|
Name |
Accession |
Description |
Interval |
E-value |
| aconitase_mito |
TIGR01340 |
aconitate hydratase, mitochondrial; This model represents mitochondrial forms of the TCA cycle ... |
45-775 |
0e+00 |
|
aconitate hydratase, mitochondrial; This model represents mitochondrial forms of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. [Energy metabolism, TCA cycle]
Pssm-ID: 273561 [Multi-domain] Cd Length: 745 Bit Score: 1230.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 45 YDLLEKNINIVRKRLN-RPLTLSEKIVYGHLDDPAN----QEIE--RGKTYLRLRPDRVAMRDATAQMAMLQFISSGLPK 117
Cdd:TIGR01340 1 YEKLYNNLDEVRRRLNsRPLTLAEKILYSHLDDPEEsllsQDIGdvRGKSYLKLRPDRVAMQDASAQMALLQFMTCGLPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 118 VAVPSTIHCDHLIEAQLGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIHQIILENYAYPGVLLIGTDSHTPN 197
Cdd:TIGR01340 81 VAVPASIHCDHLIVGQKGGDKDLARAIATNKEVFDFLESAGKKYGIGFWKPGSGIIHQIVLENYAFPGLMMLGTDSHTPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 198 GGGLGGICIGVGGADAVDVTAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISC 277
Cdd:TIGR01340 161 AGGLGTIAIGVGGADAVDALAGAPWELKAPKILGVKLTGKLNGWTSPKDIILKLAGLLTVRGGTGYIVEYFGPGVESLSC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 278 TGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFKDH---LVPDSGCHYDQLIEINLSELKPHINGPFT 354
Cdd:TIGR01340 241 TGMATICNMGAEIGATTSIFPFNEAMSRYLKATNRAQIAEDAKTGQYSffkLKADEGAQYDELIEIDLSKLEPHINGPFT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 355 PDLAHPVAEVGSVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLQCKSQFTITPGSEQIRATIERDGYAQ 434
Cdd:TIGR01340 321 PDLSTPISKFKETVQKNGWPEKLSAGLIGSCTNSSYEDMSRCASIVKDAEQAGLKPKSPFYVTPGSEQIRATLERDGILQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 435 ILRDVGGIVLANACGPCIGQWDRKD-IKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSPEIVTALAIAGTLKFNPETDF 513
Cdd:TIGR01340 401 TFEKFGGIVLANACGPCIGQWDRKDdVKKGEPNTILTSYNRNFRGRNDGNPATMNFLASPEIVTAMSYAGSLTFNPLTDS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 514 LTGKDGKKFKLEAPDADELPRAEFDPGQDTYQHPPKDS-SGQQVDVSPTSQRLQLLEPFDKWDGRDLEDLQILIKVKGKC 592
Cdd:TIGR01340 481 LTTPDGKEFKFPAPKGDELPEKGFEAGRDTFQAPPGSPnPNVEVAVSPSSDRLQLLEPFEPWNGKDLSGLRVLIKVTGKC 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 593 TTDHISAAGPWLKFRGHLDNISNNLLIGAINVENGKANSVRNaVTQEFGPVPDTARYYKKHGIRWVVIGDENYGEGSSRE 672
Cdd:TIGR01340 561 TTDHISAAGPWLKYKGHLDNISNNTLIGAVNAETGEVNKAYD-LDGSKGTIPELARDWKARGQPWVVVAEHNYGEGSARE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 673 HAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIKGLKDFAP---GKPLTCIIKHPNGTQ 749
Cdd:TIGR01340 640 HAALEPRHLGGRIIITKSFARIHETNLKKQGVLPLTFANEADYDKIQPGDEVATLNLYEMLKnggGGEVDLRVTKKNGKV 719
|
730 740
....*....|....*....|....*.
gi 27806769 750 ETILLNHTFNETQIEWFRAGSALNRM 775
Cdd:TIGR01340 720 FEIKLKHTVSKDQIGFFKAGSALNLM 745
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
61-780 |
0e+00 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 894.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 61 RPLTLSEKIVYGHLDDPanqEIERGKTyLRLRPDRVAMRDATAQMAMLQFISSGLPKVAVPSTI-HCDHlieaqlggekD 139
Cdd:PRK07229 1 MGLTLTEKILYAHLVEG---ELEPGEE-IAIRIDQTLTQDATGTMAYLQFEAMGLDRVKTELSVqYVDH----------N 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 140 LRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVTAG 219
Cdd:PRK07229 67 LLQADFENADDHRFLQSVAAKYGIYFSKPGNGICHQVHLERFAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 220 IPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPY 299
Cdd:PRK07229 147 GPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 300 NHRMKKYLSKTGRADIAnladefkDHLVPDSGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVGsvaekegwPLDIRV 379
Cdd:PRK07229 227 DERTREFLKAQGREDDW-------VELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVA--------GIKVDQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 380 GLIGSCTNSSYEDMGRSAAVAKqalAHGLQCKSQFTITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIGQwdrkD 459
Cdd:PRK07229 292 VLIGSCTNSSYEDLMRAASILK---GKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGM----G 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 460 IKKGEKNTIVTSYNRNFTGRNdANPETHAFVTSPEIVTALAIAGTLKfNPETdfLTGKDGKKFKLEAPDadelpraEFDP 539
Cdd:PRK07229 365 QAPATGNVSLRTFNRNFPGRS-GTKDAQVYLASPETAAASALTGVIT-DPRT--LALENGEYPKLEEPE-------GFAV 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 540 GQDTYQHPPKDSSGQQVDVSPTSQRLQLLEPFDkwdgrDLEDLQILIKVKGKCTTDHISAAGP-WLKFRGHLDNISNNLL 618
Cdd:PRK07229 434 DDAGIIAPAEDGSDVEVVRGPNIKPLPLLEPLP-----DLLEGKVLLKVGDNITTDHIMPAGAkWLPYRSNIPNISEFVF 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 619 IGAINVENGKAnsvrnavtQEFGPvpdtaryykkhgirWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETN 698
Cdd:PRK07229 509 EGVDNTFPERA--------KEQGG--------------GIVVGGENYGQGSSREHAALAPRYLGVKAVLAKSFARIHKAN 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 699 LKKQGLLPLTFADPADYNKIHPVDKLTIKGLKDFAPGKPLTCIIKHPNgtqETILLNHTFNETQIEWFRAGSALNRMKEL 778
Cdd:PRK07229 567 LINFGILPLTFADPADYDKIEEGDVLEIEDLREFLPGGPLTVVNVTKD---EEIEVRHTLSERQIEILLAGGALNLIKKK 643
|
..
gi 27806769 779 QK 780
Cdd:PRK07229 644 LA 645
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
95-505 |
0e+00 |
|
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Mitochondrial aconitase A catalytic domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediary product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 153134 Cd Length: 412 Bit Score: 867.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 95 RVAMRDATAQMAMLQFISSGLPKVAVPSTIHCDHLIEAQLGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIH 174
Cdd:cd01584 1 RVAMQDATAQMALLQFMSSGLPKVAVPSTIHCDHLIEAQVGGEKDLKRAKDINKEVYDFLASAGAKYGIGFWKPGSGIIH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 175 QIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVTAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGI 254
Cdd:cd01584 81 QIVLENYAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 255 LTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFK-DHLVPDSGCH 333
Cdd:cd01584 161 LTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEIADLADEFKdDLLVADEGAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 334 YDQLIEINLSELKPHINGPFTPDLAHPVAEVGSVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLQCKSQ 413
Cdd:cd01584 241 YDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAEKNGWPLDLRVGLIGSCTNSSYEDMGRAASIAKQALAHGLKCKSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 414 FTITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSP 493
Cdd:cd01584 321 FTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPATHAFVASP 400
|
410
....*....|..
gi 27806769 494 EIVTALAIAGTL 505
Cdd:cd01584 401 EIVTAMAIAGTL 412
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
41-775 |
0e+00 |
|
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle
Pssm-ID: 440669 [Multi-domain] Cd Length: 891 Bit Score: 731.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 41 EYIRYDL--LEKNINIVRKrlnrpLTLSEKIVYGHLD---DPAN------------QEIERGKTYLRLRPDRVAMRDATA 103
Cdd:COG1048 17 PYTYYSLpaLEEAGGDISR-----LPYSLKILLENLLrneDGETvteedikalanwLPKARGDDEIPFRPARVLMQDFTG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 104 QMAMLQFISSGLPKV-----------AVPSTIHCDHLIEAQLGG-----EKDLRRAKDINQEVYNFLATAGAKY-GVGFW 166
Cdd:COG1048 92 VPAVVDLAAMRDAVArlggdpkkinpLVPVDLVIDHSVQVDYFGtpdalEKNLELEFERNRERYQFLKWGQQAFdNFRVV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 167 RPGSGIIHQIILENYA--------------YPGvLLIGTDSHTPNggglggicigvggA-------------DAVDVTAG 219
Cdd:COG1048 172 PPGTGIVHQVNLEYLAfvvwtreedgetvaYPD-TLVGTDSHTTM-------------InglgvlgwgvggiEAEAAMLG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 220 IPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPY 299
Cdd:COG1048 238 QPVSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 300 NHRMKKYLSKTGRADI--------ANLADEFKDHLVPDSgcHYDQLIEINLSELKPHINGPFTPDLAHPVAEVGSVAEKE 371
Cdd:COG1048 318 DEETLDYLRLTGRSEEqielveayAKAQGLWRDPDAPEP--YYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 372 GWPL-----------------------DIRVGLIGSCTNSSYEDMGRSAA-VAKQALAHGLQCK--SQFTITPGSEQIRA 425
Cdd:COG1048 396 LAAPvgeeldkpvrvevdgeefelghgAVVIAAITSCTNTSNPSVMIAAGlLAKKAVEKGLKVKpwVKTSLAPGSKVVTD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 426 TIERDGYAQILRDVGGIVLANACGPCIGQWDR------KDIKKGE-KNTIVTSYNRNFTGRNDaNPETHAFVTSPEIVTA 498
Cdd:COG1048 476 YLERAGLLPYLEALGFNVVGYGCTTCIGNSGPlppeisEAIEENDlVVAAVLSGNRNFEGRIH-PDVKANFLASPPLVVA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 499 LAIAGTLKFNPETDFL-TGKDGKKFKLEA--PDADELPRAEFD--------------------------PGQDTYQHPPk 549
Cdd:COG1048 555 YALAGTVDIDLTTDPLgTDKDGKPVYLKDiwPSGEEIPAAVFKavtpemfraryadvfdgderwqalevPAGELYDWDP- 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 550 DSSgqQVDVSPTSQRLQLL-EPFdkwdgRDLEDLQILIKVKGKCTTDHISAAGP-----------------------WLK 605
Cdd:COG1048 634 DST--YIRRPPFFEGLQLEpEPF-----KDIKGARVLAKLGDSITTDHISPAGAikadspagryllehgvepkdfnsYGS 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 606 FRGHLDNISNNLLIGA--IN--VENGKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRHL 681
Cdd:COG1048 707 RRGNHEVMMRGTFANIriKNllAPGTEGGYTKHQPTGEVMSIYDAAMRYKAEGTPLVVLAGKEYGTGSSRDWAAKGTRLL 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 682 GGRAIITKSFARIHETNLKKQGLLPLTFADPADYNK--IHPVDKLTIKGLKD-FAPGKPLTCIIKHPNGTQETILLNHTF 758
Cdd:COG1048 787 GVKAVIAESFERIHRSNLVGMGVLPLQFPEGESAESlgLTGDETFDIEGLDEgLAPGKTVTVTATRADGSTEEFPVLHRI 866
|
890
....*....|....*...
gi 27806769 759 -NETQIEWFRAGSALNRM 775
Cdd:COG1048 867 dTPVEVEYYRAGGILQYV 884
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
67-503 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 546.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 67 EKIVYGHLDDPANQEIERgktylrlRPDRVAMRDATAQMAMLQFISSGLPK-----------VAVPSTIHCDHlieAQLG 135
Cdd:pfam00330 1 EKIWDAHLVEELDGSLLY-------IPDRVLMHDVTSPQAFVDLRAAGRAVrrpggtpatidHLVPTDLVIDH---APDA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 136 GEKDLRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIHQIILEN-YAYPGVLLIGTDSHTPNggglggicigvggA--- 211
Cdd:pfam00330 71 LDKNIEDEISRNKEQYDFLEWNAKKFGIRFVPPGQGIVHQVGLEYgLALPGMTIVGTDSHTTT-------------Hggl 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 212 ----------DAVDVTAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMA 281
Cdd:pfam00330 138 galafgvggsEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 282 TICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFK----DHLVPDSGCHYDQLIEINLSELKPHINGPFTPDL 357
Cdd:pfam00330 218 TICNMAIEYGATAGLFPPDETTFEYLRATGRPEAPKGEAYDKavawKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 358 AHPVAEVGSVAEKE------------------GWPL---DIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLQCKS--QF 414
Cdd:pfam00330 298 AVPLSELVPDPFADavkrkaaeraleymglgpGTPLsdgKVDIAFIGSCTNSSIEDLRAAAGLLKKAVEKGLKVAPgvKA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 415 TITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIGQWDRKDikkgEKNTIVTSYNRNFTGRNdaNPETHAFVTSPE 494
Cdd:pfam00330 378 SVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGNSDRLP----PGERCVSSSNRNFEGRQ--GPGGRTHLASPA 451
|
....*....
gi 27806769 495 IVTALAIAG 503
Cdd:pfam00330 452 LVAAAAIAG 460
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
95-505 |
3.98e-169 |
|
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: 492.78 E-value: 3.98e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 95 RVAMRDATAQMAMLQFISSGLP-KVAVPSTIHCDHLIEAQLggekdlrrAKDINQEVYNFLATAGAKYGVGFWRPGSGII 173
Cdd:cd01351 1 RVMLQDATGPMAMKAFEILAALgKVADPSQIACVHDHAVQL--------EKPVNNEGHKFLSFFAALQGIAFYRPGVGII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 174 HQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVTAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAG 253
Cdd:cd01351 73 HQIMVENLALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 254 ILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLADEFKDHLVPDSGCH 333
Cdd:cd01351 153 IVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWLAFPEELLADEGAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 334 YDQLIEINLSELKPHINGPFTPDLAHPVAEVGSvaekegwpLDIRVGLIGSCTNSSYEDMGRSAAVAKQALahgLQCKSQ 413
Cdd:cd01351 233 YDQVIEIDLSELEPDISGPNRPDDAVSVSEVEG--------TKIDQVLIGSCTNNRYSDMLAAAKLLKGAK---VAPGVR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 414 FTITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIGQWDRkdiKKGEKNTIVTSYNRNFTGRNDANPEtHAFVTSP 493
Cdd:cd01351 302 LIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGAR---LVADGEVGVSSGNRNFPGRLGTYER-HVYLASP 377
|
410
....*....|..
gi 27806769 494 EIVTALAIAGTL 505
Cdd:cd01351 378 ELAAATAIAGKI 389
|
|
| acon_putative |
TIGR01342 |
aconitate hydratase, putative, Aquifex type; This model represents a small family of proteins ... |
64-777 |
1.37e-121 |
|
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: 380.10 E-value: 1.37e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 64 TLSEKIVYGHLddpANQEIERGKTyLRLRPDRVAMRDATAQMAMLQFISSGLPKVAVP-STIHCDHLIEaqlggEKDLRR 142
Cdd:TIGR01342 1 TLAEKIIDDHL---VEGDLEPGEE-IAIEIDQTLSQDATGTMCWLEFEALEMDEVKTElAAQYCDHNML-----QFDFKN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 143 AKDinqevYNFLATAGAKYGVGFWRPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVTAGIPW 222
Cdd:TIGR01342 72 ADD-----HKFLMSAAGKFGAWFSKPGNGICHNVHKENFAAPGKTLLGSDSHTPTAGGLGMLAIGAGGIDIAAAMAGEAF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 223 ELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHR 302
Cdd:TIGR01342 147 YLEMPEIVGVHLEGELPEWATAKDIILELLRRLSVKGGLGKIFEYFGEGVEELSVPERATITNMGAELGATSSIFPSDDI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 303 MKKYLSKTGRADianladEFKDhLVPDSGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVgsvaekEGWPLDIRVglI 382
Cdd:TIGR01342 227 TEAWLAAFDRED------DFVD-LLADADAEYADEIEIDLSDLEPLIAEPHMPDNVVPVREI------AGIEVDQVM--I 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 383 GSCTNSSYEDMGRSAAVAKQALAHGlqcKSQFTITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIGQwdrkDIKK 462
Cdd:TIGR01342 292 GSCTNGAFEDLLPAAKLLEGREVHK---DTEFAVAPGSKQALELIAQEGALAEFLAAGANFLEAACGACIGI----GFAP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 463 GEKNTIVTSYNRNFTGRNdANPETHAFVTSPEIVTALAIAGTLkFNPETdfLTGKDGKkfkLEAPDAdELPrAEFDPGQD 542
Cdd:TIGR01342 365 ASDGVSLRSFNRNFEGRA-GIEDAKVYLASPETATAAAIAGEI-IDPRD--LADDEGD---LEAIGF-EMG-EKFPGGYD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 543 ---TYQHPPKDSSGQQVDVSPTSQRLQLLEPFdkwdGRDLEDlQILIKVKGKCTTDHISAAGP-WLKFRGHLDNISNNLL 618
Cdd:TIGR01342 436 aadIDIIPKEEREDDDIIKGPNIKPLPEFDPL----GADIEG-ETALIMEDNITTDHIIPAGAdILKFRSNIEAISEFTL 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 619 igainvengkansvrNAVTQEFGPVPDTARYYKKHGIrwvVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETN 698
Cdd:TIGR01342 511 ---------------HRIDDEFAERAKAADEKGKAGI---IIAGENYGQGSSREHAALAPMFLGVEAVIAKSFARIHHAN 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 699 LKKQGLLPLTFADPADYNKIHPVDKLTIKG--LKDFAPGKPLTCIIKHpngTQETILLNHTFNETQIEWFRAGSALNRMK 776
Cdd:TIGR01342 573 LFNFGILPLEFDNEEDYAKFELGDDIEIPDdlAAALADGEDEFTINKN---DDEEALATLDASEREKEILAAGGKLNLIK 649
|
.
gi 27806769 777 E 777
Cdd:TIGR01342 650 N 650
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
587-735 |
1.78e-108 |
|
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 238810 [Multi-domain] Cd Length: 149 Bit Score: 327.50 E-value: 1.78e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 587 KVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINVENGKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVIGDENYG 666
Cdd:cd01578 1 KAKGKCTTDHISAAGPWLKYRGHLDNISNNLLIGAINAENGKANSVKNQVTGEYGPVPDTARDYKAHGIKWVVIGDENYG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27806769 667 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIKGLKDFAPG 735
Cdd:cd01578 81 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYDKIHPDDKVDILGLTDFAPG 149
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
94-505 |
7.21e-105 |
|
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: 326.71 E-value: 7.21e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 94 DRVAMRDATAQMAMLQFISSGLPKVAVP-STIHCDHLIeAQLGGEkdlrrakdiNQEVYNFLATAGAKYGVGFWRPGSGI 172
Cdd:cd01585 1 DQTLTQDATGTMAYLQFEAMGVDRVRTElSVSYVDHNT-LQTDFE---------NADDHRFLQTVAARYGIYFSRPGNGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 173 IHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVTAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVA 252
Cdd:cd01585 71 CHQVHLERFAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 253 GILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRadianlADEFKDhLVPDSGC 332
Cdd:cd01585 151 RRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGR------EDDWVE-LAADADA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 333 HYDQLIEINLSELKPHINGPFTPDLAHPVAEVGsvaekegwPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGlqcKS 412
Cdd:cd01585 224 EYDEEIEIDLSELEPLIARPHSPDNVVPVREVA--------GIKVDQVAIGSCTNSSYEDLMTVAAILKGRRVHP---HV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 413 QFTITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIGQWDrkdiKKGEKNTIVTSYNRNFTGRNdANPETHAFVTS 492
Cdd:cd01585 293 SMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQ----APPTGGVSVRTFNRNFEGRS-GTKDDLVYLAS 367
|
410
....*....|...
gi 27806769 493 PEIVTALAIAGTL 505
Cdd:cd01585 368 PEVAAAAALTGVI 380
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
94-775 |
6.29e-75 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 261.02 E-value: 6.29e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 94 DRVAMRDATAQMAmlqfissGLPKV---AVPSTIHCDHLIEAQLGGEKD-LRRAKDI----NQEVYNFLA-TAGAKYGVG 164
Cdd:PRK12881 99 DLAAMRDAAAEAG-------GDPAKinpLVPVDLVVDHSVAVDYFGQKDaLDLNMKIefqrNAERYQFLKwGMQAFDNFR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 165 FWRPGSGIIHQIILE--------------NYAYPGVLlIGTDSHTPnggglggicigvgGADAVDVTA------------ 218
Cdd:PRK12881 172 VVPPGTGIMHQVNLEylarvvhtkeddgdTVAYPDTL-VGTDSHTT-------------MINGIGVLGwgvggieaeavm 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 219 -GIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVF 297
Cdd:PRK12881 238 lGQPVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFF 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 298 PYNHRMKKYLSKTGRAD--IANLADEFKDH---LVPDSGCHYDQLIEINLSELKPHINGP---------------FTPDL 357
Cdd:PRK12881 318 PVDEQTLDYLRLTGRTEaqIALVEAYAKAQglwGDPKAEPRYTRTLELDLSTVAPSLAGPkrpqdrialgnvksaFSDLF 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 358 AHPVAEVG-SVAEKEGWPLDIRVG-----LIGSCTNSSYEDMGRSAA-VAKQALAHGLQCKS--QFTITPGSEQIRATIE 428
Cdd:PRK12881 398 SKPVAENGfAKKAQTSNGVDLPDGavaiaAITSCTNTSNPSVLIAAGlLAKKAVERGLTVKPwvKTSLAPGSKVVTEYLE 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 429 RDGYAQILRDVG-GIVlANACGPCIGQWD------RKDIKKGE-KNTIVTSYNRNFTGRNDANPEThAFVTSPEIVTALA 500
Cdd:PRK12881 478 RAGLLPYLEKLGfGIV-GYGCTTCIGNSGpltpeiEQAITKNDlVAAAVLSGNRNFEGRIHPNIKA-NFLASPPLVVAYA 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 501 IAGTLKFNPETDFL-TGKDGKKFKLE-----APDADELPRAEFDPgqDTYQH-----PPKDSSGQQVDVsPTSQRLQ--- 566
Cdd:PRK12881 556 LAGTVRRDLMTEPLgKGKDGRPVYLKdiwpsSAEIDALVAFAVDP--EDFRKnyaevFKGSELWAAIEA-PDGPLYDwdp 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 567 ----LLEP--FDKWDG-----RDLEDLQILIKVKGKCTTDHIS---------AAGPWLKFRGHLDNISN----------- 615
Cdd:PRK12881 633 kstyIRRPpfFDFSMGpaasiATVKGARPLAVLGDSITTDHISpagaikadsPAGKYLKENGVPKADFNsygsrrgnhev 712
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 616 ------------NLLIGAINVENGkansvRNAVTQEFGPVPDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRHLGG 683
Cdd:PRK12881 713 mmrgtfanvrikNLMIPGKEGGLT-----LHQPSGEVLSIYDAAMRYQAAGTPLVVIAGEEYGTGSSRDWAAKGTRLLGV 787
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 684 RAIITKSFARIHETNLKKQGLLPLTF--ADPADYNKIHPVDKLTIKGL-KDFAPGKPLTCIIKHPNGTQETILLNHTFnE 760
Cdd:PRK12881 788 KAVIAESFERIHRSNLVGMGVLPLQFkgGDSRQSLGLTGGETFDIEGLpGEIKPRQDVTLVIHRADGSTERVPVLCRI-D 866
|
810
....*....|....*..
gi 27806769 761 TQIE--WFRAGSALNRM 775
Cdd:PRK12881 867 TPIEvdYYKAGGILPYV 883
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
62-505 |
2.96e-74 |
|
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: 247.25 E-value: 2.96e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 62 PLTLSEKIvyghLDDPANQEIERGKTYLrLRPDRVAMRDATAQMAMLQFISSGLPKVAVPSTIH--CDHLIEAqlggeKD 139
Cdd:COG0065 2 GMTLAEKI----LARHAGREVEPGEIVL-LYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVavFDHNVPT-----KD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 140 LRRAKDINQevynfLATAGAKYGVGFWRPGS-GIIHQIILEN-YAYPGVLLIGTDSHTPNggglggicigvggADAV--- 214
Cdd:COG0065 72 PKSAEQVKT-----LREFAKEFGITFFDVGDpGICHVVLPEQgLVLPGMTIVGGDSHTCT-------------HGAFgaf 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 215 -------DVTAGIP----WeLKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATI 283
Cdd:COG0065 134 afgigttDVAHVLAtgtlW-FKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 284 CNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLAdefkdhlvPDSGCHYDQLIEINLSELKPHINGPFTPDLAHPVAE 363
Cdd:COG0065 213 CNMAIEAGAKAGIIAPDETTFEYLKGRPFAPWRTLK--------SDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 364 VGSVaekegwPLDirVGLIGSCTNSSYEDMGRSAAVAKqalahGLQCKS--QFTITPGSEQIRATIERDGYAQILRDVGG 441
Cdd:COG0065 285 LEGI------KID--QVFIGSCTNGRIEDLRAAAEILK-----GRKVAPgvRAIVVPGSQEVYRQAEAEGLDEIFIEAGA 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27806769 442 IVLANACGPCIG-QWDRkdIKKGEKnTIVTSyNRNFTGRNdANPETHAFVTSPEIVTALAIAGTL 505
Cdd:COG0065 352 EWREPGCGMCLGmNMGV--LAPGER-CASTS-NRNFEGRM-GSPGSRTYLASPATAAASAIAGRI 411
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
97-774 |
4.97e-73 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 255.43 E-value: 4.97e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 97 AMRDATAQMamlqfissGL------PKVAVPSTIhcDHLIEAQLGGEKD-LRRAKDI----NQEVYNFLatagaKYGVGF 165
Cdd:PRK09277 103 AMRDAIADL--------GGdpakinPLVPVDLVI--DHSVQVDYFGTPDaFEKNVELeferNEERYQFL-----KWGQKA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 166 WR------PGSGIIHQIILE-------------NYAYPGVLlIGTDSHTPnggglggicigvgGADAVDVTA----GI-- 220
Cdd:PRK09277 168 FDnfrvvpPGTGICHQVNLEylapvvwtredgeLVAYPDTL-VGTDSHTT-------------MINGLGVLGwgvgGIea 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 221 -------PWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGAT 293
Cdd:PRK09277 234 eaamlgqPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGAT 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 294 TSVFPYNHRMKKYLSKTGRAD--IAnladefkdhLV------------PDSGCHYDQLIEINLSELKPHINGP------- 352
Cdd:PRK09277 314 CGFFPIDEETLDYLRLTGRDEeqVA---------LVeayakaqglwrdPLEEPVYTDVLELDLSTVEPSLAGPkrpqdri 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 353 FTPDLAHPVAEV--------GSVAEKEGWPLDIRVG-----LIGSCTNSS--YEDMGrsAA-VAKQALAHGLQCKS--QF 414
Cdd:PRK09277 385 PLSDVKEAFAKSaelgvqgfGLDEAEEGEDYELPDGavviaAITSCTNTSnpSVMIA--AGlLAKKAVEKGLKVKPwvKT 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 415 TITPGSEQIRATIERDGYAQILRDVG-GIVlANACGPCIG---------QwdrKDIKkgEKNTIVT---SYNRNFTGRnd 481
Cdd:PRK09277 463 SLAPGSKVVTDYLEKAGLLPYLEALGfNLV-GYGCTTCIGnsgplppeiE---KAIN--DNDLVVTavlSGNRNFEGR-- 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 482 ANPETHA-FVTSPEIVTALAIAGTLKFNPETDFL-TGKDGKKFKLEA--PDADE------------LPRAEFDP---GQD 542
Cdd:PRK09277 535 IHPLVKAnYLASPPLVVAYALAGTVDIDLEKDPLgTDKDGNPVYLKDiwPSDEEidavvakavkpeMFRKEYADvfeGDE 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 543 TYQHPPKdSSGQQVDVSPTSQRLQlLEPFdkWDG--------RDLEDLQILIKVKGKCTTDHIS---------AAGPWLK 605
Cdd:PRK09277 615 RWNAIEV-PEGPLYDWDPDSTYIR-NPPY--FEGmlaepgpvRDIKGARVLALLGDSITTDHISpagaikadsPAGKYLL 690
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 606 --------F--------------RGHLDNIS--NNLLIGainVENGKAnsvRNAVTQEFGPVPDTARYYKKHGIRWVVIG 661
Cdd:PRK09277 691 ehgvepkdFnsygsrrgnhevmmRGTFANIRirNEMVPG---VEGGYT---RHFPEGEVMSIYDAAMKYKEEGTPLVVIA 764
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 662 DENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYN--KIHPVDKLTIKGLKDFAPGKPLT 739
Cdd:PRK09277 765 GKEYGTGSSRDWAAKGTRLLGVKAVIAESFERIHRSNLVGMGVLPLQFKPGESRKtlGLDGTETFDIEGLEDLKPGATVT 844
|
810 820 830
....*....|....*....|....*....|....*.
gi 27806769 740 CIIKHPNGTQETI-LLNHTFNETQIEWFRAGSALNR 774
Cdd:PRK09277 845 VVITRADGEVVEFpVLCRIDTAVEVDYYRNGGILQY 880
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
62-503 |
1.52e-67 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 229.29 E-value: 1.52e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 62 PLTLSEKIVYGHlddpANQEIERGKtYLRLRPDRVAMRDATAQMAMLQFISSGLPKVAVPSTIH--CDHLIEAqlggeKD 139
Cdd:PRK00402 2 GMTLAEKILARH----SGRDVSPGD-IVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVivFDHFVPA-----KD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 140 LRRAKdINQEVYNFLATAGAKYgvgFWRPGSGIIHQIILEN-YAYPGVLLIGTDSHTPNggglggicigvggADAV---- 214
Cdd:PRK00402 72 IKSAE-QQKILREFAKEQGIPN---FFDVGEGICHQVLPEKgLVRPGDVVVGADSHTCT-------------YGALgafa 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 215 ------DVTAGIP----WeLKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATIC 284
Cdd:PRK00402 135 tgmgstDMAAAMAtgktW-FKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 285 NMGAEIGATTSVFPYNHRMKKYLSKTGRADIanladefkDHLVPDSGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEV 364
Cdd:PRK00402 214 NMAIEAGAKAGIFAPDEKTLEYLKERAGRDY--------KPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 365 gsvaekEGWPLDIRVglIGSCTNSSYEDMGRSAAVAK-QALAHGLQCKsqftITPGSEQIRATIERDGYAQILRDVGGIV 443
Cdd:PRK00402 286 ------EGTKVDQVF--IGSCTNGRLEDLRIAAEILKgRKVAPGVRLI----VIPASQKIYLQALKEGLIEIFVDAGAVV 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 444 LANACGPCIGqwdrkdIKKGEknTIVTSYNRNFTGRNdANPETHAFVTSPEIVTALAIAG 503
Cdd:PRK00402 354 STPTCGPCLGghm-gvLAPGE--VCLSTTNRNFKGRM-GSPESEVYLASPAVAAASAVTG 409
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
95-503 |
6.86e-64 |
|
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: 218.21 E-value: 6.86e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 95 RVAMRDATAQMAMLQFISSGLPKVAVPSTIHC--DHLIEAqlggekDLRRAKDINQEVYNFLATAGAK-YGVGfwrpGSG 171
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAvfDHNVPT------PDIKAAEQVKTLRKFAKEFGINfFDVG----RQG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 172 IIHQIILENY-AYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVTA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVIL 249
Cdd:cd01583 71 ICHVILPEKGlTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLAtGKLW-FRVPETMRVNVEGKLPPGVTAKDVIL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 250 KVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRAdianladEFKdHLVPD 329
Cdd:cd01583 150 YIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKA-------YWK-ELKSD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 330 SGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVgsvaekEGWPLDIRVglIGSCTNSSYEDMGRSAAVAKqalAHGLQ 409
Cdd:cd01583 222 EDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEV------EGIKIDQVF--IGSCTNGRLEDLRAAAEILK---GRKVA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 410 CKSQFTITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIG-QWDRkdIKKGEknTIVTSYNRNFTGR-NDANPETH 487
Cdd:cd01583 291 DGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGgHMGV--LAPGE--RCVSTSNRNFKGRmGSPGARIY 366
|
410
....*....|....*.
gi 27806769 488 afVTSPEIVTALAIAG 503
Cdd:cd01583 367 --LASPATAAASAITG 380
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
582-712 |
2.06e-61 |
|
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This domain undergoes conformational change in the enzyme mechanism.
Pssm-ID: 459908 [Multi-domain] Cd Length: 131 Bit Score: 202.60 E-value: 2.06e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 582 LQILIKVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINVENGKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVIG 661
Cdd:pfam00694 1 MPVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYGKVRYLPDGENPDFYDAAMRYKQHGAPIVVIG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 27806769 662 DENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADP 712
Cdd:pfam00694 81 GKNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPLEFPEE 131
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
94-773 |
3.10e-61 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 222.19 E-value: 3.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 94 DRVAMRDAtaqMAML----QFISsglPKVAVPSTIhcDHLIEAQLGGEKD-LRRAKDI----NQEVYNFLatagaKYGVG 164
Cdd:PTZ00092 106 DLAAMRDA---MKRLggdpAKIN---PLVPVDLVI--DHSVQVDFSRSPDaLELNQEIeferNLERFEFL-----KWGSK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 165 FWR------PGSGIIHQIILE----------NYAYPGVLlIGTDSHTP--NGGGLGGICIGVGGADAVdvTAGIPWELKC 226
Cdd:PTZ00092 173 AFKnllivpPGSGIVHQVNLEylarvvfnkdGLLYPDSV-VGTDSHTTmiNGLGVLGWGVGGIEAEAV--MLGQPISMVL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 227 PKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKY 306
Cdd:PTZ00092 250 PEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDY 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 307 LSKTGRAD-----IANLADEFKDHLVPDSGCHYDQLIEINLSELKPHINGP---------------FTPDLAHPVAEVG- 365
Cdd:PTZ00092 330 LKQTGRSEekvelIEKYLKANGLFRTYAEQIEYSDVLELDLSTVVPSVAGPkrphdrvplsdlkkdFTACLSAPVGFKGf 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 366 SVAEKE----------GWPLDIRVG-----LIGSCTNSSYED-MGRSAAVAKQALAHGLQCKS--QFTITPGSEQIRATI 427
Cdd:PTZ00092 410 GIPEEKhekkvkftykGKEYTLTHGsvviaAITSCTNTSNPSvMLAAGLLAKKAVEKGLKVPPyiKTSLSPGSKVVTKYL 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 428 ERDGYAQILRDVGGIVLANACGPCIGqwDRKDIKKGEKNTI---------VTSYNRNFTGRndANPETHA-FVTSPEIVT 497
Cdd:PTZ00092 490 EASGLLKYLEKLGFYTAGYGCMTCIG--NSGDLDPEVSEAItnndlvaaaVLSGNRNFEGR--VHPLTRAnYLASPPLVV 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 498 ALAIAGTLKFNPETDFL-TGKDGKKFKLEA--PDADEL--------------------------------PRAEF---DP 539
Cdd:PTZ00092 566 AYALAGRVNIDFETEPLgSDKTGKPVFLRDiwPSREEIqaleakyvkpemfkevysnitqgnkqwnelqvPKGKLyewDE 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 540 gQDTYQHPPKDSSGQQVDVSPTsqrlqllepfdkwdgRDLEDLQILIKVKGKCTTDHISAAG------PWLKF------- 606
Cdd:PTZ00092 646 -KSTYIHNPPFFQTMELEPPPI---------------KSIENAYCLLNLGDSITTDHISPAGniaknsPAAKYlmergve 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 607 ------------------RGHLDNIS-NNLLIGA-----INVENGKANSVRNAvtqefgpvpdtARYYKKHGIRWVVIGD 662
Cdd:PTZ00092 710 rkdfntygarrgndevmvRGTFANIRlINKLCGKvgpntVHVPTGEKMSIYDA-----------AEKYKQEGVPLIVLAG 778
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 663 ENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFAD--PADYNKIHPVDKLTIKGLK-DFAPGKPLT 739
Cdd:PTZ00092 779 KEYGSGSSRDWAAKGPYLQGVKAVIAESFERIHRSNLVGMGILPLQFLNgeNADSLGLTGKEQFSIDLNSgELKPGQDVT 858
|
810 820 830
....*....|....*....|....*....|....*
gi 27806769 740 ciIKHPNG-TQETILLNHTfnETQIEWFRAGSALN 773
Cdd:PTZ00092 859 --VKTDTGkTFDTILRIDT--EVEVEYFKHGGILQ 889
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
94-743 |
1.31e-58 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 215.05 E-value: 1.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 94 DRVAMRDATAQMAMlqfiSSGLPKVAVPSTIHCDHLIEAQLGGEKDLRRAK-----DINQEVYNFLatagaKYGVGFWR- 167
Cdd:PLN00070 138 DLACMRDAMNNLGG----DPNKINPLVPVDLVIDHSVQVDVARSENAVQANmelefQRNKERFAFL-----KWGSTAFQn 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 168 -----PGSGIIHQIILENYA----------YPGVLlIGTDSHTPNGGGLGGICIGVGGADAVDVTAGIPWELKCPKVIGV 232
Cdd:PLN00070 209 mlvvpPGSGIVHQVNLEYLGrvvfntdgilYPDSV-VGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGF 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 233 KLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGR 312
Cdd:PLN00070 288 KLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGR 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 313 AD----------IANlaDEFKDHLVPDSGCHYDQLIEINLSELKPHINGPFTPD---------------LAHPVAEVGSV 367
Cdd:PLN00070 368 SDetvamieaylRAN--KMFVDYNEPQQERVYSSYLELDLEDVEPCISGPKRPHdrvplkemkadwhscLDNKVGFKGFA 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 368 AEKE-----------GWPLDIRVG-----LIGSCTNSSYED-MGRSAAVAKQALAHGLQCKS--QFTITPGSEQIRATIE 428
Cdd:PLN00070 446 VPKEaqskvakfsfhGQPAELRHGsvviaAITSCTNTSNPSvMLGAGLVAKKACELGLEVKPwiKTSLAPGSGVVTKYLL 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 429 RDGYAQILRDVGGIVLANACGPCIGqwDRKDIKKGEKNTI---------VTSYNRNFTGRndANPETHA-FVTSPEIVTA 498
Cdd:PLN00070 526 KSGLQKYLNQQGFHIVGYGCTTCIG--NSGELDESVASAItendivaaaVLSGNRNFEGR--VHPLTRAnYLASPPLVVA 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 499 LAIAGTLKFNPETDFL-TGKDGKK--FKLEAPDADELPRAEF-----DPGQDTYQHPPKDS---------SGQQVDVSPT 561
Cdd:PLN00070 602 YALAGTVDIDFEKEPIgTGKDGKDvfFRDIWPSNEEVAEVVQssvlpDMFKSTYEAITKGNpmwnqlsvpSGTLYSWDPK 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 562 SQRLQllEP-------FDKWDGRDLEDLQILIKVKGKCTTDHISAAG------PWLKF---------------------- 606
Cdd:PLN00070 682 STYIH--EPpyfknmtMSPPGPHGVKDAYCLLNFGDSITTDHISPAGsihkdsPAAKYlmergvdrkdfnsygsrrgnde 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 607 ---RGHLDNIS--NNLLIGAINvengkANSVrNAVTQEFGPVPDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRHL 681
Cdd:PLN00070 760 imaRGTFANIRivNKLLKGEVG-----PKTV-HIPTGEKLSVFDAAMKYKSEGHDTIILAGAEYGSGSSRDWAAKGPMLL 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 682 GGRAIITKSFARIHETNLKKQGLLPLTF-----AD--------------PADYNKIHPVDKLTIKGLKdfapGKPLTCII 742
Cdd:PLN00070 834 GVKAVIAKSFERIHRSNLVGMGIIPLCFksgedADtlgltgherytidlPSNISEIKPGQDVTVTTDN----GKSFTCTL 909
|
.
gi 27806769 743 K 743
Cdd:PLN00070 910 R 910
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
94-503 |
6.47e-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: 197.67 E-value: 6.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 94 DRVAMRDATAQMAMLQFISSGLPKVAVPSTIHC--DHLIEAqlggekDLRRAKDINQEVYNFLATAGAKYgvgFWRPGSG 171
Cdd:TIGR01343 26 DLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIvfDHQVPA------DTIKAAEMQKLAREFVKKQGIKY---FYDVGEG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 172 IIHQIILEN-YAYPGVLLIGTDSHTPNGGGLGGICIGVGGAD-AVDVTAGIPWeLKCPKVIGVKLTGSLSGWTSPKDVIL 249
Cdd:TIGR01343 97 ICHQVLPEKgLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDmAYAIATGKTW-FKVPETIRVNITGKLNPGVTAKDVIL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 250 KVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADianlADEFKDhlvpD 329
Cdd:TIGR01343 176 EVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYLKERRKEP----FRVYKS----D 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 330 SGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVgsvaekEGWPLDiRVgLIGSCTNSSYEDMGRSAAVAKqalAHGLQ 409
Cdd:TIGR01343 248 EDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEV------EGTEID-QV-FIGSCTNGRLEDLRVAAKILK---GRKVA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 410 CKSQFTITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIGqwdRKDIKKGEKNTIVTSYNRNFTGRNdANPETHAF 489
Cdd:TIGR01343 317 PDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLG---SHQGVLAPGEVCISTSNRNFKGRM-GHPNAEIY 392
|
410
....*....|....
gi 27806769 490 VTSPEIVTALAIAG 503
Cdd:TIGR01343 393 LASPATAAASAVKG 406
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
94-504 |
8.95e-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: 165.94 E-value: 8.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 94 DRVAMRDATAQMAmlqfissGLP-KV--AVPSTIHCDHLIEAQLGG-----EKDLRRAKDINQEVYNFLATAGAKYG-VG 164
Cdd:cd01586 15 DLAAMRDAVKRLG-------GDPeKInpLIPVDLVIDHSVQVDFYGtadalAKNMKLEFERNRERYEFLKWGQKAFKnLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 165 FWRPGSGIIHQIILE--------------NYAYPGVLlIGTDSHTPNGGGLGGICIGVGGADAVDVTAGIPWELKCPKVI 230
Cdd:cd01586 88 VVPPGTGIIHQVNLEylarvvftseedgdGVAYPDSV-VGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 231 GVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPynhrmkkylskt 310
Cdd:cd01586 167 GVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFP------------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 311 gradianladefkdhlvPDSgchydQLIEINLSELKPHINGPFTPDlaHPVAEVGSVAekegwpldirVGLIGSCTNSSY 390
Cdd:cd01586 235 -----------------VDT-----QVVELDLSTVEPSVSGPKRPQ--DRVPLHGSVV----------IAAITSCTNTSN 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 391 ED-MGRSAAVAKQALAHGLQCKS--QFTITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIG------QWDRKDIK 461
Cdd:cd01586 281 PSvMLAAGLLAKKAVELGLKVKPyvKTSLAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGnsgplpEEVEEAIK 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 27806769 462 KGE-KNTIVTSYNRNFTGRndANPETHA-FVTSPEIVTALAIAGT 504
Cdd:cd01586 361 ENDlVVAAVLSGNRNFEGR--IHPLVRAnYLASPPLVVAYALAGT 403
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
108-505 |
1.22e-36 |
|
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: 141.60 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 108 LQFISSGLPKVAVPSTIHC--DHliEAQLGGEKDLRRAKDINqevyNFlataGAKYGVGFWRPGSGIIHQIILEN-YAYP 184
Cdd:cd01582 13 LKFMSIGATKIHNPDQIVMtlDH--DVQNKSEKNLKKYKNIE----SF----AKKHGIDFYPAGRGIGHQIMIEEgYAFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 185 GVLLIGTDSHTPNGGGLGGICIGVGGADAVDVTA-GIPWeLKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGA 263
Cdd:cd01582 83 GTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWAtGQTW-WQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLNH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 264 IVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRmkkylsktgradianladefkdHLVpdsgchydqlieINLS 343
Cdd:cd01582 162 AIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAK----------------------HLI------------LDLS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 344 ELKPHINGPFTPDLAHPVAEVgsvaekEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQA--------LAHGLqcksQFT 415
Cdd:cd01582 208 TLSPYVSGPNSVKVSTPLKEL------EAQNIKINKAYLVSCTNSRASDIAAAADVVKGKkekngkipVAPGV----EFY 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 416 ITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIGqWDRKDIKKGEKNtiVTSYNRNFTGRNdANPETHAFVTSPEI 495
Cdd:cd01582 278 VAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIG-LGQGLLEPGEVG--ISATNRNFKGRM-GSTEALAYLASPAV 353
|
410
....*....|
gi 27806769 496 VTALAIAGTL 505
Cdd:cd01582 354 VAASAISGKI 363
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
227-505 |
1.11e-30 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 126.39 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 227 PKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGA---------TTsvF 297
Cdd:PRK05478 163 PKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGAraglvapdeTT--F 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 298 PYnhrMKkylsktGR--ADIANLADEFKDH---LVPDSGCHYDQLIEINLSELKPH------------INGPF-TPDLAH 359
Cdd:PRK05478 241 EY---LK------GRpfAPKGEDWDKAVAYwktLKSDEDAVFDKVVTLDAADIEPQvtwgtnpgqvisIDGKVpDPEDFA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 360 PVAEVGSVAE-------KEGWPL-DIRVG--LIGSCTNSSYEDMGRSAAVAK--------QALahglqcksqftITPGSE 421
Cdd:PRK05478 312 DPVKRASAERalaymglKPGTPItDIKIDkvFIGSCTNSRIEDLRAAAAVVKgrkvapgvRAL-----------VVPGSG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 422 QIRATIERDGYAQILRDVG------GivlanaCGPCIGQWDrkDIKKGEKNTIVTSyNRNFTGRNDANPETHafVTSPEI 495
Cdd:PRK05478 381 LVKAQAEAEGLDKIFIEAGfewrepG------CSMCLAMNP--DKLPPGERCASTS-NRNFEGRQGKGGRTH--LVSPAM 449
|
330
....*....|
gi 27806769 496 VTALAIAGTL 505
Cdd:PRK05478 450 AAAAAITGHF 459
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
587-728 |
2.17e-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: 111.79 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 587 KVKGKCTTDHISAAGPWlkfrghldnisnnlligainvengkansvrnavtqefgpvpdtaryykkhgirwVVIGDENYG 666
Cdd:cd00404 1 KVAGNITTDHISPAGPG------------------------------------------------------VVIGDENYG 26
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27806769 667 EGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTIKG 728
Cdd:cd00404 27 TGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPLEFADPEDYLKLHTGDELDIYP 88
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
587-726 |
2.48e-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: 109.83 E-value: 2.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 587 KVKGKCTTDHISAAGP-WLKFRGHLDNISNNLLIGainvengkansvrnaVTQEFGPvpdtaryYKKHGIRWVVIGDENY 665
Cdd:cd01579 1 KVGDNITTDHIMPAGAkVLPLRSNIPAISEFVFHR---------------VDPTFAE-------RAKAAGPGFIVGGENY 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27806769 666 GEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHPVDKLTI 726
Cdd:cd01579 59 GQGSSREHAALAPMYLGVRAVLAKSFARIHRANLINFGILPLTFADEDDYDRFEQGDQLEL 119
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
227-505 |
1.17e-27 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 117.31 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 227 PKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKY 306
Cdd:PRK12466 165 PKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETTFDY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 307 LSKTGRADIANLADEFKDH---LVPDSGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVGSVAEKE------------ 371
Cdd:PRK12466 245 LRGRPRAPKGALWDAALAYwrtLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAAEadparraamera 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 372 --------GWPL-DIRVG--LIGSCTNSSYEDM--------GRSAAVAKQALahglqcksqftITPGSEQIRATIERDGY 432
Cdd:PRK12466 325 ldymgltpGTPLaGIPIDrvFIGSCTNGRIEDLraaaavlrGRKVAPGVRAM-----------VVPGSGAVRRQAEAEGL 393
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27806769 433 AQILRDVGGIVLANACGPCIGQWDRKdIKKGEKntIVTSYNRNFTGRNDANPETHafVTSPEIVTALAIAGTL 505
Cdd:PRK12466 394 ARIFIAAGFEWREPGCSMCLAMNDDV-LAPGER--CASTTNRNFEGRQGPGARTH--LMSPAMVAAAAVAGHI 461
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
89-773 |
6.76e-24 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 107.79 E-value: 6.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 89 LRLRPDRVAMRDAT----AQMAmlqfISSGLPKVAVPSTIHCDHLIEAQLGGEkdlrrakdINQEVYNFLATAGAKYGVG 164
Cdd:PRK11413 54 LKIKFDSLASHDITfvgiIQTA----KASGMERFPLPYVLTNCHNSLCAVGGT--------INEDDHVFGLSAAQKYGGI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 165 FWRPGSGIIHQIILENYAYPGVLLIGTDSHTpnggglggicigvgGADAVDVTA---GIP----------WELKCPKVIG 231
Cdd:PRK11413 122 FVPPHIAVIHQYMREMMAGGGKMILGSDSHT--------------RYGALGTMAvgeGGGelvkqllndtYDIDYPGVVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 232 VKLTGSLSGWTSPKDVILKVAGILTVKGGT-GAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKT 310
Cdd:PRK11413 188 VYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLALH 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 311 GRadianlADEFKDhLVPDSGCHYDQLIEINLSELKPHINGPFTPDLAHPVAEVGSVA-------EKEGWPLD------- 376
Cdd:PRK11413 268 GR------GQDYCE-LNPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDELNQNLtdilrevEIESERVAhgkakls 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 377 ---------IRV--GLIGSCTNSSYEDMGRSAAVAKqalahGLQCKS-QFTIT--PGSEQIRATIERDGYAQILRDVGGI 442
Cdd:PRK11413 341 lldkiengrLKVqqGIIAGCSGGNYENVIAAANALR-----GQSCGNdTFSLSvyPSSQPVFMDLAKKGVVADLMGAGAI 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 443 VLANACGPCIGQWDrkdikkgekntivTSYN---------RNFTGRNDANPeTHAFVTSPEIVTALAIAGTLKFNpetDF 513
Cdd:PRK11413 416 IRTAFCGPCFGAGD-------------TPANnglsirhttRNFPNREGSKP-ANGQMSAVALMDARSIAATAANG---GY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 514 LTGKDgkkfklEAPDADELPRAEFDPgqDTYQHPPKDSSGQQVdvspTSQRLQLLEPFDKWDgrDLEDL--QILIKVKGK 591
Cdd:PRK11413 479 LTSAT------ELDCWDNVPEYAFDV--TPYKNRVYQGFGKGA----TQQPLIYGPNIKDWP--EMGALtdNILLKVCSK 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 592 -----CTTDHISAAGPWLKFRghldniSNNLLIGAIN--------VENGKA-----NSVRNAVTQEFGPVPDTAR-YYKK 652
Cdd:PRK11413 545 ildpvTTTDELIPSGETSSYR------SNPLGLAEFTlsrrdpgyVGRSKAvaeleNQRLAGNVSELTEVFARIKqIAGQ 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 653 HGIRW--VVIGDENY----GEGSSREHAALEPRHLGGRAIITKSFA-RIHETNLKKQGLLPLTFADPadyNKIHPVDKLT 725
Cdd:PRK11413 619 EHIDPlqTEIGSMVYavkpGDGSAREQAASCQRVLGGLANIAEEYAtKRYRSNVINWGMLPFQMAEE---PTFEVGDYIY 695
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 27806769 726 IKGLKDFAPGKPLTC---IIKHPNGTQETILLNHTFNETQIEWFRAGSALN 773
Cdd:PRK11413 696 IPGIRAALDNPGTTFkgyVIHEDAPVTEITLYMESLTAEEREIIKAGCLIN 746
|
|
| AcnA_IRP_Swivel |
cd01580 |
Aconitase A swivel domain. This is the major form of the TCA cycle enzyme aconitate hydratase, ... |
593-728 |
5.17e-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: 5.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 593 TTDHISAAGPWLK-------------------------------FRGHLDNISN-NLLigainVENGKANSVRNAVTQEF 640
Cdd:cd01580 7 TTDHISPAGSIAKdspagkylaergvkprdfnsygsrrgndevmMRGTFANIRLrNKL-----VPGTEGGTTHHPPTGEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 641 GPVPDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADP--ADYNKI 718
Cdd:cd01580 82 MSIYDAAMRYKEEGVPLVILAGKEYGSGSSRDWAAKGPFLLGVKAVIAESFERIHRSNLVGMGILPLQFPPGenADSLGL 161
|
170
....*....|
gi 27806769 719 HPVDKLTIKG 728
Cdd:cd01580 162 TGEETYDIIG 171
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
658-726 |
1.23e-13 |
|
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238809 [Multi-domain] Cd Length: 91 Bit Score: 66.84 E-value: 1.23e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 658 VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYN-KIHPVDKLTI 726
Cdd:cd01577 20 IIVAGKNFGCGSSREHAPWALKDAGIRAVIAESFARIFFRNAINNGLLPVTLADEDVEEvEAKPGDEVEV 89
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
658-752 |
1.33e-11 |
|
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; 3-isopropylmalate dehydratase small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439836 [Multi-domain] Cd Length: 195 Bit Score: 64.42 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 658 VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTfADPADYNKI------HPVDKLTIkglkD 731
Cdd:COG0066 67 ILVAGRNFGCGSSREHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIE-LPEEAVDALfaaieaNPGDELTV----D 141
|
90 100
....*....|....*....|.
gi 27806769 732 FApgkplTCIIKhpNGTQETI 752
Cdd:COG0066 142 LE-----AGTVT--NGTGETY 155
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
162-505 |
4.19e-10 |
|
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle; Aconitase B catalytic domain. Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle. Aconitase has an active (4FE-4S) and an inactive (3FE-4S) form. The active cluster is part of the catalytic site that interconverts citrate, cis-aconitase and isocitrate. The domain architecture of aconitase B is different from other aconitases in that the catalytic domain is normally found at C-terminus for other aconitases, but it is at N-terminus for B family. It also has a HEAT domain before domain 4 which plays a role in protein-protein interaction. This alignment is the core domain including domains 1,2 and 3.
Pssm-ID: 153131 Cd Length: 436 Bit Score: 62.52 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 162 GVGFWRPGSGIIHQIiLENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVdVTAGIPweLKCPKVIGVKLTGSLSGW 241
Cdd:cd01581 85 GGVALRPGDGVIHSW-LNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAA-ATGVMP--LDMPESVLVRFKGKMQPG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 242 TSPKDVILKV------AGILTV--KGG----TGAIVEYHGpgVDSISCTGMATICNMGAEIGATTSVFPYNH-------- 301
Cdd:cd01581 161 ITLRDLVNAIpyyaiqQGLLTVekKGKknvfNGRILEIEG--LPDLKVEQAFELTDASAERSAAACTVRLDKepvieyle 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 302 ----RMKKYLSKtGRADIANLADEFKDH---------LVPDSGCHYDQLIEINLSELK-PHINGPFTPDlahpvaEVGSV 367
Cdd:cd01581 239 snvvLMKIMIAN-GYDDARTLLRRIIAMeewlanpplLEPDADAEYAAVIEIDLDDIKePILACPNDPD------DVKLL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 368 AEKEGWPLDIrvGLIGSC-TNssyedMGRSAAVAKQALAHGlQCKSQFTITPGSEQIRATIERDGYAQILRDVGGIVLAN 446
Cdd:cd01581 312 SEVAGKKIDE--VFIGSCmTN-----IGHFRAAAKILRGKE-FKPTRLWVAPPTRMDWAILQEEGYYSIFGDAGARTEMP 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27806769 447 ACGPCIGQWDRkdIKKGEknTIVTSYNRNFTGR--NDANpethAFVTSPEIVTALAIAGTL 505
Cdd:cd01581 384 GCSLCMGNQAR--VADGA--TVFSTSTRNFDNRvgKGAE----VYLGSAELAAVCALLGRI 436
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
152-505 |
7.54e-10 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 62.63 E-value: 7.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 152 NFLATAGakyGVGFwRPGSGIIHQIiLENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVdVTAGIPweLKCPKVIG 231
Cdd:PLN00094 525 DFIRNRG---GVSL-RPGDGVIHSW-LNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFGA-ATGVIP--LDMPESVL 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 232 VKLTGSLSGWTSPKDVILKV------AGILTV-KGG-----TGAIVEYHGpgVDSISCTGMATICNMGAEIGAT------ 293
Cdd:PLN00094 597 VRFTGTMQPGITLRDLVHAIpytaiqDGLLTVeKKGkknvfSGRILEIEG--LPHLKCEQAFELSDASAERSAAgctikl 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 294 --TSVFPY---NHRMKKYLSKTGRAD-------IANLADEFKD-HLV-PDSGCHYDQLIEINLSELK-PHINGPFTPDLA 358
Cdd:PLN00094 675 dkEPIIEYlnsNVVMLKWMIAEGYGDrrtlerrIARMQQWLADpELLeADPDAEYAAVIEIDMDEIKePILCAPNDPDDA 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 359 HPVAEVgsVAEKegwpldIRVGLIGSC-TNssyedMGRSAAVAKQALAHGLQCKSQFTITPGSEQIRATIERDGYAQILR 437
Cdd:PLN00094 755 RLLSEV--TGDK------IDEVFIGSCmTN-----IGHFRAAGKLLNDNLSQLPTRLWVAPPTKMDEAQLKAEGYYSTFG 821
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 438 DVGGIVLANACGPCIGQWDRkdikKGEKNTIVTSYNRNFTGR--NDANpethAFVTSPEIVTALAIAGTL 505
Cdd:PLN00094 822 TVGARTEMPGCSLCMGNQAR----VAEKSTVVSTSTRNFPNRlgKGAN----VYLASAELAAVAAILGRL 883
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
658-726 |
3.05e-09 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 56.76 E-value: 3.05e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27806769 658 VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADynKIHPVDKLTI 726
Cdd:PRK00439 51 IIVAGKNFGCGSSREHAPIALKAAGVSAVIAKSFARIFYRNAINIGLPVLECDEAVD--KIEDGDEVEV 117
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
644-714 |
1.16e-08 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 55.19 E-value: 1.16e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27806769 644 PDTARYYKKHGIrwvVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPAD 714
Cdd:PRK14023 41 PEFASTVRPGDI---LVAGRNFGLGSSREYAPEALKMLGIGAIIAKSYARIFYRNLVNLGIPPFESEEVVD 108
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
658-707 |
5.80e-08 |
|
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the 3-isopropylmalate dehydratase, small subunits which form TIGR00171. This subfamily includes the members of TIGR02084 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities.
Pssm-ID: 273961 [Multi-domain] Cd Length: 154 Bit Score: 52.81 E-value: 5.80e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 27806769 658 VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPL 707
Cdd:TIGR02087 50 VIVAGKNFGCGSSREQAALALKAAGIAAVIAESFARIFYRNAINIGLPLI 99
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
658-726 |
2.59e-07 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 51.67 E-value: 2.59e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27806769 658 VVIGDENYGEGSSREHA--ALEprHLGGRAIITKSFARIHETNLKKQGLLPLTfADPADYNKI------HPVDKLTI 726
Cdd:PRK01641 70 ILLAGDNFGCGSSREHApwALA--DYGFRAVIAPSFADIFYNNCFKNGLLPIV-LPEEDVDELfklveaNPGAELTV 143
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
326-505 |
3.35e-07 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 54.03 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 326 LVPDSGCHYDQLIEINLSELK-PHINGPFTPDLAHPVAEVGsvAEKegwpldIRVGLIGSC-TNssyedMGRSAAVAKQA 403
Cdd:PRK09238 647 LEADADAEYAAVIEIDLAEIKePILACPNDPDDVRLLSEVA--GTK------IDEVFIGSCmTN-----IGHFRAAGKLL 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806769 404 LAHGLQCKSQFTITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIGQWDRkdIKKGEknTIVTSYNRNFTGR--ND 481
Cdd:PRK09238 714 EGKKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMGNQAR--VADGA--TVFSTSTRNFPNRlgKG 789
|
170 180
....*....|....*....|....
gi 27806769 482 ANpethAFVTSPEIVTALAIAGTL 505
Cdd:PRK09238 790 AN----VYLGSAELAAVCALLGRI 809
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
658-694 |
2.15e-05 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 46.78 E-value: 2.15e-05
10 20 30
....*....|....*....|....*....|....*..
gi 27806769 658 VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARI 694
Cdd:PLN00072 132 IIIGGENFGCGSSREHAPVALGAAGAKAVVAESYARI 168
|
|
|