|
Name |
Accession |
Description |
Interval |
E-value |
| aconitase_mito |
TIGR01340 |
aconitate hydratase, mitochondrial; This model represents mitochondrial forms of the TCA cycle ... |
18-748 |
0e+00 |
|
aconitate hydratase, mitochondrial; This model represents mitochondrial forms of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. [Energy metabolism, TCA cycle]
Pssm-ID: 273561 [Multi-domain] Cd Length: 745 Bit Score: 1235.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 18 YDLLEKNIDIVRKRLN-RPLTLSEKIVYGHLDDPAN----QEIE--RGKTYLRLRPDRVAMQDATAQMAMLQFISSGLPK 90
Cdd:TIGR01340 1 YEKLYNNLDEVRRRLNsRPLTLAEKILYSHLDDPEEsllsQDIGdvRGKSYLKLRPDRVAMQDASAQMALLQFMTCGLPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 91 VAVPSTIHCDHLIEAQLGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIHQIILENYAYPGVLLIGTDSHTPN 170
Cdd:TIGR01340 81 VAVPASIHCDHLIVGQKGGDKDLARAIATNKEVFDFLESAGKKYGIGFWKPGSGIIHQIVLENYAFPGLMMLGTDSHTPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 171 GGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISC 250
Cdd:TIGR01340 161 AGGLGTIAIGVGGADAVDALAGAPWELKAPKILGVKLTGKLNGWTSPKDIILKLAGLLTVRGGTGYIVEYFGPGVESLSC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 251 TGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFKDH---LVPDSGCHYDQLIEINLSELKPHINGPFT 327
Cdd:TIGR01340 241 TGMATICNMGAEIGATTSIFPFNEAMSRYLKATNRAQIAEDAKTGQYSffkLKADEGAQYDELIEIDLSKLEPHINGPFT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 328 PDLAHPVAEVGSVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIERDGYAQ 407
Cdd:TIGR01340 321 PDLSTPISKFKETVQKNGWPEKLSAGLIGSCTNSSYEDMSRCASIVKDAEQAGLKPKSPFYVTPGSEQIRATLERDGILQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 408 VLRDVGGIVLANACGPCIGQWDRKD-IKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSPEIVTALAIAGTLKFNPETDF 486
Cdd:TIGR01340 401 TFEKFGGIVLANACGPCIGQWDRKDdVKKGEPNTILTSYNRNFRGRNDGNPATMNFLASPEIVTAMSYAGSLTFNPLTDS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 487 LTGKDGKKFKLEAPDADELPRAEFDPGQDTYQHPPKDS-SGQRVDVSPTSQRLQLLEPFDKWDGKDLEDLQILIKVKGKC 565
Cdd:TIGR01340 481 LTTPDGKEFKFPAPKGDELPEKGFEAGRDTFQAPPGSPnPNVEVAVSPSSDRLQLLEPFEPWNGKDLSGLRVLIKVTGKC 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 566 TTDHISAAGPWLKFRGHLDNISNNLLIGAINSENRKANSVRNaVTQEFGPVPDTARYYKQHGIRWVVIGDENYGEGSSRE 645
Cdd:TIGR01340 561 TTDHISAAGPWLKYKGHLDNISNNTLIGAVNAETGEVNKAYD-LDGSKGTIPELARDWKARGQPWVVVAEHNYGEGSARE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 646 HSALEPRFLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQGLKDFAP---GKPLTCIIKHPNGTQ 722
Cdd:TIGR01340 640 HAALEPRHLGGRIIITKSFARIHETNLKKQGVLPLTFANEADYDKIQPGDEVATLNLYEMLKnggGGEVDLRVTKKNGKV 719
|
730 740
....*....|....*....|....*.
gi 157829965 723 ETILLNHTFNETQIEWFRAGSALNRM 748
Cdd:TIGR01340 720 FEIKLKHTVSKDQIGFFKAGSALNLM 745
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
34-754 |
0e+00 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 899.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 34 RPLTLSEKIVYGHLDDPanqEIERGKTyLRLRPDRVAMQDATAQMAMLQFISSGLPKVAVPSTI-HCDHlieaqlggekD 112
Cdd:PRK07229 1 MGLTLTEKILYAHLVEG---ELEPGEE-IAIRIDQTLTQDATGTMAYLQFEAMGLDRVKTELSVqYVDH----------N 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 113 LRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAG 192
Cdd:PRK07229 67 LLQADFENADDHRFLQSVAAKYGIYFSKPGNGICHQVHLERFAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 193 IPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPY 272
Cdd:PRK07229 147 GPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 273 NHRMKKYLSKTGRADIAnladefkDHLVPDSGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVGsvaekegwPLDIRV 352
Cdd:PRK07229 227 DERTREFLKAQGREDDW-------VELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVA--------GIKVDQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 353 GLIGSCTNSSYEDMGRSAAVAKqalAHGLKCKSQFTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGQwdrkD 432
Cdd:PRK07229 292 VLIGSCTNSSYEDLMRAASILK---GKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGM----G 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 433 IKKGEKNTIVTSYNRNFTGRNdANPETHAFVTSPEIVTALAIAGTLKfNPETdfLTGKDGKKFKLEAPDadelpraEFDP 512
Cdd:PRK07229 365 QAPATGNVSLRTFNRNFPGRS-GTKDAQVYLASPETAAASALTGVIT-DPRT--LALENGEYPKLEEPE-------GFAV 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 513 GQDTYQHPPKDSSGQRVDVSPTSQRLQLLEPFDkwdgkDLEDLQILIKVKGKCTTDHISAAGP-WLKFRGHLDNISNNLL 591
Cdd:PRK07229 434 DDAGIIAPAEDGSDVEVVRGPNIKPLPLLEPLP-----DLLEGKVLLKVGDNITTDHIMPAGAkWLPYRSNIPNISEFVF 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 592 IGAINSENRKAnsvrnavtQEFGPvpdtaryykqhgirWVVIGDENYGEGSSREHSALEPRFLGGRAIITKSFARIHETN 671
Cdd:PRK07229 509 EGVDNTFPERA--------KEQGG--------------GIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKAN 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 672 LKKQGLLPLTFADPADYNKIHPVDKLTIQGLKDFAPGKPLTCIIKHPNgtqETILLNHTFNETQIEWFRAGSALNRMKEL 751
Cdd:PRK07229 567 LINFGILPLTFADPADYDKIEEGDVLEIEDLREFLPGGPLTVVNVTKD---EEIEVRHTLSERQIEILLAGGALNLIKKK 643
|
...
gi 157829965 752 QQK 754
Cdd:PRK07229 644 LAA 646
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
68-478 |
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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 68 RVAMQDATAQMAMLQFISSGLPKVAVPSTIHCDHLIEAQLGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIH 147
Cdd:cd01584 1 RVAMQDATAQMALLQFMSSGLPKVAVPSTIHCDHLIEAQVGGEKDLKRAKDINKEVYDFLASAGAKYGIGFWKPGSGIIH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 148 QIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGI 227
Cdd:cd01584 81 QIVLENYAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 228 LTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFK-DHLVPDSGCH 306
Cdd:cd01584 161 LTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEIADLADEFKdDLLVADEGAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 307 YDQLIEINLSELKPHINGPFTPDLAHPVAEVGSVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQ 386
Cdd:cd01584 241 YDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAEKNGWPLDLRVGLIGSCTNSSYEDMGRAASIAKQALAHGLKCKSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 387 FTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSP 466
Cdd:cd01584 321 FTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPATHAFVASP 400
|
410
....*....|..
gi 157829965 467 EIVTALAIAGTL 478
Cdd:cd01584 401 EIVTAMAIAGTL 412
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
11-748 |
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: 740.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 11 EPHEYIRYDLLEKNIDIVRKrlnrpLTLSEKIVYGHLD---DPAN------------QEIERGKTYLRLRPDRVAMQDAT 75
Cdd:COG1048 16 KPYTYYSLPALEEAGGDISR-----LPYSLKILLENLLrneDGETvteedikalanwLPKARGDDEIPFRPARVLMQDFT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 76 AQMAMLQFISSGLPKV-----------AVPSTIHCDHLIEAQLGG-----EKDLRRAKDINQEVYNFLATAGAKY-GVGF 138
Cdd:COG1048 91 GVPAVVDLAAMRDAVArlggdpkkinpLVPVDLVIDHSVQVDYFGtpdalEKNLELEFERNRERYQFLKWGQQAFdNFRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 139 WRPGSGIIHQIILENYA--------------YPGvLLIGTDSHTPNggglggicigvggA-------------DAVDVMA 191
Cdd:COG1048 171 VPPGTGIVHQVNLEYLAfvvwtreedgetvaYPD-TLVGTDSHTTM-------------InglgvlgwgvggiEAEAAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 192 GIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFP 271
Cdd:COG1048 237 GQPVSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 272 YNHRMKKYLSKTGRADI--------ANLADEFKDHLVPDSgcHYDQLIEINLSELKPHINGPFTPDLAHPVAEVGSVAEK 343
Cdd:COG1048 317 VDEETLDYLRLTGRSEEqielveayAKAQGLWRDPDAPEP--YYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 344 EGWPL-----------------------DIRVGLIGSCTNSSYEDMGRSAA-VAKQALAHGLKCK--SQFTITPGSEQIR 397
Cdd:COG1048 395 ALAAPvgeeldkpvrvevdgeefelghgAVVIAAITSCTNTSNPSVMIAAGlLAKKAVEKGLKVKpwVKTSLAPGSKVVT 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 398 ATIERDGYAQVLRDVGGIVLANACGPCIGQWDR------KDIKKGE-KNTIVTSYNRNFTGRNDaNPETHAFVTSPEIVT 470
Cdd:COG1048 475 DYLERAGLLPYLEALGFNVVGYGCTTCIGNSGPlppeisEAIEENDlVVAAVLSGNRNFEGRIH-PDVKANFLASPPLVV 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 471 ALAIAGTLKFNPETDFL-TGKDGKKFKLEA--PDADELPRAEFD--------------------------PGQDTYQHPP 521
Cdd:COG1048 554 AYALAGTVDIDLTTDPLgTDKDGKPVYLKDiwPSGEEIPAAVFKavtpemfraryadvfdgderwqalevPAGELYDWDP 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 522 KDSSgqrVDVSPTSQRLQLL-EPFdkwdgKDLEDLQILIKVKGKCTTDHISAAGP-----------------------WL 577
Cdd:COG1048 634 DSTY---IRRPPFFEGLQLEpEPF-----KDIKGARVLAKLGDSITTDHISPAGAikadspagryllehgvepkdfnsYG 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 578 KFRGHLDNISNNLLIGA--INS--ENRKANSVRNAVTQEFGPVPDTARYYKQHGIRWVVIGDENYGEGSSREHSALEPRF 653
Cdd:COG1048 706 SRRGNHEVMMRGTFANIriKNLlaPGTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRL 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 654 LGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNK--IHPVDKLTIQGLKD-FAPGKPLTCIIKHPNGTQETILLNHT 730
Cdd:COG1048 786 LGVKAVIAESFERIHRSNLVGMGVLPLQFPEGESAESlgLTGDETFDIEGLDEgLAPGKTVTVTATRADGSTEEFPVLHR 865
|
890
....*....|....*....
gi 157829965 731 F-NETQIEWFRAGSALNRM 748
Cdd:COG1048 866 IdTPVEVEYYRAGGILQYV 884
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
40-476 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 558.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 40 EKIVYGHLDDPANQEIERgktylrlRPDRVAMQDATAQMAMLQFISSGLPK-----------VAVPSTIHCDHlieAQLG 108
Cdd:pfam00330 1 EKIWDAHLVEELDGSLLY-------IPDRVLMHDVTSPQAFVDLRAAGRAVrrpggtpatidHLVPTDLVIDH---APDA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 109 GEKDLRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIHQIILEN-YAYPGVLLIGTDSHTPNggglggicigvggA--- 184
Cdd:pfam00330 71 LDKNIEDEISRNKEQYDFLEWNAKKFGIRFVPPGQGIVHQVGLEYgLALPGMTIVGTDSHTTT-------------Hggl 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 185 ----------DAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMA 254
Cdd:pfam00330 138 galafgvggsEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 255 TICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFK----DHLVPDSGCHYDQLIEINLSELKPHINGPFTPDL 330
Cdd:pfam00330 218 TICNMAIEYGATAGLFPPDETTFEYLRATGRPEAPKGEAYDKavawKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 331 AHPVAEVGSVAEKE------------------GWPL---DIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKS--QF 387
Cdd:pfam00330 298 AVPLSELVPDPFADavkrkaaeraleymglgpGTPLsdgKVDIAFIGSCTNSSIEDLRAAAGLLKKAVEKGLKVAPgvKA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 388 TITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGQWDRKDikkgEKNTIVTSYNRNFTGRNdaNPETHAFVTSPE 467
Cdd:pfam00330 378 SVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLP----PGERCVSSSNRNFEGRQ--GPGGRTHLASPA 451
|
....*....
gi 157829965 468 IVTALAIAG 476
Cdd:pfam00330 452 LVAAAAIAG 460
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
68-478 |
3.36e-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: 499.72 E-value: 3.36e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 68 RVAMQDATAQMAMLQFISSGLP-KVAVPSTIHCDHLIEAQLggekdlrrAKDINQEVYNFLATAGAKYGVGFWRPGSGII 146
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAALgKVADPSQIACVHDHAVQL--------EKPVNNEGHKFLSFFAALQGIAFYRPGVGII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 147 HQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAG 226
Cdd:cd01351 73 HQIMVENLALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 227 ILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFKDHLVPDSGCH 306
Cdd:cd01351 153 IVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWLAFPEELLADEGAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 307 YDQLIEINLSELKPHINGPFTPDLAHPVAEVGSvaekegwpLDIRVGLIGSCTNSSYEDMGRSAAVAKQALahgLKCKSQ 386
Cdd:cd01351 233 YDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG--------TKIDQVLIGSCTNNRYSDMLAAAKLLKGAK---VAPGVR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 387 FTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGQWDRkdiKKGEKNTIVTSYNRNFTGRNDANPEtHAFVTSP 466
Cdd:cd01351 302 LIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGAR---LVADGEVGVSSGNRNFPGRLGTYER-HVYLASP 377
|
410
....*....|..
gi 157829965 467 EIVTALAIAGTL 478
Cdd:cd01351 378 ELAAATAIAGKI 389
|
|
| acon_putative |
TIGR01342 |
aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins ... |
37-754 |
2.56e-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: 386.26 E-value: 2.56e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 37 TLSEKIVYGHLddpANQEIERGKTyLRLRPDRVAMQDATAQMAMLQFISSGLPKVAVP-STIHCDHLIEaqlggEKDLRR 115
Cdd:TIGR01342 1 TLAEKIIDDHL---VEGDLEPGEE-IAIEIDQTLSQDATGTMCWLEFEALEMDEVKTElAAQYCDHNML-----QFDFKN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 116 AKDinqevYNFLATAGAKYGVGFWRPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPW 195
Cdd:TIGR01342 72 ADD-----HKFLMSAAGKFGAWFSKPGNGICHNVHKENFAAPGKTLLGSDSHTPTAGGLGMLAIGAGGIDIAAAMAGEAF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 196 ELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHR 275
Cdd:TIGR01342 147 YLEMPEIVGVHLEGELPEWATAKDIILELLRRLSVKGGLGKIFEYFGEGVEELSVPERATITNMGAELGATSSIFPSDDI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 276 MKKYLSKTGRADianladEFKDhLVPDSGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVgsvaekEGWPLDIRVglI 355
Cdd:TIGR01342 227 TEAWLAAFDRED------DFVD-LLADADAEYADEIEIDLSDLEPLIAEPHMPDNVVPVREI------AGIEVDQVM--I 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 356 GSCTNSSYEDMGRSAAVAKQALAHGlkcKSQFTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGQwdrkDIKK 435
Cdd:TIGR01342 292 GSCTNGAFEDLLPAAKLLEGREVHK---DTEFAVAPGSKQALELIAQEGALAEFLAAGANFLEAACGACIGI----GFAP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 436 GEKNTIVTSYNRNFTGRNdANPETHAFVTSPEIVTALAIAGTLkFNPETdfLTGKDGKkfkLEAPDAdELPrAEFDPGQD 515
Cdd:TIGR01342 365 ASDGVSLRSFNRNFEGRA-GIEDAKVYLASPETATAAAIAGEI-IDPRD--LADDEGD---LEAIGF-EMG-EKFPGGYD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 516 ---TYQHPPKDSSGQRVDVSPTSQRLQLLEPFdkwdGKDLEDlQILIKVKGKCTTDHISAAGP-WLKFRGHLDNISNNLL 591
Cdd:TIGR01342 436 aadIDIIPKEEREDDDIIKGPNIKPLPEFDPL----GADIEG-ETALIMEDNITTDHIIPAGAdILKFRSNIEAISEFTL 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 592 igainsenrkansvrNAVTQEFGPvpdTARYYKQHGIRWVVIGDENYGEGSSREHSALEPRFLGGRAIITKSFARIHETN 671
Cdd:TIGR01342 511 ---------------HRIDDEFAE---RAKAADEKGKAGIIIAGENYGQGSSREHAALAPMFLGVEAVIAKSFARIHHAN 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 672 LKKQGLLPLTFADPADYNKIHPVDKLTIQG--LKDFAPGKPLTCIIKHpngTQETILLNHTFNETQIEWFRAGSALNRMK 749
Cdd:TIGR01342 573 LFNFGILPLEFDNEEDYAKFELGDDIEIPDdlAAALADGEDEFTINKN---DDEEALATLDASEREKEILAAGGKLNLIK 649
|
....*
gi 157829965 750 ELQQK 754
Cdd:TIGR01342 650 NKHRE 654
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
67-478 |
7.35e-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: 334.03 E-value: 7.35e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 67 DRVAMQDATAQMAMLQFISSGLPKVAVP-STIHCDHLIeAQLGGEkdlrrakdiNQEVYNFLATAGAKYGVGFWRPGSGI 145
Cdd:cd01585 1 DQTLTQDATGTMAYLQFEAMGVDRVRTElSVSYVDHNT-LQTDFE---------NADDHRFLQTVAARYGIYFSRPGNGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 146 IHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVA 225
Cdd:cd01585 71 CHQVHLERFAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 226 GILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRadianlADEFKDhLVPDSGC 305
Cdd:cd01585 151 RRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGR------EDDWVE-LAADADA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 306 HYDQLIEINLSELKPHINGPFTPDLAHPVAEVGsvaekegwPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGlkcKS 385
Cdd:cd01585 224 EYDEEIEIDLSELEPLIARPHSPDNVVPVREVA--------GIKVDQVAIGSCTNSSYEDLMTVAAILKGRRVHP---HV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 386 QFTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGQWDrkdiKKGEKNTIVTSYNRNFTGRNdANPETHAFVTS 465
Cdd:cd01585 293 SMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQ----APPTGGVSVRTFNRNFEGRS-GTKDDLVYLAS 367
|
410
....*....|...
gi 157829965 466 PEIVTALAIAGTL 478
Cdd:cd01585 368 PEVAAAAALTGVI 380
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
560-708 |
1.29e-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: 324.42 E-value: 1.29e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 560 KVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINSENRKANSVRNAVTQEFGPVPDTARYYKQHGIRWVVIGDENYG 639
Cdd:cd01578 1 KAKGKCTTDHISAAGPWLKYRGHLDNISNNLLIGAINAENGKANSVKNQVTGEYGPVPDTARDYKAHGIKWVVIGDENYG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157829965 640 EGSSREHSALEPRFLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQGLKDFAPG 708
Cdd:cd01578 81 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYDKIHPDDKVDILGLTDFAPG 149
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
35-478 |
2.51e-76 |
|
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: 252.26 E-value: 2.51e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 35 PLTLSEKIvyghLDDPANQEIERGKTYLrLRPDRVAMQDATAQMAMLQFISSGLPKVAVPSTIH--CDHLIEAqlggeKD 112
Cdd:COG0065 2 GMTLAEKI----LARHAGREVEPGEIVL-LYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVavFDHNVPT-----KD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 113 LRRAKDINQevynfLATAGAKYGVGFWRPGS-GIIHQIILEN-YAYPGVLLIGTDSHTPNGGglggicigvggA------ 184
Cdd:COG0065 72 PKSAEQVKT-----LREFAKEFGITFFDVGDpGICHVVLPEQgLVLPGMTIVGGDSHTCTHG-----------Afgafaf 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 185 -----DAVDVMA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICN 258
Cdd:COG0065 136 gigttDVAHVLAtGTLW-FKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCN 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 259 MGAEIGATTSVFPYNHRMKKYLSKTGRADIANLAdefkdhlvPDSGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVG 338
Cdd:COG0065 215 MAIEAGAKAGIIAPDETTFEYLKGRPFAPWRTLK--------SDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 339 SVaekegwPLDirVGLIGSCTNSSYEDMGRSAAVAKqalahGLKCKS--QFTITPGSEQIRATIERDGYAQVLRDVGGIV 416
Cdd:COG0065 287 GI------KID--QVFIGSCTNGRIEDLRAAAEILK-----GRKVAPgvRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEW 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157829965 417 LANACGPCIG-QWDRkdIKKGEKnTIVTSyNRNFTGRNdANPETHAFVTSPEIVTALAIAGTL 478
Cdd:COG0065 354 REPGCGMCLGmNMGV--LAPGER-CASTS-NRNFEGRM-GSPGSRTYLASPATAAASAIAGRI 411
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
65-753 |
1.00e-75 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 262.56 E-value: 1.00e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 65 RPDRVAMQDATAQ------MAMLQFISS--GLPKV---AVPSTIHCDHLIEAQLGGEKD-LRRAKDI----NQEVYNFLA 128
Cdd:PRK12881 82 VPARVVMQDFTGVpalvdlAAMRDAAAEagGDPAKinpLVPVDLVVDHSVAVDYFGQKDaLDLNMKIefqrNAERYQFLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 129 -TAGAKYGVGFWRPGSGIIHQIILE--------------NYAYPGVLlIGTDSHTP--NGGGLGGICIGVGGADAVdvMA 191
Cdd:PRK12881 162 wGMQAFDNFRVVPPGTGIMHQVNLEylarvvhtkeddgdTVAYPDTL-VGTDSHTTmiNGIGVLGWGVGGIEAEAV--ML 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 192 GIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFP 271
Cdd:PRK12881 239 GQPVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFP 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 272 YNHRMKKYLSKTGRAD--IANLADEFKDH---LVPDSGCHYDQLIEINLSELKPHINGP---------------FTPDLA 331
Cdd:PRK12881 319 VDEQTLDYLRLTGRTEaqIALVEAYAKAQglwGDPKAEPRYTRTLELDLSTVAPSLAGPkrpqdrialgnvksaFSDLFS 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 332 HPVAEVG-SVAEKEGWPLDIRVG-----LIGSCTNSSYEDMGRSAA-VAKQALAHGLKCKS--QFTITPGSEQIRATIER 402
Cdd:PRK12881 399 KPVAENGfAKKAQTSNGVDLPDGavaiaAITSCTNTSNPSVLIAAGlLAKKAVERGLTVKPwvKTSLAPGSKVVTEYLER 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 403 DGYAQVLRDVG-GIVlANACGPCIGQWD------RKDIKKGE-KNTIVTSYNRNFTGRNDANPEThAFVTSPEIVTALAI 474
Cdd:PRK12881 479 AGLLPYLEKLGfGIV-GYGCTTCIGNSGpltpeiEQAITKNDlVAAAVLSGNRNFEGRIHPNIKA-NFLASPPLVVAYAL 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 475 AGTLKFNPETDFL-TGKDGKKFKLE-----APDADELPRAEFDPgqDTYQH---PPKDSSGQRVDVS-PTSQRLQ----- 539
Cdd:PRK12881 557 AGTVRRDLMTEPLgKGKDGRPVYLKdiwpsSAEIDALVAFAVDP--EDFRKnyaEVFKGSELWAAIEaPDGPLYDwdpks 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 540 --LLEP--FDKWDG-----KDLEDLQILIKVKGKCTTDHIS---------AAGPWLKFRGHLDNISN------------- 588
Cdd:PRK12881 635 tyIRRPpfFDFSMGpaasiATVKGARPLAVLGDSITTDHISpagaikadsPAGKYLKENGVPKADFNsygsrrgnhevmm 714
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 589 ----------NLLIGAInsenrKANSVRNAVTQEFGPVPDTARYYKQHGIRWVVIGDENYGEGSSREHSALEPRFLGGRA 658
Cdd:PRK12881 715 rgtfanvrikNLMIPGK-----EGGLTLHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGVKA 789
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 659 IITKSFARIHETNLKKQGLLPLTF--ADPADYNKIHPVDKLTIQGL-KDFAPGKPLTCIIKHPNGTQETILLNHTFnETQ 735
Cdd:PRK12881 790 VIAESFERIHRSNLVGMGVLPLQFkgGDSRQSLGLTGGETFDIEGLpGEIKPRQDVTLVIHRADGSTERVPVLCRI-DTP 868
|
810 820
....*....|....*....|
gi 157829965 736 IE--WFRAGSALNRMkeLQQ 753
Cdd:PRK12881 869 IEvdYYKAGGILPYV--LRQ 886
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
65-747 |
1.35e-72 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 253.89 E-value: 1.35e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 65 RPDRVAMQDAT--------AQM--AMLQF------ISsglPKVAVPSTIhcDHLIEAQLGGEKD-LRRAKDI----NQEV 123
Cdd:PRK09277 83 RPARVVMQDFTgvpavvdlAAMrdAIADLggdpakIN---PLVPVDLVI--DHSVQVDYFGTPDaFEKNVELeferNEER 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 124 YNFLatagaKYGVGFWR------PGSGIIHQIILE-------------NYAYPGVLlIGTDSHTPnggglggicigvgga 184
Cdd:PRK09277 158 YQFL-----KWGQKAFDnfrvvpPGTGICHQVNLEylapvvwtredgeLVAYPDTL-VGTDSHTT--------------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 185 dAVD----------------VMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSI 248
Cdd:PRK09277 217 -MINglgvlgwgvggieaeaAMLGQPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 249 SCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRAD--IAnladefkdhLV------------PDSGCHYDQLIEIN 314
Cdd:PRK09277 296 SLADRATIANMAPEYGATCGFFPIDEETLDYLRLTGRDEeqVA---------LVeayakaqglwrdPLEEPVYTDVLELD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 315 LSELKPHINGP-------FTPDLAHPVAEV--------GSVAEKEGWPLDIRVG-----LIGSCTNSS--YEDMGrsAA- 371
Cdd:PRK09277 367 LSTVEPSLAGPkrpqdriPLSDVKEAFAKSaelgvqgfGLDEAEEGEDYELPDGavviaAITSCTNTSnpSVMIA--AGl 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 372 VAKQALAHGLKCKS--QFTITPGSEQIRATIERDGYAQVLRDVG-GIVlANACGPCIG---------QwdrKDIKkgEKN 439
Cdd:PRK09277 445 LAKKAVEKGLKVKPwvKTSLAPGSKVVTDYLEKAGLLPYLEALGfNLV-GYGCTTCIGnsgplppeiE---KAIN--DND 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 440 TIVT---SYNRNFTGRndANPETHA-FVTSPEIVTALAIAGTLKFNPETDFL-TGKDGKKFKLEA--PDADE-------- 504
Cdd:PRK09277 519 LVVTavlSGNRNFEGR--IHPLVKAnYLASPPLVVAYALAGTVDIDLEKDPLgTDKDGNPVYLKDiwPSDEEidavvaka 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 505 ----LPRAEFDP---GQDTYQHPPKdSSGQRVDVSPTSQRLQlLEPFdkWDG--------KDLEDLQILIKVKGKCTTDH 569
Cdd:PRK09277 597 vkpeMFRKEYADvfeGDERWNAIEV-PEGPLYDWDPDSTYIR-NPPY--FEGmlaepgpvRDIKGARVLALLGDSITTDH 672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 570 IS---------AAGPWLK--------F--------------RGHLDNIS-NNLLIgainseNRKANSV-RNAVTQEFGPV 616
Cdd:PRK09277 673 ISpagaikadsPAGKYLLehgvepkdFnsygsrrgnhevmmRGTFANIRiRNEMV------PGVEGGYtRHFPEGEVMSI 746
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 617 PDTARYYKQHGIRWVVIGDENYGEGSSREHSALEPRFLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYN--KIHPV 694
Cdd:PRK09277 747 YDAAMKYKEEGTPLVVIAGKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKPGESRKtlGLDGT 826
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 157829965 695 DKLTIQGLKDFAPGKPLTCIIKHPNGTQETI-LLNHTFNETQIEWFRAGSALNR 747
Cdd:PRK09277 827 ETFDIEGLEDLKPGATVTVVITRADGEVVEFpVLCRIDTAVEVDYYRNGGILQY 880
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
35-476 |
3.21e-68 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 230.83 E-value: 3.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 35 PLTLSEKIVYGHlddpANQEIERGKtYLRLRPDRVAMQDATAQMAMLQFISSGLPKVAVPSTIH--CDHLIEAqlggeKD 112
Cdd:PRK00402 2 GMTLAEKILARH----SGRDVSPGD-IVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVivFDHFVPA-----KD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 113 LRRAKdINQEVYNFLATAGAKYgvgFWRPGSGIIHQIILEN-YAYPGVLLIGTDSHTPNggglggicigvggADAV---- 187
Cdd:PRK00402 72 IKSAE-QQKILREFAKEQGIPN---FFDVGEGICHQVLPEKgLVRPGDVVVGADSHTCT-------------YGALgafa 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 188 ------D---VMA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATIC 257
Cdd:PRK00402 135 tgmgstDmaaAMAtGKTW-FKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 258 NMGAEIGATTSVFPYNHRMKKYLSKTGRADIanladefkDHLVPDSGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEV 337
Cdd:PRK00402 214 NMAIEAGAKAGIFAPDEKTLEYLKERAGRDY--------KPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 338 gsvaekEGWPLDIRVglIGSCTNSSYEDMGRSAAVAKqalAHGLKCKSQFTITPGSEQIRATIERDGYAQVLRDVGGIVL 417
Cdd:PRK00402 286 ------EGTKVDQVF--IGSCTNGRLEDLRIAAEILK---GRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVS 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 157829965 418 ANACGPCIGqwdrkdIKKGEknTIVTSYNRNFTGRNdANPETHAFVTSPEIVTALAIAG 476
Cdd:PRK00402 355 TPTCGPCLGghm-gvLAPGE--VCLSTTNRNFKGRM-GSPESEVYLASPAVAAASAVTG 409
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
68-476 |
6.16e-66 |
|
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate; Aconatase-like catalytic domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes.
Pssm-ID: 153133 Cd Length: 382 Bit Score: 223.61 E-value: 6.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 68 RVAMQDATAQMAMLQFISSGLPKVAVPSTIHC--DHLIEAqlggekDLRRAKDINQEVYNFLATAGAK-YGVGfwrpGSG 144
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAvfDHNVPT------PDIKAAEQVKTLRKFAKEFGINfFDVG----RQG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 145 IIHQIILENY-AYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVIL 222
Cdd:cd01583 71 ICHVILPEKGlTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLAtGKLW-FRVPETMRVNVEGKLPPGVTAKDVIL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 223 KVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRAdianladEFKdHLVPD 302
Cdd:cd01583 150 YIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKA-------YWK-ELKSD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 303 SGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVgsvaekEGWPLDIRVglIGSCTNSSYEDMGRSAAVAKqalAHGLK 382
Cdd:cd01583 222 EDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEV------EGIKIDQVF--IGSCTNGRLEDLRAAAEILK---GRKVA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 383 CKSQFTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIG-QWDRkdIKKGEknTIVTSYNRNFTGR-NDANPETH 460
Cdd:cd01583 291 DGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGgHMGV--LAPGE--RCVSTSNRNFKGRmGSPGARIY 366
|
410
....*....|....*.
gi 157829965 461 afVTSPEIVTALAIAG 476
Cdd:cd01583 367 --LASPATAAASAITG 380
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
67-746 |
1.63e-62 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 225.66 E-value: 1.63e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 67 DRVAMQDAtaqMAML----QFISsglPKVAVPSTIhcDHLIEAQLGGEKD-LRRAKDI----NQEVYNFLatagaKYGVG 137
Cdd:PTZ00092 106 DLAAMRDA---MKRLggdpAKIN---PLVPVDLVI--DHSVQVDFSRSPDaLELNQEIeferNLERFEFL-----KWGSK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 138 FWR------PGSGIIHQIILE----------NYAYPGVLlIGTDSHTP--NGGGLGGICIGVGGADAVdvMAGIPWELKC 199
Cdd:PTZ00092 173 AFKnllivpPGSGIVHQVNLEylarvvfnkdGLLYPDSV-VGTDSHTTmiNGLGVLGWGVGGIEAEAV--MLGQPISMVL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 200 PKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKY 279
Cdd:PTZ00092 250 PEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDY 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 280 LSKTGRAD-----IANLADEFKDHLVPDSGCHYDQLIEINLSELKPHINGP---------------FTPDLAHPVAEVG- 338
Cdd:PTZ00092 330 LKQTGRSEekvelIEKYLKANGLFRTYAEQIEYSDVLELDLSTVVPSVAGPkrphdrvplsdlkkdFTACLSAPVGFKGf 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 339 SVAEKE----------GWPLDIRVG-----LIGSCTNSSYED-MGRSAAVAKQALAHGLKCKS--QFTITPGSEQIRATI 400
Cdd:PTZ00092 410 GIPEEKhekkvkftykGKEYTLTHGsvviaAITSCTNTSNPSvMLAAGLLAKKAVEKGLKVPPyiKTSLSPGSKVVTKYL 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 401 ERDGYAQVLRDVGGIVLANACGPCIGqwDRKDIKKGEKNTI---------VTSYNRNFTGRndANPETHA-FVTSPEIVT 470
Cdd:PTZ00092 490 EASGLLKYLEKLGFYTAGYGCMTCIG--NSGDLDPEVSEAItnndlvaaaVLSGNRNFEGR--VHPLTRAnYLASPPLVV 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 471 ALAIAGTLKFNPETDFL-TGKDGKKFKLEA--PDADEL--------------------------------PRAEF---DP 512
Cdd:PTZ00092 566 AYALAGRVNIDFETEPLgSDKTGKPVFLRDiwPSREEIqaleakyvkpemfkevysnitqgnkqwnelqvPKGKLyewDE 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 513 gQDTYQHPPKDSSGQRVDVSPTsqrlqllepfdkwdgKDLEDLQILIKVKGKCTTDHISAAG------PWLKF------- 579
Cdd:PTZ00092 646 -KSTYIHNPPFFQTMELEPPPI---------------KSIENAYCLLNLGDSITTDHISPAGniaknsPAAKYlmergve 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 580 ------------------RGHLDNIS-NNLLIGainseNRKANSVrNAVTQEFGPVPDTARYYKQHGIRWVVIGDENYGE 640
Cdd:PTZ00092 710 rkdfntygarrgndevmvRGTFANIRlINKLCG-----KVGPNTV-HVPTGEKMSIYDAAEKYKQEGVPLIVLAGKEYGS 783
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 641 GSSREHSALEPRFLGGRAIITKSFARIHETNLKKQGLLPLTFAD--PADYNKIHPVDKLTIQGLK-DFAPGKPLTciIKH 717
Cdd:PTZ00092 784 GSSRDWAAKGPYLQGVKAVIAESFERIHRSNLVGMGILPLQFLNgeNADSLGLTGKEQFSIDLNSgELKPGQDVT--VKT 861
|
810 820 830
....*....|....*....|....*....|
gi 157829965 718 PNG-TQETILLNHTfnETQIEWFRAGSALN 746
Cdd:PTZ00092 862 DTGkTFDTILRIDT--EVEVEYFKHGGILQ 889
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
555-685 |
2.69e-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: 201.83 E-value: 2.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 555 LQILIKVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINSENRKANSVRNAVTQEFGPVPDTARYYKQHGIRWVVIG 634
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 157829965 635 DENYGEGSSREHSALEPRFLGGRAIITKSFARIHETNLKKQGLLPLTFADP 685
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
40-745 |
1.48e-58 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 214.67 E-value: 1.48e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 40 EKIVYGHLDDPANQEIErgktylrLRPDRVAMQDAT--------AQM--AMLQFIS-SGLPKVAVPSTIHCDHLIEAQLG 108
Cdd:PLN00070 103 EKIIDWENTSPKQVEIP-------FKPARVLLQDFTgvpavvdlACMrdAMNNLGGdPNKINPLVPVDLVIDHSVQVDVA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 109 GEKDLRRAK-----DINQEVYNFLatagaKYGVGFWR------PGSGIIHQIILENYA----------YPGVLlIGTDSH 167
Cdd:PLN00070 176 RSENAVQANmelefQRNKERFAFL-----KWGSTAFQnmlvvpPGSGIVHQVNLEYLGrvvfntdgilYPDSV-VGTDSH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 168 TPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDS 247
Cdd:PLN00070 250 TTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSE 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 248 ISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRAD----------IANlaDEFKDHLVPDSGCHYDQLIEINLSE 317
Cdd:PLN00070 330 LSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDetvamieaylRAN--KMFVDYNEPQQERVYSSYLELDLED 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 318 LKPHINGPFTPD---------------LAHPVAEVGSVAEKE-----------GWPLDIRVG-----LIGSCTNSSYED- 365
Cdd:PLN00070 408 VEPCISGPKRPHdrvplkemkadwhscLDNKVGFKGFAVPKEaqskvakfsfhGQPAELRHGsvviaAITSCTNTSNPSv 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 366 MGRSAAVAKQALAHGLKCKS--QFTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGqwDRKDIKKGEKNTI-- 441
Cdd:PLN00070 488 MLGAGLVAKKACELGLEVKPwiKTSLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIG--NSGELDESVASAIte 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 442 -------VTSYNRNFTGRndANPETHA-FVTSPEIVTALAIAGTLKFNPETDFL-TGKDGKK--FKLEAPDADELPRAEF 510
Cdd:PLN00070 566 ndivaaaVLSGNRNFEGR--VHPLTRAnYLASPPLVVAYALAGTVDIDFEKEPIgTGKDGKDvfFRDIWPSNEEVAEVVQ 643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 511 -----DPGQDTYQHPPKDS---------SGQRVDVSPTSQRLQllEP-------FDKWDGKDLEDLQILIKVKGKCTTDH 569
Cdd:PLN00070 644 ssvlpDMFKSTYEAITKGNpmwnqlsvpSGTLYSWDPKSTYIH--EPpyfknmtMSPPGPHGVKDAYCLLNFGDSITTDH 721
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 570 ISAAG------PWLKF-------------------------RGHLDNIS--NNLLIGAINSENrkansvRNAVTQEFGPV 616
Cdd:PLN00070 722 ISPAGsihkdsPAAKYlmergvdrkdfnsygsrrgndeimaRGTFANIRivNKLLKGEVGPKT------VHIPTGEKLSV 795
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 617 PDTARYYKQHGIRWVVIGDENYGEGSSREHSALEPRFLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKI----H 692
Cdd:PLN00070 796 FDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLLGVKAVIAKSFERIHRSNLVGMGIIPLCFKSGEDADTLgltgH 875
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 157829965 693 pvDKLTIQ---GLKDFAPGKPLTciIKHPNGTQETILLNHTfNETQIEWFRAGSAL 745
Cdd:PLN00070 876 --ERYTIDlpsNISEIKPGQDVT--VTTDNGKSFTCTLRFD-TEVELAYFDHGGIL 926
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
67-476 |
1.25e-56 |
|
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: 199.21 E-value: 1.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 67 DRVAMQDATAQMAMLQFISSGLPKVAVPSTIHC--DHLIEAqlggekDLRRAKDINQEVYNFLATAGAKYgvgFWRPGSG 144
Cdd:TIGR01343 26 DLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIvfDHQVPA------DTIKAAEMQKLAREFVKKQGIKY---FYDVGEG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 145 IIHQIILEN-YAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVIL 222
Cdd:TIGR01343 97 ICHQVLPEKgLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIAtGKTW-FKVPETIRVNITGKLNPGVTAKDVIL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 223 KVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADianlADEFKDhlvpD 302
Cdd:TIGR01343 176 EVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYLKERRKEP----FRVYKS----D 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 303 SGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVgsvaekEGWPLDiRVgLIGSCTNSSYEDMGRSAAVAKqalAHGLK 382
Cdd:TIGR01343 248 EDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEV------EGTEID-QV-FIGSCTNGRLEDLRVAAKILK---GRKVA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 383 CKSQFTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGqwdRKDIKKGEKNTIVTSYNRNFTGRNdANPETHAF 462
Cdd:TIGR01343 317 PDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLG---SHQGVLAPGEVCISTSNRNFKGRM-GHPNAEIY 392
|
410
....*....|....
gi 157829965 463 VTSPEIVTALAIAG 476
Cdd:TIGR01343 393 LASPATAAASAVKG 406
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
68-477 |
2.52e-46 |
|
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydrolyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes.
Pssm-ID: 153136 Cd Length: 404 Bit Score: 170.18 E-value: 2.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 68 RVAMQDATAQMAMLQFIS--------SGLP-KV--AVPSTIHCDHLIEAQLGG-----EKDLRRAKDINQEVYNFLATAG 131
Cdd:cd01586 1 RVILQDFTGVPAVVDLAAmrdavkrlGGDPeKInpLIPVDLVIDHSVQVDFYGtadalAKNMKLEFERNRERYEFLKWGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 132 AKYG-VGFWRPGSGIIHQIILE--------------NYAYPGVLlIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWE 196
Cdd:cd01586 81 KAFKnLRVVPPGTGIIHQVNLEylarvvftseedgdGVAYPDSV-VGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPIS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 197 LKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPynhrm 276
Cdd:cd01586 160 MLLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFP----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 277 kkylsktgradianladefkdhlvPDSgchydQLIEINLSELKPHINGPFTPDlaHPVAEVGSVAekegwpldirVGLIG 356
Cdd:cd01586 235 ------------------------VDT-----QVVELDLSTVEPSVSGPKRPQ--DRVPLHGSVV----------IAAIT 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 357 SCTNSSYED-MGRSAAVAKQALAHGLKCKS--QFTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIG------Q 427
Cdd:cd01586 274 SCTNTSNPSvMLAAGLLAKKAVELGLKVKPyvKTSLAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGnsgplpE 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 157829965 428 WDRKDIKKGE-KNTIVTSYNRNFTGRndANPETHA-FVTSPEIVTALAIAGT 477
Cdd:cd01586 354 EVEEAIKENDlVVAAVLSGNRNFEGR--IHPLVRAnYLASPPLVVAYALAGT 403
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
81-478 |
3.68e-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: 3.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 81 LQFISSGLPKVAVPSTIHC--DHliEAQLGGEKDLRRAKDINqevyNFlataGAKYGVGFWRPGSGIIHQIILEN-YAYP 157
Cdd:cd01582 13 LKFMSIGATKIHNPDQIVMtlDH--DVQNKSEKNLKKYKNIE----SF----AKKHGIDFYPAGRGIGHQIMIEEgYAFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 158 GVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGA 236
Cdd:cd01582 83 GTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWAtGQTW-WQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLNH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 237 IVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRmkkylsktgradianladefkdHLVpdsgchydqlieINLS 316
Cdd:cd01582 162 AIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAK----------------------HLI------------LDLS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 317 ELKPHINGPFTPDLAHPVAEVgsvaekEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQA--------LAHGLKcksqFT 388
Cdd:cd01582 208 TLSPYVSGPNSVKVSTPLKEL------EAQNIKINKAYLVSCTNSRASDIAAAADVVKGKkekngkipVAPGVE----FY 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 389 ITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGqWDRKDIKKGEKNtiVTSYNRNFTGRNdANPETHAFVTSPEI 468
Cdd:cd01582 278 VAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIG-LGQGLLEPGEVG--ISATNRNFKGRM-GSTEALAYLASPAV 353
|
410
....*....|
gi 157829965 469 VTALAIAGTL 478
Cdd:cd01582 354 VAASAISGKI 363
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
560-701 |
9.09e-31 |
|
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: 115.64 E-value: 9.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 560 KVKGKCTTDHISAAGPWlkfrghldnisnnlligainsenrkansvrnavtqefgpvpdtaryykqhgirwVVIGDENYG 639
Cdd:cd00404 1 KVAGNITTDHISPAGPG------------------------------------------------------VVIGDENYG 26
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157829965 640 EGSSREHSALEPRFLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQG 701
Cdd:cd00404 27 TGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDYLKLHTGDELDIYP 88
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
200-478 |
3.02e-30 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 124.85 E-value: 3.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 200 PKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGA---------TTsvF 270
Cdd:PRK05478 163 PKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGAraglvapdeTT--F 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 271 PYnhrMKkylsktGR--ADIANLADEFKDH---LVPDSGCHYDQLIEINLSELKPH------------INGPF-TPDLAH 332
Cdd:PRK05478 241 EY---LK------GRpfAPKGEDWDKAVAYwktLKSDEDAVFDKVVTLDAADIEPQvtwgtnpgqvisIDGKVpDPEDFA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 333 PVAEVGSVAE-------KEGWPL-DIRVG--LIGSCTNSSYEDMGRSAAVAKqalahGLKCKSQFT--ITPGSEQIRATI 400
Cdd:PRK05478 312 DPVKRASAERalaymglKPGTPItDIKIDkvFIGSCTNSRIEDLRAAAAVVK-----GRKVAPGVRalVVPGSGLVKAQA 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 401 ERDGYAQVLRDVG------GivlanaCGPCIGQWDrkDIKKGEKNTIVTSyNRNFTGRNDANPETHafVTSPEIVTALAI 474
Cdd:PRK05478 387 EAEGLDKIFIEAGfewrepG------CSMCLAMNP--DKLPPGERCASTS-NRNFEGRQGKGGRTH--LVSPAMAAAAAI 455
|
....
gi 157829965 475 AGTL 478
Cdd:PRK05478 456 TGHF 459
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
141-478 |
3.61e-28 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 118.85 E-value: 3.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 141 PGSGIIHQIILE-NYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKD 219
Cdd:PRK12466 105 PRQGIVHVVAPElGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKD 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 220 VILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFKDH- 298
Cdd:PRK12466 185 LILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETTFDYLRGRPRAPKGALWDAALAYw 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 299 --LVPDSGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVGSVAEKE--------------------GWPL-DIRVG-- 353
Cdd:PRK12466 265 rtLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAAEadparraameraldymgltpGTPLaGIPIDrv 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 354 LIGSCTNSSYEDMGRSAAVAKqalahGLKCKSQFT--ITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGQWDRK 431
Cdd:PRK12466 345 FIGSCTNGRIEDLRAAAAVLR-----GRKVAPGVRamVVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDV 419
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 157829965 432 dIKKGEKntIVTSYNRNFTGRNDANPETHafVTSPEIVTALAIAGTL 478
Cdd:PRK12466 420 -LAPGER--CASTTNRNFEGRQGPGARTH--LMSPAMVAAAAVAGHI 461
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
560-701 |
5.61e-28 |
|
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism. This distinct subfamily is found only in bacteria and archea. Its exact characteristics are not known.
Pssm-ID: 238811 [Multi-domain] Cd Length: 121 Bit Score: 109.06 E-value: 5.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 560 KVKGKCTTDHISAAGP-WLKFRGHLDNISNNLLIGainsenrkansvrnaVTQEFgpvPDTARYYKQHgirwVVIGDENY 638
Cdd:cd01579 1 KVGDNITTDHIMPAGAkVLPLRSNIPAISEFVFHR---------------VDPTF---AERAKAAGPG----FIVGGENY 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157829965 639 GEGSSREHSALEPRFLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIQG 701
Cdd:cd01579 59 GQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADEDDYDRFEQGDQLELPL 121
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
62-746 |
1.43e-24 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 109.71 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 62 LRLRPDRVAMQDAT----AQMAmlqfISSGLPKVAVPSTIHCDHLIEAQLGGEkdlrrakdINQEVYNFLATAGAKYGVG 137
Cdd:PRK11413 54 LKIKFDSLASHDITfvgiIQTA----KASGMERFPLPYVLTNCHNSLCAVGGT--------INEDDHVFGLSAAQKYGGI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 138 FWRPGSGIIHQIILENYAYPGVLLIGTDSHTpnggglggicigvgGADAVDVMA---GIP----------WELKCPKVIG 204
Cdd:PRK11413 122 FVPPHIAVIHQYMREMMAGGGKMILGSDSHT--------------RYGALGTMAvgeGGGelvkqllndtYDIDYPGVVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 205 VKLTGSLSGWTSPKDVILKVAGILTVKGGT-GAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKT 283
Cdd:PRK11413 188 VYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLALH 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 284 GRadianlADEFKDhLVPDSGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVGSVA-------EKEGWPLD------- 349
Cdd:PRK11413 268 GR------GQDYCE-LNPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDELNQNLtdilrevEIESERVAhgkakls 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 350 ---------IRV--GLIGSCTNSSYEDMgrsaavakQALAHGLKCKS----QFTIT--PGSEQIRATIERDGYAQVLRDV 412
Cdd:PRK11413 341 lldkiengrLKVqqGIIAGCSGGNYENV--------IAAANALRGQScgndTFSLSvyPSSQPVFMDLAKKGVVADLMGA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 413 GGIVLANACGPCIGQWDrkdikkgekntivTSYN---------RNFTGRNDANPeTHAFVTSPEIVTALAIAGTLKFNpe 483
Cdd:PRK11413 413 GAIIRTAFCGPCFGAGD-------------TPANnglsirhttRNFPNREGSKP-ANGQMSAVALMDARSIAATAANG-- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 484 tDFLTGKDgkkfklEAPDADELPRAEFDPgqDTYQHPPKDSSGQRVdvspTSQRLQLLEPFDKWdgKDLEDL--QILIKV 561
Cdd:PRK11413 477 -GYLTSAT------ELDCWDNVPEYAFDV--TPYKNRVYQGFGKGA----TQQPLIYGPNIKDW--PEMGALtdNILLKV 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 562 KGK-----CTTDHISAAGPWLKFRghldniSNNLLIGAINSENRKANSV-------------RNAVTQEFGPVPDTAR-Y 622
Cdd:PRK11413 542 CSKildpvTTTDELIPSGETSSYR------SNPLGLAEFTLSRRDPGYVgrskavaelenqrLAGNVSELTEVFARIKqI 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 623 YKQHGIRW--VVIGDENY----GEGSSREHSALEPRFLGGRAIITKSFA-RIHETNLKKQGLLPLTFADPadyNKIHPVD 695
Cdd:PRK11413 616 AGQEHIDPlqTEIGSMVYavkpGDGSAREQAASCQRVLGGLANIAEEYAtKRYRSNVINWGMLPFQMAEE---PTFEVGD 692
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 157829965 696 KLTIQGLKDFAPGKPLTC---IIKHPNGTQETILLNHTFNETQIEWFRAGSALN 746
Cdd:PRK11413 693 YIYIPGIRAALDNPGTTFkgyVIHEDAPVTEITLYMESLTAEEREIIKAGCLIN 746
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
566-701 |
1.95e-18 |
|
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238812 [Multi-domain] Cd Length: 171 Bit Score: 83.48 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 566 TTDHISAAGPWLK-------------------------------FRGHLDNISN-NLLIGainseNRKANSVRNAVTQEF 613
Cdd:cd01580 7 TTDHISPAGSIAKdspagkylaergvkprdfnsygsrrgndevmMRGTFANIRLrNKLVP-----GTEGGTTHHPPTGEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 614 GPVPDTARYYKQHGIRWVVIGDENYGEGSSREHSALEPRFLGGRAIITKSFARIHETNLKKQGLLPLTFADP--ADYNKI 691
Cdd:cd01580 82 MSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGenADSLGL 161
|
170
....*....|
gi 157829965 692 HPVDKLTIQG 701
Cdd:cd01580 162 TGEETYDIIG 171
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
620-699 |
3.08e-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: 62.99 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 620 ARYYKQhgirwVVIGDENYGEGSSREHSALEPRFLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYN-KIHPVDKLT 698
Cdd:cd01577 14 ARFLGD-----IIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEvEAKPGDEVE 88
|
.
gi 157829965 699 I 699
Cdd:cd01577 89 V 89
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
135-478 |
1.66e-10 |
|
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle; Aconitase B catalytic domain. Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle. Aconitase has an active (4FE-4S) and an inactive (3FE-4S) form. The active cluster is part of the catalytic site that interconverts citrate, cis-aconitase and isocitrate. The domain architecture of aconitase B is different from other aconitases in that the catalytic domain is normally found at C-terminus for other aconitases, but it is at N-terminus for B family. It also has a HEAT domain before domain 4 which plays a role in protein-protein interaction. This alignment is the core domain including domains 1,2 and 3.
Pssm-ID: 153131 Cd Length: 436 Bit Score: 64.06 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 135 GVGFWRPGSGIIHQIiLENYAYPGVLLIGTDSHT--PNGGGLGGICIGVGGADAVDVMAgipweLKCPKVIGVKLTGSLS 212
Cdd:cd01581 85 GGVALRPGDGVIHSW-LNRMLLPDTVGTGGDSHTrfPIGISFPAGSGLVAFAAATGVMP-----LDMPESVLVRFKGKMQ 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 213 GWTSPKDVILKV------AGILTV--KGG----TGAIVEYHGpgVDSISCTGMATICNMGAEIGATTSVFPYNH------ 274
Cdd:cd01581 159 PGITLRDLVNAIpyyaiqQGLLTVekKGKknvfNGRILEIEG--LPDLKVEQAFELTDASAERSAAACTVRLDKepviey 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 275 ------RMKKYLSKtGRADIANLADEFKDH---------LVPDSGCHYDQLIEINLSELK-PHINGPFTPDlahpvaEVG 338
Cdd:cd01581 237 lesnvvLMKIMIAN-GYDDARTLLRRIIAMeewlanpplLEPDADAEYAAVIEIDLDDIKePILACPNDPD------DVK 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 339 SVAEKEGWPLDIrvGLIGSC-TNssyedMGRSAAVAKQALAHGLKcKSQFTITPGSEQIRATIERDGYAQVLRDVGGIVL 417
Cdd:cd01581 310 LLSEVAGKKIDE--VFIGSCmTN-----IGHFRAAAKILRGKEFK-PTRLWVAPPTRMDWAILQEEGYYSIFGDAGARTE 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157829965 418 ANACGPCIGQWDRkdIKKGEknTIVTSYNRNFTGR--NDANpethAFVTSPEIVTALAIAGTL 478
Cdd:cd01581 382 MPGCSLCMGNQAR--VADGA--TVFSTSTRNFDNRvgKGAE----VYLGSAELAAVCALLGRI 436
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
125-478 |
2.12e-09 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 61.09 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 125 NFLATAGakyGVGFwRPGSGIIHQiILENYAYPGVLLIGTDSHT--PNGGGLGGICIGVGGADAVDVMAgipweLKCPKV 202
Cdd:PLN00094 525 DFIRNRG---GVSL-RPGDGVIHS-WLNRMLLPDTVGTGGDSHTrfPIGISFPAGSGLVAFGAATGVIP-----LDMPES 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 203 IGVKLTGSLSGWTSPKDVILKV------AGILTV-KGG-----TGAIVEYHgpGVDSISCTGMATICNMGAEIGAT---- 266
Cdd:PLN00094 595 VLVRFTGTMQPGITLRDLVHAIpytaiqDGLLTVeKKGkknvfSGRILEIE--GLPHLKCEQAFELSDASAERSAAgcti 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 267 ----TSVFPY---NHRMKKYLSKTGRAD-------IANLADEFKD-HLV-PDSGCHYDQLIEINLSELK-PHINGPFTPD 329
Cdd:PLN00094 673 kldkEPIIEYlnsNVVMLKWMIAEGYGDrrtlerrIARMQQWLADpELLeADPDAEYAAVIEIDMDEIKePILCAPNDPD 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 330 LAHPVAEVgsVAEKegwpldIRVGLIGSC-TNssyedMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIERDGYAQV 408
Cdd:PLN00094 753 DARLLSEV--TGDK------IDEVFIGSCmTN-----IGHFRAAGKLLNDNLSQLPTRLWVAPPTKMDEAQLKAEGYYST 819
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157829965 409 LRDVGGIVLANACGPCIGQWDRkdikKGEKNTIVTSYNRNFTGR--NDANpethAFVTSPEIVTALAIAGTL 478
Cdd:PLN00094 820 FGTVGARTEMPGCSLCMGNQAR----VAEKSTVVSTSTRNFPNRlgKGAN----VYLASAELAAVAAILGRL 883
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
631-724 |
5.95e-09 |
|
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: 56.33 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 631 VVIGDENYGEGSSREHSALEPRFLGGRAIITKSFARIHETNLKKQGLLPLTfADPADynkihpVDKLTIQGLKDfaPGKP 710
Cdd:COG0066 67 ILVAGRNFGCGSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIE-LPEEA------VDALFAAIEAN--PGDE 137
|
90
....*....|....*....
gi 157829965 711 LT-----CIIKHPNGTQET 724
Cdd:COG0066 138 LTvdleaGTVTNGTGETYP 156
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
617-687 |
5.77e-08 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 52.88 E-value: 5.77e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157829965 617 PDTARYYKQHGIrwvVIGDENYGEGSSREHSALEPRFLGGRAIITKSFARIHETNLKKQGLLPLTFADPAD 687
Cdd:PRK14023 41 PEFASTVRPGDI---LVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPPFESEEVVD 108
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
631-699 |
1.62e-07 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 51.37 E-value: 1.62e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157829965 631 VVIGDENYGEGSSREHSALEPRFLGGRAIITKSFARIHETNLKKQGLLPLTFADPADynKIHPVDKLTI 699
Cdd:PRK00439 51 IIVAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIGLPVLECDEAVD--KIEDGDEVEV 117
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
299-478 |
1.33e-06 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 52.10 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 299 LVPDSGCHYDQLIEINLSELK-PHINGPFTPDLAHPVAEVGsvAEKegwpldIRVGLIGSC-TNssyedMGRSAAVAKQA 376
Cdd:PRK09238 647 LEADADAEYAAVIEIDLAEIKePILACPNDPDDVRLLSEVA--GTK------IDEVFIGSCmTN-----IGHFRAAGKLL 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 377 LAHGLKCKSQFTITPGSEQIRATIERDGYAQVLRDVGGIVLANACGPCIGQWDRkdIKKGEknTIVTSYNRNFTGR--ND 454
Cdd:PRK09238 714 EGKKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMGNQAR--VADGA--TVFSTSTRNFPNRlgKG 789
|
170 180
....*....|....*....|....
gi 157829965 455 ANpethAFVTSPEIVTALAIAGTL 478
Cdd:PRK09238 790 AN----VYLGSAELAAVCALLGRI 809
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
631-712 |
1.76e-06 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 49.36 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829965 631 VVIGDENYGEGSSREHS--ALEpRFlGGRAIITKSFARIHETNLKKQGLLPLTfADPADynkihpVDKLtiQGLKDFAPG 708
Cdd:PRK01641 70 ILLAGDNFGCGSSREHApwALA-DY-GFRAVIAPSFADIFYNNCFKNGLLPIV-LPEED------VDEL--FKLVEANPG 138
|
....
gi 157829965 709 KPLT 712
Cdd:PRK01641 139 AELT 142
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
631-680 |
3.28e-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: 47.42 E-value: 3.28e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 157829965 631 VVIGDENYGEGSSREHSALEPRFLGGRAIITKSFARIHETNLKKQGLLPL 680
Cdd:TIGR02087 50 VIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLI 99
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
631-667 |
1.11e-04 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 44.46 E-value: 1.11e-04
10 20 30
....*....|....*....|....*....|....*..
gi 157829965 631 VVIGDENYGEGSSREHSALEPRFLGGRAIITKSFARI 667
Cdd:PLN00072 132 IIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARI 168
|
|
| |
