|
Name |
Accession |
Description |
Interval |
E-value |
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
4-427 |
0e+00 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 684.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 4 RVLIIGSGGREHTLAWKLAQSHHVKQVLVAPGNAGTA-CSEKIsntAISISDHTALAQFCKEKKIEFVVVGPEAPLAAGI 82
Cdd:COG0151 2 KVLVIGSGGREHALAWKLAQSPRVDKLYVAPGNAGTAqLAECV---DIDVTDIEALVAFAKEENIDLVVVGPEAPLVAGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 83 VGNLRSAGVQCFGPTAEAAQLESSKRFAKEFMDRHGIPTAQWKAFTKPEEACSFILSADFPaLVVKASGLAAGKGVIVAK 162
Cdd:COG0151 79 VDAFRAAGIPVFGPSKAAAQLEGSKAFAKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAP-IVVKADGLAAGKGVVVAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 163 SKEEACKAVQEIMQEKAFGAAGETIVIEELLDGEEVSCLCFTDGKTVAPMPPAQDHKRLLEGDGGPNTGGMGAYCPAPQV 242
Cdd:COG0151 158 TLEEALAAVDDMLADGKFGDAGARVVIEEFLEGEEASLFALTDGKTVLPLPTAQDHKRAGDGDTGPNTGGMGAYSPAPVV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 243 SNDLLLKIKDTVLQRTVDGMQQEGTPYTGILYAGIMLTKNGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTLDGLLC 322
Cdd:COG0151 238 TEELLEKIMEEIIEPTVAGMAAEGIPYRGVLYAGLMITADGPKVLEFNVRFGDPETQVVLPRLESDLLELLLAAAEGRLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 323 TSLPVWlENHTALTVVMASKGYPGDYTKGVEITGFPEAQALGLEVFHAGTALKNGKVVTHGGRVLAVTAIRENLISALEE 402
Cdd:COG0151 318 EVELEW-DDRAAVCVVLASGGYPGSYEKGDVITGLEEAEAEGVKVFHAGTALEDGKLVTNGGRVLGVTALGDTLEEARER 396
|
410 420
....*....|....*....|....*
gi 28416899 403 AKKGLAAIKFEGAIYRKDVGFRAIA 427
Cdd:COG0151 397 AYEAVEKIRFEGMFYRRDIGWRALK 421
|
|
| purD |
TIGR00877 |
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase ... |
4-426 |
0e+00 |
|
phosphoribosylamine--glycine ligase; Alternate name: glycinamide ribonucleotide synthetase (GARS). This enzyme appears as a monofunctional protein in prokaryotes but as part of a larger, multidomain protein in eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273315 [Multi-domain] Cd Length: 422 Bit Score: 678.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 4 RVLIIGSGGREHTLAWKLAQSHHVKQVLVAPGNAGTACSEKISNTAISISDHTALAQFCKEKKIEFVVVGPEAPLAAGIV 83
Cdd:TIGR00877 2 KVLVIGNGGREHALAWKLAQSPLVKYVYVAPGNAGTARLAKNKNVAIEITDIEALVEFAKKKKIDLAIIGPEAPLVLGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 84 GNLRSAGVQCFGPTAEAAQLESSKRFAKEFMDRHGIPTAQWKAFTKPEEACSFILSADFPAlVVKASGLAAGKGVIVAKS 163
Cdd:TIGR00877 82 DALEEAGIPVFGPTKEAAQLEGSKAFAKDFMKRYGIPTAEYEVFTDPEEAKSYIQEKGAPI-VVKADGLAAGKGVIVAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 164 KEEACKAVQEIMQEKaFGAAGETIVIEELLDGEEVSCLCFTDGKTVAPMPPAQDHKRLLEGDGGPNTGGMGAYCPAPQVS 243
Cdd:TIGR00877 161 NEEAIKAVEDILEQK-FGDAGERVVIEEFLDGEEFSLLAFVDGKTVIPMPPAQDHKRALEGDKGPNTGGMGAYSPAPVFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 244 NDLLLKIKDTVLQRTVDGMQQEGTPYTGILYAGIMLTKNGPKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTLDGLLCt 323
Cdd:TIGR00877 240 EEVERRIAEEIVEPTVKAMRKEGTPYKGVLYAGLMLTKEGPKVLEFNCRFGDPETQAVLPLLKSDLLEVCLAAVEGKLD- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 324 SLPVWLENHTALTVVMASKGYPGDYTKGVEITGFPEAQALGLEVFHAGTALKNGKVVTHGGRVLAVTAIRENLISALEEA 403
Cdd:TIGR00877 319 EVELRFDNRAAVTVVLASEGYPEDYRKGDPITGEPLAEAEGVKVFHAGTKADNGKLVTNGGRVLAVTALGKTLEEARERA 398
|
410 420
....*....|....*....|...
gi 28416899 404 KKGLAAIKFEGAIYRKDVGFRAI 426
Cdd:TIGR00877 399 YEAVEYIKFEGMFYRKDIGFRAL 421
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
6-433 |
3.71e-169 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 481.55 E-value: 3.71e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 6 LIIGSGGREHTLAWKLAQSHHVKQVLVAPGNAGTACSEKISNTA-ISISDHTALAQFCKEKKIEFVVVGPEAPLAAGIVG 84
Cdd:PLN02257 1 LVIGGGGREHALCYALQRSPSCDAVFCAPGNAGIATSGDATCVPdLDISDSAAVISFCRKWGVGLVVVGPEAPLVAGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 85 NLRSAGVQCFGPTAEAAQLESSKRFAKEFMDRHGIPTAQWKAFTKPEEACSFILSADFPaLVVKASGLAAGKGVIVAKSK 164
Cdd:PLN02257 81 DLVKAGIPTFGPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAP-IVVKADGLAAGKGVVVAMTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 165 EEACKAVQEIMQEKAFGAAGETIVIEELLDGEEVSCLCFTDGKTVAPMPPAQDHKRLLEGDGGPNTGGMGAYCPAPQVSN 244
Cdd:PLN02257 160 EEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 245 DLLLKIKDTVLQRTVDGMQQEGTPYTGILYAGIMLTKNG--PKVLEFNCRFGDPECQVILPLLKSDLYEVIQSTLDGLLC 322
Cdd:PLN02257 240 ELESKVMETIIYPTVKGMAAEGCKFVGVLYAGLMIEKKSglPKLLEYNVRFGDPECQVLMMRLESDLAQVLLAACKGELS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 323 TSLPVWLENhTALTVVMASKGYPGDYTKGVEITGFPEAQAL--GLEVFHAGTALK-NGKVVTHGGRVLAVTAIRENLISA 399
Cdd:PLN02257 320 GVSLTWSPD-SAMVVVMASNGYPGSYKKGTVIKNLDEAEAVapGVKVFHAGTALDsDGNVVAAGGRVLGVTAKGKDIAEA 398
|
410 420 430
....*....|....*....|....*....|....
gi 28416899 400 LEEAKKGLAAIKFEGAIYRKDVGFRAIAFLQQPR 433
Cdd:PLN02257 399 RARAYDAVDQIDWPGGFFRRDIGWRAVARLQVAN 432
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
105-298 |
2.92e-128 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 368.53 E-value: 2.92e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 105 SSKRFAKEFMDRHGIPTAQWKAFTKPEEACSFILSADFPALVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKAFGAAG 184
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVVKADGLAAGKGVIVASSNEEAIKAVDEILEQKKFGEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 185 ETIVIEELLDGEEVSCLCFTDGKTVAPMPPAQDHKRLLEGDGGPNTGGMGAYCPAPQVSNDLLLKIKDTVLQRTVDGMQQ 264
Cdd:pfam01071 81 ETVVIEEFLEGEEVSVLAFVDGKTVKPLPPAQDHKRAGEGDTGPNTGGMGAYSPAPVITPELLERIKETIVEPTVDGLRK 160
|
170 180 190
....*....|....*....|....*....|....
gi 28416899 265 EGTPYTGILYAGIMLTKNGPKVLEFNCRFGDPEC 298
Cdd:pfam01071 161 EGIPFKGVLYAGLMLTKDGPKVLEFNCRFGDPET 194
|
|
| GARS_N |
pfam02844 |
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes ... |
4-104 |
1.18e-49 |
|
Phosphoribosylglycinamide synthetase, N domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the N-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam00289). This domain is structurally related to the PreATP-grasp domain.
Pssm-ID: 460723 [Multi-domain] Cd Length: 102 Bit Score: 163.68 E-value: 1.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 4 RVLIIGSGGREHTLAWKLAQSHHVKQVLVAPGNAGTACSEKisNTAISISDHTALAQFCKEKKIEFVVVGPEAPLAAGIV 83
Cdd:pfam02844 2 KVLVIGSGGREHALAWKLAQSPLVEKLYVAPGNGGTAQLAE--CVDIDATDFEALVAFAKENNIDLVVVGPEAPLVAGIV 79
|
90 100
....*....|....*....|...
gi 28416899 84 GNL--RSAGVQCFGPTAEAAQLE 104
Cdd:pfam02844 80 DALreRAAGIPVFGPSKAAAQLE 102
|
|
| GARS_C |
pfam02843 |
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes ... |
334-424 |
1.85e-38 |
|
Phosphoribosylglycinamide synthetase, C domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the C-terminal domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02787).
Pssm-ID: 460722 [Multi-domain] Cd Length: 88 Bit Score: 133.73 E-value: 1.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 334 ALTVVMASKGYPGDYTKGVEITGFPEAqalGLEVFHAGTALKNGKVVTHGGRVLAVTAIRENLISALEEAKKGLAAIKFE 413
Cdd:pfam02843 1 AVCVVLASGGYPGSYEKGDVITGLDEA---GVKVFHAGTKLKDGKLVTSGGRVLAVTALGDTLEEAREKAYEAVEKIDFE 77
|
90
....*....|.
gi 28416899 414 GAIYRKDVGFR 424
Cdd:pfam02843 78 GMFYRKDIGTR 88
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
57-294 |
1.12e-18 |
|
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: 85.31 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 57 ALAQFCKEKKIEFVVVGPEA--PLAAGIVGNLRsagvqCFGPTAEAAQLESSKRFAKEFMDRHGIPTAQWKAFTKPEEAC 134
Cdd:COG0439 8 AAAELARETGIDAVLSESEFavETAAELAEELG-----LPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 135 SFILSADFPaLVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKAFGAAGETIVIEELLDGEEVSCLCFTDGKTVAPMPP 214
Cdd:COG0439 83 AFAEEIGYP-VVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 215 AQDHKrllegdGGPNTGGMGAYCPAPqVSNDLLLKIKDTVlQRTVD--GMQqegtpyTGILYAGIMLTKNG-PKVLEFNC 291
Cdd:COG0439 162 TRKHQ------KPPYFVELGHEAPSP-LPEELRAEIGELV-ARALRalGYR------RGAFHTEFLLTPDGePYLIEINA 227
|
...
gi 28416899 292 RFG 294
Cdd:COG0439 228 RLG 230
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
107-256 |
2.77e-11 |
|
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: 63.97 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 107 KRFAKEFMDRHGIPTAQWKAFTKPEEACSFILSADFPA-LVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEkafgaaGE 185
Cdd:COG1181 96 KALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLpLFVKPAREGSSVGVSKVKNAEELAAALEEAFKY------DD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 186 TIVIEELLDGEEVSCLCFTDGKTVApMPPAQ----------DHKRllegdggpnTGGMGAY-CPAPqVSNDLLLKIKDTV 254
Cdd:COG1181 170 KVLVEEFIDGREVTVGVLGNGGPRA-LPPIEivpengfydyEAKY---------TDGGTEYiCPAR-LPEELEERIQELA 238
|
..
gi 28416899 255 LQ 256
Cdd:COG1181 239 LK 240
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
79-290 |
9.09e-10 |
|
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: 59.18 E-value: 9.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 79 AAGIVGNLRSAGVQCFGPtAEAAQLESSKRFAKEFMDRHGIPTAQWKAFTKPEEACSFILSADFPaLVVKASGLAAGKGV 158
Cdd:COG0189 70 GLALLRQLEAAGVPVVND-PEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGP-VVLKPLDGSGGRGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 159 IVAKSKEEAckavQEIMqEKAFGAAGETIVIEELL---DGEEVSCLCFtDGKTVAPM---PPAQDHKRllegdggpNT-- 230
Cdd:COG0189 148 FLVEDEDAL----ESIL-EALTELGSEPVLVQEFIpeeDGRDIRVLVV-GGEPVAAIrriPAEGEFRT--------NLar 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28416899 231 GGMGAYCPAPQVSNDLLLKIkdtvlqrtvdgmqqegTPYTGILYAGI--MLTKNGPKVLEFN 290
Cdd:COG0189 214 GGRAEPVELTDEERELALRA----------------APALGLDFAGVdlIEDDDGPLVLEVN 259
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
57-294 |
3.82e-09 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 57.97 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 57 ALAQFCKEKKIEFVVVG--PEAPLAAGIVGNLRSAGVQCFGPTAEAAQLESSKRFAKEFMDRHGIPTAQ-WKAFTKPE-E 132
Cdd:PRK12767 60 RLLDICKKEKIDLLIPLidPELPLLAQNRDRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKsYLPESLEDfK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 133 ACSFILSADFPaLVVKASGLAAGKGVIVAKSKEEACKAVQEImqekafgaagETIVIEELLDGEE--VSCLCFTDGKTVA 210
Cdd:PRK12767 140 AALAKGELQFP-LFVKPRDGSASIGVFKVNDKEELEFLLEYV----------PNLIIQEFIEGQEytVDVLCDLNGEVIS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 211 PMPpaqdHKRLLEGDGGPNTGGMGAYcpaPQVsNDLLLKIKDTVlqrtvdgmqqegtPYTGILYAGIMLTKNGPKVLEFN 290
Cdd:PRK12767 209 IVP----RKRIEVRAGETSKGVTVKD---PEL-FKLAERLAEAL-------------GARGPLNIQCFVTDGEPYLFEIN 267
|
....
gi 28416899 291 CRFG 294
Cdd:PRK12767 268 PRFG 271
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
66-292 |
8.09e-08 |
|
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: 54.62 E-value: 8.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 66 KIEFVVVGPEAPLAAGIVGNLRSAGVQCFGPTAEAA-QLESSKRFAkEFMDRHGIPTAQWKAFTKPEEACSFILSADFPA 144
Cdd:TIGR01369 629 KPEGVIVQFGGQTPLNLAKALEEAGVPILGTSPESIdRAEDREKFS-ELLDELGIPQPKWKTATSVEEAVEFASEIGYPV 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 145 LvVKASGLAAGKGVIVAKSKEEackaVQEIMQEKAFGAAGETIVIEELL-DGEEVSCLCFTDGKTVApMPPAQDHkrlLE 223
Cdd:TIGR01369 708 L-VRPSYVLGGRAMEIVYNEEE----LRRYLEEAVAVSPEHPVLIDKYLeDAVEVDVDAVSDGEEVL-IPGIMEH---IE 778
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28416899 224 gDGGPNTGGMGAYCPAPQVSNDLLLKIKDTVlQRTVDGMQqegtpYTGILYAGIMLTKNGPKVLEFNCR 292
Cdd:TIGR01369 779 -EAGVHSGDSTCVLPPQTLSAEIVDRIKDIV-RKIAKELN-----VKGLMNIQFAVKDGEVYVIEVNPR 840
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
89-193 |
2.12e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 53.06 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 89 AGVQCFGPTAEAAQLESSKRFAKEFMDRHGIPTAQW--KAFTKPEEACSFILSADFPaLVVKASGLAAGKGVIVAKSKEE 166
Cdd:PRK08654 98 AGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGteEGIEDIEEAKEIAEEIGYP-VIIKASAGGGGIGMRVVYSEEE 176
|
90 100
....*....|....*....|....*....
gi 28416899 167 ACKAVQEIMQ--EKAFGAAgeTIVIEELL 193
Cdd:PRK08654 177 LEDAIESTQSiaQSAFGDS--TVFIEKYL 203
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
111-199 |
3.93e-07 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 51.61 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 111 KEFMDRHGIPTAQWKAFTKPEEACSFILSADFPAlVVKasglAA-----GKGVIVAKSKEEACKAVQEImqekafgaAGE 185
Cdd:COG0026 94 KAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPA-VLK----TRrggydGKGQVVIKSAADLEAAWAAL--------GGG 160
|
90
....*....|....*
gi 28416899 186 TIVIEELLDGE-EVS 199
Cdd:COG0026 161 PCILEEFVPFErELS 175
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
110-194 |
6.55e-07 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 49.57 E-value: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 110 AKEFMDRHGIPTAQWKAFTKPEEACSFILSADFPALVVKASGLAAGK----GVIVAKSKEEACKAVQEIM-------QEK 178
Cdd:pfam08442 7 AKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLAGGRgkagGVKLAKSPEEAKEVAKEMLgknlvtkQTG 86
|
90
....*....|....*.
gi 28416899 179 AFGAAGETIVIEELLD 194
Cdd:pfam08442 87 PDGQPVNKVLVEEALD 102
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
62-209 |
9.57e-07 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 51.12 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 62 CKEKKIEFVVVGPEAPLAAGIVGNLRSAGVQCFGPTAEAA-QLESSKRFaKEFMDRHGIPTAQWKAFTKPEEACSFILSA 140
Cdd:PRK12815 626 AEAENIKGVIVQFGGQTAINLAKGLEEAGLTILGTSPDTIdRLEDRDRF-YQLLDELGLPHVPGLTATDEEEAFAFAKRI 704
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28416899 141 DFPALvVKASGLAAGKGVIVAKSKeeacKAVQEIMQEKAfgAAGETIVIEELLDGEEVSCLCFTDGKTV 209
Cdd:PRK12815 705 GYPVL-IRPSYVIGGQGMAVVYDE----PALEAYLAENA--SQLYPILIDQFIDGKEYEVDAISDGEDV 766
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
96-294 |
1.05e-06 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 50.31 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 96 PTAEA-AQLESSKRFAkEFMDRHGIPTAQWKAFTKPEEACSFILSADFPaLVVKAS--------GLAAGKGVIVAKSKEE 166
Cdd:COG3919 107 PDADLlDRLLDKERFY-ELAEELGVPVPKTVVLDSADDLDALAEDLGFP-VVVKPAdsvgydelSFPGKKKVFYVDDREE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 167 ACKAVQEImqekafGAAGETIVIEELLDGEE-----VSCLCFTDGKTVApmppAQDHKRLLEGdggPNTGGMGAYCPApq 241
Cdd:COG3919 185 LLALLRRI------AAAGYELIVQEYIPGDDgemrgLTAYVDRDGEVVA----TFTGRKLRHY---PPAGGNSAARES-- 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 28416899 242 VSNDLLLKIKDTVLqrtvdgmqqEGTPYTGILYAGIMLT-KNG-PKVLEFNCRFG 294
Cdd:COG3919 250 VDDPELEEAARRLL---------EALGYHGFANVEFKRDpRDGeYKLIEINPRFW 295
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
115-220 |
5.40e-06 |
|
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: 46.48 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 115 DRHGIPTAQWKAFTKPEEACSFILSADFPAlVVKASGLA-AGKGVIVAKSKEEACKAVQEimqekafgAAGETIVIEELL 193
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPC-VVKARRGGyDGKGQYVVRSEADLPQAWEE--------LGDGPVIVEEFV 71
|
90 100 110
....*....|....*....|....*....|
gi 28416899 194 DGE-EVSCLC--FTDGKTVAPmPPAQDHKR 220
Cdd:pfam02222 72 PFDrELSVLVvrSVDGETAFY-PVVETIQE 100
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
111-199 |
1.15e-05 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 47.07 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 111 KEFMDRHGIPTAQWKAFTKPEEACSFILSADFPAlVVKasglAA-----GKGVIVAKSKEEACKAVQEImqekafgaAGE 185
Cdd:PRK06019 105 KQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPA-VLK----TRrggydGKGQWVIRSAEDLEAAWALL--------GSV 171
|
90
....*....|....*
gi 28416899 186 TIVIEELLDGE-EVS 199
Cdd:PRK06019 172 PCILEEFVPFErEVS 186
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
78-207 |
4.34e-05 |
|
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: 45.64 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 78 LAAGIVGNLRSAGVQCFGPTAEAAQL-ESSKRFaKEFMDRHGIPTAQWKAFTKPEEACSFILSADFPaLVVKAS---Gla 153
Cdd:COG0458 86 LAVELEEAGILEGVKILGTSPDAIDLaEDRELF-KELLDKLGIPQPKSGTATSVEEALAIAEEIGYP-VIVRPSyvlG-- 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 28416899 154 aGKGVIVAKSKEEackaVQEIMqEKAFGAAGET-IVIEELLDG--E-EVSCLCftDGK 207
Cdd:COG0458 162 -GRGMGIVYNEEE----LEEYL-ERALKVSPDHpVLIDESLLGakEiEVDVVR--DGE 211
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
52-194 |
7.60e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 44.70 E-value: 7.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 52 ISDHTALAQFCKEKKIEFVvvgpeaplaagivgnlrsagvqcfGPTAEAAQLESSKRFAKEFMDRHGIPT--AQWKAFTK 129
Cdd:PRK05586 85 LSENSKFAKMCKECNIVFI------------------------GPDSETIELMGNKSNAREIMIKAGVPVvpGSEGEIEN 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28416899 130 PEEACSFILSADFPaLVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKAFGAAGETIVIEELLD 194
Cdd:PRK05586 141 EEEALEIAKEIGYP-VMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIE 204
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
78-198 |
9.43e-05 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 44.96 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 78 LAAGIvgnLRSAGVQCFGPTAEAAQL-ESSKRFaKEFMDRHGIPTAQWKAFTKPEEACSFILSADFPALVVKASGLaAGK 156
Cdd:PRK12815 103 HEDGI---LEQYGVELLGTNIEAIQKgEDRERF-RALMKELGEPVPESEIVTSVEEALAFAEKIGFPIIVRPAYTL-GGT 177
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 28416899 157 GVIVAKSKEEACKAVQEIMQEKAFgaagETIVIEELLDG-EEV 198
Cdd:PRK12815 178 GGGIAENLEELEQLFKQGLQASPI----HQCLLEESIAGwKEI 216
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
110-194 |
1.15e-04 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 43.93 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 110 AKEFMDRHGIPTAQWKAFTKPEEACSFILSADFPALVVKASGLAAGK----GVIVAKSKEEACKAVQEI--MQ--EKAFG 181
Cdd:PRK00696 8 AKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVWVVKAQVHAGGRgkagGVKLAKSPEEAREFAKQIlgMTlvTHQTG 87
|
90
....*....|....*.
gi 28416899 182 AAGET---IVIEELLD 194
Cdd:PRK00696 88 PKGQPvnkVLVEEGAD 103
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
142-209 |
1.56e-04 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 316093 [Multi-domain] Cd Length: 160 Bit Score: 41.89 E-value: 1.56e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28416899 142 FPaLVVKASGLAAGKGVIVAKSKEE---ACKAVQEIMQE-----KAFGAAGETIVIEELLDGEEVSCLCF--TDGKTV 209
Cdd:pfam13535 3 YP-CVIKPSVGFFSVGVYKINNREEwkaAFAAIREEIEQwkemyPEAVVDGGSFLVEEYIEGEEFAVDAYfdENGEPV 79
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
105-296 |
2.17e-04 |
|
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: 41.60 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 105 SSKRFAKEFMDRHGIPTaqwkaftkPEEACSFILSADFPALVVKASGLAAGKGVIVAKSKEEACkavqeimqekafgAAG 184
Cdd:pfam02655 2 SDKLKTYKALKNAGVPT--------PETLQAEELLREEKKYVVKPRDGCGGEGVRKVENGREDE-------------AFI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 185 ETIVIEELLDGEEVSCLCFTDGKTVAPMPPaqdHKRLLEGDGGPN--TGGMGaycPAPQVSNDLLLKIKDTVLQRtvdgm 262
Cdd:pfam02655 61 ENVLVQEFIEGEPLSVSLLSDGEKALPLSV---NRQYIDNGGSGFvyAGNVT---PSRTELKEEIIELAEEVVEC----- 129
|
170 180 190
....*....|....*....|....*....|....*..
gi 28416899 263 qqegtpYTGIL-YAGI--MLTKNGPKVLEFNCRFGDP 296
Cdd:pfam02655 130 ------LPGLRgYVGVdlVLKDNEPYVIEVNPRITTS 160
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
86-290 |
2.20e-04 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 42.72 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 86 LRSAGVQCFGPTaEAAQLESSKRFAKEFMDRHGIPTAQWKAFTKPEEACSFILSADFPAlVVKASGLAAGKGVIVAKSKE 165
Cdd:TIGR00768 69 LESLGVPVINSS-DAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPV-VLKPVFGSWGRGVSLARDRQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 166 EACKAvqeIMQEKAFGAAGETIVIEELLD---GEEVSCLCfTDGKTVAPMppaqdhKRLLEGDGGPNT--GGMGAYCPAP 240
Cdd:TIGR00768 147 AAESL---LEHFEQLNGPQNLFLVQEYIKkpgGRDIRVFV-VGDEVVAAI------YRITSGHWRSNLarGGKAEPCSLT 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 28416899 241 QVSNDLLLKIKDTVlqrtvdgmqqegtpytGILYAGIML--TKNGPKVLEFN 290
Cdd:TIGR00768 217 EEIEELAIKAAKAL----------------GLDVAGVDLleSEDGLLVNEVN 252
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
110-194 |
3.24e-04 |
|
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439815 [Multi-domain] Cd Length: 388 Bit Score: 42.73 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 110 AKEFMDRHGIPTAQWKAFTKPEEACSFILSADFPALVVKASGLAAGK----GVIVAKSKEEACKAVQEIM----QEKAFG 181
Cdd:COG0045 8 AKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVVKAQVHAGGRgkagGVKLAKSPEEAREAAEEILgmtlVTHQTG 87
|
90
....*....|....*.
gi 28416899 182 AAG---ETIVIEELLD 194
Cdd:COG0045 88 PKGkpvNKVLVEEGVD 103
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
113-200 |
6.80e-04 |
|
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: 40.76 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 113 FMDRHGIPTAQWKAFTK------PEEACSFILSA-DFPaLVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKafgaagE 185
Cdd:pfam07478 1 LLKAAGLPVVPFVTFTRadwklnPKEWCAQVEEAlGYP-VFVKPARLGSSVGVSKVESREELQAAIEEAFQYD------E 73
|
90
....*....|....*
gi 28416899 186 TIVIEELLDGEEVSC 200
Cdd:pfam07478 74 KVLVEEGIEGREIEC 88
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
86-200 |
1.07e-03 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 40.87 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 86 LRSAGVQCFGPTAEAAQLESSKRFAKEFMDRHGIPTAQWKAFTKPEEACSFILSA----DFPaLVVKASGLAAGKGVIVA 161
Cdd:PRK01966 103 LELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVVLTRGDWEEASLAEIeaklGLP-VFVKPANLGSSVGISKV 181
|
90 100 110
....*....|....*....|....*....|....*....
gi 28416899 162 KSKEEACKAVqeimqEKAFGAAgETIVIEELLDGEEVSC 200
Cdd:PRK01966 182 KNEEELAAAL-----DLAFEYD-RKVLVEQGIKGREIEC 214
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
89-209 |
1.66e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 40.40 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 89 AGVQCFGPTAEAAQLESSKRFAKEFMDRHGIPTAQW--KAFTKPEEACSFILSADFPaLVVKASGLAAGKGVIVAKSKEE 166
Cdd:PRK06111 98 EGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGitTNLEDAEEAIAIARQIGYP-VMLKASAGGGGIGMQLVETEQE 176
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 28416899 167 ACKAVqEIMQEKAFGAAGE-TIVIEELLDGE---EVSCLCFTDGKTV 209
Cdd:PRK06111 177 LTKAF-ESNKKRAANFFGNgEMYIEKYIEDPrhiEIQLLADTHGNTV 222
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
84-195 |
6.35e-03 |
|
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: 38.83 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 84 GNLRSAGVQCFGPTAEAAQLESSKRFAKEFMDRHGIPTAQWKAFTKPEEACSFILSADFPAlVVKASGLAAGKGVIVAKS 163
Cdd:TIGR01369 105 GVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPV-IVRPAFTLGGTGGGIAYN 183
|
90 100 110
....*....|....*....|....*....|...
gi 28416899 164 KEEAckavqEIMQEKAFGAAGET-IVIEELLDG 195
Cdd:TIGR01369 184 REEL-----KEIAERALSASPINqVLVEKSLAG 211
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
95-184 |
6.77e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 38.63 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28416899 95 GPTAEAAQLESSKRFAKEFMDRHGIPT--AQWKAFTKPEEACSFILSADFPaLVVKASGLAAGKGVIVAKSKEEACKAVQ 172
Cdd:PRK08591 104 GPSAETIRLMGDKVTAKATMKKAGVPVvpGSDGPVDDEEEALAIAKEIGYP-VIIKATAGGGGRGMRVVRTEAELEKAFS 182
|
90
....*....|....
gi 28416899 173 EIMQE--KAFGAAG 184
Cdd:PRK08591 183 MARAEakAAFGNPG 196
|
|
| |
