|
Name |
Accession |
Description |
Interval |
E-value |
| aconitase_mito |
TIGR01340 |
aconitate hydratase, mitochondrial; This model represents mitochondrial forms of the TCA cycle ... |
12-742 |
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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 12 YDLLEKNINIVRKRLN-RPLTLSEKIVYGHLDDPAG----QEIE--RGKSYLRLRPDRVAMQDATAQMAMLQFISSGLPK 84
Cdd:TIGR01340 1 YEKLYNNLDEVRRRLNsRPLTLAEKILYSHLDDPEEsllsQDIGdvRGKSYLKLRPDRVAMQDASAQMALLQFMTCGLPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 85 VAVPSTIHCDHLIEAQLGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWKPGSGIIHQIILENYAYPGVLLIGTDSHTPN 164
Cdd:TIGR01340 81 VAVPASIHCDHLIVGQKGGDKDLARAIATNKEVFDFLESAGKKYGIGFWKPGSGIIHQIVLENYAFPGLMMLGTDSHTPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 165 GGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISC 244
Cdd:TIGR01340 161 AGGLGTIAIGVGGADAVDALAGAPWELKAPKILGVKLTGKLNGWTSPKDIILKLAGLLTVRGGTGYIVEYFGPGVESLSC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 245 TGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFKDH---LVPDPGCHYDQLIEVNLSELKPHINGPFT 321
Cdd:TIGR01340 241 TGMATICNMGAEIGATTSIFPFNEAMSRYLKATNRAQIAEDAKTGQYSffkLKADEGAQYDELIEIDLSKLEPHINGPFT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 322 PDLAHPVAEVGKVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIERDGYAQ 401
Cdd:TIGR01340 321 PDLSTPISKFKETVQKNGWPEKLSAGLIGSCTNSSYEDMSRCASIVKDAEQAGLKPKSPFYVTPGSEQIRATLERDGILQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 402 ILRDLGGIVLANACGPCIGQWDRKD-IKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSPEIVTALAIAGTLKFNPETDY 480
Cdd:TIGR01340 401 TFEKFGGIVLANACGPCIGQWDRKDdVKKGEPNTILTSYNRNFRGRNDGNPATMNFLASPEIVTAMSYAGSLTFNPLTDS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 481 LTGTDGKKFKLEAPDADELPKGEFDPGQDTYQHPPKDS-SGQHVDVSPTSQRLQLLEPFDKWDGKDLEDLQILIKVKGKC 559
Cdd:TIGR01340 481 LTTPDGKEFKFPAPKGDELPEKGFEAGRDTFQAPPGSPnPNVEVAVSPSSDRLQLLEPFEPWNGKDLSGLRVLIKVTGKC 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 560 TTDHISAAGPWLKFRGHLDNISNNLLIGAINIENGKANSVRNaVTQEFGPVPDTARYYKKHGIRWVVIGDENYGEGSSRE 639
Cdd:TIGR01340 561 TTDHISAAGPWLKYKGHLDNISNNTLIGAVNAETGEVNKAYD-LDGSKGTIPELARDWKARGQPWVVVAEHNYGEGSARE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 640 HAALEPRHLGARAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQGLKDFTP---GKPLKCIIKHPNGTQ 716
Cdd:TIGR01340 640 HAALEPRHLGGRIIITKSFARIHETNLKKQGVLPLTFANEADYDKIQPGDEVATLNLYEMLKnggGGEVDLRVTKKNGKV 719
|
730 740
....*....|....*....|....*.
gi 1622836733 717 ETILLNHTFNETQIEWFRAGSALNRM 742
Cdd:TIGR01340 720 FEIKLKHTVSKDQIGFFKAGSALNLM 745
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
28-744 |
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 1622836733 28 RPLTLSEKIVYGHLDDPagqEIERGKSyLRLRPDRVAMQDATAQMAMLQFISSGLPKVAVPSTI-HCDHlieaqlggekD 106
Cdd:PRK07229 1 MGLTLTEKILYAHLVEG---ELEPGEE-IAIRIDQTLTQDATGTMAYLQFEAMGLDRVKTELSVqYVDH----------N 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 107 LRRAKDINQEVYNFLATAGAKYGVGFWKPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAG 186
Cdd:PRK07229 67 LLQADFENADDHRFLQSVAAKYGIYFSKPGNGICHQVHLERFAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 187 IPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPY 266
Cdd:PRK07229 147 GPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 267 NHRMKKYLSKTGRADIAnladefkDHLVPDPGCHYDQLIEVNLSELKPHINGPFTPDLAHPVAEVGKVAekegwpldIRV 346
Cdd:PRK07229 227 DERTREFLKAQGREDDW-------VELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVAGIK--------VDQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 347 GLIGSCTNSSYEDMGRSAAVAKqalAHGLKCKSQFTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGQwdrkD 426
Cdd:PRK07229 292 VLIGSCTNSSYEDLMRAASILK---GKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGM----G 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 427 IKKGEKNTIVTSYNRNFTGRNdANPETHAFVTSPEIVTALAIAGTLKfNPETdyLTGTDGKKFKLEAPDadelpkgEFDP 506
Cdd:PRK07229 365 QAPATGNVSLRTFNRNFPGRS-GTKDAQVYLASPETAAASALTGVIT-DPRT--LALENGEYPKLEEPE-------GFAV 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 507 GQDTYQHPPKDSSGQHVDVSPTSQRLQLLEPFDkwdgkDLEDLQILIKVKGKCTTDHISAAGP-WLKFRGHLDNISNNLL 585
Cdd:PRK07229 434 DDAGIIAPAEDGSDVEVVRGPNIKPLPLLEPLP-----DLLEGKVLLKVGDNITTDHIMPAGAkWLPYRSNIPNISEFVF 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 586 IGAINIENGKAnsvrnavtQEFGPvpdtaryykkhgirWVVIGDENYGEGSSREHAALEPRHLGARAIITKSFARIHETN 665
Cdd:PRK07229 509 EGVDNTFPERA--------KEQGG--------------GIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKAN 566
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622836733 666 LKKQGLLPLTFADPADYNKIHPVDKLTIQGLKDFTPGKPLKCIIKHPNgtqETILLNHTFNETQIEWFRAGSALNRMKE 744
Cdd:PRK07229 567 LINFGILPLTFADPADYDKIEEGDVLEIEDLREFLPGGPLTVVNVTKD---EEIEVRHTLSERQIEILLAGGALNLIKK 642
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
62-472 |
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: 872.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 62 RVAMQDATAQMAMLQFISSGLPKVAVPSTIHCDHLIEAQLGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWKPGSGIIH 141
Cdd:cd01584 1 RVAMQDATAQMALLQFMSSGLPKVAVPSTIHCDHLIEAQVGGEKDLKRAKDINKEVYDFLASAGAKYGIGFWKPGSGIIH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 142 QIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGI 221
Cdd:cd01584 81 QIVLENYAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 222 LTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFK-DHLVPDPGCH 300
Cdd:cd01584 161 LTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEIADLADEFKdDLLVADEGAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 301 YDQLIEVNLSELKPHINGPFTPDLAHPVAEVGKVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQ 380
Cdd:cd01584 241 YDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAEKNGWPLDLRVGLIGSCTNSSYEDMGRAASIAKQALAHGLKCKSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 381 FTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSP 460
Cdd:cd01584 321 FTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPATHAFVASP 400
|
410
....*....|..
gi 1622836733 461 EIVTALAIAGTL 472
Cdd:cd01584 401 EIVTAMAIAGTL 412
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
8-742 |
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: 746.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 8 EYIHYDL--LEKNINIVRKrlnrpLTLSEKIVYGHLD---DPAG------------QEIERGKSYLRLRPDRVAMQDATA 70
Cdd:COG1048 17 PYTYYSLpaLEEAGGDISR-----LPYSLKILLENLLrneDGETvteedikalanwLPKARGDDEIPFRPARVLMQDFTG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 71 QMAMLQFISSGLPKV-----------AVPSTIHCDHLIEAQLGG-----EKDLRRAKDINQEVYNFLATAGAKY-GVGFW 133
Cdd:COG1048 92 VPAVVDLAAMRDAVArlggdpkkinpLVPVDLVIDHSVQVDYFGtpdalEKNLELEFERNRERYQFLKWGQQAFdNFRVV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 134 KPGSGIIHQIILENYA--------------YPGvLLIGTDSHTPNggglggicigvggA-------------DAVDVMAG 186
Cdd:COG1048 172 PPGTGIVHQVNLEYLAfvvwtreedgetvaYPD-TLVGTDSHTTM-------------InglgvlgwgvggiEAEAAMLG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 187 IPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPY 266
Cdd:COG1048 238 QPVSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 267 NHRMKKYLSKTGRADI--------ANLADEFKDHLVPDPgcHYDQLIEVNLSELKPHINGPFTPDLAHPVAEVGKVAEKE 338
Cdd:COG1048 318 DEETLDYLRLTGRSEEqielveayAKAQGLWRDPDAPEP--YYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 339 GWPL-----------------------DIRVGLIGSCTNSSYEDMGRSAA-VAKQALAHGLKCK--SQFTITPGSEQIRA 392
Cdd:COG1048 396 LAAPvgeeldkpvrvevdgeefelghgAVVIAAITSCTNTSNPSVMIAAGlLAKKAVEKGLKVKpwVKTSLAPGSKVVTD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 393 TIERDGYAQILRDLGGIVLANACGPCIGQWDR------KDIKKGE-KNTIVTSYNRNFTGRNDaNPETHAFVTSPEIVTA 465
Cdd:COG1048 476 YLERAGLLPYLEALGFNVVGYGCTTCIGNSGPlppeisEAIEENDlVVAAVLSGNRNFEGRIH-PDVKANFLASPPLVVA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 466 LAIAGTLKFNPETDYL-TGTDGKKFKLEA--PDADELPK----------------GEFD----------PGQDTYQHPPK 516
Cdd:COG1048 555 YALAGTVDIDLTTDPLgTDKDGKPVYLKDiwPSGEEIPAavfkavtpemfraryaDVFDgderwqalevPAGELYDWDPD 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 517 DSSgqhVDVSPTSQRLQLL-EPFdkwdgKDLEDLQILIKVKGKCTTDHISAAGP-----------------------WLK 572
Cdd:COG1048 635 STY---IRRPPFFEGLQLEpEPF-----KDIKGARVLAKLGDSITTDHISPAGAikadspagryllehgvepkdfnsYGS 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 573 FRGHLDNISNNLLIGaINIEN-----GKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRH 647
Cdd:COG1048 707 RRGNHEVMMRGTFAN-IRIKNllapgTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRL 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 648 LGARAIITKSFARIHETNLKKQGLLPLTFADPADYNK--IHPVDKLTIQGLKD-FTPGKPLKCIIKHPNGTQETILLNHT 724
Cdd:COG1048 786 LGVKAVIAESFERIHRSNLVGMGVLPLQFPEGESAESlgLTGDETFDIEGLDEgLAPGKTVTVTATRADGSTEEFPVLHR 865
|
890
....*....|....*....
gi 1622836733 725 F-NETQIEWFRAGSALNRM 742
Cdd:COG1048 866 IdTPVEVEYYRAGGILQYV 884
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
34-470 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 563.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 34 EKIVYGHLDDPAGQEIergkSYLrlrPDRVAMQDATAQMAMLQFISSGLPK-----------VAVPSTIHCDHlieAQLG 102
Cdd:pfam00330 1 EKIWDAHLVEELDGSL----LYI---PDRVLMHDVTSPQAFVDLRAAGRAVrrpggtpatidHLVPTDLVIDH---APDA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 103 GEKDLRRAKDINQEVYNFLATAGAKYGVGFWKPGSGIIHQIILEN-YAYPGVLLIGTDSHTPNggglggicigvggA--- 178
Cdd:pfam00330 71 LDKNIEDEISRNKEQYDFLEWNAKKFGIRFVPPGQGIVHQVGLEYgLALPGMTIVGTDSHTTT-------------Hggl 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 179 ----------DAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMA 248
Cdd:pfam00330 138 galafgvggsEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 249 TICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFK----DHLVPDPGCHYDQLIEVNLSELKPHINGPFTPDL 324
Cdd:pfam00330 218 TICNMAIEYGATAGLFPPDETTFEYLRATGRPEAPKGEAYDKavawKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 325 AHPVAEVGKVAEKE------------------GWPL---DIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKS--QF 381
Cdd:pfam00330 298 AVPLSELVPDPFADavkrkaaeraleymglgpGTPLsdgKVDIAFIGSCTNSSIEDLRAAAGLLKKAVEKGLKVAPgvKA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 382 TITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGQWDRKDikkgEKNTIVTSYNRNFTGRNdaNPETHAFVTSPE 461
Cdd:pfam00330 378 SVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLP----PGERCVSSSNRNFEGRQ--GPGGRTHLASPA 451
|
....*....
gi 1622836733 462 IVTALAIAG 470
Cdd:pfam00330 452 LVAAAAIAG 460
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
62-472 |
7.68e-170 |
|
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: 493.55 E-value: 7.68e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 62 RVAMQDATAQMAMLQFISSGLP-KVAVPSTIHCDHLIEAQLggekdlrrAKDINQEVYNFLATAGAKYGVGFWKPGSGII 140
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAALgKVADPSQIACVHDHAVQL--------EKPVNNEGHKFLSFFAALQGIAFYRPGVGII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 141 HQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAG 220
Cdd:cd01351 73 HQIMVENLALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 221 ILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFKDHLVPDPGCH 300
Cdd:cd01351 153 IVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWLAFPEELLADEGAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 301 YDQLIEVNLSELKPHINGPFTPDLAHPVAEVGKvaekegwpLDIRVGLIGSCTNSSYEDMGRSAAVAKQALahgLKCKSQ 380
Cdd:cd01351 233 YDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG--------TKIDQVLIGSCTNNRYSDMLAAAKLLKGAK---VAPGVR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 381 FTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGQWDRkdiKKGEKNTIVTSYNRNFTGRNDANPEtHAFVTSP 460
Cdd:cd01351 302 LIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGAR---LVADGEVGVSSGNRNFPGRLGTYER-HVYLASP 377
|
410
....*....|..
gi 1622836733 461 EIVTALAIAGTL 472
Cdd:cd01351 378 ELAAATAIAGKI 389
|
|
| acon_putative |
TIGR01342 |
aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins ... |
31-744 |
1.09e-124 |
|
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: 387.03 E-value: 1.09e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 31 TLSEKIVYGHL---DDPAGQEIErgksylrLRPDRVAMQDATAQMAMLQFISSGLPKVAVP-STIHCDHLIEaqlggEKD 106
Cdd:TIGR01342 1 TLAEKIIDDHLvegDLEPGEEIA-------IEIDQTLSQDATGTMCWLEFEALEMDEVKTElAAQYCDHNML-----QFD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 107 LRRAKDinqevYNFLATAGAKYGVGFWKPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAG 186
Cdd:TIGR01342 69 FKNADD-----HKFLMSAAGKFGAWFSKPGNGICHNVHKENFAAPGKTLLGSDSHTPTAGGLGMLAIGAGGIDIAAAMAG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 187 IPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPY 266
Cdd:TIGR01342 144 EAFYLEMPEIVGVHLEGELPEWATAKDIILELLRRLSVKGGLGKIFEYFGEGVEELSVPERATITNMGAELGATSSIFPS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 267 NHRMKKYLSKTGRADianladEFKDhLVPDPGCHYDQLIEVNLSELKPHINGPFTPDLAHPVAEVgkvaekEGWPLDIRV 346
Cdd:TIGR01342 224 DDITEAWLAAFDRED------DFVD-LLADADAEYADEIEIDLSDLEPLIAEPHMPDNVVPVREI------AGIEVDQVM 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 347 glIGSCTNSSYEDMGRSAAVAKQALAHGlkcKSQFTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGQwdrkD 426
Cdd:TIGR01342 291 --IGSCTNGAFEDLLPAAKLLEGREVHK---DTEFAVAPGSKQALELIAQEGALAEFLAAGANFLEAACGACIGI----G 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 427 IKKGEKNTIVTSYNRNFTGRNdANPETHAFVTSPEIVTALAIAGTLkFNPETdyLTGTDGKkfkLEAPDAdELPK---GE 503
Cdd:TIGR01342 362 FAPASDGVSLRSFNRNFEGRA-GIEDAKVYLASPETATAAAIAGEI-IDPRD--LADDEGD---LEAIGF-EMGEkfpGG 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 504 FDPGqDTYQHPPKDSSGQHVDVSPTSQRLQLLEPFdkwdGKDLEDlQILIKVKGKCTTDHISAAGP-WLKFRGHLDNISN 582
Cdd:TIGR01342 434 YDAA-DIDIIPKEEREDDDIIKGPNIKPLPEFDPL----GADIEG-ETALIMEDNITTDHIIPAGAdILKFRSNIEAISE 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 583 NLLigainiengkansvrNAVTQEFGPVPDTARYYKKHGIrwvVIGDENYGEGSSREHAALEPRHLGARAIITKSFARIH 662
Cdd:TIGR01342 508 FTL---------------HRIDDEFAERAKAADEKGKAGI---IIAGENYGQGSSREHAALAPMFLGVEAVIAKSFARIH 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 663 ETNLKKQGLLPLTFADPADYNKIHPVDKLTI-----QGLKDftpGKPLKCIIKHpngTQETILLNHTFNETQIEWFRAGS 737
Cdd:TIGR01342 570 HANLFNFGILPLEFDNEEDYAKFELGDDIEIpddlaAALAD---GEDEFTINKN---DDEEALATLDASEREKEILAAGG 643
|
....*..
gi 1622836733 738 ALNRMKE 744
Cdd:TIGR01342 644 KLNLIKN 650
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
61-472 |
6.94e-108 |
|
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: 333.65 E-value: 6.94e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 61 DRVAMQDATAQMAMLQFISSGLPKVAVP-STIHCDHLIeAQLGGEkdlrrakdiNQEVYNFLATAGAKYGVGFWKPGSGI 139
Cdd:cd01585 1 DQTLTQDATGTMAYLQFEAMGVDRVRTElSVSYVDHNT-LQTDFE---------NADDHRFLQTVAARYGIYFSRPGNGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 140 IHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVA 219
Cdd:cd01585 71 CHQVHLERFAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 220 GILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRadianlADEFKDhLVPDPGC 299
Cdd:cd01585 151 RRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGR------EDDWVE-LAADADA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 300 HYDQLIEVNLSELKPHINGPFTPDlahpvaEVGKVAEKEGWPLDiRVgLIGSCTNSSYEDMGRSAAVAKQALAHGlkcKS 379
Cdd:cd01585 224 EYDEEIEIDLSELEPLIARPHSPD------NVVPVREVAGIKVD-QV-AIGSCTNSSYEDLMTVAAILKGRRVHP---HV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 380 QFTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGQWDrkdiKKGEKNTIVTSYNRNFTGRNdANPETHAFVTS 459
Cdd:cd01585 293 SMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQ----APPTGGVSVRTFNRNFEGRS-GTKDDLVYLAS 367
|
410
....*....|...
gi 1622836733 460 PEIVTALAIAGTL 472
Cdd:cd01585 368 PEVAAAAALTGVI 380
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
554-702 |
2.31e-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: 323.65 E-value: 2.31e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 554 KVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINIENGKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVIGDENYG 633
Cdd:cd01578 1 KAKGKCTTDHISAAGPWLKYRGHLDNISNNLLIGAINAENGKANSVKNQVTGEYGPVPDTARDYKAHGIKWVVIGDENYG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622836733 634 EGSSREHAALEPRHLGARAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQGLKDFTPG 702
Cdd:cd01578 81 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYDKIHPDDKVDILGLTDFAPG 149
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
29-472 |
2.15e-77 |
|
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: 254.96 E-value: 2.15e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 29 PLTLSEKIvyghLDDPAGQEIERGKSYLrLRPDRVAMQDATAQMAMLQFISSGLPKVAVPSTIH--CDHLIEAqlggeKD 106
Cdd:COG0065 2 GMTLAEKI----LARHAGREVEPGEIVL-LYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVavFDHNVPT-----KD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 107 LRRAKDINQevynfLATAGAKYGVGFWKPGS-GIIHQIILEN-YAYPGVLLIGTDSHTPNGGglggicigvggA------ 178
Cdd:COG0065 72 PKSAEQVKT-----LREFAKEFGITFFDVGDpGICHVVLPEQgLVLPGMTIVGGDSHTCTHG-----------Afgafaf 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 179 -----DAVDVMA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICN 252
Cdd:COG0065 136 gigttDVAHVLAtGTLW-FKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCN 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 253 MGAEIGATTSVFPYNHRMKKYLSKTGRADIANLAdefkdhlvPDPGCHYDQLIEVNLSELKPHINGPFTPDLAHPVAEVG 332
Cdd:COG0065 215 MAIEAGAKAGIIAPDETTFEYLKGRPFAPWRTLK--------SDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 333 KVaekegwPLDirVGLIGSCTNSSYEDMGRSAAVAKqalahGLKCKS--QFTITPGSEQIRATIERDGYAQILRDLGGIV 410
Cdd:COG0065 287 GI------KID--QVFIGSCTNGRIEDLRAAAEILK-----GRKVAPgvRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEW 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622836733 411 LANACGPCIG-QWDRkdIKKGEKnTIVTSyNRNFTGRNdANPETHAFVTSPEIVTALAIAGTL 472
Cdd:COG0065 354 REPGCGMCLGmNMGV--LAPGER-CASTS-NRNFEGRM-GSPGSRTYLASPATAAASAIAGRI 411
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
40-747 |
3.99e-75 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 260.63 E-value: 3.99e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 40 HLDDPAGQEIERgKSYLRL--RPDRVAMQDATAQ------MAMLQFISS--GLPKV---AVPSTIHCDHLIEAQLGGEKD 106
Cdd:PRK12881 62 HLEALANWLPER-KSDDEIpfVPARVVMQDFTGVpalvdlAAMRDAAAEagGDPAKinpLVPVDLVVDHSVAVDYFGQKD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 107 -LRRAKDI----NQEVYNFLA-TAGAKYGVGFWKPGSGIIHQIILE--------------NYAYPGVLlIGTDSHTP--N 164
Cdd:PRK12881 141 aLDLNMKIefqrNAERYQFLKwGMQAFDNFRVVPPGTGIMHQVNLEylarvvhtkeddgdTVAYPDTL-VGTDSHTTmiN 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 165 GGGLGGICIGVGGADAVdvMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISC 244
Cdd:PRK12881 220 GIGVLGWGVGGIEAEAV--MLGQPVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 245 TGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRAD--IANLADEFKDH---LVPDPGCHYDQLIEVNLSELKPHINGP 319
Cdd:PRK12881 298 GDRATIANMAPEYGATMGFFPVDEQTLDYLRLTGRTEaqIALVEAYAKAQglwGDPKAEPRYTRTLELDLSTVAPSLAGP 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 320 ---------------FTPDLAHPVAEVGKVAEKEGWPL------DIRVGLIGSCTNSSYEDMGRSAA-VAKQALAHGLKC 377
Cdd:PRK12881 378 krpqdrialgnvksaFSDLFSKPVAENGFAKKAQTSNGvdlpdgAVAIAAITSCTNTSNPSVLIAAGlLAKKAVERGLTV 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 378 KS--QFTITPGSEQIRATIERDGYAQILRDLG-GIVlANACGPCIGQWD------RKDIKKGE-KNTIVTSYNRNFTGRN 447
Cdd:PRK12881 458 KPwvKTSLAPGSKVVTEYLERAGLLPYLEKLGfGIV-GYGCTTCIGNSGpltpeiEQAITKNDlVAAAVLSGNRNFEGRI 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 448 DANPEThAFVTSPEIVTALAIAGTLKFNPETDYL-TGTDGKKFKLE-----APDADELPKGEFDPgqDTYQH---PPKDS 518
Cdd:PRK12881 537 HPNIKA-NFLASPPLVVAYALAGTVRRDLMTEPLgKGKDGRPVYLKdiwpsSAEIDALVAFAVDP--EDFRKnyaEVFKG 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 519 SGQ-HVDVSPTSQRLQ-------LLEP--FDKWDG-----KDLEDLQILIKVKGKCTTDHIS---------AAGPWLKFR 574
Cdd:PRK12881 614 SELwAAIEAPDGPLYDwdpkstyIRRPpfFDFSMGpaasiATVKGARPLAVLGDSITTDHISpagaikadsPAGKYLKEN 693
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 575 GHLDNISN-----------------------NLLIGAinIENGkanSVRNAVTQEFGPVPDTARYYKKHGIRWVVIGDEN 631
Cdd:PRK12881 694 GVPKADFNsygsrrgnhevmmrgtfanvrikNLMIPG--KEGG---LTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEE 768
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 632 YGEGSSREHAALEPRHLGARAIITKSFARIHETNLKKQGLLPLTF--ADPADYNKIHPVDKLTIQGL-KDFTPGKPLKCI 708
Cdd:PRK12881 769 YGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFkgGDSRQSLGLTGGETFDIEGLpGEIKPRQDVTLV 848
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 1622836733 709 IKHPNGTQETILLNHTFnETQIE--WFRAGSALNRMkeLQQ 747
Cdd:PRK12881 849 IHRADGSTERVPVLCRI-DTPIEvdYYKAGGILPYV--LRQ 886
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
59-741 |
1.67e-74 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 258.90 E-value: 1.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 59 RPDRVAMQDAT--------AQM--AMLQF------ISsglPKVAVPSTIhcDHLIEAQLGGEKD-LRRAKDI----NQEV 117
Cdd:PRK09277 83 RPARVVMQDFTgvpavvdlAAMrdAIADLggdpakIN---PLVPVDLVI--DHSVQVDYFGTPDaFEKNVELeferNEER 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 118 YNFLatagaKYGVGFWK------PGSGIIHQIILE-------------NYAYPGVLlIGTDSHTPnggglggicigvgga 178
Cdd:PRK09277 158 YQFL-----KWGQKAFDnfrvvpPGTGICHQVNLEylapvvwtredgeLVAYPDTL-VGTDSHTT--------------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 179 dAVD----------------VMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSI 242
Cdd:PRK09277 217 -MINglgvlgwgvggieaeaAMLGQPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 243 SCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRAD--IAnladefkdhLV------------PDPGCHYDQLIEVN 308
Cdd:PRK09277 296 SLADRATIANMAPEYGATCGFFPIDEETLDYLRLTGRDEeqVA---------LVeayakaqglwrdPLEEPVYTDVLELD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 309 LSELKPHINGP-------FTPDLAHPVAEV--------GKVAEKEGWPLDIRVG-----LIGSCTNSS--YEDMGrsAA- 365
Cdd:PRK09277 367 LSTVEPSLAGPkrpqdriPLSDVKEAFAKSaelgvqgfGLDEAEEGEDYELPDGavviaAITSCTNTSnpSVMIA--AGl 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 366 VAKQALAHGLKCKS--QFTITPGSEQIRATIERDGYAQILRDLG-GIVlANACGPCIG---------QwdrKDIKkgEKN 433
Cdd:PRK09277 445 LAKKAVEKGLKVKPwvKTSLAPGSKVVTDYLEKAGLLPYLEALGfNLV-GYGCTTCIGnsgplppeiE---KAIN--DND 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 434 TIVT---SYNRNFTGRndANPETHA-FVTSPEIVTALAIAGTLKFNPETDYL-TGTDGKKFKLEA--PDADEL------- 499
Cdd:PRK09277 519 LVVTavlSGNRNFEGR--IHPLVKAnYLASPPLVVAYALAGTVDIDLEKDPLgTDKDGNPVYLKDiwPSDEEIdavvaka 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 500 -------------------------PKGE---FDPgQDTY-QHPpkdssgqhvdvsptsqrlqllePFdkWDG------- 543
Cdd:PRK09277 597 vkpemfrkeyadvfegderwnaievPEGPlydWDP-DSTYiRNP----------------------PY--FEGmlaepgp 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 544 -KDLEDLQILIKVKGKCTTDHIS---------AAGPWLK--------F--------------RGHLDNIS--NNLLIGai 589
Cdd:PRK09277 652 vRDIKGARVLALLGDSITTDHISpagaikadsPAGKYLLehgvepkdFnsygsrrgnhevmmRGTFANIRirNEMVPG-- 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 590 nIENGKAnsvRNAVTQEFGPVPDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRHLGARAIITKSFARIHETNLKKQ 669
Cdd:PRK09277 730 -VEGGYT---RHFPEGEVMSIYDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGM 805
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622836733 670 GLLPLTFADPADYN--KIHPVDKLTIQGLKDFTPGKPLKCIIKHPNGTQETI-LLNHTFNETQIEWFRAGSALNR 741
Cdd:PRK09277 806 GVLPLQFKPGESRKtlGLDGTETFDIEGLEDLKPGATVTVVITRADGEVVEFpVLCRIDTAVEVDYYRNGGILQY 880
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
29-470 |
2.31e-70 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 236.23 E-value: 2.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 29 PLTLSEKIVYGHlddpAGQEIERGKsYLRLRPDRVAMQDATAQMAMLQFISSGLPKVAVPSTIH--CDHLIEAqlggeKD 106
Cdd:PRK00402 2 GMTLAEKILARH----SGRDVSPGD-IVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVivFDHFVPA-----KD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 107 LRRAKdINQEVYNFLATAGAKYgvgFWKPGSGIIHQIILEN-YAYPGVLLIGTDSHTPNggglggicigvggADAV---- 181
Cdd:PRK00402 72 IKSAE-QQKILREFAKEQGIPN---FFDVGEGICHQVLPEKgLVRPGDVVVGADSHTCT-------------YGALgafa 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 182 ------D---VMA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATIC 251
Cdd:PRK00402 135 tgmgstDmaaAMAtGKTW-FKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 252 NMGAEIGATTSVFPYNHRMKKYLSKTGRADIanladefkDHLVPDPGCHYDQLIEVNLSELKPHINGPFTPDLAHPVAEV 331
Cdd:PRK00402 214 NMAIEAGAKAGIFAPDEKTLEYLKERAGRDY--------KPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 332 GKVaekegwPLDIRVglIGSCTNSSYEDMGRSAAVAKqalAHGLKCKSQFTITPGSEQIRATIERDGYAQILRDLGGIVL 411
Cdd:PRK00402 286 EGT------KVDQVF--IGSCTNGRLEDLRIAAEILK---GRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVS 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622836733 412 ANACGPCIGqwdrkdIKKGEknTIVTSYNRNFTGRNdANPETHAFVTSPEIVTALAIAG 470
Cdd:PRK00402 355 TPTCGPCLGghm-gvLAPGE--VCLSTTNRNFKGRM-GSPESEVYLASPAVAAASAVTG 409
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
62-470 |
2.69e-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: 227.07 E-value: 2.69e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 62 RVAMQDATAQMAMLQFISSGLPKVAVPSTIHC--DHLIEAqlggeKDLRRAKDINQEVYNFlatagAKYGVGFWKPG-SG 138
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAvfDHNVPT-----PDIKAAEQVKTLRKFA-----KEFGINFFDVGrQG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 139 IIHQIILENY-AYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVIL 216
Cdd:cd01583 71 ICHVILPEKGlTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLAtGKLW-FRVPETMRVNVEGKLPPGVTAKDVIL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 217 KVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRAdianladEFKdHLVPD 296
Cdd:cd01583 150 YIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKA-------YWK-ELKSD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 297 PGCHYDQLIEVNLSELKPHINGPFTPDLAHPVAEVGKVaekegwPLDIRVglIGSCTNSSYEDMGRSAAVAKqalAHGLK 376
Cdd:cd01583 222 EDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEGI------KIDQVF--IGSCTNGRLEDLRAAAEILK---GRKVA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 377 CKSQFTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIG-QWDRkdIKKGEknTIVTSYNRNFTGR-NDANPETH 454
Cdd:cd01583 291 DGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGgHMGV--LAPGE--RCVSTSNRNFKGRmGSPGARIY 366
|
410
....*....|....*.
gi 1622836733 455 afVTSPEIVTALAIAG 470
Cdd:cd01583 367 --LASPATAAASAITG 380
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
61-740 |
3.66e-65 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 232.98 E-value: 3.66e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 61 DRVAMQDAtaqMAML----QFISsglPKVAVPSTIhcDHLIEAQLGGEKD-LRRAKDI----NQEVYNFLatagaKYGVG 131
Cdd:PTZ00092 106 DLAAMRDA---MKRLggdpAKIN---PLVPVDLVI--DHSVQVDFSRSPDaLELNQEIeferNLERFEFL-----KWGSK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 132 FWK------PGSGIIHQIILE----------NYAYPGVLlIGTDSHTP--NGGGLGGICIGVGGADAVdvMAGIPWELKC 193
Cdd:PTZ00092 173 AFKnllivpPGSGIVHQVNLEylarvvfnkdGLLYPDSV-VGTDSHTTmiNGLGVLGWGVGGIEAEAV--MLGQPISMVL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 194 PKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKY 273
Cdd:PTZ00092 250 PEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDY 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 274 LSKTGRAD-----IANLADEFKDHLVPDPGCHYDQLIEVNLSELKPHINGP---------------FTPDLAHPVA---- 329
Cdd:PTZ00092 330 LKQTGRSEekvelIEKYLKANGLFRTYAEQIEYSDVLELDLSTVVPSVAGPkrphdrvplsdlkkdFTACLSAPVGfkgf 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 330 -----EVGKVAEKE--GWPLDIRVG-----LIGSCTNSSYED-MGRSAAVAKQALAHGLKCKS--QFTITPGSEQIRATI 394
Cdd:PTZ00092 410 gipeeKHEKKVKFTykGKEYTLTHGsvviaAITSCTNTSNPSvMLAAGLLAKKAVEKGLKVPPyiKTSLSPGSKVVTKYL 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 395 ERDGYAQILRDLGGIVLANACGPCIGqwDRKDIKKGEKNTI---------VTSYNRNFTGRndANPETHA-FVTSPEIVT 464
Cdd:PTZ00092 490 EASGLLKYLEKLGFYTAGYGCMTCIG--NSGDLDPEVSEAItnndlvaaaVLSGNRNFEGR--VHPLTRAnYLASPPLVV 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 465 ALAIAGTLKFNPETDYL-TGTDGKKFKLEA--PDADEL--------------------------------PKGEF---DP 506
Cdd:PTZ00092 566 AYALAGRVNIDFETEPLgSDKTGKPVFLRDiwPSREEIqaleakyvkpemfkevysnitqgnkqwnelqvPKGKLyewDE 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 507 gQDTYQHPPKDSSGQHVDVSPTsqrlqllepfdkwdgKDLEDLQILIKVKGKCTTDHISAAG------PWLKF------- 573
Cdd:PTZ00092 646 -KSTYIHNPPFFQTMELEPPPI---------------KSIENAYCLLNLGDSITTDHISPAGniaknsPAAKYlmergve 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 574 ------------------RGHLDNIS-NNLLIGA-----INIENGKANSVRNAvtqefgpvpdtARYYKKHGIRWVVIGD 629
Cdd:PTZ00092 710 rkdfntygarrgndevmvRGTFANIRlINKLCGKvgpntVHVPTGEKMSIYDA-----------AEKYKQEGVPLIVLAG 778
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 630 ENYGEGSSREHAALEPRHLGARAIITKSFARIHETNLKKQGLLPLTFAD--PADYNKIHPVDKLTIQGLK-DFTPGKPLK 706
Cdd:PTZ00092 779 KEYGSGSSRDWAAKGPYLQGVKAVIAESFERIHRSNLVGMGILPLQFLNgeNADSLGLTGKEQFSIDLNSgELKPGQDVT 858
|
810 820 830
....*....|....*....|....*....|....*
gi 1622836733 707 ciIKHPNG-TQETILLNHTfnETQIEWFRAGSALN 740
Cdd:PTZ00092 859 --VKTDTGkTFDTILRIDT--EVEVEYFKHGGILQ 889
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
549-679 |
1.22e-60 |
|
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: 200.28 E-value: 1.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 549 LQILIKVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINIENGKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVIG 628
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1622836733 629 DENYGEGSSREHAALEPRHLGARAIITKSFARIHETNLKKQGLLPLTFADP 679
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
59-681 |
3.68e-59 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 216.21 E-value: 3.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 59 RPDRVAMQDAT--------AQM--AMLQFIS-SGLPKVAVPSTIHCDHLIEAQLGGEKDLRRAK-----DINQEVYNFLa 122
Cdd:PLN00070 121 KPARVLLQDFTgvpavvdlACMrdAMNNLGGdPNKINPLVPVDLVIDHSVQVDVARSENAVQANmelefQRNKERFAFL- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 123 tagaKYGVGFWK------PGSGIIHQIILENYA----------YPGVLlIGTDSHTPNGGGLGGICIGVGGADAVDVMAG 186
Cdd:PLN00070 200 ----KWGSTAFQnmlvvpPGSGIVHQVNLEYLGrvvfntdgilYPDSV-VGTDSHTTMIDGLGVAGWGVGGIEAEAAMLG 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 187 IPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPY 266
Cdd:PLN00070 275 QPMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPV 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 267 NHRMKKYLSKTGRAD----------IANlaDEFKDHLVPDPGCHYDQLIEVNLSELKPHINGPFTP-------------- 322
Cdd:PLN00070 355 DHVTLQYLKLTGRSDetvamieaylRAN--KMFVDYNEPQQERVYSSYLELDLEDVEPCISGPKRPhdrvplkemkadwh 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 323 ----------DLAHPVAEVGKVAE--KEGWPLDIRVG-----LIGSCTNSSYED-MGRSAAVAKQALAHGLKCKS--QFT 382
Cdd:PLN00070 433 scldnkvgfkGFAVPKEAQSKVAKfsFHGQPAELRHGsvviaAITSCTNTSNPSvMLGAGLVAKKACELGLEVKPwiKTS 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 383 ITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGqwDRKDIKKGEKNTI---------VTSYNRNFTGRndANPET 453
Cdd:PLN00070 513 LAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIG--NSGELDESVASAItendivaaaVLSGNRNFEGR--VHPLT 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 454 HA-FVTSPEIVTALAIAGTLKFNPETDYL-TGTDGKK--FKLEAPDADELPKGEF-----DPGQDTYQHPPK-------- 516
Cdd:PLN00070 589 RAnYLASPPLVVAYALAGTVDIDFEKEPIgTGKDGKDvfFRDIWPSNEEVAEVVQssvlpDMFKSTYEAITKgnpmwnql 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 517 ----------DSSGQHVDVSPTSQRLQLLEPfdkwDGKDLEDLQILIKVKGKCTTDHISAAG------PWLKF------- 573
Cdd:PLN00070 669 svpsgtlyswDPKSTYIHEPPYFKNMTMSPP----GPHGVKDAYCLLNFGDSITTDHISPAGsihkdsPAAKYlmergvd 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 574 ------------------RGHLDNIS--NNLLIG-----AINIENGKANSVRnavtqefgpvpDTARYYKKHGIRWVVIG 628
Cdd:PLN00070 745 rkdfnsygsrrgndeimaRGTFANIRivNKLLKGevgpkTVHIPTGEKLSVF-----------DAAMKYKSEGHDTIILA 813
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1622836733 629 DENYGEGSSREHAALEPRHLGARAIITKSFARIHETNLKKQGLLPLTFADPAD 681
Cdd:PLN00070 814 GAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGED 866
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
31-470 |
1.47e-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: 204.22 E-value: 1.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 31 TLSEKIVYGHlddpAGQEIERGKSyLRLRPDRVAMQDATAQMAMLQFISSGLPKVAVPSTIHC--DHLIEAqlggekDLR 108
Cdd:TIGR01343 1 TIAEKILSKK----SGKEVYAGDL-IEAEIDLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIvfDHQVPA------DTI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 109 RAKDINQEVYNFLATAGAKYgvgFWKPGSGIIHQIILEN-YAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMA-G 186
Cdd:TIGR01343 70 KAAEMQKLAREFVKKQGIKY---FYDVGEGICHQVLPEKgLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIAtG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 187 IPWeLKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPY 266
Cdd:TIGR01343 147 KTW-FKVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 267 NHRMKKYLSKTGRADianlADEFKDhlvpDPGCHYDQLIEVNLSELKPHINGPFTPDLAHPVAEVgkvaekEGWPLDiRV 346
Cdd:TIGR01343 226 DEKTIQYLKERRKEP----FRVYKS----DEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEV------EGTEID-QV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 347 gLIGSCTNSSYEDMGRSAAVAKqalAHGLKCKSQFTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGqwdRKD 426
Cdd:TIGR01343 291 -FIGSCTNGRLEDLRVAAKILK---GRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLG---SHQ 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1622836733 427 IKKGEKNTIVTSYNRNFTGRNdANPETHAFVTSPEIVTALAIAG 470
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 ... |
62-471 |
1.44e-45 |
|
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: 167.87 E-value: 1.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 62 RVAMQDATAQMAMLQFIS--------SGLP-KV--AVPSTIHCDHLIEAQLGG-----EKDLRRAKDINQEVYNFLatag 125
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAmrdavkrlGGDPeKInpLIPVDLVIDHSVQVDFYGtadalAKNMKLEFERNRERYEFL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 126 aKYGVGFWK------PGSGIIHQIILE--------------NYAYPGVLlIGTDSHTPNGGGLGGICIGVGGADAVDVMA 185
Cdd:cd01586 77 -KWGQKAFKnlrvvpPGTGIIHQVNLEylarvvftseedgdGVAYPDSV-VGTDSHTTMINGLGVLGWGVGGIEAEAVML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 186 GIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFP 265
Cdd:cd01586 155 GQPISMLLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 266 YNhrmkkylsktgradianladefkdhlvpdpgchyDQLIEVNLSELKPHINGPFTPDlaHPVAEVGKVAekegwpldir 345
Cdd:cd01586 235 VD----------------------------------TQVVELDLSTVEPSVSGPKRPQ--DRVPLHGSVV---------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 346 VGLIGSCTNSSYED-MGRSAAVAKQALAHGLKCKS--QFTITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIG-- 420
Cdd:cd01586 269 IAAITSCTNTSNPSvMLAAGLLAKKAVELGLKVKPyvKTSLAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGns 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622836733 421 ----QWDRKDIKKGE-KNTIVTSYNRNFTGRndANPETHA-FVTSPEIVTALAIAGT 471
Cdd:cd01586 349 gplpEEVEEAIKENDlVVAAVLSGNRNFEGR--IHPLVRAnYLASPPLVVAYALAGT 403
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
75-472 |
9.17e-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: 141.98 E-value: 9.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 75 LQFISSGLPKVAVPSTIHC--DHliEAQLGGEKDLRRAKDINqevyNFlataGAKYGVGFWKPGSGIIHQIILEN-YAYP 151
Cdd:cd01582 13 LKFMSIGATKIHNPDQIVMtlDH--DVQNKSEKNLKKYKNIE----SF----AKKHGIDFYPAGRGIGHQIMIEEgYAFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 152 GVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGA 230
Cdd:cd01582 83 GTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWAtGQTW-WQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLNH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 231 IVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRmkkylsktgradianladefkdHLVPDpgchydqlievnLS 310
Cdd:cd01582 162 AIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAK----------------------HLILD------------LS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 311 ELKPHINGPFTPDLAHPVAEVgkvaekEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQA--------LAHGLKcksqFT 382
Cdd:cd01582 208 TLSPYVSGPNSVKVSTPLKEL------EAQNIKINKAYLVSCTNSRASDIAAAADVVKGKkekngkipVAPGVE----FY 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 383 ITPGSEQIRATIERDGYAQILRDLGGIVLANACGPCIGqWDRKDIKKGEKNtiVTSYNRNFTGRNdANPETHAFVTSPEI 462
Cdd:cd01582 278 VAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIG-LGQGLLEPGEVG--ISATNRNFKGRM-GSTEALAYLASPAV 353
|
410
....*....|
gi 1622836733 463 VTALAIAGTL 472
Cdd:cd01582 354 VAASAISGKI 363
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
194-472 |
1.19e-30 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 126.00 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 194 PKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGA---------TTsvF 264
Cdd:PRK05478 163 PKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGAraglvapdeTT--F 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 265 PYnhrMKkylsktGR--ADIANLADEFKDH---LVPDPGCHYDQLIEVNLSELKPH------------INGPFtPDLAHP 327
Cdd:PRK05478 241 EY---LK------GRpfAPKGEDWDKAVAYwktLKSDEDAVFDKVVTLDAADIEPQvtwgtnpgqvisIDGKV-PDPEDF 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 328 VAEVGKVAEKE---------GWPL-DIRVG--LIGSCTNSSYEDMGRSAAVAKqalahGLKCKSQFT--ITPGSEQIRAT 393
Cdd:PRK05478 311 ADPVKRASAERalaymglkpGTPItDIKIDkvFIGSCTNSRIEDLRAAAAVVK-----GRKVAPGVRalVVPGSGLVKAQ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 394 IERDGYAQILRDLG------GivlanaCGPCIGQWDrkDIKKGEKNTIVTSyNRNFTGRNDANPETHafVTSPEIVTALA 467
Cdd:PRK05478 386 AEAEGLDKIFIEAGfewrepG------CSMCLAMNP--DKLPPGERCASTS-NRNFEGRQGKGGRTH--LVSPAMAAAAA 454
|
....*
gi 1622836733 468 IAGTL 472
Cdd:PRK05478 455 ITGHF 459
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
554-695 |
1.48e-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: 112.18 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 554 KVKGKCTTDHISAAGPWlkfrghldnisnnlligainiengkansvrnavtqefgpvpdtaryykkhgirwVVIGDENYG 633
Cdd:cd00404 1 KVAGNITTDHISPAGPG------------------------------------------------------VVIGDENYG 26
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622836733 634 EGSSREHAALEPRHLGARAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQG 695
Cdd:cd00404 27 TGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDYLKLHTGDELDIYP 88
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
554-695 |
7.72e-29 |
|
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: 111.38 E-value: 7.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 554 KVKGKCTTDHISAAGP-WLKFRGHLDNISNNLLIGainiengkansvrnaVTQEFGPvpdtaryYKKHGIRWVVIGDENY 632
Cdd:cd01579 1 KVGDNITTDHIMPAGAkVLPLRSNIPAISEFVFHR---------------VDPTFAE-------RAKAAGPGFIVGGENY 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622836733 633 GEGSSREHAALEPRHLGARAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQG 695
Cdd:cd01579 59 GQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADEDDYDRFEQGDQLELPL 121
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
27-472 |
8.61e-29 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 120.78 E-value: 8.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 27 NRPLTLSEKIVYGHL--DDPAGQEIergksylrLRPDRVAMQDATAQMAMLQFISSGLPkVAVPSTIHC--DHLIEAQLG 102
Cdd:PRK12466 1 MMPRTLYDKLWDSHTvaRLDDGHVL--------LYIDRHLLNEYTSPQAFSGLRARGRT-VRRPDLTLAvvDHVVPTRPG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 103 GEKDLRRAKDINQEVYnfLATAGAKYGV---GFWKPGSGIIHQIILE-NYAYPGVLLIGTDSHTPNGGGLGGICIGVGGA 178
Cdd:PRK12466 72 RDRGITDPGGALQVDY--LRENCADFGIrlfDVDDPRQGIVHVVAPElGLTLPGMVIVCGDSHTTTYGALGALAFGIGTS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 179 DAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIG 258
Cdd:PRK12466 150 EVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 259 ATTSVFPYNHRMKKYLSKTGRADIANLADEFKDH---LVPDPGCHYDQLIEVNLSELKPHINGPFTPDLAHPVAEVGKVA 335
Cdd:PRK12466 230 ARGGLIAPDETTFDYLRGRPRAPKGALWDAALAYwrtLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 336 EKE--------------------GWPL-DIRVG--LIGSCTNSSYEDMGRSAAVAKqalahGLKCKSQFT--ITPGSEQI 390
Cdd:PRK12466 310 AAEadparraameraldymgltpGTPLaGIPIDrvFIGSCTNGRIEDLRAAAAVLR-----GRKVAPGVRamVVPGSGAV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 391 RATIERDGYAQILRDLGGIVLANACGPCIGQWDRKdIKKGEKntIVTSYNRNFTGRNDANPETHafVTSPEIVTALAIAG 470
Cdd:PRK12466 385 RRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDV-LAPGER--CASTTNRNFEGRQGPGARTH--LMSPAMVAAAAVAG 459
|
..
gi 1622836733 471 TL 472
Cdd:PRK12466 460 HI 461
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
56-698 |
9.59e-25 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 110.10 E-value: 9.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 56 LRLRPDRVAMQDAT----AQMAmlqfISSGLPKVAVPSTIHCDHLIEAQLGGEkdlrrakdINQEVYNFLATAGAKYGVG 131
Cdd:PRK11413 54 LKIKFDSLASHDITfvgiIQTA----KASGMERFPLPYVLTNCHNSLCAVGGT--------INEDDHVFGLSAAQKYGGI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 132 FWKPGSGIIHQIILENYAYPGVLLIGTDSHTpnggglggicigvgGADAVDVMA---GIP----------WELKCPKVIG 198
Cdd:PRK11413 122 FVPPHIAVIHQYMREMMAGGGKMILGSDSHT--------------RYGALGTMAvgeGGGelvkqllndtYDIDYPGVVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 199 VKLTGSLSGWTSPKDVILKVAGILTVKGGT-GAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKT 277
Cdd:PRK11413 188 VYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLALH 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 278 GRadianlADEFKDhLVPDPGCHYDQLIEVNLSELKPHINGPFTPDLAHPVAEVGKVA-------EKEGWPLD------- 343
Cdd:PRK11413 268 GR------GQDYCE-LNPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDELNQNLtdilrevEIESERVAhgkakls 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 344 ---------IRV--GLIGSCTNSSYEDMgrsaavakQALAHGLKCKS----QFTIT--PGSEQIRATIERDGYAQILRDL 406
Cdd:PRK11413 341 lldkiengrLKVqqGIIAGCSGGNYENV--------IAAANALRGQScgndTFSLSvyPSSQPVFMDLAKKGVVADLMGA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 407 GGIVLANACGPCIGQWDrkdikkgekntivTSYNRNF----TGRNDANPE----THAFVTSPEIVTALAIAGTLKFNpet 478
Cdd:PRK11413 413 GAIIRTAFCGPCFGAGD-------------TPANNGLsirhTTRNFPNREgskpANGQMSAVALMDARSIAATAANG--- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 479 DYLTGTDgkkfklEAPDADELPKGEFDPgqDTYQHPPKDSSGQHVdvspTSQRLQLLEPFDKWdgKDLEDL--QILIKVK 556
Cdd:PRK11413 477 GYLTSAT------ELDCWDNVPEYAFDV--TPYKNRVYQGFGKGA----TQQPLIYGPNIKDW--PEMGALtdNILLKVC 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 557 GK-----CTTDHISAAGPWLKFRghldniSNNLLIGAIN--------IENGKA-----NSVRNAVTQEFGPVPDTAR-YY 617
Cdd:PRK11413 543 SKildpvTTTDELIPSGETSSYR------SNPLGLAEFTlsrrdpgyVGRSKAvaeleNQRLAGNVSELTEVFARIKqIA 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 618 KKHGIRW--VVIGDENY----GEGSSREHAALEPRHLGARAIITKSFA-RIHETNLKKQGLLPLTFADPadyNKIHPVDK 690
Cdd:PRK11413 617 GQEHIDPlqTEIGSMVYavkpGDGSAREQAASCQRVLGGLANIAEEYAtKRYRSNVINWGMLPFQMAEE---PTFEVGDY 693
|
....*...
gi 1622836733 691 LTIQGLKD 698
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, ... |
560-695 |
4.77e-19 |
|
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: 85.02 E-value: 4.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 560 TTDHISAAGPWLK-------------------------------FRGHLDNISN-NLLIGainieNGKANSVRNAVTQEF 607
Cdd:cd01580 7 TTDHISPAGSIAKdspagkylaergvkprdfnsygsrrgndevmMRGTFANIRLrNKLVP-----GTEGGTTHHPPTGEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 608 GPVPDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRHLGARAIITKSFARIHETNLKKQGLLPLTFADP--ADYNKI 685
Cdd:cd01580 82 MSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGenADSLGL 161
|
170
....*....|
gi 1622836733 686 HPVDKLTIQG 695
Cdd:cd01580 162 TGEETYDIIG 171
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
625-693 |
1.63e-14 |
|
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: 69.54 E-value: 1.63e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 625 VVIGDENYGEGSSREHAALEPRHLGARAIITKSFARIHETNLKKQGLLPLTFADPADYN-KIHPVDKLTI 693
Cdd:cd01577 20 IIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEvEAKPGDEVEV 89
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
625-693 |
5.97e-12 |
|
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: 65.19 E-value: 5.97e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622836733 625 VVIGDENYGEGSSREHAALEPRHLGARAIITKSFARIHETNLKKQGLLPLTfADPADYNKI------HPVDKLTI 693
Cdd:COG0066 67 ILVAGRNFGCGSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIE-LPEEAVDALfaaieaNPGDELTV 140
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
625-707 |
4.99e-10 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 58.68 E-value: 4.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 625 VVIGDENYGEGSSREHAALEPRHLGARAIITKSFARIHETNLKKQGLLPLTFADPADynKIHPVDKLTI---QG-LKDFT 700
Cdd:PRK00439 51 IIVAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIGLPVLECDEAVD--KIEDGDEVEVdleTGvITNLT 128
|
....*..
gi 1622836733 701 PGKPLKC 707
Cdd:PRK00439 129 TGEEYKF 135
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
129-472 |
1.81e-09 |
|
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: 60.59 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 129 GVGFWKPGSGIIHQIiLENYAYPGVLLIGTDSHT--PNGGGLGGICIGVGGADAVDVMAgipweLKCPKVIGVKLTGSLS 206
Cdd:cd01581 85 GGVALRPGDGVIHSW-LNRMLLPDTVGTGGDSHTrfPIGISFPAGSGLVAFAAATGVMP-----LDMPESVLVRFKGKMQ 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 207 GWTSPKDVILKV------AGILTV--KGG----TGAIVEYHGpgVDSISCTGMATICNMGAEIGATTSVFPYNH------ 268
Cdd:cd01581 159 PGITLRDLVNAIpyyaiqQGLLTVekKGKknvfNGRILEIEG--LPDLKVEQAFELTDASAERSAAACTVRLDKepviey 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 269 ------RMKKYLSKtGRADIANLADEFKDH---------LVPDPGCHYDQLIEVNLSELK-PHINGPFTPDLAHPVAEV- 331
Cdd:cd01581 237 lesnvvLMKIMIAN-GYDDARTLLRRIIAMeewlanpplLEPDADAEYAAVIEIDLDDIKePILACPNDPDDVKLLSEVa 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 332 GKVaekegwpldIRVGLIGSC-TNssyedMGRSAAVAKQALAHGLKcKSQFTITPGSEQIRATIERDGYAQILRDLGGIV 410
Cdd:cd01581 316 GKK---------IDEVFIGSCmTN-----IGHFRAAAKILRGKEFK-PTRLWVAPPTRMDWAILQEEGYYSIFGDAGART 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622836733 411 LANACGPCIGQWDRkdIKKGEknTIVTSYNRNFTGR--NDANpethAFVTSPEIVTALAIAGTL 472
Cdd:cd01581 381 EMPGCSLCMGNQAR--VADGA--TVFSTSTRNFDNRvgKGAE----VYLGSAELAAVCALLGRI 436
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
611-681 |
4.64e-09 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 55.96 E-value: 4.64e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622836733 611 PDTARYYKKHGIrwvVIGDENYGEGSSREHAALEPRHLGARAIITKSFARIHETNLKKQGLLPLTFADPAD 681
Cdd:PRK14023 41 PEFASTVRPGDI---LVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPPFESEEVVD 108
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
119-500 |
4.67e-09 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 59.94 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 119 NFLATAGakyGVGFwKPGSGIIHQIiLENYAYPGVLLIGTDSHT--PNGGGLGGICIGVGGADAVDVMAgipweLKCPKV 196
Cdd:PLN00094 525 DFIRNRG---GVSL-RPGDGVIHSW-LNRMLLPDTVGTGGDSHTrfPIGISFPAGSGLVAFGAATGVIP-----LDMPES 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 197 IGVKLTGSLSGWTSPKDVILKV------AGILTV-KGG-----TGAIVEYHGpgVDSISCTGMATICNMGAEIGAT---- 260
Cdd:PLN00094 595 VLVRFTGTMQPGITLRDLVHAIpytaiqDGLLTVeKKGkknvfSGRILEIEG--LPHLKCEQAFELSDASAERSAAgcti 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 261 ----TSVFPY---NHRMKKYLSKTGRAD-------IANLADEFKD-HLV-PDPGCHYDQLIEVNLSELK-PHINGPFTPD 323
Cdd:PLN00094 673 kldkEPIIEYlnsNVVMLKWMIAEGYGDrrtlerrIARMQQWLADpELLeADPDAEYAAVIEIDMDEIKePILCAPNDPD 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 324 LAHPVAEV--GKVAEKegwpldirvgLIGSC-TNssyedMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIERDGYA 400
Cdd:PLN00094 753 DARLLSEVtgDKIDEV----------FIGSCmTN-----IGHFRAAGKLLNDNLSQLPTRLWVAPPTKMDEAQLKAEGYY 817
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622836733 401 QILRDLGGIVLANACGPCIGQWDRKdikkGEKNTIVTSYNRNFTGR--NDANpethAFVTSPEIVTALAIAGTLKfNPEt 478
Cdd:PLN00094 818 STFGTVGARTEMPGCSLCMGNQARV----AEKSTVVSTSTRNFPNRlgKGAN----VYLASAELAAVAAILGRLP-TVE- 887
|
410 420
....*....|....*....|....*...
gi 1622836733 479 DYLTGTDgkKFKLEAPDA------DELP 500
Cdd:PLN00094 888 EYLSYME--KLDATASDTyrylnfDELP 913
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
625-674 |
2.22e-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: 53.96 E-value: 2.22e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1622836733 625 VVIGDENYGEGSSREHAALEPRHLGARAIITKSFARIHETNLKKQGLLPL 674
Cdd:TIGR02087 50 VIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLI 99
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
625-693 |
1.54e-07 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 52.44 E-value: 1.54e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622836733 625 VVIGDENYGEGSSREHA--ALEprHLGARAIITKSFARIHETNLKKQGLLPLTfADPADYNKI------HPVDKLTI 693
Cdd:PRK01641 70 ILLAGDNFGCGSSREHApwALA--DYGFRAVIAPSFADIFYNNCFKNGLLPIV-LPEEDVDELfklveaNPGAELTV 143
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
625-661 |
3.61e-06 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 49.09 E-value: 3.61e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1622836733 625 VVIGDENYGEGSSREHAALEPRHLGARAIITKSFARI 661
Cdd:PLN00072 132 IIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARI 168
|
|
| |
