|
Name |
Accession |
Description |
Interval |
E-value |
| aconitase_mito |
TIGR01340 |
aconitate hydratase, mitochondrial; This model represents mitochondrial forms of the TCA cycle ... |
17-747 |
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: 1231.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 17 YDLLEKNIDIVRKRLN-RPLTLSEKIVYGHLDDPAN----QEIE--RGKTYLRLRPDRVAMQDATAQMAMLQFISSGLPK 89
Cdd:TIGR01340 1 YEKLYNNLDEVRRRLNsRPLTLAEKILYSHLDDPEEsllsQDIGdvRGKSYLKLRPDRVAMQDASAQMALLQFMTCGLPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 90 VAVPSTIHCDHLIEAQLGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIHQIILENYAYPGVLLIGTDSHTPN 169
Cdd:TIGR01340 81 VAVPASIHCDHLIVGQKGGDKDLARAIATNKEVFDFLESAGKKYGIGFWKPGSGIIHQIVLENYAFPGLMMLGTDSHTPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 170 GGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISC 249
Cdd:TIGR01340 161 AGGLGTIAIGVGGADAVDALAGAPWELKAPKILGVKLTGKLNGWTSPKDIILKLAGLLTVRGGTGYIVEYFGPGVESLSC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 250 TGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFKDH---LVPDPGCHYDQVIEINLSELKPHINGPFT 326
Cdd:TIGR01340 241 TGMATICNMGAEIGATTSIFPFNEAMSRYLKATNRAQIAEDAKTGQYSffkLKADEGAQYDELIEIDLSKLEPHINGPFT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 327 PDLAHPVAEVGSVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIERDGYAQ 406
Cdd:TIGR01340 321 PDLSTPISKFKETVQKNGWPEKLSAGLIGSCTNSSYEDMSRCASIVKDAEQAGLKPKSPFYVTPGSEQIRATLERDGILQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 407 VLRDVGGIVLANACGPCIGQWDRKD-IKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSPEIVTALAIAGTLKFNPETDF 485
Cdd:TIGR01340 401 TFEKFGGIVLANACGPCIGQWDRKDdVKKGEPNTILTSYNRNFRGRNDGNPATMNFLASPEIVTAMSYAGSLTFNPLTDS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 486 LTGKDGKKFKLEAPDADELPRAEFDPGQDTYQHPPKDS-SGQRVDVSPTSQRLQLLEPFDKWDGKDLEDLQILIKVKGKC 564
Cdd:TIGR01340 481 LTTPDGKEFKFPAPKGDELPEKGFEAGRDTFQAPPGSPnPNVEVAVSPSSDRLQLLEPFEPWNGKDLSGLRVLIKVTGKC 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 565 TTDHISAAGPWLKFRGHLDNISNNLLIGAINIENRKANSVRNaVTQEFGPVPDTARYYKQHGIRWVVIGDENYGEGASRE 644
Cdd:TIGR01340 561 TTDHISAAGPWLKYKGHLDNISNNTLIGAVNAETGEVNKAYD-LDGSKGTIPELARDWKARGQPWVVVAEHNYGEGSARE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 645 HSALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQGLKDFAP---GKPLKCIIKHPNGTQ 721
Cdd:TIGR01340 640 HAALEPRHLGGRIIITKSFARIHETNLKKQGVLPLTFANEADYDKIQPGDEVATLNLYEMLKnggGGEVDLRVTKKNGKV 719
|
730 740
....*....|....*....|....*.
1B0K_A 722 ETILLNHTFNETQIEWFRAGSALNRM 747
Cdd:TIGR01340 720 FEIKLKHTVSKDQIGFFKAGSALNLM 745
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
33-753 |
0e+00 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 896.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 33 RPLTLSEKIVYGHLDDPanqEIERGKTyLRLRPDRVAMQDATAQMAMLQFISSGLPKVAVPSTI-HCDHlieaqlggekD 111
Cdd:PRK07229 1 MGLTLTEKILYAHLVEG---ELEPGEE-IAIRIDQTLTQDATGTMAYLQFEAMGLDRVKTELSVqYVDH----------N 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 112 LRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAG 191
Cdd:PRK07229 67 LLQADFENADDHRFLQSVAAKYGIYFSKPGNGICHQVHLERFAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 192 IPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPY 271
Cdd:PRK07229 147 GPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 272 NHRMKKYLSKTGRADIAnladefkDHLVPDPGCHYDQVIEINLSELKPHINGPFTPDLAHPVAEVGsvaekegwPLDIRV 351
Cdd:PRK07229 227 DERTREFLKAQGREDDW-------VELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVA--------GIKVDQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 352 GLIGSCTNSSYEDMGRSAAVAKqalAHGLKCKSQFTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGQwdrkD 431
Cdd:PRK07229 292 VLIGSCTNSSYEDLMRAASILK---GKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGM----G 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 432 IKKGEKNTIVTSYNRNFTGRNdANPETHAFVTSPEIVTALAIAGTLKfNPETdfLTGKDGKKFKLEAPDadelpraEFDP 511
Cdd:PRK07229 365 QAPATGNVSLRTFNRNFPGRS-GTKDAQVYLASPETAAASALTGVIT-DPRT--LALENGEYPKLEEPE-------GFAV 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 512 GQDTYQHPPKDSSGQRVDVSPTSQRLQLLEPFDkwdgkDLEDLQILIKVKGKCTTDHISAAGP-WLKFRGHLDNISNNLL 590
Cdd:PRK07229 434 DDAGIIAPAEDGSDVEVVRGPNIKPLPLLEPLP-----DLLEGKVLLKVGDNITTDHIMPAGAkWLPYRSNIPNISEFVF 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 591 IGAINIENRKAnsvrnavtQEFGPvpdtaryykqhgirWVVIGDENYGEGASREHSALEPRHLGGRAIITKSFARIHETN 670
Cdd:PRK07229 509 EGVDNTFPERA--------KEQGG--------------GIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKAN 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 671 LKKQGLLPLTFADPADYNKIHPVDKLTIQGLKDFAPGKPLKCIIKHPNgtqETILLNHTFNETQIEWFRAGSALNRMKEL 750
Cdd:PRK07229 567 LINFGILPLTFADPADYDKIEEGDVLEIEDLREFLPGGPLTVVNVTKD---EEIEVRHTLSERQIEILLAGGALNLIKKK 643
|
...
1B0K_A 751 QQK 753
Cdd:PRK07229 644 LAA 646
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
67-477 |
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: 875.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 67 RVAMQDATAQMAMLQFISSGLPKVAVPSTIHCDHLIEAQLGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIH 146
Cdd:cd01584 1 RVAMQDATAQMALLQFMSSGLPKVAVPSTIHCDHLIEAQVGGEKDLKRAKDINKEVYDFLASAGAKYGIGFWKPGSGIIH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 147 QIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGI 226
Cdd:cd01584 81 QIVLENYAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 227 LTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFK-DHLVPDPGCH 305
Cdd:cd01584 161 LTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEIADLADEFKdDLLVADEGAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 306 YDQVIEINLSELKPHINGPFTPDLAHPVAEVGSVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQ 385
Cdd:cd01584 241 YDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAEKNGWPLDLRVGLIGSCTNSSYEDMGRAASIAKQALAHGLKCKSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 386 FTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSP 465
Cdd:cd01584 321 FTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPATHAFVASP 400
|
410
....*....|..
1B0K_A 466 EIVTALAIAGTL 477
Cdd:cd01584 401 EIVTAMAIAGTL 412
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
10-747 |
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: 743.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 10 EPHEYIRYDLLEKNIDIVRKrlnrpLTLSEKIVYGHLD---DPAN------------QEIERGKTYLRLRPDRVAMQDAT 74
Cdd:COG1048 16 KPYTYYSLPALEEAGGDISR-----LPYSLKILLENLLrneDGETvteedikalanwLPKARGDDEIPFRPARVLMQDFT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 75 AQMAMLQFISSGLPKV-----------AVPSTIHCDHLIEAQLGG-----EKDLRRAKDINQEVYNFLATAGAKY-GVGF 137
Cdd:COG1048 91 GVPAVVDLAAMRDAVArlggdpkkinpLVPVDLVIDHSVQVDYFGtpdalEKNLELEFERNRERYQFLKWGQQAFdNFRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 138 WRPGSGIIHQIILENYA--------------YPGvLLIGTDSHTPNggglggicigvggA-------------DAVDVMA 190
Cdd:COG1048 171 VPPGTGIVHQVNLEYLAfvvwtreedgetvaYPD-TLVGTDSHTTM-------------InglgvlgwgvggiEAEAAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 191 GIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFP 270
Cdd:COG1048 237 GQPVSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 271 YNHRMKKYLSKTGRADI--------ANLADEFKDHLVPDPgcHYDQVIEINLSELKPHINGPFTPDLAHPVAEVGSVAEK 342
Cdd:COG1048 317 VDEETLDYLRLTGRSEEqielveayAKAQGLWRDPDAPEP--YYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 343 EGWPL-----------------------DIRVGLIGSCTNSSYEDMGRSAA-VAKQALAHGLKCK--SQFTITPGSEQIR 396
Cdd:COG1048 395 ALAAPvgeeldkpvrvevdgeefelghgAVVIAAITSCTNTSNPSVMIAAGlLAKKAVEKGLKVKpwVKTSLAPGSKVVT 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 397 ATIERDGYAQVLRDVGGIVLANACGPCIGQWDR------KDIKKGE-KNTIVTSYNRNFTGRNDaNPETHAFVTSPEIVT 469
Cdd:COG1048 475 DYLERAGLLPYLEALGFNVVGYGCTTCIGNSGPlppeisEAIEENDlVVAAVLSGNRNFEGRIH-PDVKANFLASPPLVV 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 470 ALAIAGTLKFNPETDFL-TGKDGKKFKLEA--PDADELPRAEFD--------------------------PGQDTYQHPP 520
Cdd:COG1048 554 AYALAGTVDIDLTTDPLgTDKDGKPVYLKDiwPSGEEIPAAVFKavtpemfraryadvfdgderwqalevPAGELYDWDP 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 521 KDSSgqrVDVSPTSQRLQLL-EPFdkwdgKDLEDLQILIKVKGKCTTDHISAAGP-----------------------WL 576
Cdd:COG1048 634 DSTY---IRRPPFFEGLQLEpEPF-----KDIKGARVLAKLGDSITTDHISPAGAikadspagryllehgvepkdfnsYG 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 577 KFRGHLDNISNNLLIGaINIEN-----RKANSVRNAVTQEFGPVPDTARYYKQHGIRWVVIGDENYGEGASREHSALEPR 651
Cdd:COG1048 706 SRRGNHEVMMRGTFAN-IRIKNllapgTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTR 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 652 HLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNK--IHPVDKLTIQGLKD-FAPGKPLKCIIKHPNGTQETILLNH 728
Cdd:COG1048 785 LLGVKAVIAESFERIHRSNLVGMGVLPLQFPEGESAESlgLTGDETFDIEGLDEgLAPGKTVTVTATRADGSTEEFPVLH 864
|
890 900
....*....|....*....|
1B0K_A 729 TF-NETQIEWFRAGSALNRM 747
Cdd:COG1048 865 RIdTPVEVEYYRAGGILQYV 884
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
39-475 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 561.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 39 EKIVYGHLDDPANQEIERgktylrlRPDRVAMQDATAQMAMLQFISSGLPK-----------VAVPSTIHCDHlieAQLG 107
Cdd:pfam00330 1 EKIWDAHLVEELDGSLLY-------IPDRVLMHDVTSPQAFVDLRAAGRAVrrpggtpatidHLVPTDLVIDH---APDA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 108 GEKDLRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIHQIILEN-YAYPGVLLIGTDSHTPNggglggicigvggA--- 183
Cdd:pfam00330 71 LDKNIEDEISRNKEQYDFLEWNAKKFGIRFVPPGQGIVHQVGLEYgLALPGMTIVGTDSHTTT-------------Hggl 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 184 ----------DAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMA 253
Cdd:pfam00330 138 galafgvggsEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 254 TICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFK----DHLVPDPGCHYDQVIEINLSELKPHINGPFTPDL 329
Cdd:pfam00330 218 TICNMAIEYGATAGLFPPDETTFEYLRATGRPEAPKGEAYDKavawKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 330 AHPVAEVGSVAEKE------------------GWPL---DIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKS--QF 386
Cdd:pfam00330 298 AVPLSELVPDPFADavkrkaaeraleymglgpGTPLsdgKVDIAFIGSCTNSSIEDLRAAAGLLKKAVEKGLKVAPgvKA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 387 TITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGQWDRKDikkgEKNTIVTSYNRNFTGRNdaNPETHAFVTSPE 466
Cdd:pfam00330 378 SVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLP----PGERCVSSSNRNFEGRQ--GPGGRTHLASPA 451
|
....*....
1B0K_A 467 IVTALAIAG 475
Cdd:pfam00330 452 LVAAAAIAG 460
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
67-477 |
7.68e-172 |
|
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: 498.95 E-value: 7.68e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 67 RVAMQDATAQMAMLQFISSGLP-KVAVPSTIHCDHLIEAQLggekdlrrAKDINQEVYNFLATAGAKYGVGFWRPGSGII 145
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAALgKVADPSQIACVHDHAVQL--------EKPVNNEGHKFLSFFAALQGIAFYRPGVGII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 146 HQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAG 225
Cdd:cd01351 73 HQIMVENLALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 226 ILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFKDHLVPDPGCH 305
Cdd:cd01351 153 IVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWLAFPEELLADEGAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 306 YDQVIEINLSELKPHINGPFTPDLAHPVAEVGSvaekegwpLDIRVGLIGSCTNSSYEDMGRSAAVAKQALahgLKCKSQ 385
Cdd:cd01351 233 YDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG--------TKIDQVLIGSCTNNRYSDMLAAAKLLKGAK---VAPGVR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 386 FTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGQWDRkdiKKGEKNTIVTSYNRNFTGRNDANPEtHAFVTSP 465
Cdd:cd01351 302 LIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGAR---LVADGEVGVSSGNRNFPGRLGTYER-HVYLASP 377
|
410
....*....|..
1B0K_A 466 EIVTALAIAGTL 477
Cdd:cd01351 378 ELAAATAIAGKI 389
|
|
| acon_putative |
TIGR01342 |
aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins ... |
36-753 |
1.46e-123 |
|
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: 384.34 E-value: 1.46e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 36 TLSEKIVYGHLddpANQEIERGKTyLRLRPDRVAMQDATAQMAMLQFISSGLPKVAVP-STIHCDHLIEaqlggEKDLRR 114
Cdd:TIGR01342 1 TLAEKIIDDHL---VEGDLEPGEE-IAIEIDQTLSQDATGTMCWLEFEALEMDEVKTElAAQYCDHNML-----QFDFKN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 115 AKDinqevYNFLATAGAKYGVGFWRPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPW 194
Cdd:TIGR01342 72 ADD-----HKFLMSAAGKFGAWFSKPGNGICHNVHKENFAAPGKTLLGSDSHTPTAGGLGMLAIGAGGIDIAAAMAGEAF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 195 ELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHR 274
Cdd:TIGR01342 147 YLEMPEIVGVHLEGELPEWATAKDIILELLRRLSVKGGLGKIFEYFGEGVEELSVPERATITNMGAELGATSSIFPSDDI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 275 MKKYLSKTGRADianladEFKDhLVPDPGCHYDQVIEINLSELKPHINGPFTPDLAHPVAEVgsvaekEGWPLDIRVglI 354
Cdd:TIGR01342 227 TEAWLAAFDRED------DFVD-LLADADAEYADEIEIDLSDLEPLIAEPHMPDNVVPVREI------AGIEVDQVM--I 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 355 GSCTNSSYEDMGRSAAVAKQALAHGlkcKSQFTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGQwdrkDIKK 434
Cdd:TIGR01342 292 GSCTNGAFEDLLPAAKLLEGREVHK---DTEFAVAPGSKQALELIAQEGALAEFLAAGANFLEAACGACIGI----GFAP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 435 GEKNTIVTSYNRNFTGRNdANPETHAFVTSPEIVTALAIAGTLkFNPETdfLTGKDGKkfkLEAPDAdELPrAEFDPGQD 514
Cdd:TIGR01342 365 ASDGVSLRSFNRNFEGRA-GIEDAKVYLASPETATAAAIAGEI-IDPRD--LADDEGD---LEAIGF-EMG-EKFPGGYD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 515 ---TYQHPPKDSSGQRVDVSPTSQRLQLLEPFdkwdGKDLEDlQILIKVKGKCTTDHISAAGP-WLKFRGHLDNISNNLL 590
Cdd:TIGR01342 436 aadIDIIPKEEREDDDIIKGPNIKPLPEFDPL----GADIEG-ETALIMEDNITTDHIIPAGAdILKFRSNIEAISEFTL 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 591 igainienrkansvrNAVTQEFGPvpdTARYYKQHGIRWVVIGDENYGEGASREHSALEPRHLGGRAIITKSFARIHETN 670
Cdd:TIGR01342 511 ---------------HRIDDEFAE---RAKAADEKGKAGIIIAGENYGQGSSREHAALAPMFLGVEAVIAKSFARIHHAN 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 671 LKKQGLLPLTFADPADYNKIHPVDKLTIQG--LKDFAPGKPLKCIIKHpngTQETILLNHTFNETQIEWFRAGSALNRMK 748
Cdd:TIGR01342 573 LFNFGILPLEFDNEEDYAKFELGDDIEIPDdlAAALADGEDEFTINKN---DDEEALATLDASEREKEILAAGGKLNLIK 649
|
....*
1B0K_A 749 ELQQK 753
Cdd:TIGR01342 650 NKHRE 654
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
66-477 |
3.42e-109 |
|
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: 337.50 E-value: 3.42e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 66 DRVAMQDATAQMAMLQFISSGLPKVAVP-STIHCDHLIeAQLGGEkdlrrakdiNQEVYNFLATAGAKYGVGFWRPGSGI 144
Cdd:cd01585 1 DQTLTQDATGTMAYLQFEAMGVDRVRTElSVSYVDHNT-LQTDFE---------NADDHRFLQTVAARYGIYFSRPGNGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 145 IHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVA 224
Cdd:cd01585 71 CHQVHLERFAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 225 GILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRadianlADEFKDhLVPDPGC 304
Cdd:cd01585 151 RRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGR------EDDWVE-LAADADA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 305 HYDQVIEINLSELKPHINGPFTPDLAHPVAEVGsvaekegwPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGlkcKS 384
Cdd:cd01585 224 EYDEEIEIDLSELEPLIARPHSPDNVVPVREVA--------GIKVDQVAIGSCTNSSYEDLMTVAAILKGRRVHP---HV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 385 QFTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGQWDrkdiKKGEKNTIVTSYNRNFTGRNdANPETHAFVTS 464
Cdd:cd01585 293 SMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQ----APPTGGVSVRTFNRNFEGRS-GTKDDLVYLAS 367
|
410
....*....|...
1B0K_A 465 PEIVTALAIAGTL 477
Cdd:cd01585 368 PEVAAAAALTGVI 380
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
559-707 |
3.97e-107 |
|
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: 323.27 E-value: 3.97e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 559 KVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINIENRKANSVRNAVTQEFGPVPDTARYYKQHGIRWVVIGDENYG 638
Cdd:cd01578 1 KAKGKCTTDHISAAGPWLKYRGHLDNISNNLLIGAINAENGKANSVKNQVTGEYGPVPDTARDYKAHGIKWVVIGDENYG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1B0K_A 639 EGASREHSALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQGLKDFAPG 707
Cdd:cd01578 81 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYDKIHPDDKVDILGLTDFAPG 149
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
34-477 |
2.48e-78 |
|
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: 257.65 E-value: 2.48e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 34 PLTLSEKIvyghLDDPANQEIERGKTYLrLRPDRVAMQDATAQMAMLQFISSGLPKVAVPSTIH--CDHLIEAqlggeKD 111
Cdd:COG0065 2 GMTLAEKI----LARHAGREVEPGEIVL-LYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVavFDHNVPT-----KD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 112 LRRAKDINQevynfLATAGAKYGVGFWRPGS-GIIHQIILEN-YAYPGVLLIGTDSHTPNGGglggicigvggA------ 183
Cdd:COG0065 72 PKSAEQVKT-----LREFAKEFGITFFDVGDpGICHVVLPEQgLVLPGMTIVGGDSHTCTHG-----------Afgafaf 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 184 -----DAVDVMA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICN 257
Cdd:COG0065 136 gigttDVAHVLAtGTLW-FKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCN 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 258 MGAEIGATTSVFPYNHRMKKYLSKTGRADIANLAdefkdhlvPDPGCHYDQVIEINLSELKPHINGPFTPDLAHPVAEVG 337
Cdd:COG0065 215 MAIEAGAKAGIIAPDETTFEYLKGRPFAPWRTLK--------SDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 338 SVaekegwPLDirVGLIGSCTNSSYEDMGRSAAVAKqalahGLKCKS--QFTITPGSEQIRATIERDGYAQVLRDVGGIV 415
Cdd:COG0065 287 GI------KID--QVFIGSCTNGRIEDLRAAAEILK-----GRKVAPgvRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEW 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
1B0K_A 416 LANACGPCIG-QWDRkdIKKGEKnTIVTSyNRNFTGRNdANPETHAFVTSPEIVTALAIAGTL 477
Cdd:COG0065 354 REPGCGMCLGmNMGV--LAPGER-CASTS-NRNFEGRM-GSPGSRTYLASPATAAASAIAGRI 411
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
64-752 |
2.36e-73 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 256.01 E-value: 2.36e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 64 RPDRVAMQDATAQ------MAMLQFISS--GLPKV---AVPSTIHCDHLIEAQLGGEKD-LRRAKDI----NQEVYNFLA 127
Cdd:PRK12881 82 VPARVVMQDFTGVpalvdlAAMRDAAAEagGDPAKinpLVPVDLVVDHSVAVDYFGQKDaLDLNMKIefqrNAERYQFLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 128 -TAGAKYGVGFWRPGSGIIHQIILE--------------NYAYPGVLlIGTDSHTP--NGGGLGGICIGVGGADAVdvMA 190
Cdd:PRK12881 162 wGMQAFDNFRVVPPGTGIMHQVNLEylarvvhtkeddgdTVAYPDTL-VGTDSHTTmiNGIGVLGWGVGGIEAEAV--ML 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 191 GIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFP 270
Cdd:PRK12881 239 GQPVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFP 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 271 YNHRMKKYLSKTGRAD--IANLADEFKDH---LVPDPGCHYDQVIEINLSELKPHINGP---------------FTPDLA 330
Cdd:PRK12881 319 VDEQTLDYLRLTGRTEaqIALVEAYAKAQglwGDPKAEPRYTRTLELDLSTVAPSLAGPkrpqdrialgnvksaFSDLFS 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 331 HPVAEVG-SVAEKEGWPLDIRVG-----LIGSCTNSSYEDMGRSAA-VAKQALAHGLKCKS--QFTITPGSEQIRATIER 401
Cdd:PRK12881 399 KPVAENGfAKKAQTSNGVDLPDGavaiaAITSCTNTSNPSVLIAAGlLAKKAVERGLTVKPwvKTSLAPGSKVVTEYLER 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 402 DGYAQVLRDVG-GIVlANACGPCIGQWD------RKDIKKGE-KNTIVTSYNRNFTGRNDANPEThAFVTSPEIVTALAI 473
Cdd:PRK12881 479 AGLLPYLEKLGfGIV-GYGCTTCIGNSGpltpeiEQAITKNDlVAAAVLSGNRNFEGRIHPNIKA-NFLASPPLVVAYAL 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 474 AGTLKFNPETDFL-TGKDGKKFKLE-----APDADELPRAEFDPgqDTYQH---PPKDSSGQRVDVS-PTSQRLQ----- 538
Cdd:PRK12881 557 AGTVRRDLMTEPLgKGKDGRPVYLKdiwpsSAEIDALVAFAVDP--EDFRKnyaEVFKGSELWAAIEaPDGPLYDwdpks 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 539 --LLEP--FDKWDG-----KDLEDLQILIKVKGKCTTDHIS---------AAGPWLKFRGHLDNISN------------- 587
Cdd:PRK12881 635 tyIRRPpfFDFSMGpaasiATVKGARPLAVLGDSITTDHISpagaikadsPAGKYLKENGVPKADFNsygsrrgnhevmm 714
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 588 ----------NLLIGAInienrKANSVRNAVTQEFGPVPDTARYYKQHGIRWVVIGDENYGEGASREHSALEPRHLGGRA 657
Cdd:PRK12881 715 rgtfanvrikNLMIPGK-----EGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGVKA 789
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 658 IITKSFARIHETNLKKQGLLPLTF--ADPADYNKIHPVDKLTIQGL-KDFAPGKPLKCIIKHPNGTQETILLNHTFnETQ 734
Cdd:PRK12881 790 VIAESFERIHRSNLVGMGVLPLQFkgGDSRQSLGLTGGETFDIEGLpGEIKPRQDVTLVIHRADGSTERVPVLCRI-DTP 868
|
810 820
....*....|....*....|
1B0K_A 735 IE--WFRAGSALNRMkeLQQ 752
Cdd:PRK12881 869 IEvdYYKAGGILPYV--LRQ 886
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
64-746 |
2.60e-72 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 253.12 E-value: 2.60e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 64 RPDRVAMQDAT--------AQM--AMLQF------ISsglPKVAVPSTIhcDHLIEAQLGGEKD-LRRAKDI----NQEV 122
Cdd:PRK09277 83 RPARVVMQDFTgvpavvdlAAMrdAIADLggdpakIN---PLVPVDLVI--DHSVQVDYFGTPDaFEKNVELeferNEER 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 123 YNFLatagaKYGVGFWR------PGSGIIHQIILE-------------NYAYPGVLlIGTDSHTPnggglggicigvgga 183
Cdd:PRK09277 158 YQFL-----KWGQKAFDnfrvvpPGTGICHQVNLEylapvvwtredgeLVAYPDTL-VGTDSHTT--------------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 184 dAVD----------------VMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSI 247
Cdd:PRK09277 217 -MINglgvlgwgvggieaeaAMLGQPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 248 SCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRAD--IAnladefkdhLV------------PDPGCHYDQVIEIN 313
Cdd:PRK09277 296 SLADRATIANMAPEYGATCGFFPIDEETLDYLRLTGRDEeqVA---------LVeayakaqglwrdPLEEPVYTDVLELD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 314 LSELKPHINGP-------FTPDLAHPVAEV--------GSVAEKEGWPLDIRVG-----LIGSCTNSS--YEDMGrsAA- 370
Cdd:PRK09277 367 LSTVEPSLAGPkrpqdriPLSDVKEAFAKSaelgvqgfGLDEAEEGEDYELPDGavviaAITSCTNTSnpSVMIA--AGl 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 371 VAKQALAHGLKCKS--QFTITPGSEQIRATIERDGYAQVLRDVG-GIVlANACGPCIG---------QwdrKDIKkgEKN 438
Cdd:PRK09277 445 LAKKAVEKGLKVKPwvKTSLAPGSKVVTDYLEKAGLLPYLEALGfNLV-GYGCTTCIGnsgplppeiE---KAIN--DND 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 439 TIVT---SYNRNFTGRndANPETHA-FVTSPEIVTALAIAGTLKFNPETDFL-TGKDGKKFKLEA--PDADE-------- 503
Cdd:PRK09277 519 LVVTavlSGNRNFEGR--IHPLVKAnYLASPPLVVAYALAGTVDIDLEKDPLgTDKDGNPVYLKDiwPSDEEidavvaka 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 504 ----LPRAEFDP---GQDTYQHPPKdSSGQRVDVSPTSQRLQlLEPFdkWDG--------KDLEDLQILIKVKGKCTTDH 568
Cdd:PRK09277 597 vkpeMFRKEYADvfeGDERWNAIEV-PEGPLYDWDPDSTYIR-NPPY--FEGmlaepgpvRDIKGARVLALLGDSITTDH 672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 569 IS---------AAGPWLK--------F--------------RGHLDNisnnlligaINIENRKANSVRNAVT-----QEF 612
Cdd:PRK09277 673 ISpagaikadsPAGKYLLehgvepkdFnsygsrrgnhevmmRGTFAN---------IRIRNEMVPGVEGGYTrhfpeGEV 743
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 613 GPVPDTARYYKQHGIRWVVIGDENYGEGASREHSALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYN--KI 690
Cdd:PRK09277 744 MSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKPGESRKtlGL 823
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
1B0K_A 691 HPVDKLTIQGLKDFAPGKPLKCIIKHPNGTQETI-LLNHTFNETQIEWFRAGSALNR 746
Cdd:PRK09277 824 DGTETFDIEGLEDLKPGATVTVVITRADGEVVEFpVLCRIDTAVEVDYYRNGGILQY 880
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
34-475 |
1.14e-69 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 234.69 E-value: 1.14e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 34 PLTLSEKIVYGHlddpANQEIERGKtYLRLRPDRVAMQDATAQMAMLQFISSGLPKVAVPSTIH--CDHLIEAqlggeKD 111
Cdd:PRK00402 2 GMTLAEKILARH----SGRDVSPGD-IVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVivFDHFVPA-----KD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 112 LRRAKdINQEVYNFLATAGAKYgvgFWRPGSGIIHQIILEN-YAYPGVLLIGTDSHTPNggglggicigvggADAV---- 186
Cdd:PRK00402 72 IKSAE-QQKILREFAKEQGIPN---FFDVGEGICHQVLPEKgLVRPGDVVVGADSHTCT-------------YGALgafa 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 187 ------D---VMA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATIC 256
Cdd:PRK00402 135 tgmgstDmaaAMAtGKTW-FKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 257 NMGAEIGATTSVFPYNHRMKKYLSKTGRADIanladefkDHLVPDPGCHYDQVIEINLSELKPHINGPFTPDLAHPVAEV 336
Cdd:PRK00402 214 NMAIEAGAKAGIFAPDEKTLEYLKERAGRDY--------KPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 337 gsvaekEGWPLDIRVglIGSCTNSSYEDMGRSAAVAKqalAHGLKCKSQFTITPGSEQIRATIERDGYAQVLRDVGGIVL 416
Cdd:PRK00402 286 ------EGTKVDQVF--IGSCTNGRLEDLRIAAEILK---GRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVS 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
1B0K_A 417 ANACGPCIGqwdrkdIKKGEknTIVTSYNRNFTGRNdANPETHAFVTSPEIVTALAIAG 475
Cdd:PRK00402 355 TPTCGPCLGghm-gvLAPGE--VCLSTTNRNFKGRM-GSPESEVYLASPAVAAASAVTG 409
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
67-475 |
1.66e-67 |
|
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: 227.84 E-value: 1.66e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 67 RVAMQDATAQMAMLQFISSGLPKVAVPSTIHC--DHLIEAqlggekDLRRAKDINQEVYNFLATAGAK-YGVGfwrpGSG 143
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAvfDHNVPT------PDIKAAEQVKTLRKFAKEFGINfFDVG----RQG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 144 IIHQIILENY-AYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVIL 221
Cdd:cd01583 71 ICHVILPEKGlTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLAtGKLW-FRVPETMRVNVEGKLPPGVTAKDVIL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 222 KVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRAdianladEFKdHLVPD 301
Cdd:cd01583 150 YIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKA-------YWK-ELKSD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 302 PGCHYDQVIEINLSELKPHINGPFTPDLAHPVAEVgsvaekEGWPLDIRVglIGSCTNSSYEDMGRSAAVAKqalAHGLK 381
Cdd:cd01583 222 EDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEV------EGIKIDQVF--IGSCTNGRLEDLRAAAEILK---GRKVA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 382 CKSQFTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIG-QWDRkdIKKGEknTIVTSYNRNFTGR-NDANPETH 459
Cdd:cd01583 291 DGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGgHMGV--LAPGE--RCVSTSNRNFKGRmGSPGARIY 366
|
410
....*....|....*.
1B0K_A 460 afVTSPEIVTALAIAG 475
Cdd:cd01583 367 --LASPATAAASAITG 380
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
554-684 |
6.71e-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: 201.06 E-value: 6.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 554 LQILIKVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINIENRKANSVRNAVTQEFGPVPDTARYYKQHGIRWVVIG 633
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
1B0K_A 634 DENYGEGASREHSALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADP 684
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
66-745 |
1.09e-60 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 220.27 E-value: 1.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 66 DRVAMQDAtaqMAML----QFISsglPKVAVPSTIhcDHLIEAQLGGEKD-LRRAKDI----NQEVYNFLatagaKYGVG 136
Cdd:PTZ00092 106 DLAAMRDA---MKRLggdpAKIN---PLVPVDLVI--DHSVQVDFSRSPDaLELNQEIeferNLERFEFL-----KWGSK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 137 FWR------PGSGIIHQIILE----------NYAYPGVLlIGTDSHTP--NGGGLGGICIGVGGADAVdvMAGIPWELKC 198
Cdd:PTZ00092 173 AFKnllivpPGSGIVHQVNLEylarvvfnkdGLLYPDSV-VGTDSHTTmiNGLGVLGWGVGGIEAEAV--MLGQPISMVL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 199 PKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKY 278
Cdd:PTZ00092 250 PEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDY 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 279 LSKTGRAD-----IANLADEFKDHLVPDPGCHYDQVIEINLSELKPHINGP---------------FTPDLAHPVAEVG- 337
Cdd:PTZ00092 330 LKQTGRSEekvelIEKYLKANGLFRTYAEQIEYSDVLELDLSTVVPSVAGPkrphdrvplsdlkkdFTACLSAPVGFKGf 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 338 SVAEKE----------GWPLDIRVG-----LIGSCTNSSYED-MGRSAAVAKQALAHGLKCKS--QFTITPGSEQIRATI 399
Cdd:PTZ00092 410 GIPEEKhekkvkftykGKEYTLTHGsvviaAITSCTNTSNPSvMLAAGLLAKKAVEKGLKVPPyiKTSLSPGSKVVTKYL 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 400 ERDGYAQVLRDVGGIVLANACGPCIGqwDRKDIKKGEKNTI---------VTSYNRNFTGRndANPETHA-FVTSPEIVT 469
Cdd:PTZ00092 490 EASGLLKYLEKLGFYTAGYGCMTCIG--NSGDLDPEVSEAItnndlvaaaVLSGNRNFEGR--VHPLTRAnYLASPPLVV 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 470 ALAIAGTLKFNPETDFL-TGKDGKKFKLEA--PDADEL--------------------------------PRAEF---DP 511
Cdd:PTZ00092 566 AYALAGRVNIDFETEPLgSDKTGKPVFLRDiwPSREEIqaleakyvkpemfkevysnitqgnkqwnelqvPKGKLyewDE 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 512 gQDTYQHPPKDSSGQRVDVSPTsqrlqllepfdkwdgKDLEDLQILIKVKGKCTTDHISAAG------PWLKF------- 578
Cdd:PTZ00092 646 -KSTYIHNPPFFQTMELEPPPI---------------KSIENAYCLLNLGDSITTDHISPAGniaknsPAAKYlmergve 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 579 ------------------RGHLDNIS-NNLLIGainieNRKANSVrNAVTQEFGPVPDTARYYKQHGIRWVVIGDENYGE 639
Cdd:PTZ00092 710 rkdfntygarrgndevmvRGTFANIRlINKLCG-----KVGPNTV-HVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGS 783
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 640 GASREHSALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFAD--PADYNKIHPVDKLTIQGLK-DFAPGKPLKciIKH 716
Cdd:PTZ00092 784 GSSRDWAAKGPYLQGVKAVIAESFERIHRSNLVGMGILPLQFLNgeNADSLGLTGKEQFSIDLNSgELKPGQDVT--VKT 861
|
810 820 830
....*....|....*....|....*....|
1B0K_A 717 PNG-TQETILLNHTfnETQIEWFRAGSALN 745
Cdd:PTZ00092 862 DTGkTFDTILRIDT--EVEVEYFKHGGILQ 889
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
66-475 |
5.00e-58 |
|
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: 203.06 E-value: 5.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 66 DRVAMQDATAQMAMLQFISSGLPKVAVPSTIHC--DHLIEAqlggekDLRRAKDINQEVYNFLATAGAKYgvgFWRPGSG 143
Cdd:TIGR01343 26 DLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIvfDHQVPA------DTIKAAEMQKLAREFVKKQGIKY---FYDVGEG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 144 IIHQIILEN-YAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVIL 221
Cdd:TIGR01343 97 ICHQVLPEKgLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIAtGKTW-FKVPETIRVNITGKLNPGVTAKDVIL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 222 KVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADianlADEFKDhlvpD 301
Cdd:TIGR01343 176 EVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYLKERRKEP----FRVYKS----D 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 302 PGCHYDQVIEINLSELKPHINGPFTPDLAHPVAEVgsvaekEGWPLDiRVgLIGSCTNSSYEDMGRSAAVAKqalAHGLK 381
Cdd:TIGR01343 248 EDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEV------EGTEID-QV-FIGSCTNGRLEDLRVAAKILK---GRKVA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 382 CKSQFTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGqwdRKDIKKGEKNTIVTSYNRNFTGRNdANPETHAF 461
Cdd:TIGR01343 317 PDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLG---SHQGVLAPGEVCISTSNRNFKGRM-GHPNAEIY 392
|
410
....*....|....
1B0K_A 462 VTSPEIVTALAIAG 475
Cdd:TIGR01343 393 LASPATAAASAVKG 406
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
39-686 |
1.81e-57 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 211.20 E-value: 1.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 39 EKIVYGHLDDPANQEIErgktylrLRPDRVAMQDAT--------AQM--AMLQFIS-SGLPKVAVPSTIHCDHLIEAQLG 107
Cdd:PLN00070 103 EKIIDWENTSPKQVEIP-------FKPARVLLQDFTgvpavvdlACMrdAMNNLGGdPNKINPLVPVDLVIDHSVQVDVA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 108 GEKDLRRAK-----DINQEVYNFLatagaKYGVGFWR------PGSGIIHQIILENYA----------YPGVLlIGTDSH 166
Cdd:PLN00070 176 RSENAVQANmelefQRNKERFAFL-----KWGSTAFQnmlvvpPGSGIVHQVNLEYLGrvvfntdgilYPDSV-VGTDSH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 167 TPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDS 246
Cdd:PLN00070 250 TTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSE 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 247 ISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRAD----------IANlaDEFKDHLVPDPGCHYDQVIEINLSE 316
Cdd:PLN00070 330 LSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDetvamieaylRAN--KMFVDYNEPQQERVYSSYLELDLED 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 317 LKPHINGPFTPD---------------LAHPVAEVGSVAEKE-----------GWPLDIRVG-----LIGSCTNSSYED- 364
Cdd:PLN00070 408 VEPCISGPKRPHdrvplkemkadwhscLDNKVGFKGFAVPKEaqskvakfsfhGQPAELRHGsvviaAITSCTNTSNPSv 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 365 MGRSAAVAKQALAHGLKCKS--QFTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGqwDRKDIKKGEKNTI-- 440
Cdd:PLN00070 488 MLGAGLVAKKACELGLEVKPwiKTSLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIG--NSGELDESVASAIte 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 441 -------VTSYNRNFTGRndANPETHA-FVTSPEIVTALAIAGTLKFNPETDFL-TGKDGKK--FKLEAPDADELPRAEF 509
Cdd:PLN00070 566 ndivaaaVLSGNRNFEGR--VHPLTRAnYLASPPLVVAYALAGTVDIDFEKEPIgTGKDGKDvfFRDIWPSNEEVAEVVQ 643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 510 -----DPGQDTYQHPPKDS---------SGQRVDVSPTSQRLQllEP-------FDKWDGKDLEDLQILIKVKGKCTTDH 568
Cdd:PLN00070 644 ssvlpDMFKSTYEAITKGNpmwnqlsvpSGTLYSWDPKSTYIH--EPpyfknmtMSPPGPHGVKDAYCLLNFGDSITTDH 721
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 569 ISAAG------PWLKF-----------------RGHlDNISNNLLIGAINIENRKANSvrnavtqEFGP----VP----- 616
Cdd:PLN00070 722 ISPAGsihkdsPAAKYlmergvdrkdfnsygsrRGN-DEIMARGTFANIRIVNKLLKG-------EVGPktvhIPtgekl 793
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1B0K_A 617 ---DTARYYKQHGIRWVVIGDENYGEGASREHSALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPAD 686
Cdd:PLN00070 794 svfDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGED 866
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
67-476 |
6.05e-47 |
|
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: 172.10 E-value: 6.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 67 RVAMQDATAQMAMLQFIS--------SGLP-KV--AVPSTIHCDHLIEAQLGG-----EKDLRRAKDINQEVYNFLATAG 130
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAmrdavkrlGGDPeKInpLIPVDLVIDHSVQVDFYGtadalAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 131 AKYG-VGFWRPGSGIIHQIILE--------------NYAYPGVLlIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWE 195
Cdd:cd01586 81 KAFKnLRVVPPGTGIIHQVNLEylarvvftseedgdGVAYPDSV-VGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPIS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 196 LKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNhrm 275
Cdd:cd01586 160 MLLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 276 kkylsktgradianladefkdhlvpdpgchyDQVIEINLSELKPHINGPFTPDlaHPVAEVGSVAekegwpldirVGLIG 355
Cdd:cd01586 237 -------------------------------TQVVELDLSTVEPSVSGPKRPQ--DRVPLHGSVV----------IAAIT 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 356 SCTNSSYED-MGRSAAVAKQALAHGLKCKS--QFTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIG------Q 426
Cdd:cd01586 274 SCTNTSNPSvMLAAGLLAKKAVELGLKVKPyvKTSLAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGnsgplpE 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
1B0K_A 427 WDRKDIKKGE-KNTIVTSYNRNFTGRndANPETHA-FVTSPEIVTALAIAGT 476
Cdd:cd01586 354 EVEEAIKENDlVVAAVLSGNRNFEGR--IHPLVRAnYLASPPLVVAYALAGT 403
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
80-477 |
3.60e-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: 143.14 E-value: 3.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 80 LQFISSGLPKVAVPSTIHC--DHliEAQLGGEKDLRRAKDINqevyNFlataGAKYGVGFWRPGSGIIHQIILEN-YAYP 156
Cdd:cd01582 13 LKFMSIGATKIHNPDQIVMtlDH--DVQNKSEKNLKKYKNIE----SF----AKKHGIDFYPAGRGIGHQIMIEEgYAFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 157 GVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGA 235
Cdd:cd01582 83 GTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWAtGQTW-WQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLNH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 236 IVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRmkkylsktgradianladefkdHLVpdpgchydqvieINLS 315
Cdd:cd01582 162 AIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAK----------------------HLI------------LDLS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 316 ELKPHINGPFTPDLAHPVAEVgsvaekEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQA--------LAHGLKcksqFT 387
Cdd:cd01582 208 TLSPYVSGPNSVKVSTPLKEL------EAQNIKINKAYLVSCTNSRASDIAAAADVVKGKkekngkipVAPGVE----FY 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 388 ITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGqWDRKDIKKGEKNtiVTSYNRNFTGRNdANPETHAFVTSPEI 467
Cdd:cd01582 278 VAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIG-LGQGLLEPGEVG--ISATNRNFKGRM-GSTEALAYLASPAV 353
|
410
....*....|
1B0K_A 468 VTALAIAGTL 477
Cdd:cd01582 354 VAASAISGKI 363
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
199-477 |
1.14e-31 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 129.08 E-value: 1.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 199 PKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGA---------TTsvF 269
Cdd:PRK05478 163 PKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGAraglvapdeTT--F 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 270 PYnhrMKkylsktGR--ADIANLADEFKDH---LVPDPGCHYDQVIEINLSELKPH------------INGPF-TPDLAH 331
Cdd:PRK05478 241 EY---LK------GRpfAPKGEDWDKAVAYwktLKSDEDAVFDKVVTLDAADIEPQvtwgtnpgqvisIDGKVpDPEDFA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 332 PVAEVGSVAE-------KEGWPL-DIRVG--LIGSCTNSSYEDMGRSAAVAKqalahGLKCKSQFT--ITPGSEQIRATI 399
Cdd:PRK05478 312 DPVKRASAERalaymglKPGTPItDIKIDkvFIGSCTNSRIEDLRAAAAVVK-----GRKVAPGVRalVVPGSGLVKAQA 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 400 ERDGYAQVLRDVG------GivlanaCGPCIGQWDrkDIKKGEKNTIVTSyNRNFTGRNDANPETHafVTSPEIVTALAI 473
Cdd:PRK05478 387 EAEGLDKIFIEAGfewrepG------CSMCLAMNP--DKLPPGERCASTS-NRNFEGRQGKGGRTH--LVSPAMAAAAAI 455
|
....
1B0K_A 474 AGTL 477
Cdd:PRK05478 456 TGHF 459
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
140-477 |
4.08e-29 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 121.55 E-value: 4.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 140 PGSGIIHQIILE-NYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKD 218
Cdd:PRK12466 105 PRQGIVHVVAPElGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKD 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 219 VILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFKDH- 297
Cdd:PRK12466 185 LILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETTFDYLRGRPRAPKGALWDAALAYw 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 298 --LVPDPGCHYDQVIEINLSELKPHINGPFTPDLAHPVAEVGSVAEKE--------------------GWPL-DIRVG-- 352
Cdd:PRK12466 265 rtLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAAEadparraameraldymgltpGTPLaGIPIDrv 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 353 LIGSCTNSSYEDMGRSAAVAKqalahGLKCKSQFT--ITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGQWDRK 430
Cdd:PRK12466 345 FIGSCTNGRIEDLRAAAAVLR-----GRKVAPGVRamVVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDV 419
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
1B0K_A 431 dIKKGEKntIVTSYNRNFTGRNDANPETHafVTSPEIVTALAIAGTL 477
Cdd:PRK12466 420 -LAPGER--CASTTNRNFEGRQGPGARTH--LMSPAMVAAAAVAGHI 461
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
559-700 |
8.96e-29 |
|
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: 109.87 E-value: 8.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 559 KVKGKCTTDHISAAGPWlkfrghldnisnnlligainienrkansvrnavtqefgpvpdtaryykqhgirwVVIGDENYG 638
Cdd:cd00404 1 KVAGNITTDHISPAGPG------------------------------------------------------VVIGDENYG 26
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
1B0K_A 639 EGASREHSALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQG 700
Cdd:cd00404 27 TGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDYLKLHTGDELDIYP 88
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
559-700 |
3.61e-27 |
|
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: 106.75 E-value: 3.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 559 KVKGKCTTDHISAAGP-WLKFRGHLDNISNNLLIGainienrkansvrnaVTQEFgpvPDTARYYKQHgirwVVIGDENY 637
Cdd:cd01579 1 KVGDNITTDHIMPAGAkVLPLRSNIPAISEFVFHR---------------VDPTF---AERAKAAGPG----FIVGGENY 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
1B0K_A 638 GEGASREHSALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQG 700
Cdd:cd01579 59 GQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADEDDYDRFEQGDQLELPL 121
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
61-703 |
4.83e-24 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 107.79 E-value: 4.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 61 LRLRPDRVAMQDAT----AQMAmlqfISSGLPKVAVPSTIHCDHLIEAQLGGEkdlrrakdINQEVYNFLATAGAKYGVG 136
Cdd:PRK11413 54 LKIKFDSLASHDITfvgiIQTA----KASGMERFPLPYVLTNCHNSLCAVGGT--------INEDDHVFGLSAAQKYGGI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 137 FWRPGSGIIHQIILENYAYPGVLLIGTDSHTpnggglggicigvgGADAVDVMA---GIP----------WELKCPKVIG 203
Cdd:PRK11413 122 FVPPHIAVIHQYMREMMAGGGKMILGSDSHT--------------RYGALGTMAvgeGGGelvkqllndtYDIDYPGVVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 204 VKLTGSLSGWTSPKDVILKVAGILTVKGGT-GAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKT 282
Cdd:PRK11413 188 VYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLALH 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 283 GRadianlADEFKDhLVPDPGCHYDQVIEINLSELKPHINGPFTPDLAHPVAEVGSVA-------EKEGWPLD------- 348
Cdd:PRK11413 268 GR------GQDYCE-LNPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDELNQNLtdilrevEIESERVAhgkakls 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 349 ---------IRV--GLIGSCTNSSYEDMgrsaavakQALAHGLKCKS----QFTIT--PGSEQIRATIERDGYAQVLRDV 411
Cdd:PRK11413 341 lldkiengrLKVqqGIIAGCSGGNYENV--------IAAANALRGQScgndTFSLSvyPSSQPVFMDLAKKGVVADLMGA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 412 GGIVLANACGPCIGQWDrkdikkgekntivTSYN---------RNFTGRNDANPeTHAFVTSPEIVTALAIAGTLKFNpe 482
Cdd:PRK11413 413 GAIIRTAFCGPCFGAGD-------------TPANnglsirhttRNFPNREGSKP-ANGQMSAVALMDARSIAATAANG-- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 483 tDFLTGKDgkkfklEAPDADELPRAEFDPgqDTYQHPPKDSSGQRVdvspTSQRLQLLEPFDKWdgKDLEDL--QILIKV 560
Cdd:PRK11413 477 -GYLTSAT------ELDCWDNVPEYAFDV--TPYKNRVYQGFGKGA----TQQPLIYGPNIKDW--PEMGALtdNILLKV 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 561 KGK-----CTTDHISAAGPWLKFRghldniSNNLLIGAINIENRKANSV-------------RNAVTQEFGPVPDTAR-Y 621
Cdd:PRK11413 542 CSKildpvTTTDELIPSGETSSYR------SNPLGLAEFTLSRRDPGYVgrskavaelenqrLAGNVSELTEVFARIKqI 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 622 YKQHGIRW--VVIGDENY----GEGASREHSALEPRHLGGRAIITKSFA-RIHETNLKKQGLLPLTFADPadyNKIHPVD 694
Cdd:PRK11413 616 AGQEHIDPlqTEIGSMVYavkpGDGSAREQAASCQRVLGGLANIAEEYAtKRYRSNVINWGMLPFQMAEE---PTFEVGD 692
|
....*....
1B0K_A 695 KLTIQGLKD 703
Cdd:PRK11413 693 YIYIPGIRA 701
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
565-700 |
4.90e-17 |
|
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: 79.24 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 565 TTDHISAAGPWLK-------------------------------FRGHLDNISN-NLLIGainieNRKANSVRNAVTQEF 612
Cdd:cd01580 7 TTDHISPAGSIAKdspagkylaergvkprdfnsygsrrgndevmMRGTFANIRLrNKLVP-----GTEGGTTHHPPTGEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 613 GPVPDTARYYKQHGIRWVVIGDENYGEGASREHSALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADP--ADYNKI 690
Cdd:cd01580 82 MSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGenADSLGL 161
|
170
....*....|
1B0K_A 691 HPVDKLTIQG 700
Cdd:cd01580 162 TGEETYDIIG 171
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
619-698 |
7.18e-12 |
|
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: 61.84 E-value: 7.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 619 ARYYKQhgirwVVIGDENYGEGASREHSALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPA-DYNKIHPVDKLT 697
Cdd:cd01577 14 ARFLGD-----IIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFARIFFRNAINNGLLPVTLADEDvEEVEAKPGDEVE 88
|
.
1B0K_A 698 I 698
Cdd:cd01577 89 V 89
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
134-477 |
2.89e-11 |
|
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: 66.37 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 134 GVGFWRPGSGIIHQIiLENYAYPGVLLIGTDSHT--PNGGGLGGICIGVGGADAVDVMAgipweLKCPKVIGVKLTGSLS 211
Cdd:cd01581 85 GGVALRPGDGVIHSW-LNRMLLPDTVGTGGDSHTrfPIGISFPAGSGLVAFAAATGVMP-----LDMPESVLVRFKGKMQ 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 212 GWTSPKDVILKV------AGILTV--KGG----TGAIVEYHGpgVDSISCTGMATICNMGAEIGATTSVFPYNH------ 273
Cdd:cd01581 159 PGITLRDLVNAIpyyaiqQGLLTVekKGKknvfNGRILEIEG--LPDLKVEQAFELTDASAERSAAACTVRLDKepviey 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 274 ------RMKKYLSKtGRADIANLADEFKDH---------LVPDPGCHYDQVIEINLSELK-PHINGPFTPDlahpvaEVG 337
Cdd:cd01581 237 lesnvvLMKIMIAN-GYDDARTLLRRIIAMeewlanpplLEPDADAEYAAVIEIDLDDIKePILACPNDPD------DVK 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 338 SVAEKEGWPLDIrvGLIGSC-TNssyedMGRSAAVAKQALAHGLKcKSQFTITPGSEQIRATIERDGYAQVLRDVGGIVL 416
Cdd:cd01581 310 LLSEVAGKKIDE--VFIGSCmTN-----IGHFRAAAKILRGKEFK-PTRLWVAPPTRMDWAILQEEGYYSIFGDAGARTE 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
1B0K_A 417 ANACGPCIGQWDRkdIKKGEknTIVTSYNRNFTGR--NDANpethAFVTSPEIVTALAIAGTL 477
Cdd:cd01581 382 MPGCSLCMGNQAR--VADGA--TVFSTSTRNFDNRvgKGAE----VYLGSAELAAVCALLGRI 436
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
124-477 |
2.30e-10 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 64.17 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 124 NFLATAGakyGVGFwRPGSGIIHQIiLENYAYPGVLLIGTDSHT--PNGGGLGGICIGVGGADAVDVMAgipweLKCPKV 201
Cdd:PLN00094 525 DFIRNRG---GVSL-RPGDGVIHSW-LNRMLLPDTVGTGGDSHTrfPIGISFPAGSGLVAFGAATGVIP-----LDMPES 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 202 IGVKLTGSLSGWTSPKDVILKV------AGILTV-KGG-----TGAIVEYHGpgVDSISCTGMATICNMGAEIGAT---- 265
Cdd:PLN00094 595 VLVRFTGTMQPGITLRDLVHAIpytaiqDGLLTVeKKGkknvfSGRILEIEG--LPHLKCEQAFELSDASAERSAAgcti 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 266 ----TSVFPY---NHRMKKYLSKTGRAD-------IANLADEFKD-HLV-PDPGCHYDQVIEINLSELK-PHINGPFTPD 328
Cdd:PLN00094 673 kldkEPIIEYlnsNVVMLKWMIAEGYGDrrtlerrIARMQQWLADpELLeADPDAEYAAVIEIDMDEIKePILCAPNDPD 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 329 LAHPVAEVgsVAEKegwpldIRVGLIGSC-TNssyedMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIERDGYAQV 407
Cdd:PLN00094 753 DARLLSEV--TGDK------IDEVFIGSCmTN-----IGHFRAAGKLLNDNLSQLPTRLWVAPPTKMDEAQLKAEGYYST 819
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1B0K_A 408 LRDVGGIVLANACGPCIGQWDRkdikKGEKNTIVTSYNRNFTGR--NDANpethAFVTSPEIVTALAIAGTL 477
Cdd:PLN00094 820 FGTVGARTEMPGCSLCMGNQAR----VAEKSTVVSTSTRNFPNRlgKGAN----VYLASAELAAVAAILGRL 883
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
630-724 |
1.99e-08 |
|
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: 54.79 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 630 VVIGDENYGEGASREHSALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTfADPADYNKI------HPVDKLTIqglkD 703
Cdd:COG0066 67 ILVAGRNFGCGSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIE-LPEEAVDALfaaieaNPGDELTV----D 141
|
90 100
....*....|....*....|.
1B0K_A 704 FApgkplKCIIKhpNGTQETI 724
Cdd:COG0066 142 LE-----AGTVT--NGTGETY 155
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
616-686 |
2.13e-07 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 51.34 E-value: 2.13e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1B0K_A 616 PDTARYYKQHGIrwvVIGDENYGEGASREHSALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPAD 686
Cdd:PRK14023 41 PEFASTVRPGDI---LVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPPFESEEVVD 108
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
298-477 |
3.11e-07 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 54.03 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 298 LVPDPGCHYDQVIEINLSELK-PHINGPFTPDLAHPVAEVGsvAEKegwpldIRVGLIGSC-TNssyedMGRSAAVAKQA 375
Cdd:PRK09238 647 LEADADAEYAAVIEIDLAEIKePILACPNDPDDVRLLSEVA--GTK------IDEVFIGSCmTN-----IGHFRAAGKLL 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B0K_A 376 LAHGLKCKSQFTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGQWDRkdIKKGEknTIVTSYNRNFTGR--ND 453
Cdd:PRK09238 714 EGKKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMGNQAR--VADGA--TVFSTSTRNFPNRlgKG 789
|
170 180
....*....|....*....|....
1B0K_A 454 ANpethAFVTSPEIVTALAIAGTL 477
Cdd:PRK09238 790 AN----VYLGSAELAAVCALLGRI 809
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
630-698 |
4.85e-07 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 50.21 E-value: 4.85e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1B0K_A 630 VVIGDENYGEGASREHSALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADynKIHPVDKLTI 698
Cdd:PRK00439 51 IIVAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIGLPVLECDEAVD--KIEDGDEVEV 117
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
630-679 |
1.81e-06 |
|
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: 48.19 E-value: 1.81e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
1B0K_A 630 VVIGDENYGEGASREHSALEPRHLGGRAIITKSFARIHETNLKKQGLLPL 679
Cdd:TIGR02087 50 VIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLI 99
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
630-698 |
1.00e-04 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 43.96 E-value: 1.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1B0K_A 630 VVIGDENYGEGASREHS--ALEprHLGGRAIITKSFARIHETNLKKQGLLPLTfADPADYNKI------HPVDKLTI 698
Cdd:PRK01641 70 ILLAGDNFGCGSSREHApwALA--DYGFRAVIAPSFADIFYNNCFKNGLLPIV-LPEEDVDELfklveaNPGAELTV 143
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
630-666 |
4.27e-04 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 42.54 E-value: 4.27e-04
10 20 30
....*....|....*....|....*....|....*..
1B0K_A 630 VVIGDENYGEGASREHSALEPRHLGGRAIITKSFARI 666
Cdd:PLN00072 132 IIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARI 168
|
|
| |
