|
Name |
Accession |
Description |
Interval |
E-value |
| aconitase_mito |
TIGR01340 |
aconitate hydratase, mitochondrial; This model represents mitochondrial forms of the TCA cycle ... |
45-775 |
0e+00 |
|
aconitate hydratase, mitochondrial; This model represents mitochondrial forms of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. [Energy metabolism, TCA cycle]
Pssm-ID: 273561 [Multi-domain] Cd Length: 745 Bit Score: 1235.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 45 YDLLEKNINIVRKRLN-RPLTLSEKIVYGHLDDPA----SQEIE--RGKSYLRLRPDRVAMQDATAQMAMLQFISSGLSK 117
Cdd:TIGR01340 1 YEKLYNNLDEVRRRLNsRPLTLAEKILYSHLDDPEesllSQDIGdvRGKSYLKLRPDRVAMQDASAQMALLQFMTCGLPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 118 VAVPSTIHCDHLIEAQVGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWKPGSGIIHQIILENYAYPGVLLIGTDSHTPN 197
Cdd:TIGR01340 81 VAVPASIHCDHLIVGQKGGDKDLARAIATNKEVFDFLESAGKKYGIGFWKPGSGIIHQIVLENYAFPGLMMLGTDSHTPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 198 GGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISC 277
Cdd:TIGR01340 161 AGGLGTIAIGVGGADAVDALAGAPWELKAPKILGVKLTGKLNGWTSPKDIILKLAGLLTVRGGTGYIVEYFGPGVESLSC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 278 TGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGREDIANLADEFKDH---LVPDPGCHYDQLIEINLSELKPHINGPFT 354
Cdd:TIGR01340 241 TGMATICNMGAEIGATTSIFPFNEAMSRYLKATNRAQIAEDAKTGQYSffkLKADEGAQYDELIEIDLSKLEPHINGPFT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 355 PDLAHPVAEVGKVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIERDGYAQ 434
Cdd:TIGR01340 321 PDLSTPISKFKETVQKNGWPEKLSAGLIGSCTNSSYEDMSRCASIVKDAEQAGLKPKSPFYVTPGSEQIRATLERDGILQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 435 ILRDLGGIVLANACGPCIGQWDRKD-IKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSPEIVTALAIAGTLKFNPETDY 513
Cdd:TIGR01340 401 TFEKFGGIVLANACGPCIGQWDRKDdVKKGEPNTILTSYNRNFRGRNDGNPATMNFLASPEIVTAMSYAGSLTFNPLTDS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 514 LTGTDGKKFRLEAPDADELPKGEFDPGQDTYQHPPKDS-SGQHVDVSPTSQRLQLLEPFDKWDGKDLEDLQILIKVKGKC 592
Cdd:TIGR01340 481 LTTPDGKEFKFPAPKGDELPEKGFEAGRDTFQAPPGSPnPNVEVAVSPSSDRLQLLEPFEPWNGKDLSGLRVLIKVTGKC 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 593 TTDHISAAGPWLKFRGHLDNISNNLLIGAINIENGKANSVRNaVTQEFGPVPDTARYYKKHGIRWVVIGDENYGEGSSRE 672
Cdd:TIGR01340 561 TTDHISAAGPWLKYKGHLDNISNNTLIGAVNAETGEVNKAYD-LDGSKGTIPELARDWKARGQPWVVVAEHNYGEGSARE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 673 HAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQGLKDFTP---GKPLKCIIKHPNGTQ 749
Cdd:TIGR01340 640 HAALEPRHLGGRIIITKSFARIHETNLKKQGVLPLTFANEADYDKIQPGDEVATLNLYEMLKnggGGEVDLRVTKKNGKV 719
|
730 740
....*....|....*....|....*.
gi 4501867 750 ETILLNHTFNETQIEWFRAGSALNRM 775
Cdd:TIGR01340 720 FEIKLKHTVSKDQIGFFKAGSALNLM 745
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
61-777 |
0e+00 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 902.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 61 RPLTLSEKIVYGHLDDPasqEIERGKSyLRLRPDRVAMQDATAQMAMLQFISSGLSKVAVPSTI-HCDHlieaqvggekD 139
Cdd:PRK07229 1 MGLTLTEKILYAHLVEG---ELEPGEE-IAIRIDQTLTQDATGTMAYLQFEAMGLDRVKTELSVqYVDH----------N 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 140 LRRAKDINQEVYNFLATAGAKYGVGFWKPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAG 219
Cdd:PRK07229 67 LLQADFENADDHRFLQSVAAKYGIYFSKPGNGICHQVHLERFAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 220 IPWELKCPKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPY 299
Cdd:PRK07229 147 GPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 300 NHRMKKYLSKTGREDIAnladefkDHLVPDPGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVGKVAekegwpldIRV 379
Cdd:PRK07229 227 DERTREFLKAQGREDDW-------VELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVAGIK--------VDQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 380 GLIGSCTNSSYEDMGRSAAVAKqalAHGLKCKSQFTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGQwdrkD 459
Cdd:PRK07229 292 VLIGSCTNSSYEDLMRAASILK---GKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGM----G 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 460 IKKGEKNTIVTSYNRNFTGRNdANPETHAFVTSPEIVTALAIAGTLKfNPETdyLTGTDGKKFRLEAPDadelpkgEFDP 539
Cdd:PRK07229 365 QAPATGNVSLRTFNRNFPGRS-GTKDAQVYLASPETAAASALTGVIT-DPRT--LALENGEYPKLEEPE-------GFAV 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 540 GQDTYQHPPKDSSGQHVDVSPTSQRLQLLEPFDkwdgkDLEDLQILIKVKGKCTTDHISAAGP-WLKFRGHLDNISNNLL 618
Cdd:PRK07229 434 DDAGIIAPAEDGSDVEVVRGPNIKPLPLLEPLP-----DLLEGKVLLKVGDNITTDHIMPAGAkWLPYRSNIPNISEFVF 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 619 IGAINIENGKAnsvrnavtQEFGPvpdtaryykkhgirWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETN 698
Cdd:PRK07229 509 EGVDNTFPERA--------KEQGG--------------GIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKAN 566
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4501867 699 LKKQGLLPLTFADPADYNKIHPVDKLTIQGLKDFTPGKPLKCIIKHPNgtqETILLNHTFNETQIEWFRAGSALNRMKE 777
Cdd:PRK07229 567 LINFGILPLTFADPADYDKIEEGDVLEIEDLREFLPGGPLTVVNVTKD---EEIEVRHTLSERQIEILLAGGALNLIKK 642
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
95-505 |
0e+00 |
|
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Mitochondrial aconitase A catalytic domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediary product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 153134 Cd Length: 412 Bit Score: 872.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 95 RVAMQDATAQMAMLQFISSGLSKVAVPSTIHCDHLIEAQVGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWKPGSGIIH 174
Cdd:cd01584 1 RVAMQDATAQMALLQFMSSGLPKVAVPSTIHCDHLIEAQVGGEKDLKRAKDINKEVYDFLASAGAKYGIGFWKPGSGIIH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 175 QIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWSSPKDVILKVAGI 254
Cdd:cd01584 81 QIVLENYAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 255 LTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGREDIANLADEFK-DHLVPDPGCH 333
Cdd:cd01584 161 LTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEIADLADEFKdDLLVADEGAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 334 YDQLIEINLSELKPHINGPFTPDLAHPVAEVGKVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQ 413
Cdd:cd01584 241 YDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAEKNGWPLDLRVGLIGSCTNSSYEDMGRAASIAKQALAHGLKCKSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 414 FTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSP 493
Cdd:cd01584 321 FTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPATHAFVASP 400
|
410
....*....|..
gi 4501867 494 EIVTALAIAGTL 505
Cdd:cd01584 401 EIVTAMAIAGTL 412
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
41-775 |
0e+00 |
|
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle
Pssm-ID: 440669 [Multi-domain] Cd Length: 891 Bit Score: 748.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 41 EYIHYDL--LEKNINIVRKrlnrpLTLSEKIVYGHLD---DPAS------------QEIERGKSYLRLRPDRVAMQDATA 103
Cdd:COG1048 17 PYTYYSLpaLEEAGGDISR-----LPYSLKILLENLLrneDGETvteedikalanwLPKARGDDEIPFRPARVLMQDFTG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 104 QMAMLQFISSGLSKV-----------AVPSTIHCDHLIEAQVGG-----EKDLRRAKDINQEVYNFLATAGAKY-GVGFW 166
Cdd:COG1048 92 VPAVVDLAAMRDAVArlggdpkkinpLVPVDLVIDHSVQVDYFGtpdalEKNLELEFERNRERYQFLKWGQQAFdNFRVV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 167 KPGSGIIHQIILENYA--------------YPGvLLIGTDSHTPNggglggicigvggA-------------DAVDVMAG 219
Cdd:COG1048 172 PPGTGIVHQVNLEYLAfvvwtreedgetvaYPD-TLVGTDSHTTM-------------InglgvlgwgvggiEAEAAMLG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 220 IPWELKCPKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPY 299
Cdd:COG1048 238 QPVSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 300 NHRMKKYLSKTGREDI--------ANLADEFKDHLVPDPgcHYDQLIEINLSELKPHINGPFTPDLAHPVAEVGKVAEKE 371
Cdd:COG1048 318 DEETLDYLRLTGRSEEqielveayAKAQGLWRDPDAPEP--YYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 372 GWPL-----------------------DIRVGLIGSCTNSSYEDMGRSAA-VAKQALAHGLKCK--SQFTITPGSEQIRA 425
Cdd:COG1048 396 LAAPvgeeldkpvrvevdgeefelghgAVVIAAITSCTNTSNPSVMIAAGlLAKKAVEKGLKVKpwVKTSLAPGSKVVTD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 426 TIERDGYAQILRDLGGIVLANACGPCIGQWDR------KDIKKGE-KNTIVTSYNRNFTGRNDaNPETHAFVTSPEIVTA 498
Cdd:COG1048 476 YLERAGLLPYLEALGFNVVGYGCTTCIGNSGPlppeisEAIEENDlVVAAVLSGNRNFEGRIH-PDVKANFLASPPLVVA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 499 LAIAGTLKFNPETDYL-TGTDGKKFRLEA--PDADELPK----------------GEFD----------PGQDTYQHPPK 549
Cdd:COG1048 555 YALAGTVDIDLTTDPLgTDKDGKPVYLKDiwPSGEEIPAavfkavtpemfraryaDVFDgderwqalevPAGELYDWDPD 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 550 DSSgqhVDVSPTSQRLQLL-EPFdkwdgKDLEDLQILIKVKGKCTTDHISAAGP-----------------------WLK 605
Cdd:COG1048 635 STY---IRRPPFFEGLQLEpEPF-----KDIKGARVLAKLGDSITTDHISPAGAikadspagryllehgvepkdfnsYGS 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 606 FRGHLDNISNNLLIGaINIEN-----GKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRH 680
Cdd:COG1048 707 RRGNHEVMMRGTFAN-IRIKNllapgTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRL 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 681 LGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNK--IHPVDKLTIQGLKD-FTPGKPLKCIIKHPNGTQETILLNHT 757
Cdd:COG1048 786 LGVKAVIAESFERIHRSNLVGMGVLPLQFPEGESAESlgLTGDETFDIEGLDEgLAPGKTVTVTATRADGSTEEFPVLHR 865
|
890
....*....|....*....
gi 4501867 758 F-NETQIEWFRAGSALNRM 775
Cdd:COG1048 866 IdTPVEVEYYRAGGILQYV 884
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
67-503 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 564.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 67 EKIVYGHLDDPASQEIergkSYLrlrPDRVAMQDATAQMAMLQFISSGLSK-----------VAVPSTIHCDHlieAQVG 135
Cdd:pfam00330 1 EKIWDAHLVEELDGSL----LYI---PDRVLMHDVTSPQAFVDLRAAGRAVrrpggtpatidHLVPTDLVIDH---APDA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 136 GEKDLRRAKDINQEVYNFLATAGAKYGVGFWKPGSGIIHQIILEN-YAYPGVLLIGTDSHTPNggglggicigvggA--- 211
Cdd:pfam00330 71 LDKNIEDEISRNKEQYDFLEWNAKKFGIRFVPPGQGIVHQVGLEYgLALPGMTIVGTDSHTTT-------------Hggl 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 212 ----------DAVDVMAGIPWELKCPKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMA 281
Cdd:pfam00330 138 galafgvggsEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 282 TICNMGAEIGATTSVFPYNHRMKKYLSKTGREDIANLADEFK----DHLVPDPGCHYDQLIEINLSELKPHINGPFTPDL 357
Cdd:pfam00330 218 TICNMAIEYGATAGLFPPDETTFEYLRATGRPEAPKGEAYDKavawKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 358 AHPVAEVGKVAEKE------------------GWPL---DIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKS--QF 414
Cdd:pfam00330 298 AVPLSELVPDPFADavkrkaaeraleymglgpGTPLsdgKVDIAFIGSCTNSSIEDLRAAAGLLKKAVEKGLKVAPgvKA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 415 TITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGQWDRKDikkgEKNTIVTSYNRNFTGRNdaNPETHAFVTSPE 494
Cdd:pfam00330 378 SVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLP----PGERCVSSSNRNFEGRQ--GPGGRTHLASPA 451
|
....*....
gi 4501867 495 IVTALAIAG 503
Cdd:pfam00330 452 LVAAAAIAG 460
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
95-505 |
4.18e-168 |
|
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Aconitase catalytic domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. Aconitase, in its active form, contains a 4Fe-4S iron-sulfur cluster; three cysteine residues have been shown to be ligands of the 4Fe-4S cluster. This is the Aconitase core domain, including structural domains 1, 2 and 3, which binds the Fe-S cluster. The aconitase family also contains the following proteins: - Iron-responsive element binding protein (IRE-BP), a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid.
Pssm-ID: 153129 [Multi-domain] Cd Length: 389 Bit Score: 490.09 E-value: 4.18e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 95 RVAMQDATAQMAMLQFISSG-LSKVAVPSTIHCDHLIEAQVggekdlrrAKDINQEVYNFLATAGAKYGVGFWKPGSGII 173
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAaLGKVADPSQIACVHDHAVQL--------EKPVNNEGHKFLSFFAALQGIAFYRPGVGII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 174 HQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWSSPKDVILKVAG 253
Cdd:cd01351 73 HQIMVENLALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 254 ILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGREDIANLADEFKDHLVPDPGCH 333
Cdd:cd01351 153 IVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWLAFPEELLADEGAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 334 YDQLIEINLSELKPHINGPFTPDLAHPVAEVGKvaekegwpLDIRVGLIGSCTNSSYEDMGRSAAVAKQALahgLKCKSQ 413
Cdd:cd01351 233 YDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG--------TKIDQVLIGSCTNNRYSDMLAAAKLLKGAK---VAPGVR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 414 FTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGQWDRkdiKKGEKNTIVTSYNRNFTGRNDANPEtHAFVTSP 493
Cdd:cd01351 302 LIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGAR---LVADGEVGVSSGNRNFPGRLGTYER-HVYLASP 377
|
410
....*....|..
gi 4501867 494 EIVTALAIAGTL 505
Cdd:cd01351 378 ELAAATAIAGKI 389
|
|
| acon_putative |
TIGR01342 |
aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins ... |
64-777 |
5.29e-125 |
|
aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins homologous (and likely functionally equivalent to) aconitase 1. Members are found, so far in the anaerobe Clostridium acetobutylicum, in the microaerophilic, early-branching bacterium Aquifex aeolicus, and in the halophilic archaeon Halobacterium sp. NRC-1. No member is experimentally characterized. [Energy metabolism, TCA cycle]
Pssm-ID: 130409 [Multi-domain] Cd Length: 658 Bit Score: 388.96 E-value: 5.29e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 64 TLSEKIVYGHLddpASQEIERGKSyLRLRPDRVAMQDATAQMAMLQFISSGLSKVAVP-STIHCDHLIEaqvggEKDLRR 142
Cdd:TIGR01342 1 TLAEKIIDDHL---VEGDLEPGEE-IAIEIDQTLSQDATGTMCWLEFEALEMDEVKTElAAQYCDHNML-----QFDFKN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 143 AKDinqevYNFLATAGAKYGVGFWKPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPW 222
Cdd:TIGR01342 72 ADD-----HKFLMSAAGKFGAWFSKPGNGICHNVHKENFAAPGKTLLGSDSHTPTAGGLGMLAIGAGGIDIAAAMAGEAF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 223 ELKCPKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHR 302
Cdd:TIGR01342 147 YLEMPEIVGVHLEGELPEWATAKDIILELLRRLSVKGGLGKIFEYFGEGVEELSVPERATITNMGAELGATSSIFPSDDI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 303 MKKYLSKTGREDianladEFKDhLVPDPGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVgkvaekEGWPLDIRVglI 382
Cdd:TIGR01342 227 TEAWLAAFDRED------DFVD-LLADADAEYADEIEIDLSDLEPLIAEPHMPDNVVPVREI------AGIEVDQVM--I 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 383 GSCTNSSYEDMGRSAAVAKQALAHGlkcKSQFTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGQwdrkDIKK 462
Cdd:TIGR01342 292 GSCTNGAFEDLLPAAKLLEGREVHK---DTEFAVAPGSKQALELIAQEGALAEFLAAGANFLEAACGACIGI----GFAP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 463 GEKNTIVTSYNRNFTGRNdANPETHAFVTSPEIVTALAIAGTLkFNPETDYLTGTDGKKFRLEAPDadELPKGeFDPGqD 542
Cdd:TIGR01342 365 ASDGVSLRSFNRNFEGRA-GIEDAKVYLASPETATAAAIAGEI-IDPRDLADDEGDLEAIGFEMGE--KFPGG-YDAA-D 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 543 TYQHPPKDSSGQHVDVSPTSQRLQLLEPFdkwdGKDLEDlQILIKVKGKCTTDHISAAGP-WLKFRGHLDNISNNLLiga 621
Cdd:TIGR01342 439 IDIIPKEEREDDDIIKGPNIKPLPEFDPL----GADIEG-ETALIMEDNITTDHIIPAGAdILKFRSNIEAISEFTL--- 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 622 iniengkansvrNAVTQEFGPVPDTARYYKKHGIrwvVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKK 701
Cdd:TIGR01342 511 ------------HRIDDEFAERAKAADEKGKAGI---IIAGENYGQGSSREHAALAPMFLGVEAVIAKSFARIHHANLFN 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 702 QGLLPLTFADPADYNKIHPVDKLTI-----QGLKDftpGKPLKCIIKHpngTQETILLNHTFNETQIEWFRAGSALNRMK 776
Cdd:TIGR01342 576 FGILPLEFDNEEDYAKFELGDDIEIpddlaAALAD---GEDEFTINKN---DDEEALATLDASEREKEILAAGGKLNLIK 649
|
.
gi 4501867 777 E 777
Cdd:TIGR01342 650 N 650
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
587-735 |
1.37e-108 |
|
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 238810 [Multi-domain] Cd Length: 149 Bit Score: 327.50 E-value: 1.37e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 587 KVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINIENGKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVIGDENYG 666
Cdd:cd01578 1 KAKGKCTTDHISAAGPWLKYRGHLDNISNNLLIGAINAENGKANSVKNQVTGEYGPVPDTARDYKAHGIKWVVIGDENYG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4501867 667 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQGLKDFTPG 735
Cdd:cd01578 81 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYDKIHPDDKVDILGLTDFAPG 149
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
94-505 |
1.04e-107 |
|
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Bacterial Aconitase-like catalytic domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This distinct subfamily is found only in bacteria and Archaea. Its exact characteristics are not known.
Pssm-ID: 153135 Cd Length: 380 Bit Score: 334.42 E-value: 1.04e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 94 DRVAMQDATAQMAMLQFISSGLSKVAVP-STIHCDHLIEAQvggekDLRRAKDinqevYNFLATAGAKYGVGFWKPGSGI 172
Cdd:cd01585 1 DQTLTQDATGTMAYLQFEAMGVDRVRTElSVSYVDHNTLQT-----DFENADD-----HRFLQTVAARYGIYFSRPGNGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 173 IHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWSSPKDVILKVA 252
Cdd:cd01585 71 CHQVHLERFAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 253 GILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGREdianlaDEFKDhLVPDPGC 332
Cdd:cd01585 151 RRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGRE------DDWVE-LAADADA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 333 HYDQLIEINLSELKPHINGPFTPDlahpvaEVGKVAEKEGWPLDiRVgLIGSCTNSSYEDMGRSAAVAKQALAHGlkcKS 412
Cdd:cd01585 224 EYDEEIEIDLSELEPLIARPHSPD------NVVPVREVAGIKVD-QV-AIGSCTNSSYEDLMTVAAILKGRRVHP---HV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 413 QFTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGQWDrkdiKKGEKNTIVTSYNRNFTGRNdANPETHAFVTS 492
Cdd:cd01585 293 SMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQ----APPTGGVSVRTFNRNFEGRS-GTKDDLVYLAS 367
|
410
....*....|...
gi 4501867 493 PEIVTALAIAGTL 505
Cdd:cd01585 368 PEVAAAAALTGVI 380
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
92-780 |
7.51e-76 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 263.33 E-value: 7.51e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 92 RPDRVAMQDATAQMAM--LQFISSGLSKVA---------VPSTIHCDHLIEAQVGGEKD-LRRAKDI----NQEVYNFLA 155
Cdd:PRK12881 82 VPARVVMQDFTGVPALvdLAAMRDAAAEAGgdpakinplVPVDLVVDHSVAVDYFGQKDaLDLNMKIefqrNAERYQFLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 156 -TAGAKYGVGFWKPGSGIIHQIILE--------------NYAYPGVLlIGTDSHTP--NGGGLGGICIGVGGADAVdvMA 218
Cdd:PRK12881 162 wGMQAFDNFRVVPPGTGIMHQVNLEylarvvhtkeddgdTVAYPDTL-VGTDSHTTmiNGIGVLGWGVGGIEAEAV--ML 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 219 GIPWELKCPKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFP 298
Cdd:PRK12881 239 GQPVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFP 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 299 YNHRMKKYLSKTGRED--IANLADEFKDH---LVPDPGCHYDQLIEINLSELKPHINGP---------------FTPDLA 358
Cdd:PRK12881 319 VDEQTLDYLRLTGRTEaqIALVEAYAKAQglwGDPKAEPRYTRTLELDLSTVAPSLAGPkrpqdrialgnvksaFSDLFS 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 359 HPVAEVGKVAEKEGWPL------DIRVGLIGSCTNSSYEDMGRSAA-VAKQALAHGLKCKS--QFTITPGSEQIRATIER 429
Cdd:PRK12881 399 KPVAENGFAKKAQTSNGvdlpdgAVAIAAITSCTNTSNPSVLIAAGlLAKKAVERGLTVKPwvKTSLAPGSKVVTEYLER 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 430 DGYAQILRDLG-GIVlANACGPCIGQWD------RKDIKKGE-KNTIVTSYNRNFTGRNDANPEThAFVTSPEIVTALAI 501
Cdd:PRK12881 479 AGLLPYLEKLGfGIV-GYGCTTCIGNSGpltpeiEQAITKNDlVAAAVLSGNRNFEGRIHPNIKA-NFLASPPLVVAYAL 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 502 AGTLKFNPETDYL-TGTDGKKFRLE-----APDADELPKGEFDPgqDTYQH---PPKDSSGQ-HVDVSPTSQRLQ----- 566
Cdd:PRK12881 557 AGTVRRDLMTEPLgKGKDGRPVYLKdiwpsSAEIDALVAFAVDP--EDFRKnyaEVFKGSELwAAIEAPDGPLYDwdpks 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 567 --LLEP--FDKWDG-----KDLEDLQILIKVKGKCTTDHIS---------AAGPWLKFRGHLDNISN------------- 615
Cdd:PRK12881 635 tyIRRPpfFDFSMGpaasiATVKGARPLAVLGDSITTDHISpagaikadsPAGKYLKENGVPKADFNsygsrrgnhevmm 714
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 616 ----------NLLIGAinIENGkanSVRNAVTQEFGPVPDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRHLGGRA 685
Cdd:PRK12881 715 rgtfanvrikNLMIPG--KEGG---LTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGVKA 789
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 686 IITKSFARIHETNLKKQGLLPLTF--ADPADYNKIHPVDKLTIQGL-KDFTPGKPLKCIIKHPNGTQETILLNHTFnETQ 762
Cdd:PRK12881 790 VIAESFERIHRSNLVGMGVLPLQFkgGDSRQSLGLTGGETFDIEGLpGEIKPRQDVTLVIHRADGSTERVPVLCRI-DTP 868
|
810 820
....*....|....*....|
gi 4501867 763 IE--WFRAGSALNRMkeLQQ 780
Cdd:PRK12881 869 IEvdYYKAGGILPYV--LRQ 886
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
62-505 |
3.15e-75 |
|
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism]; Homoaconitase/3-isopropylmalate dehydratase large subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439835 Cd Length: 417 Bit Score: 249.95 E-value: 3.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 62 PLTLSEKIvyghLDDPASQEIERGKSYLrLRPDRVAMQDATAQMAMLQFISSGLSKVAVPSTIH--CDHLIEAqvggeKD 139
Cdd:COG0065 2 GMTLAEKI----LARHAGREVEPGEIVL-LYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVavFDHNVPT-----KD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 140 LRRAKDINQevynfLATAGAKYGVGFWKPGS-GIIHQIILEN-YAYPGVLLIGTDSHTPNGGglggicigvggA------ 211
Cdd:COG0065 72 PKSAEQVKT-----LREFAKEFGITFFDVGDpGICHVVLPEQgLVLPGMTIVGGDSHTCTHG-----------Afgafaf 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 212 -----DAVDVMA-GIPWeLKCPKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICN 285
Cdd:COG0065 136 gigttDVAHVLAtGTLW-FKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCN 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 286 MGAEIGATTSVFPYNHRMKKYLSKTGREDIANLAdefkdhlvPDPGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVG 365
Cdd:COG0065 215 MAIEAGAKAGIIAPDETTFEYLKGRPFAPWRTLK--------SDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 366 KVaekegwPLDirVGLIGSCTNSSYEDMGRSAAVAKqalahGLKCKS--QFTITPGSEQIRATIERDGYAQILRDLGGIV 443
Cdd:COG0065 287 GI------KID--QVFIGSCTNGRIEDLRAAAEILK-----GRKVAPgvRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEW 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4501867 444 LANACGPCIG-QWDRkdIKKGEKnTIVTSyNRNFTGRNdANPETHAFVTSPEIVTALAIAGTL 505
Cdd:COG0065 354 REPGCGMCLGmNMGV--LAPGER-CASTS-NRNFEGRM-GSPGSRTYLASPATAAASAIAGRI 411
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
92-774 |
1.47e-74 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 259.67 E-value: 1.47e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 92 RPDRVAMQDAT--------AQM--AMLQFissGL--SKV--AVPSTIHCDHLIEAQVGGEKD-LRRAKDI----NQEVYN 152
Cdd:PRK09277 83 RPARVVMQDFTgvpavvdlAAMrdAIADL---GGdpAKInpLVPVDLVIDHSVQVDYFGTPDaFEKNVELeferNEERYQ 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 153 FLatagaKYGVGFWK------PGSGIIHQIILE-------------NYAYPGVLlIGTDSHTPnggglggicigvggadA 213
Cdd:PRK09277 160 FL-----KWGQKAFDnfrvvpPGTGICHQVNLEylapvvwtredgeLVAYPDTL-VGTDSHTT----------------M 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 214 VD----------------VMAGIPWELKCPKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISC 277
Cdd:PRK09277 218 INglgvlgwgvggieaeaAMLGQPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 278 TGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRED--IAnladefkdhLV------------PDPGCHYDQLIEINLS 343
Cdd:PRK09277 298 ADRATIANMAPEYGATCGFFPIDEETLDYLRLTGRDEeqVA---------LVeayakaqglwrdPLEEPVYTDVLELDLS 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 344 ELKPHINGP-------FTPDLAHPVAEV--------GKVAEKEGWPLDIRVG-----LIGSCTNSS--YEDMGrsAA-VA 400
Cdd:PRK09277 369 TVEPSLAGPkrpqdriPLSDVKEAFAKSaelgvqgfGLDEAEEGEDYELPDGavviaAITSCTNTSnpSVMIA--AGlLA 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 401 KQALAHGLKCKS--QFTITPGSEQIRATIERDGYAQILRDLG-GIVlANACGPCIG---------QwdrKDIKkgEKNTI 468
Cdd:PRK09277 447 KKAVEKGLKVKPwvKTSLAPGSKVVTDYLEKAGLLPYLEALGfNLV-GYGCTTCIGnsgplppeiE---KAIN--DNDLV 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 469 VT---SYNRNFTGRndANPETHA-FVTSPEIVTALAIAGTLKFNPETDYL-TGTDGKKFRLEA--PDADEL--------- 532
Cdd:PRK09277 521 VTavlSGNRNFEGR--IHPLVKAnYLASPPLVVAYALAGTVDIDLEKDPLgTDKDGNPVYLKDiwPSDEEIdavvakavk 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 533 -----------------------PKGE---FDPgQDTY-QHPpkdssgqhvdvsptsqrlqllePFdkWDG--------K 577
Cdd:PRK09277 599 pemfrkeyadvfegderwnaievPEGPlydWDP-DSTYiRNP----------------------PY--FEGmlaepgpvR 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 578 DLEDLQILIKVKGKCTTDHIS---------AAGPWLK--------F--------------RGHLDNIS--NNLLIGainI 624
Cdd:PRK09277 654 DIKGARVLALLGDSITTDHISpagaikadsPAGKYLLehgvepkdFnsygsrrgnhevmmRGTFANIRirNEMVPG---V 730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 625 ENGKAnsvRNAVTQEFGPVPDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGL 704
Cdd:PRK09277 731 EGGYT---RHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGV 807
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4501867 705 LPLTFADPADYN--KIHPVDKLTIQGLKDFTPGKPLKCIIKHPNGTQETI-LLNHTFNETQIEWFRAGSALNR 774
Cdd:PRK09277 808 LPLQFKPGESRKtlGLDGTETFDIEGLEDLKPGATVTVVITRADGEVVEFpVLCRIDTAVEVDYYRNGGILQY 880
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
62-503 |
2.29e-69 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 234.30 E-value: 2.29e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 62 PLTLSEKIVYGHL-DDPASQEIergksyLRLRPDRVAMQDATAQMAMLQFISSGLSKVAVPSTIH--CDHLIEAqvggeK 138
Cdd:PRK00402 2 GMTLAEKILARHSgRDVSPGDI------VEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVivFDHFVPA-----K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 139 DLRRAKdINQEVYNFLATAGAKYgvgFWKPGSGIIHQIILEN-YAYPGVLLIGTDSHTPNggglggicigvggADAV--- 214
Cdd:PRK00402 71 DIKSAE-QQKILREFAKEQGIPN---FFDVGEGICHQVLPEKgLVRPGDVVVGADSHTCT-------------YGALgaf 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 215 -------D---VMA-GIPWeLKCPKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATI 283
Cdd:PRK00402 134 atgmgstDmaaAMAtGKTW-FKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 284 CNMGAEIGATTSVFPYNhrmkkylsKTGREDIANLADEFKDHLVPDPGCHYDQLIEINLSELKPHINGPFTPDLAHPVAE 363
Cdd:PRK00402 213 ANMAIEAGAKAGIFAPD--------EKTLEYLKERAGRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 364 VGKVaekegwPLDIRVglIGSCTNSSYEDMGRSAAVAKqalAHGLKCKSQFTITPGSEQIRATIERDGYAQILRDLGGIV 443
Cdd:PRK00402 285 VEGT------KVDQVF--IGSCTNGRLEDLRIAAEILK---GRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVV 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 444 LANACGPCIGqwdrkdIKKGEknTIVTSYNRNFTGRNdANPETHAFVTSPEIVTALAIAG 503
Cdd:PRK00402 354 STPTCGPCLGghm-gvLAPGE--VCLSTTNRNFKGRM-GSPESEVYLASPAVAAASAVTG 409
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
95-503 |
1.69e-66 |
|
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate; Aconatase-like catalytic domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes.
Pssm-ID: 153133 Cd Length: 382 Bit Score: 225.53 E-value: 1.69e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 95 RVAMQDATAQMAMLQFISSGLSKVAVPSTIHC--DHLIEAqvggeKDLRRAKDINQEVYNFlatagAKYGVGFWKPG-SG 171
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAvfDHNVPT-----PDIKAAEQVKTLRKFA-----KEFGINFFDVGrQG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 172 IIHQIILENY-AYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMA-GIPWeLKCPKVIGVKLTGSLSGWSSPKDVIL 249
Cdd:cd01583 71 ICHVILPEKGlTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLAtGKLW-FRVPETMRVNVEGKLPPGVTAKDVIL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 250 KVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGREdianladEFKdHLVPD 329
Cdd:cd01583 150 YIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKA-------YWK-ELKSD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 330 PGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVGKVaekegwPLDIRVglIGSCTNSSYEDMGRSAAVAKqalAHGLK 409
Cdd:cd01583 222 EDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEGI------KIDQVF--IGSCTNGRLEDLRAAAEILK---GRKVA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 410 CKSQFTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIG-QWDRkdIKKGEknTIVTSYNRNFTGR-NDANPETH 487
Cdd:cd01583 291 DGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGgHMGV--LAPGE--RCVSTSNRNFKGRmGSPGARIY 366
|
410
....*....|....*.
gi 4501867 488 afVTSPEIVTALAIAG 503
Cdd:cd01583 367 --LASPATAAASAITG 380
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
94-773 |
3.48e-64 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 230.67 E-value: 3.48e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 94 DRVAMQDATAQMAmlqfisSGLSKV--AVPSTIHCDHLIEAQVGGEKD-LRRAKDI----NQEVYNFLatagaKYGVGFW 166
Cdd:PTZ00092 106 DLAAMRDAMKRLG------GDPAKInpLVPVDLVIDHSVQVDFSRSPDaLELNQEIeferNLERFEFL-----KWGSKAF 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 167 K------PGSGIIHQIILE----------NYAYPGVLlIGTDSHTP--NGGGLGGICIGVGGADAVdvMAGIPWELKCPK 228
Cdd:PTZ00092 175 KnllivpPGSGIVHQVNLEylarvvfnkdGLLYPDSV-VGTDSHTTmiNGLGVLGWGVGGIEAEAV--MLGQPISMVLPE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 229 VIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLS 308
Cdd:PTZ00092 252 VVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLK 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 309 KTGR-EDIANLADEF--KDHLVPDPGCH--YDQLIEINLSELKPHINGP---------------FTPDLAHPVA------ 362
Cdd:PTZ00092 332 QTGRsEEKVELIEKYlkANGLFRTYAEQieYSDVLELDLSTVVPSVAGPkrphdrvplsdlkkdFTACLSAPVGfkgfgi 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 363 ---EVGKVAEKE--GWPLDIRVG-----LIGSCTNSSYED-MGRSAAVAKQALAHGLKCKS--QFTITPGSEQIRATIER 429
Cdd:PTZ00092 412 peeKHEKKVKFTykGKEYTLTHGsvviaAITSCTNTSNPSvMLAAGLLAKKAVEKGLKVPPyiKTSLSPGSKVVTKYLEA 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 430 DGYAQILRDLGGIVLANACGPCIGqwDRKDIKKGEKNTI---------VTSYNRNFTGRndANPETHA-FVTSPEIVTAL 499
Cdd:PTZ00092 492 SGLLKYLEKLGFYTAGYGCMTCIG--NSGDLDPEVSEAItnndlvaaaVLSGNRNFEGR--VHPLTRAnYLASPPLVVAY 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 500 AIAGTLKFNPETDYL-TGTDGKKFRLEA--PDADEL--------------------------------PKGEF---DPgQ 541
Cdd:PTZ00092 568 ALAGRVNIDFETEPLgSDKTGKPVFLRDiwPSREEIqaleakyvkpemfkevysnitqgnkqwnelqvPKGKLyewDE-K 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 542 DTYQHPPKDSSGQHVDVSPTsqrlqllepfdkwdgKDLEDLQILIKVKGKCTTDHISAAG------PWLKF--------- 606
Cdd:PTZ00092 647 STYIHNPPFFQTMELEPPPI---------------KSIENAYCLLNLGDSITTDHISPAGniaknsPAAKYlmergverk 711
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 607 ----------------RGHLDNIS-NNLLIGA-----INIENGKANSVRNAvtqefgpvpdtARYYKKHGIRWVVIGDEN 664
Cdd:PTZ00092 712 dfntygarrgndevmvRGTFANIRlINKLCGKvgpntVHVPTGEKMSIYDA-----------AEKYKQEGVPLIVLAGKE 780
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 665 YGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFAD--PADYNKIHPVDKLTIQGLK-DFTPGKPLKci 741
Cdd:PTZ00092 781 YGSGSSRDWAAKGPYLQGVKAVIAESFERIHRSNLVGMGILPLQFLNgeNADSLGLTGKEQFSIDLNSgELKPGQDVT-- 858
|
810 820 830
....*....|....*....|....*....|...
gi 4501867 742 IKHPNG-TQETILLNHTfnETQIEWFRAGSALN 773
Cdd:PTZ00092 859 VKTDTGkTFDTILRIDT--EVEVEYFKHGGILQ 889
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
582-712 |
1.51e-61 |
|
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This domain undergoes conformational change in the enzyme mechanism.
Pssm-ID: 459908 [Multi-domain] Cd Length: 131 Bit Score: 202.98 E-value: 1.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 582 LQILIKVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINIENGKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVIG 661
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 4501867 662 DENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADP 712
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
67-714 |
2.25e-60 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 220.45 E-value: 2.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 67 EKIVYGHLDDPASQEIErgksylrLRPDRVAMQDAT--------AQM--AMLQfISSGLSKV--AVPSTIHCDHLIEAQV 134
Cdd:PLN00070 103 EKIIDWENTSPKQVEIP-------FKPARVLLQDFTgvpavvdlACMrdAMNN-LGGDPNKInpLVPVDLVIDHSVQVDV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 135 GGEKDLRRAK-----DINQEVYNFLatagaKYGVGFWK------PGSGIIHQIILENYA----------YPGVLlIGTDS 193
Cdd:PLN00070 175 ARSENAVQANmelefQRNKERFAFL-----KWGSTAFQnmlvvpPGSGIVHQVNLEYLGrvvfntdgilYPDSV-VGTDS 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 194 HTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVD 273
Cdd:PLN00070 249 HTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMS 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 274 SISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRED----------IANlaDEFKDHLVPDPGCHYDQLIEINLS 343
Cdd:PLN00070 329 ELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDetvamieaylRAN--KMFVDYNEPQQERVYSSYLELDLE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 344 ELKPHINGPFTP------------------------DLAHPVAEVGKVAE--KEGWPLDIRVG-----LIGSCTNSSYED 392
Cdd:PLN00070 407 DVEPCISGPKRPhdrvplkemkadwhscldnkvgfkGFAVPKEAQSKVAKfsFHGQPAELRHGsvviaAITSCTNTSNPS 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 393 -MGRSAAVAKQALAHGLKCKS--QFTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGqwDRKDIKKGEKNTI- 468
Cdd:PLN00070 487 vMLGAGLVAKKACELGLEVKPwiKTSLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIG--NSGELDESVASAIt 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 469 --------VTSYNRNFTGRndANPETHA-FVTSPEIVTALAIAGTLKFNPETDYL-TGTDGKK--FRLEAPDADELPKGE 536
Cdd:PLN00070 565 endivaaaVLSGNRNFEGR--VHPLTRAnYLASPPLVVAYALAGTVDIDFEKEPIgTGKDGKDvfFRDIWPSNEEVAEVV 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 537 F-----DPGQDTYQHPPK------------------DSSGQHVDVSPTSQRLQLLEPfdkwDGKDLEDLQILIKVKGKCT 593
Cdd:PLN00070 643 QssvlpDMFKSTYEAITKgnpmwnqlsvpsgtlyswDPKSTYIHEPPYFKNMTMSPP----GPHGVKDAYCLLNFGDSIT 718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 594 TDHISAAG------PWLKF-------------------------RGHLDNIS--NNLLIG-----AINIENGKANSVRna 635
Cdd:PLN00070 719 TDHISPAGsihkdsPAAKYlmergvdrkdfnsygsrrgndeimaRGTFANIRivNKLLKGevgpkTVHIPTGEKLSVF-- 796
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4501867 636 vtqefgpvpDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPAD 714
Cdd:PLN00070 797 ---------DAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGED 866
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
64-503 |
2.60e-59 |
|
homoaconitate hydratase family protein; This model represents a subfamily of proteins consisting of aconitase, homoaconitase, 3-isopropylmalate dehydratase, and uncharacterized proteins. The majority of the members of this family have been designated as 3-isopropylmalate dehydratase large subunit (LeuC) in microbial genome annotation, but the only characterized member is Thermus thermophilus homoaconitase, an enzyme of a non-aspartate pathway of Lys biosynthesis.
Pssm-ID: 273563 Cd Length: 412 Bit Score: 206.91 E-value: 2.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 64 TLSEKIVYGHlddpASQEIERGKSyLRLRPDRVAMQDATAQMAMLQFISSGLSKVAVPSTIHC--DHLIEAqvggekDLR 141
Cdd:TIGR01343 1 TIAEKILSKK----SGKEVYAGDL-IEAEIDLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIvfDHQVPA------DTI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 142 RAKDINQEVYNFLATAGAKYgvgFWKPGSGIIHQIILEN-YAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMA-G 219
Cdd:TIGR01343 70 KAAEMQKLAREFVKKQGIKY---FYDVGEGICHQVLPEKgLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIAtG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 220 IPWeLKCPKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPY 299
Cdd:TIGR01343 147 KTW-FKVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 300 NHRMKKYLSKTGREDianlADEFKDhlvpDPGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVgkvaekEGWPLDiRV 379
Cdd:TIGR01343 226 DEKTIQYLKERRKEP----FRVYKS----DEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEV------EGTEID-QV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 380 gLIGSCTNSSYEDMGRSAAVAKqalAHGLKCKSQFTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGqwdRKD 459
Cdd:TIGR01343 291 -FIGSCTNGRLEDLRVAAKILK---GRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLG---SHQ 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 4501867 460 IKKGEKNTIVTSYNRNFTGRNdANPETHAFVTSPEIVTALAIAG 503
Cdd:TIGR01343 364 GVLAPGEVCISTSNRNFKGRM-GHPNAEIYLASPATAAASAVKG 406
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
95-504 |
1.83e-46 |
|
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydrolyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes.
Pssm-ID: 153136 Cd Length: 404 Bit Score: 170.95 E-value: 1.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 95 RVAMQDAT--------AQM--AMlQFISSGLSKV--AVPSTIHCDHLIEAQVGG-----EKDLRRAKDINQEVYNFLata 157
Cdd:cd01586 1 RVILQDFTgvpavvdlAAMrdAV-KRLGGDPEKInpLIPVDLVIDHSVQVDFYGtadalAKNMKLEFERNRERYEFL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 158 gaKYGVGFWK------PGSGIIHQIILE--------------NYAYPGVLlIGTDSHTPNGGGLGGICIGVGGADAVDVM 217
Cdd:cd01586 77 --KWGQKAFKnlrvvpPGTGIIHQVNLEylarvvftseedgdGVAYPDSV-VGTDSHTTMINGLGVLGWGVGGIEAEAVM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 218 AGIPWELKCPKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVF 297
Cdd:cd01586 154 LGQPISMLLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 298 PYNhrmkkylsktgredianladefkdhlvpdpgchyDQLIEINLSELKPHINGPFTPDlaHPVAEVGKVAekegwpldi 377
Cdd:cd01586 234 PVD----------------------------------TQVVELDLSTVEPSVSGPKRPQ--DRVPLHGSVV--------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 378 rVGLIGSCTNSSYED-MGRSAAVAKQALAHGLKCKS--QFTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIG- 453
Cdd:cd01586 269 -IAAITSCTNTSNPSvMLAAGLLAKKAVELGLKVKPyvKTSLAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGn 347
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 4501867 454 -----QWDRKDIKKGE-KNTIVTSYNRNFTGRndANPETHA-FVTSPEIVTALAIAGT 504
Cdd:cd01586 348 sgplpEEVEEAIKENDlVVAAVLSGNRNFEGR--IHPLVRAnYLASPPLVVAYALAGT 403
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
108-505 |
2.70e-37 |
|
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase catalytic domain. Homoaconitase and other uncharacterized proteins of the Aconitase family. Homoaconitase is part of an unusual lysine biosynthesis pathway found only in filamentous fungi, in which lysine is synthesized via the alpha-aminoadipate pathway. In this pathway, homoaconitase catalyzes the conversion of cis-homoaconitic acid into homoisocitric acid. The reaction mechanism is believed to be similar to that of other aconitases.
Pssm-ID: 153132 [Multi-domain] Cd Length: 363 Bit Score: 143.52 E-value: 2.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 108 LQFISSGLSKVAVPSTIHC--DHliEAQVGGEKDLRRAKDINqevyNFlataGAKYGVGFWKPGSGIIHQIILEN-YAYP 184
Cdd:cd01582 13 LKFMSIGATKIHNPDQIVMtlDH--DVQNKSEKNLKKYKNIE----SF----AKKHGIDFYPAGRGIGHQIMIEEgYAFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 185 GVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMA-GIPWeLKCPKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGA 263
Cdd:cd01582 83 GTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWAtGQTW-WQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLNH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 264 IVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRmkkylsktgredianladefkdHLVpdpgchydqlieINLS 343
Cdd:cd01582 162 AIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAK----------------------HLI------------LDLS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 344 ELKPHINGPFTPDLAHPVAEVgkvaekEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQA--------LAHGLKcksqFT 415
Cdd:cd01582 208 TLSPYVSGPNSVKVSTPLKEL------EAQNIKINKAYLVSCTNSRASDIAAAADVVKGKkekngkipVAPGVE----FY 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 416 ITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGqWDRKDIKKGEKNtiVTSYNRNFTGRNdANPETHAFVTSPEI 495
Cdd:cd01582 278 VAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIG-LGQGLLEPGEVG--ISATNRNFKGRM-GSTEALAYLASPAV 353
|
410
....*....|
gi 4501867 496 VTALAIAGTL 505
Cdd:cd01582 354 VAASAISGKI 363
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
227-505 |
1.23e-31 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 129.08 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 227 PKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGA---------TTsvF 297
Cdd:PRK05478 163 PKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGAraglvapdeTT--F 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 298 PYnhrMKkylsktGREDIANLAD-----EFKDHLVPDPGCHYDQLIEINLSELKPH------------INGPFtPDLAHP 360
Cdd:PRK05478 241 EY---LK------GRPFAPKGEDwdkavAYWKTLKSDEDAVFDKVVTLDAADIEPQvtwgtnpgqvisIDGKV-PDPEDF 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 361 VAEVGKVAEKE---------GWPL-DIRVG--LIGSCTNSSYEDMGRSAAVAKqalahGLKCKSQFT--ITPGSEQIRAT 426
Cdd:PRK05478 311 ADPVKRASAERalaymglkpGTPItDIKIDkvFIGSCTNSRIEDLRAAAAVVK-----GRKVAPGVRalVVPGSGLVKAQ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 427 IERDGYAQILRDLG------GivlanaCGPCIGQWDrkDIKKGEKNTIVTSyNRNFTGRNDANPETHafVTSPEIVTALA 500
Cdd:PRK05478 386 AEAEGLDKIFIEAGfewrepG------CSMCLAMNP--DKLPPGERCASTS-NRNFEGRQGKGGRTH--LVSPAMAAAAA 454
|
....*
gi 4501867 501 IAGTL 505
Cdd:PRK05478 455 ITGHF 459
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
587-728 |
4.44e-30 |
|
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. The aconitase family contains the following proteins: - Iron-responsive element binding protein (IRE-BP). IRE-BP is a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid.
Pssm-ID: 238236 [Multi-domain] Cd Length: 88 Bit Score: 113.72 E-value: 4.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 587 KVKGKCTTDHISAAGPWlkfrghldnisnnlligainiengkansvrnavtqefgpvpdtaryykkhgirwVVIGDENYG 666
Cdd:cd00404 1 KVAGNITTDHISPAGPG------------------------------------------------------VVIGDENYG 26
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4501867 667 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQG 728
Cdd:cd00404 27 TGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDYLKLHTGDELDIYP 88
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
587-728 |
1.93e-28 |
|
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism. This distinct subfamily is found only in bacteria and archea. Its exact characteristics are not known.
Pssm-ID: 238811 [Multi-domain] Cd Length: 121 Bit Score: 110.22 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 587 KVKGKCTTDHISAAGP-WLKFRGHLDNISNNLLIGainiengkansvrnaVTQEFGPvpdtaryYKKHGIRWVVIGDENY 665
Cdd:cd01579 1 KVGDNITTDHIMPAGAkVLPLRSNIPAISEFVFHR---------------VDPTFAE-------RAKAAGPGFIVGGENY 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4501867 666 GEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQG 728
Cdd:cd01579 59 GQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADEDDYDRFEQGDQLELPL 121
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
60-505 |
9.57e-28 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 117.70 E-value: 9.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 60 NRPLTLSEKIVYGH----LDDPASQeiergksylrLRPDRVAMQDATAQMAMLQFISSGLsKVAVPSTIHC--DHLIEAQ 133
Cdd:PRK12466 1 MMPRTLYDKLWDSHtvarLDDGHVL----------LYIDRHLLNEYTSPQAFSGLRARGR-TVRRPDLTLAvvDHVVPTR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 134 VGGEKDLRRAKDINQEVYnfLATAGAKYGV---GFWKPGSGIIHQIILE-NYAYPGVLLIGTDSHTPNGGGLGGICIGVG 209
Cdd:PRK12466 70 PGRDRGITDPGGALQVDY--LRENCADFGIrlfDVDDPRQGIVHVVAPElGLTLPGMVIVCGDSHTTTYGALGALAFGIG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 210 GADAVDVMAGIPWELKCPKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAE 289
Cdd:PRK12466 148 TSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 290 IGATTSVFPYNHRMKKYLSKTGREDIANLADEFKDH---LVPDPGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVGK 366
Cdd:PRK12466 228 AGARGGLIAPDETTFDYLRGRPRAPKGALWDAALAYwrtLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 367 VAEKE--------------------GWPL-DIRVG--LIGSCTNSSYEDMGRSAAVAKqalahGLKCKSQFT--ITPGSE 421
Cdd:PRK12466 308 DPAAEadparraameraldymgltpGTPLaGIPIDrvFIGSCTNGRIEDLRAAAAVLR-----GRKVAPGVRamVVPGSG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 422 QIRATIERDGYAQILRDLGGIVLANACGPCIGQWDRKdIKKGEKntIVTSYNRNFTGRNDANPETHafVTSPEIVTALAI 501
Cdd:PRK12466 383 AVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDV-LAPGER--CASTTNRNFEGRQGPGARTH--LMSPAMVAAAAV 457
|
....
gi 4501867 502 AGTL 505
Cdd:PRK12466 458 AGHI 461
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
89-731 |
9.67e-27 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 116.65 E-value: 9.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 89 LRLRPDRVAMQDAT----AQMAmlqfISSGLSKVAVPSTIHCDHLIEAQVGGEkdlrrakdINQEVYNFLATAGAKYGVG 164
Cdd:PRK11413 54 LKIKFDSLASHDITfvgiIQTA----KASGMERFPLPYVLTNCHNSLCAVGGT--------INEDDHVFGLSAAQKYGGI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 165 FWKPGSGIIHQIILENYAYPGVLLIGTDSHTpnggglggicigvgGADAVDVMA---GIP----------WELKCPKVIG 231
Cdd:PRK11413 122 FVPPHIAVIHQYMREMMAGGGKMILGSDSHT--------------RYGALGTMAvgeGGGelvkqllndtYDIDYPGVVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 232 VKLTGSLSGWSSPKDVILKVAGILTVKGGT-GAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKT 310
Cdd:PRK11413 188 VYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLALH 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 311 GREdianlaDEFKDhLVPDPGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVGKVA-------EKEGWPLD------- 376
Cdd:PRK11413 268 GRG------QDYCE-LNPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDELNQNLtdilrevEIESERVAhgkakls 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 377 ---------IRV--GLIGSCTNSSYEDMgrsaavakQALAHGLKCKS----QFTIT--PGSEQIRATIERDGYAQILRDL 439
Cdd:PRK11413 341 lldkiengrLKVqqGIIAGCSGGNYENV--------IAAANALRGQScgndTFSLSvyPSSQPVFMDLAKKGVVADLMGA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 440 GGIVLANACGPCIGQWDrkdikkgekntivTSYNRNF----TGRNDANPE----THAFVTSPEIVTALAIAGTLKFNpet 511
Cdd:PRK11413 413 GAIIRTAFCGPCFGAGD-------------TPANNGLsirhTTRNFPNREgskpANGQMSAVALMDARSIAATAANG--- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 512 DYLTGTDgkkfrlEAPDADELPKGEFDPgqDTYQHPPKDSSGQHVdvspTSQRLQLLEPFDKWdgKDLEDL--QILIKVK 589
Cdd:PRK11413 477 GYLTSAT------ELDCWDNVPEYAFDV--TPYKNRVYQGFGKGA----TQQPLIYGPNIKDW--PEMGALtdNILLKVC 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 590 GK-----CTTDHISAAGPWLKFRghldniSNNLLIGAIN--------IENGKA-----NSVRNAVTQEFGPVPDTAR-YY 650
Cdd:PRK11413 543 SKildpvTTTDELIPSGETSSYR------SNPLGLAEFTlsrrdpgyVGRSKAvaeleNQRLAGNVSELTEVFARIKqIA 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 651 KKHGIRW--VVIGDENY----GEGSSREHAALEPRHLGGRAIITKSFA-RIHETNLKKQGLLPLTFADPadyNKIHPVDK 723
Cdd:PRK11413 617 GQEHIDPlqTEIGSMVYavkpGDGSAREQAASCQRVLGGLANIAEEYAtKRYRSNVINWGMLPFQMAEE---PTFEVGDY 693
|
....*...
gi 4501867 724 LTIQGLKD 731
Cdd:PRK11413 694 IYIPGIRA 701
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
593-728 |
1.13e-18 |
|
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238812 [Multi-domain] Cd Length: 171 Bit Score: 84.25 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 593 TTDHISAAGPWLK-------------------------------FRGHLDNISN-NLLIGainieNGKANSVRNAVTQEF 640
Cdd:cd01580 7 TTDHISPAGSIAKdspagkylaergvkprdfnsygsrrgndevmMRGTFANIRLrNKLVP-----GTEGGTTHHPPTGEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 641 GPVPDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADP--ADYNKI 718
Cdd:cd01580 82 MSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGenADSLGL 161
|
170
....*....|
gi 4501867 719 HPVDKLTIQG 728
Cdd:cd01580 162 TGEETYDIIG 171
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
658-726 |
1.06e-13 |
|
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238809 [Multi-domain] Cd Length: 91 Bit Score: 67.23 E-value: 1.06e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 658 VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYN-KIHPVDKLTI 726
Cdd:cd01577 20 IIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEvEAKPGDEVEV 89
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
658-726 |
1.79e-11 |
|
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; 3-isopropylmalate dehydratase small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439836 [Multi-domain] Cd Length: 195 Bit Score: 64.04 E-value: 1.79e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4501867 658 VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTfADPADYNKI------HPVDKLTI 726
Cdd:COG0066 67 ILVAGRNFGCGSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIE-LPEEAVDALfaaieaNPGDELTV 140
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
162-505 |
5.13e-10 |
|
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle; Aconitase B catalytic domain. Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle. Aconitase has an active (4FE-4S) and an inactive (3FE-4S) form. The active cluster is part of the catalytic site that interconverts citrate, cis-aconitase and isocitrate. The domain architecture of aconitase B is different from other aconitases in that the catalytic domain is normally found at C-terminus for other aconitases, but it is at N-terminus for B family. It also has a HEAT domain before domain 4 which plays a role in protein-protein interaction. This alignment is the core domain including domains 1,2 and 3.
Pssm-ID: 153131 Cd Length: 436 Bit Score: 62.52 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 162 GVGFWKPGSGIIHQIiLENYAYPGVLLIGTDSHT--PNGGGLGGICIGVGGADAVDVMAgipweLKCPKVIGVKLTGSLS 239
Cdd:cd01581 85 GGVALRPGDGVIHSW-LNRMLLPDTVGTGGDSHTrfPIGISFPAGSGLVAFAAATGVMP-----LDMPESVLVRFKGKMQ 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 240 GWSSPKDVILKV------AGILTV--KGG----TGAIVEYHGpgVDSISCTGMATICNMGAEIGATTSVFPYNH------ 301
Cdd:cd01581 159 PGITLRDLVNAIpyyaiqQGLLTVekKGKknvfNGRILEIEG--LPDLKVEQAFELTDASAERSAAACTVRLDKepviey 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 302 ------RMKKYLSKtGREDIANLADEFKDH---------LVPDPGCHYDQLIEINLSELK-PHINGPFTPDLAHPVAEV- 364
Cdd:cd01581 237 lesnvvLMKIMIAN-GYDDARTLLRRIIAMeewlanpplLEPDADAEYAAVIEIDLDDIKePILACPNDPDDVKLLSEVa 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 365 GKVaekegwpldIRVGLIGSC-TNssyedMGRSAAVAKQALAHGLKcKSQFTITPGSEQIRATIERDGYAQILRDLGGIV 443
Cdd:cd01581 316 GKK---------IDEVFIGSCmTN-----IGHFRAAAKILRGKEFK-PTRLWVAPPTRMDWAILQEEGYYSIFGDAGART 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4501867 444 LANACGPCIGQWDRkdIKKGEknTIVTSYNRNFTGR--NDANpethAFVTSPEIVTALAIAGTL 505
Cdd:cd01581 381 EMPGCSLCMGNQAR--VADGA--TVFSTSTRNFDNRvgKGAE----VYLGSAELAAVCALLGRI 436
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
658-740 |
1.06e-09 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 57.91 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 658 VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADynKIHPVDKLTI---QG-LKDFT 733
Cdd:PRK00439 51 IIVAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIGLPVLECDEAVD--KIEDGDEVEVdleTGvITNLT 128
|
....*..
gi 4501867 734 PGKPLKC 740
Cdd:PRK00439 129 TGEEYKF 135
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
152-538 |
8.81e-09 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 59.17 E-value: 8.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 152 NFLATAGakyGVGFwKPGSGIIHQIiLENYAYPGVLLIGTDSHT--PNGGGLGGICIGVGGADAVDVMAgipweLKCPKV 229
Cdd:PLN00094 525 DFIRNRG---GVSL-RPGDGVIHSW-LNRMLLPDTVGTGGDSHTrfPIGISFPAGSGLVAFGAATGVIP-----LDMPES 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 230 IGVKLTGSLSGWSSPKDVILKV------AGILTV-KGG-----TGAIVEYHGpgVDSISCTGMATICNMGAEIGAT---- 293
Cdd:PLN00094 595 VLVRFTGTMQPGITLRDLVHAIpytaiqDGLLTVeKKGkknvfSGRILEIEG--LPHLKCEQAFELSDASAERSAAgcti 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 294 ----TSVFPY---NHRMKKYLSKTGRED-------IANLADEFKD-HLV-PDPGCHYDQLIEINLSELK-PHINGPFTPD 356
Cdd:PLN00094 673 kldkEPIIEYlnsNVVMLKWMIAEGYGDrrtlerrIARMQQWLADpELLeADPDAEYAAVIEIDMDEIKePILCAPNDPD 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 357 LAHPVAEV--GKVAEKegwpldirvgLIGSC-TNssyedMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIERDGYA 433
Cdd:PLN00094 753 DARLLSEVtgDKIDEV----------FIGSCmTN-----IGHFRAAGKLLNDNLSQLPTRLWVAPPTKMDEAQLKAEGYY 817
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4501867 434 QILRDLGGIVLANACGPCIGQWDRKdikkGEKNTIVTSYNRNFTGR--NDANpethAFVTSPEIVTALAIAGTLKfNPEt 511
Cdd:PLN00094 818 STFGTVGARTEMPGCSLCMGNQARV----AEKSTVVSTSTRNFPNRlgKGAN----VYLASAELAAVAAILGRLP-TVE- 887
|
410 420
....*....|....*....|....*..
gi 4501867 512 DYLTGTDgkkfRLEAPDADELPKGEFD 538
Cdd:PLN00094 888 EYLSYME----KLDATASDTYRYLNFD 910
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
644-714 |
1.16e-08 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 55.19 E-value: 1.16e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4501867 644 PDTARYYKKHGIrwvVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPAD 714
Cdd:PRK14023 41 PEFASTVRPGDI---LVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPPFESEEVVD 108
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
658-707 |
5.22e-08 |
|
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the 3-isopropylmalate dehydratase, small subunits which form TIGR00171. This subfamily includes the members of TIGR02084 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities.
Pssm-ID: 273961 [Multi-domain] Cd Length: 154 Bit Score: 52.81 E-value: 5.22e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 4501867 658 VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPL 707
Cdd:TIGR02087 50 VIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLI 99
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
658-726 |
2.19e-07 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 52.05 E-value: 2.19e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4501867 658 VVIGDENYGEGSSREHA--ALEprHLGGRAIITKSFARIHETNLKKQGLLPLTfADPADYNKI------HPVDKLTI 726
Cdd:PRK01641 70 ILLAGDNFGCGSSREHApwALA--DYGFRAVIAPSFADIFYNNCFKNGLLPIV-LPEEDVDELfklveaNPGAELTV 143
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
658-694 |
2.15e-05 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 46.78 E-value: 2.15e-05
10 20 30
....*....|....*....|....*....|....*..
gi 4501867 658 VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARI 694
Cdd:PLN00072 132 IIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARI 168
|
|
| |
