRALKEFKVEG-I 415
|
490 500
....*....|....*....|....*...
gi 767994502 595 RTTVEYLIKLLETESFQMNRIDTGWLDR 622
Cdd:PRK08462 416 KTTIPFHLEMMENADFINNKYDTKYLEE 443
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
125-630 |
4.60e-96 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 319.39 E-value: 4.60e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 125 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDLKANAeyIKMADHYVPVPGGPNNNNYANVELILDIA 204
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAAR---------ELGMRTVAACSDADRDSLA--ARMADEAVHIGPSHAAKSYLNPAAILAAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 205 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 284
Cdd:PRK12833 74 RQCGADAIHPGYGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGS---------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 285 ilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IFVMRLAK 360
Cdd:PRK12833 138 ----------DGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAELPLAQREAQaafGDGgVYLERFIA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 361 QSRHLEVQILADQYgNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLY-SQDGS 439
Cdd:PRK12833 208 RARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFdDARGE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 440 FYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmygvspwgdspidfedsahvpcpRGHVIAARIT 518
Cdd:PRK12833 287 FYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLrFAQGDIAL-----------------------RGAALECRIN 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 519 SENPDEGFKPSSGTVQELNF------RSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRG 592
Cdd:PRK12833 344 AEDPLRDFFPNPGRIDALVWpqgpgvRVDSLLYPGYRVPP------FYDSLLAKLIVHGEDRAAALARAARALRELRIDG 417
|
490 500 510
....*....|....*....|....*....|....*...
gi 767994502 593 dFRTTVEYLIKLLETESFQMNRIDTGWLDRLIAEKVQA 630
Cdd:PRK12833 418 -MKTTAPLHRALLADADVRAGRFHTNFLEAWLAEWRAA 454
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
125-622 |
1.53e-95 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 317.42 E-value: 1.53e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 125 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIA 204
Cdd:PRK05586 2 FKKILIANRGEIAVRIIRACR---------EMGIETVAVYSEAD--KDALHVQLADEAVCIGPASSKDSYLNIQNIISAT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 205 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 284
Cdd:PRK05586 71 VLTGAQAIHPGFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGS---------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 285 ilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGS----PIFVMRLAK 360
Cdd:PRK05586 135 ----------EGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAfgddSMYIEKFIE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 361 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 440
Cdd:PRK05586 205 NPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 441 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmygvspwgdspidfedsahvpcpRGHVIAARITS 519
Cdd:PRK05586 285 YFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLsIKQEDIKI-----------------------NGHSIECRINA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 520 ENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTVE 599
Cdd:PRK05586 342 EDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEAIQKMKRALGEFIIEG-VNTNID 420
|
490 500
....*....|....*....|...
gi 767994502 600 YLIKLLETESFQMNRIDTGWLDR 622
Cdd:PRK05586 421 FQFIILEDEEFIKGTYDTSFIEK 443
|
|
| urea_carbox |
TIGR02712 |
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including ... |
126-623 |
5.04e-92 |
|
urea carboxylase; Members of this family are ATP-dependent urea carboxylase, including characterized members from Oleomonas sagaranensis (alpha class Proteobacterium) and yeasts such as Saccharomyces cerevisiae. The allophanate hydrolase domain of the yeast enzyme is not included in this model and is represented by an adjacent gene in Oleomonas sagaranensis. The fusion of urea carboxylase and allophanate hydrolase is designated urea amidolyase. The enzyme from Oleomonas sagaranensis was shown to be highly active on acetamide and formamide as well as urea. [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 274264 [Multi-domain] Cd Length: 1201 Bit Score: 327.76 E-value: 5.04e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 126 EKVLIANNGIAAVKCMRSIRRWsyemfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIAK 205
Cdd:TIGR02712 2 DTVLIANRGEIAVRIIRTLRRM---------GIRSVAVYSDAD--AASQHVLDADEAVCLGGAPAAESYLDIDKILAAAK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 206 RIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPwsGSGLrvdwqendfskri 285
Cdd:TIGR02712 71 KTGAQAIHPGYGFLSENAAFAEACEAAGIVFVGPTPEQIRKFGLKHTARELAEAAGVPLLP--GTGL------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 286 lnvpqelyekgyVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLF----RQVQAEVPGSPIFVMRLAKQ 361
Cdd:TIGR02712 136 ------------LSSLDEALEAAKEIGYPVMLKSTAGGGGIGMQKCDSAAELAEAFetvkRLGESFFGDAGVFLERFVEN 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 362 SRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLY-SQDGSF 440
Cdd:TIGR02712 204 ARHVEVQIFGDGKGKVVALGERDCSLQRRNQKVVEETPAPNLPPETRQALLAAAERLGEAVNYRSAGTVEFIYdEARDEF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 441 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAmgiplyrikdirmmygvspwGDSPIDFEDSAHVPCPRGHVIAARITSE 520
Cdd:TIGR02712 284 YFLEVNTRLQVEHPVTEMVTGLDLVEWMIRIA--------------------AGELPDFASLNISLTPRGAAIEARVYAE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 521 NPDEGFKPSSGTVQELNFRSNKNVWGYfsVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdFRTTVEY 600
Cdd:TIGR02712 344 NPAKNFQPSPGLLTDVQFPDDVRVDTW--VETGTEVSPEYDPMLAKIIVHGSDREDAILKLHQALAETRVYG-IETNLDY 420
|
490 500
....*....|....*....|...
gi 767994502 601 LIKLLETESFQMNRIDTGWLDRL 623
Cdd:TIGR02712 421 LRSILSSETFRSAQVSTRTLNSF 443
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
124-621 |
4.05e-89 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 299.71 E-value: 4.05e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 124 VIEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYV-----PVPGgpnnnnYANVE 198
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACA---------EMGIRSVAIYSEAD--RHALHVKRADEAYsigadPLAG------YLNPR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 199 LILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqe 278
Cdd:PRK07178 64 RLVNLAVETGCDALHPGYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGS---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 279 ndfskrilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVP---GSP-IF 354
Cdd:PRK07178 134 ----------------EGNLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEATkafGSAeVF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 355 VMRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLY 434
Cdd:PRK07178 198 LEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 435 SQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL-YRIKDIRMmygvspwgdspidfedsahvpcpRGHVI 513
Cdd:PRK07178 278 DADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLsYKQEDIQH-----------------------RGFAL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 514 AARITSENPDEGFKPSSGTVQElnfrsnknvwgYFSVAAAG---------GLH--EFADSQFGHCFSWGENREEAISNMV 582
Cdd:PRK07178 335 QFRINAEDPKNDFLPSFGKITR-----------YYAPGGPGvrtdtaiytGYTipPYYDSMCAKLIVWALTWEEALDRGR 403
|
490 500 510
....*....|....*....|....*....|....*....
gi 767994502 583 VALKELSIRGdFRTTVEYLIKLLETESFQMNRIDTGWLD 621
Cdd:PRK07178 404 RALDDMRVQG-VKTTIPYYQEILRNPEFRSGQFNTSFVE 441
|
|
| pyruv_carbox |
TIGR01235 |
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy ... |
127-621 |
9.47e-88 |
|
pyruvate carboxylase; This enzyme plays a role in gluconeogensis but not glycolysis. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130302 [Multi-domain] Cd Length: 1143 Bit Score: 313.69 E-value: 9.47e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 127 KVLIANNGIAAVKCMRSIrrwsyemfrNERAIRFVVMVTPED------LKANAEY-IKMADHYVPVpggpnnNNYANVEL 199
Cdd:TIGR01235 1 KILVANRGEIAIRVFRAA---------NELGIRTVAIYSEEDklslhrQKADESYqVGEGPDLGPI------EAYLSIDE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 200 ILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqen 279
Cdd:TIGR01235 66 IIRVAKLNGVDAIHPGYGFLSENSEFADACNKAGIIFIGPKAEVMDQLGDKVAARNLAIKAGVPVVPGT----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 280 dfskrilnvpqelyeKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGS----PIFV 355
Cdd:TIGR01235 135 ---------------DGPPETMEEVLDFAAAIGYPVIIKASWGGGGRGMRVVRSEADVADAFQRAKSEAKAAfgndEVYV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 356 MRLAKQSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYS 435
Cdd:TIGR01235 200 EKLIERPRHIEVQLLGDKHGNVVHLFERDCSVQRRHQKVVEVAPAPYLSREVRDEIAEYAVKLAKAVNYINAGTVEFLVD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 436 QDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLyrikdirmmygvsPWGDSPIDFEDSAHVpcpRGHVIAA 515
Cdd:TIGR01235 280 NDGKFYFIEVNPRIQVEHTVTEEITGIDIVQAQIHIADGASL-------------PTPQLGVPNQEDIRT---NGYAIQC 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 516 RITSENPDEGFKPSSGTVQElnFRSNknvwGYFSVAAAGG-------LHEFADSQFGHCFSWGENREEAISNMVVALKEL 588
Cdd:TIGR01235 344 RVTTEDPANNFQPDTGRIEA--YRSA----GGFGIRLDGGnsyagaiITPYYDSLLVKVSAWASTPEEAAAKMDRALREF 417
|
490 500 510
....*....|....*....|....*....|...
gi 767994502 589 SIRGdFRTTVEYLIKLLETESFQMNRIDTGWLD 621
Cdd:TIGR01235 418 RIRG-VKTNIPFLENVLGHPKFLDGSYDTRFID 449
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
125-644 |
1.73e-71 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 248.96 E-value: 1.73e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 125 IEKVLIANNGIAAVKCMRSIRrwsyemfrnERAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNnYANVELILDIA 204
Cdd:PRK08463 2 IHKILIANRGEIAVRVIRACR---------DLHIKSVAIYTEPD--RECLHVKIADEAYRIGTDPIKG-YLDVKRIVEIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 205 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWALGDKIASSIVAQTAGIPTLPWSgsglrvdwqendfskr 284
Cdd:PRK08463 70 KACGADAIHPGYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGT---------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 285 ilnvpqelyEKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLF----RQVQAEVPGSPIFVMRLAK 360
Cdd:PRK08463 134 ---------EKLNSESMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDLENAFesckREALAYFNNDEVFMEKYVV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 361 QSRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSF 440
Cdd:PRK08463 205 NPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYNRF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 441 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMG-IPLYRIKDIRmmygvspwgdspidfedsahvpcPRGHVIAARITS 519
Cdd:PRK08463 285 YFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGeILDLEQSDIK-----------------------PRGFAIEARITA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 520 ENPDEGFKPSSGTVQEL------NFRSNKNVWGYFSVAAagglheFADSQFGHCFSWGENREEAISNMVVALKELSIRGd 593
Cdd:PRK08463 342 ENVWKNFIPSPGKITEYypalgpSVRVDSHIYKDYTIPP------YYDSMLAKLIVKATSYDLAVNKLERALKEFVIDG- 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 767994502 594 FRTTVEYLIKLLETESFQMNRIDTGWLDRLIAEKVQA------ERPDTMLGVVCGAL 644
Cdd:PRK08463 415 IRTTIPFLIAITKTREFRRGYFDTSYIETHMQELLEKtedrhqENKEEVIAAIAAAL 471
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
286-477 |
1.16e-61 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 210.24 E-value: 1.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 286 LNVPQELYEKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSP----IFVMRLAKQ 361
Cdd:pfam02786 12 AGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSLKG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 362 SRHLEVQILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQD-GSF 440
Cdd:pfam02786 92 PKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALDPFsGEY 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 767994502 441 YFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL 477
Cdd:pfam02786 172 YFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
125-243 |
2.35e-43 |
|
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes, and propionyl-CoA carboxylase A chain.
Pssm-ID: 425585 [Multi-domain] Cd Length: 108 Bit Score: 153.80 E-value: 2.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 125 IEKVLIANNGIAAVKCMRSIRRWsyemfrnerAIRFVVMVTPEDlkANAEYIKMADHYVPVPGGPNNNNYANVELILDIA 204
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACREL---------GIRTVAVYSEAD--ANSLHVRLADEAVCLGPGPASESYLNIDAIIDAA 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 767994502 205 KRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQA 243
Cdd:pfam00289 70 KETGADAIHPGYGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
197-476 |
5.30e-43 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 158.88 E-value: 5.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 197 VELILDIAKRIPVQAVWAGWGHASEnpKLPELLLKNGIAfmGPPSQAMWALGDKIASSIVAQTAGIPTlPWSGSglrvdw 276
Cdd:COG0439 6 IAAAAELARETGIDAVLSESEFAVE--TAAELAEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPV-PGFAL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 277 qendfskrilnvpqelyekgyVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEV----PGSP 352
Cdd:COG0439 75 ---------------------VDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAkagsPNGE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 353 IFVMRLAkQSRHLEVQILADQyGNAISlfgrdCSVQRRHQK---IIE---EAPATIaTPAVFEHMEQCAVKLAKMVGYV- 425
Cdd:COG0439 134 VLVEEFL-EGREYSVEGLVRD-GEVVV-----CSITRKHQKppyFVElghEAPSPL-PEELRAEIGELVARALRALGYRr 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 767994502 426 SAGTVEYLYSQDGSFYFLELNPRLQVEH--PCTEMVADVNLPAAQLQIAMGIP 476
Cdd:COG0439 206 GAFHTEFLLTPDGEPYLIEINARLGGEHipPLTELATGVDLVREQIRLALGEP 258
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
515-621 |
1.58e-32 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 214878 [Multi-domain] Cd Length: 107 Bit Score: 122.91 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 515 ARITSENPDEGFKPSSGTVQELNFRSNKNVwgYFSVAAAGGLHE--FADSQFGHCFSWGENREEAISNMVVALKELSIRG 592
Cdd:smart00878 2 CRINAEDPANGFLPSPGRITRYRFPGGPGV--RVDSGVYEGYEVppYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRG 79
|
90 100
....*....|....*....|....*....
gi 767994502 593 dFRTTVEYLIKLLETESFQMNRIDTGWLD 621
Cdd:smart00878 80 -VKTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
515-622 |
5.43e-30 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 426981 [Multi-domain] Cd Length: 108 Bit Score: 115.67 E-value: 5.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 515 ARITSENPDEGFKPSSGTVQELNFRSNKNVWGYFSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGdF 594
Cdd:pfam02785 2 ARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEG-V 80
|
90 100
....*....|....*....|....*...
gi 767994502 595 RTTVEYLIKLLETESFQMNRIDTGWLDR 622
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
1663-1994 |
2.20e-19 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 94.32 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1663 EIGM-VAWKMTFKSPEYP-----------EGRDIIVIGNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVSANSGAR 1730
Cdd:COG4799 51 ELGAlAGHRMYDDDDRVPgdgvvtgigtvDGRPVVVVANDFTVKGGSLGPMTAKKILRAQDIALENGLPVIYLVDSGGAR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1731 IGLAEEIRHMFhvawvdpedpykgyrylyltpqdykrvsalnsvhcehvedeGESRYKitdiigkeegigpeNLRGSGMI 1810
Cdd:COG4799 131 LQEGVESFAGY-----------------------------------------GRIFYR--------------NARSSGGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1811 AgesslayneiiTISLVTCRAIGIGAYLVRLGQRTIQVE-NSHLILTGAGALNKVLGREVytSNNQLGGIQiMHN--NGV 1887
Cdd:COG4799 156 P-----------QISVIMGPCAAGGAYSPALSDFVIMVKgTSQMFLGGPPVVKAATGEEV--TAEELGGAD-VHArvSGV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1888 THCTVCDDFEGVFTVLHWLSYMPKSVHSSVPLLNSKDP---IDRIIEFVPT--KTPYDPRWMLAGrphptqkgqwlsgFF 1962
Cdd:COG4799 222 ADYLAEDEEEALALARRLLSYLPSNNLEDPPRAEPAPPardPEELYGIVPEdpRKPYDMREVIAR-------------LV 288
|
330 340 350
....*....|....*....|....*....|..
gi 767994502 1963 DYGSFSEIMQPWAQTVVVGRARLGGIPVGVVA 1994
Cdd:COG4799 289 DGGSFFEFKPLYGPNIVTGFARIDGRPVGIVA 320
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
760-825 |
1.90e-17 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 78.80 E-value: 1.90e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767994502 760 VMRSPSAGKLI-----QYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVKRP-GAALDPGCVLAKM 825
Cdd:pfam00364 2 EIKSPMIGESVregvvEWLVKVGDKVKAGQPLAEVEAMKMEMEIPAPVAGVVKEILVPeGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
762-825 |
2.53e-14 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 69.37 E-value: 2.53e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767994502 762 RSPSAGKLIQYIVEDGGHVFAGQCYAEIEVMKMVMTLTAVESGCIHYVK-RPGAALDPGCVLAKM 825
Cdd:cd06850 3 TAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPVAGVVKEILvKEGDQVEAGQLLVVI 67
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
179-484 |
2.54e-14 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 77.28 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 179 ADHYVPVPGgPNNNNYANVELILDIAKRIPVQAVWA---GWGHA-SEN-PKLPElllknGIAFMGPPSQAMWALGDKIAS 253
Cdd:COG3919 48 VDEVVVVPD-PGDDPEAFVDALLELAERHGPDVLIPtgdEYVELlSRHrDELEE-----HYRLPYPDADLLDRLLDKERF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 254 SIVAQTAGIPtlpwsgsglrvdwqendfskrilnVPQELYekgyVKDVDDGLQAAEEVGYPVMIKASEG--------GGG 325
Cdd:COG3919 122 YELAEELGVP------------------------VPKTVV----LDSADDLDALAEDLGFPVVVKPADSvgydelsfPGK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 326 KGIRKVNNADDFPNLFRQ---------VQAEVPGSpifvmrlakQSRHLEVQILADQYGNAISLFGrdcsvqrrHQKIIE 396
Cdd:COG3919 174 KKVFYVDDREELLALLRRiaaagyeliVQEYIPGD---------DGEMRGLTAYVDRDGEVVATFT--------GRKLRH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 397 eAPATIATPAVFEH-----MEQCAVKLAKMVGYVSAGTVEYLY-SQDGSFYFLELNPRLQVEHPCTEmVADVNLPAAQLQ 470
Cdd:COG3919 237 -YPPAGGNSAARESvddpeLEEAARRLLEALGYHGFANVEFKRdPRDGEYKLIEINPRFWRSLYLAT-AAGVNFPYLLYD 314
|
330
....*....|....
gi 767994502 471 IAMGIPLYRIKDIR 484
Cdd:COG3919 315 DAVGRPLEPVPAYR 328
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
281-477 |
6.49e-09 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 61.55 E-value: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 281 FSKRI--LNVPQElyEKGYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRL 358
Cdd:TIGR01369 673 FSELLdeLGIPQP--KWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKY 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 359 AKQSRHLEVQILADqyGNAISLFGrdcsvQRRHqkiIEEA-----------PATIATPAVFEHMEQCAVKLAKMVGYVSA 427
Cdd:TIGR01369 751 LEDAVEVDVDAVSD--GEEVLIPG-----IMEH---IEEAgvhsgdstcvlPPQTLSAEIVDRIKDIVRKIAKELNVKGL 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767994502 428 GTVEYLYSqDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPL 477
Cdd:TIGR01369 821 MNIQFAVK-DGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKL 869
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
296-448 |
1.00e-08 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 60.95 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 296 GYVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDfpnLFRQVQAEV---PGSPIFVMRLAKQSRHLEVQILAD 372
Cdd:PLN02735 721 GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDK---LKTYLETAVevdPERPVLVDKYLSDATEIDVDALAD 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 373 QYGNAI-----------SLFGRDCSVQRRHQKIIEEAPATI--ATPavfehmeqcavKLAKMVGYVSAGTVEYLYSQDGS 439
Cdd:PLN02735 798 SEGNVViggimehieqaGVHSGDSACSLPTQTIPSSCLATIrdWTT-----------KLAKRLNVCGLMNCQYAITPSGE 866
|
....*....
gi 767994502 440 FYFLELNPR 448
Cdd:PLN02735 867 VYIIEANPR 875
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
227-447 |
3.54e-08 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 57.42 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 227 ELLlknGIAFMGPPSQAMwALG-DKIASSIVAQTAGIPTLPWsgsglrvdwqendfskrilnvpqELYEKGYVKDVDdgl 305
Cdd:COG1181 76 ELL---GIPYTGSGVLAS-ALAmDKALTKRVLAAAGLPTPPY-----------------------VVLRRGELADLE--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 306 QAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNlfrqvqaevpgspifVMRLAKQSRHlevQILADQYgnaISlfGRD- 384
Cdd:COG1181 126 AIEEELGLPLFVKPAREGSSVGVSKVKNAEELAA---------------ALEEAFKYDD---KVLVEEF---ID--GREv 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 385 -CSV-QRRHQK---IIE----------EA-----------PATIaTPAVFEHMEQCAVKLAKMV---GYvsaGTVEYLYS 435
Cdd:COG1181 183 tVGVlGNGGPRalpPIEivpengfydyEAkytdggteyicPARL-PEELEERIQELALKAFRALgcrGY---ARVDFRLD 258
|
250
....*....|..
gi 767994502 436 QDGSFYFLELNP 447
Cdd:COG1181 259 EDGEPYLLEVNT 270
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
281-448 |
3.57e-07 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 55.27 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 281 FSKRI--LNVPQElyEKGYVKDVDDGLQAAEEVGYPVMIKASE--GGGGKGIrkVNNADDFPNLFRQVQAEVPGSPIFVM 356
Cdd:COG0458 118 FKELLdkLGIPQP--KSGTATSVEEALAIAEEIGYPVIVRPSYvlGGRGMGI--VYNEEELEEYLERALKVSPDHPVLID 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 357 RLAKQSRHLEVQILADQYGNAISLfgrdCSVQrrHqkiIEEA-----------PATIATPAVFEHMEQCAVKLAKMVGYV 425
Cdd:COG0458 194 ESLLGAKEIEVDVVRDGEDNVIIV----GIME--H---IEPAgvhsgdsicvaPPQTLSDKEYQRLRDATLKIARALGVV 264
|
170 180
....*....|....*....|...
gi 767994502 426 SAGTVEYLYsQDGSFYFLELNPR 448
Cdd:COG0458 265 GLCNIQFAV-DDGRVYVIEVNPR 286
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
297-448 |
3.96e-07 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 52.26 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 297 YVKDVDDGLQAAEEVGYPVMIKASEGG-GGKGIRKVNNADDFPnlfrQVQAEVPGSPIFVMRLAKQSRHLEVQILADQYG 375
Cdd:pfam02222 12 AAESLEELIEAGQELGYPCVVKARRGGyDGKGQYVVRSEADLP----QAWEELGDGPVIVEEFVPFDRELSVLVVRSVDG 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767994502 376 NAISlfgrdCS-VQRRHQK---IIEEAPATIaTPAVFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNPR 448
Cdd:pfam02222 88 ETAF-----YPvVETIQEDgicRLSVAPARV-PQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDGDLLINELAPR 158
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
286-449 |
1.23e-06 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 54.23 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 286 LNVPQElyEKGYVKDVDDGLQAAEEVGYPVMIKASE--GGGGKGIrkVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSR 363
Cdd:TIGR01369 138 IGEPVP--ESEIAHSVEEALAAAKEIGYPVIVRPAFtlGGTGGGI--AYNREELKEIAERALSASPINQVLVEKSLAGWK 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 364 HLEVQILADQYGNAISLfgrdCSVQR-----RHQ-KIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSAGTVEY-LYSQ 436
Cdd:TIGR01369 214 EIEYEVMRDSNDNCITV----CNMENfdpmgVHTgDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFaLNPD 289
|
170
....*....|...
gi 767994502 437 DGSFYFLELNPRL 449
Cdd:TIGR01369 290 SGRYYVIEVNPRV 302
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
307-475 |
3.68e-06 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 51.84 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 307 AAEEVGYPVMIKASEGGGGKGIRKVNNAD-DFPNLFrqVQAEVPGSPIfvmrlakqSrhleVQILADqygnaislfGRDC 385
Cdd:COG2232 133 EPPPDPGPWLVKPIGGAGGWHIRPADSEApPAPGRY--FQRYVEGTPA--------S----VLFLAD---------GSDA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 386 SVQRRHQKIIEEAP------ATIATPAVFEH-----MEQCAVKLAKMVGYVSAGTVEYLYSQDGsFYFLELNPRLQVEHP 454
Cdd:COG2232 190 RVLGFNRQLIGPAGerpfryGGNIGPLALPPalaeeMRAIAEALVAALGLVGLNGVDFILDGDG-PYVLEVNPRPQASLD 268
|
170 180
....*....|....*....|.
gi 767994502 455 CTEMVADVNLPAAQLQIAMGI 475
Cdd:COG2232 269 LYEDATGGNLFDAHLRACRGE 289
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
281-448 |
9.40e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 50.27 E-value: 9.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 281 FSKRILNVPQElYEKGYVKDVDDGLqAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQ-----VQAEVPGSPIfv 355
Cdd:PRK12767 119 LKENGIPTPKS-YLPESLEDFKAAL-AKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYvpnliIQEFIEGQEY-- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 356 mrlakqsrhlEVQILADQYGNAISLFGRdcsvqRRHQKIIEEA--PATIATPAVFEHMEQCAVKLakmvGYVSAGTVEYL 433
Cdd:PRK12767 195 ----------TVDVLCDLNGEVISIVPR-----KRIEVRAGETskGVTVKDPELFKLAERLAEAL----GARGPLNIQCF 255
|
170
....*....|....*
gi 767994502 434 YSqDGSFYFLELNPR 448
Cdd:PRK12767 256 VT-DGEPYLFEINPR 269
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
246-342 |
1.12e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 49.72 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 246 ALG-DKIASSIVAQTAGIPTLPWsgsglrvdwqendfskRILNvpqelyekgyvkDVDDGLQAAEEVGYPVMIKASEGGG 324
Cdd:PRK01372 94 ALAmDKLRTKLVWQAAGLPTPPW----------------IVLT------------REEDLLAAIDKLGLPLVVKPAREGS 145
|
90
....*....|....*...
gi 767994502 325 GKGIRKVNNADDFPNLFR 342
Cdd:PRK01372 146 SVGVSKVKEEDELQAALE 163
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
308-450 |
2.55e-05 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 46.61 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 308 AEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQ--VQAEVPGSPIFVMRLAKQSRHLEVQIlADQY-GNAISLFGRD 384
Cdd:pfam02655 27 LLREEKKYVVKPRDGCGGEGVRKVENGREDEAFIENvlVQEFIEGEPLSVSLLSDGEKALPLSV-NRQYiDNGGSGFVYA 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 385 -CSVQRRH---QKIIEEApatiatpavfehmEQCAVKLAKMVGYVSagtVEYLYSqDGSFYFLELNPRLQ 450
Cdd:pfam02655 106 gNVTPSRTelkEEIIELA-------------EEVVECLPGLRGYVG---VDLVLK-DNEPYVIEVNPRIT 158
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
258-447 |
5.11e-05 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 46.54 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 258 QTAGIPTLPWSGSgLRVDWQENdfskrilnvPQELYEkgyvkdvddglQAAEEVGYPVMIKASEGGGGKGIRKVNNAD-- 335
Cdd:pfam07478 3 KAAGLPVVPFVTF-TRADWKLN---------PKEWCA-----------QVEEALGYPVFVKPARLGSSVGVSKVESREel 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 336 -DFPNLFRQVQAEVpgspifVMRLAKQSRHLEVQILADQYGNAISLfGR---DCSVQRRHQKIIEEA-----PATIaTPA 406
Cdd:pfam07478 62 qAAIEEAFQYDEKV------LVEEGIEGREIECAVLGNEDPEVSPV-GEivpSGGFYDYEAKYIDDSaqivvPADL-EEE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767994502 407 VFEHMEQCAVKLAKMVGYVSAGTVEYLYSQDGSFYFLELNP 447
Cdd:pfam07478 134 QEEQIQELALKAYKALGCRGLARVDFFLTEDGEIVLNEVNT 174
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
286-448 |
2.26e-04 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 46.50 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 286 LNVPQELYEKgyVKDVDDGLQAAEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRqvQAEVPGSPIFVMRL--AKQsr 363
Cdd:PRK12815 681 LGLPHVPGLT--ATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLA--ENASQLYPILIDQFidGKE-- 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 364 hLEVQILADqyGNAISLFGrdcsvqrrhqkI---IEEA-----------PATIATPAVFEHMEQCAVKLAKMVGYVSAGT 429
Cdd:PRK12815 755 -YEVDAISD--GEDVTIPG-----------IiehIEQAgvhsgdsiavlPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMN 820
|
170
....*....|....*....
gi 767994502 430 VEYLYsQDGSFYFLELNPR 448
Cdd:PRK12815 821 IQFVL-ANDEIYVLEVNPR 838
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
277-328 |
3.58e-04 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 45.92 E-value: 3.58e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 767994502 277 QENDFSKRILN-----VPqelyeKGY-VKDVDDGLQAAEEVGYPVMIKASEGGGGKGI 328
Cdd:PRK14016 213 CDKELTKRLLAaagvpVP-----EGRvVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGV 265
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
240-467 |
3.66e-04 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 44.93 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 240 PSQAMWALGDKIASSIVAQTAGIPTlpwsgsglrvdwqendfskrilnvPQELYekgyVKDVDDGLQAAEEVGYPVMIKA 319
Cdd:COG0189 87 DPEAIRRARDKLFTLQLLARAGIPV------------------------PPTLV----TRDPDDLRAFLEELGGPVVLKP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 320 SEGGGGKGIRKVNNADDFPNLFRQ----------VQAEVP-------------GSPIFVMRlaKQSRHLEVQIladqygN 376
Cdd:COG0189 139 LDGSGGRGVFLVEDEDALESILEAltelgsepvlVQEFIPeedgrdirvlvvgGEPVAAIR--RIPAEGEFRT------N 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 377 aISLFGRdcsvqrrhqkiIEEAPATiatpavfEHMEQCAVKLAKMVGYVSAGtVEYLYSQDGsFYFLELNPRLQVEHpcT 456
Cdd:COG0189 211 -LARGGR-----------AEPVELT-------DEERELALRAAPALGLDFAG-VDLIEDDDG-PLVLEVNVTPGFRG--L 267
|
250
....*....|.
gi 767994502 457 EMVADVNLPAA 467
Cdd:COG0189 268 ERATGVDIAEA 278
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
1822-2075 |
4.76e-04 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 45.18 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1822 ITISLVTCRAiGiGAYLVRLGQRTIQV-ENSHLILTGAGALNKVLGREVytSNNQLGGIQImhnngvtHCT---VCDDF- 1896
Cdd:PLN02820 209 IALVLGSCTA-G-GAYVPAMADESVIVkGNGTIFLAGPPLVKAATGEEV--SAEDLGGADV-------HCKvsgVSDHFa 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1897 ----------EGVFTVLHWLSYMPKSVHSSVPLLNSKDPIDRIIEF---VPT--KTPYDPRWMLAGrphptqkgqwlsgF 1961
Cdd:PLN02820 278 qdelhalaigRNIVKNLHLAAKQGMENTLGSKNPEYKEPLYDVKELrgiVPAdhKQSFDVRSVIAR-------------I 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 1962 FDYGSFSEIMQPWAQTVVVGRARLGGIPVGVVAvetrtvelsipadpanldseakiiqqAGQVWFPDSAFKTYQAIKDFN 2041
Cdd:PLN02820 345 VDGSEFDEFKKNYGTTLVTGFARIYGQPVGIIG--------------------------NNGILFTESALKGAHFIELCA 398
|
250 260 270
....*....|....*....|....*....|....
gi 767994502 2042 REGLPLMVFANWRGFSGGMKDMYDQVLKFGAYIV 2075
Cdd:PLN02820 399 QRGIPLLFLQNITGFMVGSRSEASGIAKAGAKMV 432
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
298-448 |
4.80e-04 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 44.76 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 298 VKDVDDGLQAAEEVGYPVMIKASEGG-GGKGIRKVNNADDFPNLFRQVQAE-------VPgspiFVMrlakqsrhlEVQI 369
Cdd:PRK06019 121 VDSAEDLEAALADLGLPAVLKTRRGGyDGKGQWVIRSAEDLEAAWALLGSVpcileefVP----FER---------EVSV 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767994502 370 LAdqygnAISLFGRDCS---VQRRHQKII---EEAPATIaTPAVFEHMEQCAVKLAKMVGYVsaGT--VEYLYSQDGSFY 441
Cdd:PRK06019 188 IV-----ARGRDGEVVFyplVENVHRNGIlrtSIAPARI-SAELQAQAEEIASRIAEELDYV--GVlaVEFFVTGDGELL 259
|
....*..
gi 767994502 442 FLELNPR 448
Cdd:PRK06019 260 VNEIAPR 266
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
296-337 |
2.57e-03 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 43.16 E-value: 2.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767994502 296 GYVKDVDDGLQAAEEVGYPVMIKAS--EGGGGKGIrkVNNADDF 337
Cdd:PRK05294 147 GIAHSMEEALEVAEEIGYPVIIRPSftLGGTGGGI--AYNEEEL 188
|
|
| |
