|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
8-422 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 577.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 8 PQTMAEKILSRRGTQVVYAGDLAVVEVDQVMVVDSIAQSFIQRMQQDLNATPKYPERVSIVIDHVAPASTVSVAQAQKEA 87
Cdd:PRK00402 2 GMTLAEKILARHSGRDVSPGDIVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVIVFDHFVPAKDIKSAEQQKIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 88 REYAAQTGVR-LFDVGRGICHQVLMEEGLARPGWIVLGSDSHSTTYGAVAAFGSGMGATDIALAAASGKTWLKVPDSVKV 166
Cdd:PRK00402 82 REFAKEQGIPnFFDVGEGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKTWFKVPETIKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 167 TFTGDLRPGVTAKDVALEMIRRLGADGATYQSIEMH--AGDRFTRGERMTLANLCVEAGAKAGLVVPGGEI---LTAYGY 241
Cdd:PRK00402 162 VLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTgeTIEALSMDERMTLANMAIEAGAKAGIFAPDEKTleyLKERAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 242 DIPEWVYPDEGATYVQSIEIDLATLNPRMSAPSEVDNVFDVaqlrEELRDQHVDQVFIGTCTNGRIEDLHAAAEVLRGRR 321
Cdd:PRK00402 242 RDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPV----SEVEGTKVDQVFIGSCTNGRLEDLRIAAEILKGRK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 322 VAPGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGRHQGVLAPGEVCVSTSNRNFIGRMGDKDARIYLA 401
Cdd:PRK00402 318 VAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGSPESEVYLA 397
|
410 420
....*....|....*....|.
gi 1906333327 402 SPAVAAATAVMGRVALPEDVL 422
Cdd:PRK00402 398 SPAVAAASAVTGKITDPREVL 418
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
10-419 |
0e+00 |
|
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: 575.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 10 TMAEKILSRRGTQVVYAGDLAVVEVDQVMVVDSIAQSFIQRMQQDLNATPKYPERVSIVIDHVAPASTVSVAQAQKEARE 89
Cdd:TIGR01343 1 TIAEKILSKKSGKEVYAGDLIEAEIDLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIVFDHQVPADTIKAAEMQKLARE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 90 YAAQTGVR-LFDVGRGICHQVLMEEGLARPGWIVLGSDSHSTTYGAVAAFGSGMGATDIALAAASGKTWLKVPDSVKVTF 168
Cdd:TIGR01343 81 FVKKQGIKyFYDVGEGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFKVPETIRVNI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 169 TGDLRPGVTAKDVALEMIRRLGADGATYQSIEMHAG--DRFTRGERMTLANLCVEAGAKAGLVVPGGEILT--AYGYDIP 244
Cdd:TIGR01343 161 TGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGEtvKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQylKERRKEP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 245 EWVYP-DEGATYVQSIEIDLATLNPRMSAPSEVDNVFDVAqlreELRDQHVDQVFIGTCTNGRIEDLHAAAEVLRGRRVA 323
Cdd:TIGR01343 241 FRVYKsDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVS----EVEGTEIDQVFIGSCTNGRLEDLRVAAKILKGRKVA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 324 PGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGRHQGVLAPGEVCVSTSNRNFIGRMGDKDARIYLASP 403
Cdd:TIGR01343 317 PDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMGHPNAEIYLASP 396
|
410
....*....|....*.
gi 1906333327 404 AVAAATAVMGRVALPE 419
Cdd:TIGR01343 397 ATAAASAVKGYIADPR 412
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
8-400 |
9.29e-175 |
|
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: 494.93 E-value: 9.29e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 8 PQTMAEKILSRRGTQVVYAGDLAVVEVDQVMVVDSIAQSFIQRMQQDLNATPKYPERVSIVIDHVAPASTVSVAQAQKEA 87
Cdd:COG0065 2 GMTLAEKILARHAGREVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVAVFDHNVPTKDPKSAEQVKTL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 88 REYAAQTGVRLFDVGR-GICHQVLMEEGLARPGWIVLGSDSHSTTYGAVAAFGSGMGATDIALAAASGKTWLKVPDSVKV 166
Cdd:COG0065 82 REFAKEFGITFFDVGDpGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWFKVPETMRI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 167 TFTGDLRPGVTAKDVALEMIRRLGADGATYQSIEMH--AGDRFTRGERMTLANLCVEAGAKAGLVVPGgEILTAY----G 240
Cdd:COG0065 162 EVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAgeAIRALSMEERMTLCNMAIEAGAKAGIIAPD-ETTFEYlkgrP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 241 YDIPEWVYPDEGATYVQSIEIDLATLNPRMSAPSEVDNVFDVAqlreELRDQHVDQVFIGTCTNGRIEDLHAAAEVLRGR 320
Cdd:COG0065 241 FAPWRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVS----ELEGIKIDQVFIGSCTNGRIEDLRAAAEILKGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 321 RVAPGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGRHQGVLAPGEVCVSTSNRNFIGRMGDKDARIYL 400
Cdd:COG0065 317 KVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGSPGSRTYL 396
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
48-400 |
1.64e-147 |
|
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: 424.29 E-value: 1.64e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 48 IQRMQQDLNATPKYPERVSIVIDHVAPASTVSVAQAQKEAREYAAQTGVRLFDVGR-GICHQVLMEEGLARPGWIVLGSD 126
Cdd:cd01583 13 FEGLREAGREKVWDPEKIVAVFDHNVPTPDIKAAEQVKTLRKFAKEFGINFFDVGRqGICHVILPEKGLTLPGMTIVGGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 127 SHSTTYGAVAAFGSGMGATDIALAAASGKTWLKVPDSVKVTFTGDLRPGVTAKDVALEMIRRLGADGATYQSIEMH--AG 204
Cdd:cd01583 93 SHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGATYKAMEFAgeAI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 205 DRFTRGERMTLANLCVEAGAKAGLVVPGgEILTAY--GYDIPEW--VYPDEGATYVQSIEIDLATLNPRMSAPSEVDNVF 280
Cdd:cd01583 173 ESLSMEERMTLCNMAIEAGAKAGIVAPD-ETTFEYlkGRGKAYWkeLKSDEDAEYDKVVEIDASELEPQVAWPHSPDNVV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 281 DVaqlrEELRDQHVDQVFIGTCTNGRIEDLHAAAEVLRGRRVAPGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTP 360
Cdd:cd01583 252 PV----SEVEGIKIDQVFIGSCTNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPP 327
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1906333327 361 GCGPCMGRHQGVLAPGEVCVSTSNRNFIGRMGDKDARIYL 400
Cdd:cd01583 328 GCGACLGGHMGVLAPGERCVSTSNRNFKGRMGSPGARIYL 367
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
10-400 |
3.68e-118 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 350.98 E-value: 3.68e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 10 TMAEKILSRRGTQVVYAGDLAVVEVDQVMVVDSIAQSFIQRMQQdLNATPKYPERVSIVIDHVAPASTVSVAQAQKEARE 89
Cdd:NF040615 2 TLAEKILSKKLGKEVYAGDTVEVDVDLAMTHDGTTPLTYKAFKE-ISDKVWDNEKIVIVFDHNVPANTVKAANMQKITRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 90 YAAQTGVRLFDV-GRGICHQVLMEEGLARPGWIVLGSDSHSTTYGAVAAFGSGMGATDIALAAASGKTWLKVPDSVKVTF 168
Cdd:NF040615 81 FVKEQGIKNFYLgGEGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVNI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 169 TGdLRPGVTAKDVALEMIRRLGADGATYQSIEM--HAGDRFTRGERMTLANLCVEAGAKAGLVVPGGeilTAYGY----- 241
Cdd:NF040615 161 VG-KNENISGKDIILKVCKEIGRRGATYMAIEYggEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADE---ITYEYlrkeg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 242 ----DIPEW-----VYPDEGATYVQSIEIDLATLNPRMSAPSEVDNVFDVAqlreELRDQHVDQVFIGTCTNGRIEDLHA 312
Cdd:NF040615 237 vseeEIAELkknriTVNEKEENYYKEIEIDITDMEEQVACPHHPDNVKPVS----EVEGTEIDQVFIGSCTNGRLSDLRI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 313 AAEVLRGRRVAPGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGRHQGVLAPGEVCVSTSNRNFIGRMG 392
Cdd:NF040615 313 AAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMG 392
|
....*...
gi 1906333327 393 DKDARIYL 400
Cdd:NF040615 393 NINSYIYL 400
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
65-400 |
2.63e-91 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 283.54 E-value: 2.63e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 65 VSIVIDHVAPASTVSVAQAQKEARE-Y------AAQTGVRLFDVGRGICHQVLMEEGLARPGWIVLGSDSHSTTYGAVAA 137
Cdd:pfam00330 60 TDLVIDHAPDALDKNIEDEISRNKEqYdflewnAKKFGIRFVPPGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 138 FGSGMGATDIALAAASGKTWLKVPDSVKVTFTGDLRPGVTAKDVALEMIRRLGADGATYQSIEmhagdrFTrGE------ 211
Cdd:pfam00330 140 LAFGVGGSEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVE------FF-GPgvrsls 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 212 ---RMTLANLCVEAGAKAGLVVPGGEI---LTAYG---------YD-IPEW--VYPDEGATYVQSIEIDLATLNPRMSAP 273
Cdd:pfam00330 213 megRATICNMAIEYGATAGLFPPDETTfeyLRATGrpeapkgeaYDkAVAWktLASDPGAEYDKVVEIDLSTIEPMVTGP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 274 SEVDNVFDVAQL-------------------------REELRDQHVDQVFIGTCTNGRIEDLHAAAEVLR-----GRRVA 323
Cdd:pfam00330 293 TRPQDAVPLSELvpdpfadavkrkaaeraleymglgpGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVA 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906333327 324 PGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGRhQGVLAPGEVCVSTSNRNFIGRMGdKDARIYL 400
Cdd:pfam00330 373 PGVKASVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGN-SDRLPPGERCVSSSNRNFEGRQG-PGGRTHL 447
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
8-422 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 577.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 8 PQTMAEKILSRRGTQVVYAGDLAVVEVDQVMVVDSIAQSFIQRMQQDLNATPKYPERVSIVIDHVAPASTVSVAQAQKEA 87
Cdd:PRK00402 2 GMTLAEKILARHSGRDVSPGDIVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVIVFDHFVPAKDIKSAEQQKIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 88 REYAAQTGVR-LFDVGRGICHQVLMEEGLARPGWIVLGSDSHSTTYGAVAAFGSGMGATDIALAAASGKTWLKVPDSVKV 166
Cdd:PRK00402 82 REFAKEQGIPnFFDVGEGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKTWFKVPETIKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 167 TFTGDLRPGVTAKDVALEMIRRLGADGATYQSIEMH--AGDRFTRGERMTLANLCVEAGAKAGLVVPGGEI---LTAYGY 241
Cdd:PRK00402 162 VLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTgeTIEALSMDERMTLANMAIEAGAKAGIFAPDEKTleyLKERAG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 242 DIPEWVYPDEGATYVQSIEIDLATLNPRMSAPSEVDNVFDVaqlrEELRDQHVDQVFIGTCTNGRIEDLHAAAEVLRGRR 321
Cdd:PRK00402 242 RDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPV----SEVEGTKVDQVFIGSCTNGRLEDLRIAAEILKGRK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 322 VAPGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGRHQGVLAPGEVCVSTSNRNFIGRMGDKDARIYLA 401
Cdd:PRK00402 318 VAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGSPESEVYLA 397
|
410 420
....*....|....*....|.
gi 1906333327 402 SPAVAAATAVMGRVALPEDVL 422
Cdd:PRK00402 398 SPAVAAASAVTGKITDPREVL 418
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
10-419 |
0e+00 |
|
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: 575.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 10 TMAEKILSRRGTQVVYAGDLAVVEVDQVMVVDSIAQSFIQRMQQDLNATPKYPERVSIVIDHVAPASTVSVAQAQKEARE 89
Cdd:TIGR01343 1 TIAEKILSKKSGKEVYAGDLIEAEIDLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIVFDHQVPADTIKAAEMQKLARE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 90 YAAQTGVR-LFDVGRGICHQVLMEEGLARPGWIVLGSDSHSTTYGAVAAFGSGMGATDIALAAASGKTWLKVPDSVKVTF 168
Cdd:TIGR01343 81 FVKKQGIKyFYDVGEGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFKVPETIRVNI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 169 TGDLRPGVTAKDVALEMIRRLGADGATYQSIEMHAG--DRFTRGERMTLANLCVEAGAKAGLVVPGGEILT--AYGYDIP 244
Cdd:TIGR01343 161 TGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGEtvKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQylKERRKEP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 245 EWVYP-DEGATYVQSIEIDLATLNPRMSAPSEVDNVFDVAqlreELRDQHVDQVFIGTCTNGRIEDLHAAAEVLRGRRVA 323
Cdd:TIGR01343 241 FRVYKsDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVS----EVEGTEIDQVFIGSCTNGRLEDLRVAAKILKGRKVA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 324 PGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGRHQGVLAPGEVCVSTSNRNFIGRMGDKDARIYLASP 403
Cdd:TIGR01343 317 PDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMGHPNAEIYLASP 396
|
410
....*....|....*.
gi 1906333327 404 AVAAATAVMGRVALPE 419
Cdd:TIGR01343 397 ATAAASAVKGYIADPR 412
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
9-420 |
4.56e-177 |
|
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA family (Homoaconitate hydratase family, TIGR01343) and is most closely related to the 3-isopropylmalate dehydratase, large subunits which form TIGR00170. This subfamily includes the members of TIGR01343 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: 273960 Cd Length: 413 Bit Score: 500.44 E-value: 4.56e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 9 QTMAEKILSRRGTQVVYAGDLAVVEVDQVMVVDSIAQSFIQRMQQDLNATPKYPERVSIVIDHVAPASTVSVAQAQKEAR 88
Cdd:TIGR02086 1 MTLAEKILSEKVGRPVCAGEIVEVEVDLAMTHDGTGPLAIKALRELGVARVWDPEKIVIAFDHNVPPPTVEAAEMQKEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 89 EYAAQTGVRLFDVGRGICHQVLMEEGLARPGWIVLGSDSHSTTYGAVAAFGSGMGATDIALAAASGKTWLKVPDSVKVTF 168
Cdd:TIGR02086 81 EFAKRHGIKNFDVGEGICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTWIKVPETIRVVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 169 TGDLRPGVTAKDVALEMIRRLGADGATYQSIEMHAGD--RFTRGERMTLANLCVEAGAKAGLVVPGGEI---LTAYGYDI 243
Cdd:TIGR02086 161 EGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPieNMDMDGRLTLCNMAVEMGAKAGIIEPDEETyeyLKKRRGLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 244 PEWVYPDEGATYVQSIEIDLATLNPRMSAPSEVDNVFDVaqlrEELRDQHVDQVFIGTCTNGRIEDLHAAAEVLRGRRVA 323
Cdd:TIGR02086 241 FRILVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPV----SDVEGTEIDQVFIGSCTNGRLEDLRIAAEILKGRRVH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 324 PGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGRHQGVLAPGEVCVSTSNRNFIGRMGDKDARIYLASP 403
Cdd:TIGR02086 317 PDVRLIVIPASRKVYLRALEEGIILTLVRAGAMICPPGCGPCLGAHMGVLGDGEVCLSTTNRNFKGRMGSPNAEIYLASP 396
|
410
....*....|....*..
gi 1906333327 404 AVAAATAVMGRVALPED 420
Cdd:TIGR02086 397 ATAAASAVEGYITDPED 413
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
8-400 |
9.29e-175 |
|
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: 494.93 E-value: 9.29e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 8 PQTMAEKILSRRGTQVVYAGDLAVVEVDQVMVVDSIAQSFIQRMQQDLNATPKYPERVSIVIDHVAPASTVSVAQAQKEA 87
Cdd:COG0065 2 GMTLAEKILARHAGREVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVAVFDHNVPTKDPKSAEQVKTL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 88 REYAAQTGVRLFDVGR-GICHQVLMEEGLARPGWIVLGSDSHSTTYGAVAAFGSGMGATDIALAAASGKTWLKVPDSVKV 166
Cdd:COG0065 82 REFAKEFGITFFDVGDpGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWFKVPETMRI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 167 TFTGDLRPGVTAKDVALEMIRRLGADGATYQSIEMH--AGDRFTRGERMTLANLCVEAGAKAGLVVPGgEILTAY----G 240
Cdd:COG0065 162 EVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAgeAIRALSMEERMTLCNMAIEAGAKAGIIAPD-ETTFEYlkgrP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 241 YDIPEWVYPDEGATYVQSIEIDLATLNPRMSAPSEVDNVFDVAqlreELRDQHVDQVFIGTCTNGRIEDLHAAAEVLRGR 320
Cdd:COG0065 241 FAPWRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVS----ELEGIKIDQVFIGSCTNGRIEDLRAAAEILKGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 321 RVAPGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGRHQGVLAPGEVCVSTSNRNFIGRMGDKDARIYL 400
Cdd:COG0065 317 KVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGSPGSRTYL 396
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
48-400 |
1.64e-147 |
|
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: 424.29 E-value: 1.64e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 48 IQRMQQDLNATPKYPERVSIVIDHVAPASTVSVAQAQKEAREYAAQTGVRLFDVGR-GICHQVLMEEGLARPGWIVLGSD 126
Cdd:cd01583 13 FEGLREAGREKVWDPEKIVAVFDHNVPTPDIKAAEQVKTLRKFAKEFGINFFDVGRqGICHVILPEKGLTLPGMTIVGGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 127 SHSTTYGAVAAFGSGMGATDIALAAASGKTWLKVPDSVKVTFTGDLRPGVTAKDVALEMIRRLGADGATYQSIEMH--AG 204
Cdd:cd01583 93 SHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDGATYKAMEFAgeAI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 205 DRFTRGERMTLANLCVEAGAKAGLVVPGgEILTAY--GYDIPEW--VYPDEGATYVQSIEIDLATLNPRMSAPSEVDNVF 280
Cdd:cd01583 173 ESLSMEERMTLCNMAIEAGAKAGIVAPD-ETTFEYlkGRGKAYWkeLKSDEDAEYDKVVEIDASELEPQVAWPHSPDNVV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 281 DVaqlrEELRDQHVDQVFIGTCTNGRIEDLHAAAEVLRGRRVAPGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTP 360
Cdd:cd01583 252 PV----SEVEGIKIDQVFIGSCTNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPP 327
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1906333327 361 GCGPCMGRHQGVLAPGEVCVSTSNRNFIGRMGDKDARIYL 400
Cdd:cd01583 328 GCGACLGGHMGVLAPGERCVSTSNRNFKGRMGSPGARIYL 367
|
|
| LEU2 |
TIGR02083 |
3-isopropylmalate dehydratase, large subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
10-421 |
1.44e-121 |
|
3-isopropylmalate dehydratase, large subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. These homologs are described by a separate model of subfamily (rather than equivalog) homology type (TIGR01343). This model along with TIGR00170 describe clades which consist only of LeuC sequences. Here, the genes from Pyrococcus furiosus, Clostridium acetobutylicum, Thermotoga maritima and others are gene clustered with related genes from the leucine biosynthesis pathway. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 131138 Cd Length: 419 Bit Score: 359.90 E-value: 1.44e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 10 TMAEKILSRR-GTQVVYAGDLAVVEVDQVMVVDSIAQSFIQRMQQDLNATPKYPERVSIVIDHVAPASTVSVAQAQKEAR 88
Cdd:TIGR02083 2 TMAEKILAQHaGLESVEPGELILAKLDIVLGNDITTPLAIKAFKEYGGKKVFDPDRVALVPDHFTPNKDIKSAEQCKMMR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 89 EYAAQTGVR-LFDVGR-GICHQVLMEEGLARPGWIVLGSDSHSTTYGAVAAFGSGMGATDIALAAASGKTWLKVPDSVKV 166
Cdd:TIGR02083 82 EFAREQGIEkFFEIGNmGIEHALLPEEGIVKPGDLIIGADSHTCTYGALGAFATGVGSTDMAVGMATGKAWFRVPEAIKF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 167 TFTGDLRPGVTAKDVALEMIRRLGADGATYQSIEMhAGD---RFTRGERMTLANLCVEAGAKAGLVvPGGEILTAY--GY 241
Cdd:TIGR02083 162 VLKGKLKPWVTGKDLILHIIGIIGVDGALYKSMEF-SGEglkELSMDDRFTIANMAIEAGAKTGIF-PVDEITIEYekGR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 242 DIPEW-VYP-DEGATYVQSIEIDLATLNPRMSAPSEVDNVFDVAQLREElrDQHVDQVFIGTCTNGRIEDLHAAAEVLRG 319
Cdd:TIGR02083 240 GKREEkIYKaDEDAKYVRVIEIDLSELEPQVAFPHLPENTKDISEAGKE--EIKIDQVVIGSCTNGRLEDLRLAAEILKG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 320 RRVAPGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGRHQGVLAPGEVCVSTSNRNFIGRMGDKDARIY 399
Cdd:TIGR02083 318 KTVAPDVRCIIIPGSQNVYLEAMKEGLLEIFIEAGAVVSTPTCGPCLGGHMGILAEGERAISTTNRNFVGRMGHPKSEVY 397
|
410 420
....*....|....*....|..
gi 1906333327 400 LASPAVAAATAVMGRVALPEDV 421
Cdd:TIGR02083 398 LASPAVAAASAIKGYIASPEEV 419
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
10-400 |
3.68e-118 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 350.98 E-value: 3.68e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 10 TMAEKILSRRGTQVVYAGDLAVVEVDQVMVVDSIAQSFIQRMQQdLNATPKYPERVSIVIDHVAPASTVSVAQAQKEARE 89
Cdd:NF040615 2 TLAEKILSKKLGKEVYAGDTVEVDVDLAMTHDGTTPLTYKAFKE-ISDKVWDNEKIVIVFDHNVPANTVKAANMQKITRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 90 YAAQTGVRLFDV-GRGICHQVLMEEGLARPGWIVLGSDSHSTTYGAVAAFGSGMGATDIALAAASGKTWLKVPDSVKVTF 168
Cdd:NF040615 81 FVKEQGIKNFYLgGEGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVNI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 169 TGdLRPGVTAKDVALEMIRRLGADGATYQSIEM--HAGDRFTRGERMTLANLCVEAGAKAGLVVPGGeilTAYGY----- 241
Cdd:NF040615 161 VG-KNENISGKDIILKVCKEIGRRGATYMAIEYggEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADE---ITYEYlrkeg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 242 ----DIPEW-----VYPDEGATYVQSIEIDLATLNPRMSAPSEVDNVFDVAqlreELRDQHVDQVFIGTCTNGRIEDLHA 312
Cdd:NF040615 237 vseeEIAELkknriTVNEKEENYYKEIEIDITDMEEQVACPHHPDNVKPVS----EVEGTEIDQVFIGSCTNGRLSDLRI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 313 AAEVLRGRRVAPGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGRHQGVLAPGEVCVSTSNRNFIGRMG 392
Cdd:NF040615 313 AAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMG 392
|
....*...
gi 1906333327 393 DKDARIYL 400
Cdd:NF040615 393 NINSYIYL 400
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
65-400 |
2.63e-91 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 283.54 E-value: 2.63e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 65 VSIVIDHVAPASTVSVAQAQKEARE-Y------AAQTGVRLFDVGRGICHQVLMEEGLARPGWIVLGSDSHSTTYGAVAA 137
Cdd:pfam00330 60 TDLVIDHAPDALDKNIEDEISRNKEqYdflewnAKKFGIRFVPPGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 138 FGSGMGATDIALAAASGKTWLKVPDSVKVTFTGDLRPGVTAKDVALEMIRRLGADGATYQSIEmhagdrFTrGE------ 211
Cdd:pfam00330 140 LAFGVGGSEAEHVLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVE------FF-GPgvrsls 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 212 ---RMTLANLCVEAGAKAGLVVPGGEI---LTAYG---------YD-IPEW--VYPDEGATYVQSIEIDLATLNPRMSAP 273
Cdd:pfam00330 213 megRATICNMAIEYGATAGLFPPDETTfeyLRATGrpeapkgeaYDkAVAWktLASDPGAEYDKVVEIDLSTIEPMVTGP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 274 SEVDNVFDVAQL-------------------------REELRDQHVDQVFIGTCTNGRIEDLHAAAEVLR-----GRRVA 323
Cdd:pfam00330 293 TRPQDAVPLSELvpdpfadavkrkaaeraleymglgpGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVA 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1906333327 324 PGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGRhQGVLAPGEVCVSTSNRNFIGRMGdKDARIYL 400
Cdd:pfam00330 373 PGVKASVVPGSEVVRAYAEAEGLDKILEEAGFEWRGPGCSMCIGN-SDRLPPGERCVSSSNRNFEGRQG-PGGRTHL 447
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
62-400 |
8.58e-84 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 264.46 E-value: 8.58e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 62 PERVSIVIDHVAP-------ASTVSVAQAQKEA-REYAAQTGVRLFDVG---RGICHQVLMEEGLARPGWIVLGSDSHST 130
Cdd:PRK12466 55 PDLTLAVVDHVVPtrpgrdrGITDPGGALQVDYlRENCADFGIRLFDVDdprQGIVHVVAPELGLTLPGMVIVCGDSHTT 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 131 TYGAVAAFGSGMGATDIALAAASGKTWLKVPDSVKVTFTGDLRPGVTAKDVALEMIRRLGADGATYQSIEmHAG---DRF 207
Cdd:PRK12466 135 TYGALGALAFGIGTSEVEHVLATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIE-FAGeaiRAL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 208 TRGERMTLANLCVEAGAKAGLVVPgGEILTAYGYDIP-------------EW--VYPDEGATYVQSIEIDLATLNPRMS- 271
Cdd:PRK12466 214 SMEGRMTLCNMAVEAGARGGLIAP-DETTFDYLRGRPrapkgalwdaalaYWrtLRSDADAVFDREVEIDAADIAPQVTw 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 272 --APSEV----DNVFDVAQLREELRDQH--------------------VDQVFIGTCTNGRIEDLHAAAEVLRGRRVAPG 325
Cdd:PRK12466 293 gtSPDQAvpitGRVPDPAAEADPARRAAmeraldymgltpgtplagipIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPG 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1906333327 326 TRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGRHQGVLAPGEVCVSTSNRNFIGRMGdKDARIYL 400
Cdd:PRK12466 373 VRAMVVPGSGAVRRQAEAEGLARIFIAAGFEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQG-PGARTHL 446
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
62-400 |
5.77e-81 |
|
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: 254.73 E-value: 5.77e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 62 PERVSIVIDHVAPASTVSVAQAQKEAREYAAQTGVRLFDVGRGICHQvLMEEGLARPGWIVLGSDSHSTTYGAVAAFGSG 141
Cdd:cd01351 28 PSQIACVHDHAVQLEKPVNNEGHKFLSFFAALQGIAFYRPGVGIIHQ-IMVENLALPGDLLVGSDSHTTSYGGLGAISTG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 142 MGATDIALAAASGKTWLKVPDSVKVTFTGDLRPGVTAKDVALEMIRRLGADGATYQSIEMH--AGDRFTRGERMTLANLC 219
Cdd:cd01351 107 AGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYgeGVSSLSIEDRLTICNMM 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 220 VEAGAKAGLVVPGGEILTAY-----------GYDIPEWVYPDEGATYVQSIEIDLATLNPRMSAPSEVDNVFDVAQLREE 288
Cdd:cd01351 187 AELGATTGIFPEDKTTLKWLeatgrpllknlWLAFPEELLADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSEVEGT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 289 LrdqhVDQVFIGTCTNGRIEDLHAAAEVLRGRRVAPGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGR 368
Cdd:cd01351 267 K----IDQVLIGSCTNNRYSDMLAAAKLLKGAKVAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGN 342
|
330 340 350
....*....|....*....|....*....|..
gi 1906333327 369 HQGVLAPGEVCVSTSNRNFIGRMGDKDARIYL 400
Cdd:cd01351 343 GARLVADGEVGVSSGNRNFPGRLGTYERHVYL 374
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
102-400 |
6.09e-73 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 240.82 E-value: 6.09e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 102 GRGICHQVLMEEgLARPGWIVLGSDSHSTTYGAVAAFGSGMGATDIALAAASGKTWLKVPDSVKVTFTGDLRPGVTAKDV 181
Cdd:PRK07229 96 GNGICHQVHLER-FAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 182 ALEMIRRLGADGATYQSIEMHaGDrftrG-------ERMTLANLCVEAGAKAGlVVPGGEILTAY------GYDIPEwVY 248
Cdd:PRK07229 175 ILELLRRLTVKGGVGKIIEYF-GP----GvatlsvpERATITNMGAELGATTS-IFPSDERTREFlkaqgrEDDWVE-LL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 249 PDEGATYVQSIEIDLATLNPRMSAPSEVDNVFDVAqlreELRDQHVDQVFIGTCTNGRIEDLHAAAEVLRGRRVAPGTRL 328
Cdd:PRK07229 248 ADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVS----EVAGIKVDQVLIGSCTNSSYEDLMRAASILKGKKVHPKVSL 323
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1906333327 329 LVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGRHQgvlAPGE--VCVSTSNRNFIGRMGDKDARIYL 400
Cdd:PRK07229 324 VINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMGQ---APATgnVSLRTFNRNFPGRSGTKDAQVYL 394
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
58-400 |
6.55e-73 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 236.17 E-value: 6.55e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 58 TPKYPERVSIVIDHVAPASTVS------VAQAQKEA-REYAAQTGVRLFDVG---RGICHQVLMEEGLARPGW-IVLGsD 126
Cdd:PRK05478 50 KVRRPDLTFATMDHNVPTTDRDlpiadpVSRIQVETlEKNCKEFGITLFDLGdprQGIVHVVGPEQGLTLPGMtIVCG-D 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 127 SHSTTYGAVAAFGSGMGATDIALAAASGKTWLKVPDSVKVTFTGDLRPGVTAKDVALEMIRRLGADGATYQSIEmHAGDR 206
Cdd:PRK05478 129 SHTSTHGAFGALAFGIGTSEVEHVLATQTLLQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIE-FAGEA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 207 FtRG----ERMTLANLCVEAGAKAGLVVPGgEILTAY---------GYD----IPEW--VYPDEGATYVQSIEIDLATL- 266
Cdd:PRK05478 208 I-RAlsmeGRMTICNMSIEAGARAGLVAPD-ETTFEYlkgrpfapkGEDwdkaVAYWktLKSDEDAVFDKVVTLDAADIe 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 267 -------NPRMSAP---------SEVDNVFDVAQLR----------EELRDQHVDQVFIGTCTNGRIEDLHAAAEVLRGR 320
Cdd:PRK05478 286 pqvtwgtNPGQVISidgkvpdpeDFADPVKRASAERalaymglkpgTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGR 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 321 RVAPGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGRHQGVLAPGEVCVSTSNRNFIGRMGdKDARIYL 400
Cdd:PRK05478 366 KVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQG-KGGRTHL 444
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
88-400 |
1.58e-71 |
|
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: 230.03 E-value: 1.58e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 88 REYAAQTGVRLFDVGRGICHQVLMEEgLARPGWIVLGSDSHSTTYGAVAAFGSGMGATDIALAAASGKTWLKVPDSVKVT 167
Cdd:cd01585 53 QTVAARYGIYFSRPGNGICHQVHLER-FAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 168 FTGDLRPGVTAKDVALEMIRRLGADGATYQSIEmHAGD---RFTRGERMTLANLCVEAGAKAGlVVPGGEI----LTAYG 240
Cdd:cd01585 132 LTGELPPWVTAKDVILELLRRLTVKGGVGKIFE-YTGPgvaTLSVPERATITNMGAELGATTS-IFPSDERtrefLAAQG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 241 YDiPEWV--YPDEGATYVQSIEIDLATLNPRMSAPSEVDNVFDVAqlreELRDQHVDQVFIGTCTNGRIEDLHAAAEVLR 318
Cdd:cd01585 210 RE-DDWVelAADADAEYDEEIEIDLSELEPLIARPHSPDNVVPVR----EVAGIKVDQVAIGSCTNSSYEDLMTVAAILK 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 319 GRRVAPGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGRHQgVLAPGEVCVSTSNRNFIGRMGDKDARI 398
Cdd:cd01585 285 GRRVHPHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQ-APPTGGVSVRTFNRNFEGRSGTKDDLV 363
|
..
gi 1906333327 399 YL 400
Cdd:cd01585 364 YL 365
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
62-415 |
2.23e-68 |
|
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: 221.33 E-value: 2.23e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 62 PERVSIVIDHVAPASTVSVAQAQKEAREYAAQTGVRLFDVGRGICHQVLMEEGLARPGWIVLGSDSHSTTYGAVAAFGSG 141
Cdd:cd01582 26 PDQIVMTLDHDVQNKSEKNLKKYKNIESFAKKHGIDFYPAGRGIGHQIMIEEGYAFPGTLAVASDSHSNMYGGVGCLGTP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 142 MGATDIALAAASGKTWLKVPDSVKVTFTGDLRPGVTAKDVALEMIRRLGADGATYQSIEMHAG--DRFTRGERMTLANLC 219
Cdd:cd01582 106 IVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQVLNHAIEFTGSglNSLSVDTRLTIANMT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 220 VEAGAKAGLvvpggeiltaygydipewvYPdegaTYVQSIEIDLATLNPRMSAPSEVDNVFDVAQLreELRDQHVDQVFI 299
Cdd:cd01582 186 TEWGALSGL-------------------FP----TDAKHLILDLSTLSPYVSGPNSVKVSTPLKEL--EAQNIKINKAYL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 300 GTCTNGRIEDLHAAAEVLRGRR-------VAPGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGRHQGV 372
Cdd:cd01582 241 VSCTNSRASDIAAAADVVKGKKekngkipVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQGL 320
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1906333327 373 LAPGEVCVSTSNRNFIGRMGDKDARIYLASPAVAAATAVMGRV 415
Cdd:cd01582 321 LEPGEVGISATNRNFKGRMGSTEALAYLASPAVVAASAISGKI 363
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
62-416 |
1.29e-66 |
|
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate dehydratase, large subunit, or the large subunit domain of single-chain forms. Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. These homologs are now described by a separate model of subfamily (rather than equivalog) homology type, and the priors and cutoffs for this model have been changed to focus this equivalog family more narrowly. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 272940 Cd Length: 465 Bit Score: 219.73 E-value: 1.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 62 PERVSIVIDHVAPASTVSVAQAQKEAR-------EYAAQTGVRLFDVG---RGICHQVLMEEGLARPGWIVLGSDSHSTT 131
Cdd:TIGR00170 54 PQKTFATMDHNIPTQNRDFNIKDEVAKiqvteleKNCKEFGVRLFDLHsvdQGIVHVMGPEQGLTLPGMTIVCGDSHTST 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 132 YGAVAAFGSGMGATDIALAAASGKTWLKVPDSVKVTFTGDLRPGVTAKDVALEMIRRLGADGATYQSIEmHAGDRF---T 208
Cdd:TIGR00170 134 HGAFGALAFGIGTSEVEHVLATQTLKQARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIE-FCGEAIrdlS 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 209 RGERMTLANLCVEAGAKAGLVVPG--------GEILTAYGYD----IPEW--VYPDEGATYVQSIEIDLATLNPRMS--- 271
Cdd:TIGR00170 213 MEGRMTVCNMAIEAGARAGLIAPDettfeyckGRPHAPKGKEfdkaVAYWktLKTDEGAVFDTVITLEANDISPQVTwgt 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 272 APSEV----DNVFDVAQLREE--------------------LRDQHVDQVFIGTCTNGRIEDLHAAAEVLRGRRVAPGTR 327
Cdd:TIGR00170 293 NPGQVlpvnSEVPDPESFADPvdkasaeralaymglepgtpLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVK 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 328 LLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGRHQGVLAPGEVCVSTSNRNFIGRMGdKDARIYLASPAVAA 407
Cdd:TIGR00170 373 ALVVPGSGLVKLQAEKEGLDKIFIEAGFEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQG-RGGRTHLVSPAMAA 451
|
....*....
gi 1906333327 408 ATAVMGRVA 416
Cdd:TIGR00170 452 AAAIHGHFV 460
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
102-415 |
1.88e-38 |
|
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: 143.79 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 102 GRGICHQVLMEEGLarPGWIVLGSDSHsTTYGAVAAFGSGMGAtdIALAAASGKTWLKVPDSVKVTFTGDLRPGVTAKDV 181
Cdd:cd01581 92 GDGVIHSWLNRMLL--PDTVGTGGDSH-TRFPIGISFPAGSGL--VAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 182 A----LEMIRRLGADGATYQS--------IEMHAGDRFTRGERMTLANLCVEAGAKAGLVVPGGEILTAY---------- 239
Cdd:cd01581 167 VnaipYYAIQQGLLTVEKKGKknvfngriLEIEGLPDLKVEQAFELTDASAERSAAACTVRLDKEPVIEYlesnvvlmki 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 240 ----GYDIP-----------EWV------YPDEGATYVQSIEIDLATLN-PRMSAPSEVDNVfdvaQLREELRDQHVDQV 297
Cdd:cd01581 247 mianGYDDArtllrriiameEWLanppllEPDADAEYAAVIEIDLDDIKePILACPNDPDDV----KLLSEVAGKKIDEV 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 298 FIGTC-TNgrIEDLHAAAEVLRGRRVAPgTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGrHQGVLAPG 376
Cdd:cd01581 323 FIGSCmTN--IGHFRAAAKILRGKEFKP-TRLWVAPPTRMDWAILQEEGYYSIFGDAGARTEMPGCSLCMG-NQARVADG 398
|
330 340 350
....*....|....*....|....*....|....*....
gi 1906333327 377 EVCVSTSNRNFIGRMGdKDARIYLASPAVAAATAVMGRV 415
Cdd:cd01581 399 ATVFSTSTRNFDNRVG-KGAEVYLGSAELAAVCALLGRI 436
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
95-400 |
6.06e-36 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 140.70 E-value: 6.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 95 GVRLFDvGRGICHQVLMEEGLarPGWIVLGSDSHsTTYGAVAAFGSGMGAtdIALAAASGKTWLKVPDSVKVTFTGDLRP 174
Cdd:PRK09238 458 GVSLRP-GDGVIHSWLNRMLL--PDTVGTGGDSH-TRFPIGISFPAGSGL--VAFAAATGVMPLDMPESVLVRFKGEMQP 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 175 GVTAKDVA----LEMIRR--LGADGATYQSI------EMHAGDRFTRGERMTLANLCVEAGAKAGLVVPGGEILTAY--- 239
Cdd:PRK09238 532 GITLRDLVhaipYYAIKQglLTVEKKGKKNIfsgrilEIEGLPDLKVEQAFELTDASAERSAAGCTIKLSKEPIIEYlrs 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 240 -----------GYD-----------IPEWV------YPDEGATYVQSIEIDLATLN-PRMSAPSEVDnvfDVAQLREELR 290
Cdd:PRK09238 612 nivllkwmiaeGYGdartlerriaaMEEWLanpellEADADAEYAAVIEIDLAEIKePILACPNDPD---DVRLLSEVAG 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 291 DQhVDQVFIGTC-TNgrIEDLHAAAEVLRGRRVAPGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGrH 369
Cdd:PRK09238 689 TK-IDEVFIGSCmTN--IGHFRAAGKLLEGKKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMG-N 764
|
330 340 350
....*....|....*....|....*....|.
gi 1906333327 370 QGVLAPGEVCVSTSNRNFIGRMGdKDARIYL 400
Cdd:PRK09238 765 QARVADGATVFSTSTRNFPNRLG-KGANVYL 794
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
41-390 |
1.34e-32 |
|
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: 127.56 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 41 DSIAQ-SFIQRMQQDLnatPKYPERVSIVIDHVAPAS---TVSVAQAQKEAREY-------AAQTGVRLFDVGRGICHQV 109
Cdd:cd01584 6 DATAQmALLQFMSSGL---PKVAVPSTIHCDHLIEAQvggEKDLKRAKDINKEVydflasaGAKYGIGFWKPGSGIIHQI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 110 LMEEgLARPGWIVLGSDSHSTTYGAVAAFGSGMGATDiALAAASGKTW-LKVPDSVKVTFTGDLRPGVTAKDVALEMIRR 188
Cdd:cd01584 83 VLEN-YAFPGLLMIGTDSHTPNAGGLGGIAIGVGGAD-AVDVMAGIPWeLKCPKVIGVKLTGKLSGWTSPKDVILKVAGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 189 LGADGATYQSIEMHAG--DRFTRGERMTLANLCVEAGAKAGlVVPGGEILTAY--------------GYDIPEwVYPDEG 252
Cdd:cd01584 161 LTVKGGTGAIVEYFGPgvDSLSCTGMGTICNMGAEIGATTS-VFPYNERMKKYlkatgraeiadladEFKDDL-LVADEG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 253 ATYVQSIEIDLATLNPRMSAPSEVDNVFDVAQLREELRDQ----HVDQVFIGTCTNGRIEDLHAAAEVLR---GRRVAPG 325
Cdd:cd01584 239 AEYDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAEKNgwplDLRVGLIGSCTNSSYEDMGRAASIAKqalAHGLKCK 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 326 TRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMG---RHQgvLAPGE--VCVSTSNRNFIGR 390
Cdd:cd01584 319 SIFTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGqwdRKD--IKKGEknTIVTSYNRNFTGR 386
|
|
| acnB |
TIGR00117 |
aconitate hydratase 2; Aconitate hydratase (aconitase) is an enzyme of the TCA cycle. This ... |
53-423 |
6.03e-28 |
|
aconitate hydratase 2; Aconitate hydratase (aconitase) is an enzyme of the TCA cycle. This model describes aconitase 2, AcnB, which has weak similarity to aconitase 1. It is found almost exclusively in the Proteobacteria. [Energy metabolism, TCA cycle]
Pssm-ID: 129223 [Multi-domain] Cd Length: 844 Bit Score: 116.93 E-value: 6.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 53 QDLNATPKYPERVSIVIDHVAPastvsvaqaqkearEYAAQTGVRLFDVGRGICHQVLMEEGLarPGWIVLGSDSHsTTY 132
Cdd:TIGR00117 430 QSFCHTAAYPKPVDVNTHHTLP--------------DFIMNRGGVALRPGDGVIHSWLNRMLL--PDTVGTGGDSH-TRF 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 133 GAVAAFGSGMGAtdIALAAASGKTWLKVPDSVKVTFTGDLRPGVTAKDV-----------ALEMIRRLGA---------- 191
Cdd:TIGR00117 493 PLGISFPAGSGL--VAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLvnaiplyaikqGLLTVEKKGKknvfngrile 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 192 -----DGATYQSIEMH--AGDRFTRGERMTLANLCVEAGAKAGLVVPGGEILTAYG---------------YDIPEWVYP 249
Cdd:TIGR00117 571 ieglpDLKVEQAFELTdaSAERSAAGCTIKLNKEPIIEYLNSNIVLLKWMIAEGYGdrrtlerriqgmekwLANPELLEA 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 250 DEGATYVQSIEIDLATLN-PRMSAPSEVDnvfDVAQLREELRDQhVDQVFIGTC-TNgrIEDLHAAAEVLRGRRVAPGtR 327
Cdd:TIGR00117 651 DADAEYAAVIEIDLAEIKePILAAPNDPD---DVRPLSEVQGDK-IDEVFIGSCmTN--IGHFRAAGKILDAAGQLPT-R 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 328 LLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGrHQGVLAPGEVCVSTSNRNFIGRMGdKDARIYLASPAVAA 407
Cdd:TIGR00117 724 LWVAPPTRMDEQQLTEEGYYSIFGAAGARTEIPGCSLCMG-NQARVADGATVFSTSTRNFPNRMG-TGANVYLGSAELAA 801
|
410
....*....|....*.
gi 1906333327 408 ATAVMGRVALPEDVLA 423
Cdd:TIGR00117 802 VCALLGKIPTPEEYQT 817
|
|
| AcnB |
COG1049 |
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ... |
124-423 |
5.94e-25 |
|
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440670 [Multi-domain] Cd Length: 852 Bit Score: 107.63 E-value: 5.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 124 GSDSHsTTYGAVAAF--GSGMgatdIALAAASGKTWLKVPDSVKVTFTGDLRPGVTAKDVA----LEMIRR--LGADGAT 195
Cdd:COG1049 484 GGDSH-TRFPIGISFpaGSGL----VAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVnaipYYAIKQglLTVEKKG 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 196 YQSI------EMHAgdrftrgermtLANLCVE-------AGAK---AGLVV-----PGGEILT----------AYGY--- 241
Cdd:COG1049 559 KKNIfsgrilEIEG-----------LPDLKVEqafelsdASAErsaAGCTIklskePVIEYLRsniallkwmiAEGYgda 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 242 --------------DIPEWVYPDEGATYVQSIEIDLATLN-PRMSAPSEVDnvfDVAQLREELRDqHVDQVFIGTC-TNg 305
Cdd:COG1049 628 rtlerriaameewlANPELLEADADAEYAAVIEIDLNEIKePILACPNDPD---DVKLLSEVAGT-KIDEVFIGSCmTN- 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 306 rIEDLHAAAEVLRGRRVAPgTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGrHQGVLAPGEVCVSTSNR 385
Cdd:COG1049 703 -IGHFRAAGKLLEGKGNLP-TRLWIAPPTKMDEAQLTEEGYYSIFGAAGARTEMPGCSLCMG-NQARVADGATVFSTSTR 779
|
330 340 350
....*....|....*....|....*....|....*...
gi 1906333327 386 NFIGRMGdKDARIYLASPAVAAATAVMGRVALPEDVLA 423
Cdd:COG1049 780 NFPNRLG-KGANVYLGSAELAAVCALLGRLPTVEEYME 816
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
41-423 |
1.56e-24 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 106.55 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 41 DSIAQSFIQrmqqdlnaTPKYPERVSIVIDHVAPASTVSvaqaqkeareyaaQTGVRLfDVGRGICHQVLMEEGLarPGW 120
Cdd:PLN00094 499 DLVMQSFCH--------TAAYPKPVDVVTHHTLPDFIRN-------------RGGVSL-RPGDGVIHSWLNRMLL--PDT 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 121 IVLGSDSHsTTYGAVAAFGSGMGAtdIALAAASGKTWLKVPDSVKVTFTGDLRPGVTAKDV-------ALEMI------- 186
Cdd:PLN00094 555 VGTGGDSH-TRFPIGISFPAGSGL--VAFGAATGVIPLDMPESVLVRFTGTMQPGITLRDLvhaipytAIQDGlltvekk 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 187 --------RRLGADGATY----QSIEMH--AGDRFTRGERMTLANLCVEAGAKAGLVVPGGEILTAYG------------ 240
Cdd:PLN00094 632 gkknvfsgRILEIEGLPHlkceQAFELSdaSAERSAAGCTIKLDKEPIIEYLNSNVVMLKWMIAEGYGdrrtlerriarm 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 241 ---YDIPEWVYPDEGATYVQSIEIDLATLN-PRMSAPSEVDNvfdvAQLREELRDQHVDQVFIGTC-TNgrIEDLHAAAE 315
Cdd:PLN00094 712 qqwLADPELLEADPDAEYAAVIEIDMDEIKePILCAPNDPDD----ARLLSEVTGDKIDEVFIGSCmTN--IGHFRAAGK 785
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 316 VLRGRRVAPGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGrHQGVLAPGEVCVSTSNRNFIGRMGdKD 395
Cdd:PLN00094 786 LLNDNLSQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPGCSLCMG-NQARVAEKSTVVSTSTRNFPNRLG-KG 863
|
410 420
....*....|....*....|....*...
gi 1906333327 396 ARIYLASPAVAAATAVMGRVALPEDVLA 423
Cdd:PLN00094 864 ANVYLASAELAAVAAILGRLPTVEEYLS 891
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
107-394 |
6.61e-23 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 101.62 E-value: 6.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 107 HQvLMEEGLARPGWIVLGSDSHsTTYGAVA--AFGSGMGATDIALAaasGKTW-LKVPDSVKVTFTGDLRPGVTAKDVAL 183
Cdd:PRK11413 131 HQ-YMREMMAGGGKMILGSDSH-TRYGALGtmAVGEGGGELVKQLL---NDTYdIDYPGVVAVYLTGKPAPGVGPQDVAL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 184 EMIRRLGADGATYQSIEMHAGD-------RFTRG-ERMTLANLCV------EAGAKAGLVVPGGEilTAYgydipEWVYP 249
Cdd:PRK11413 206 AIIGAVFKNGYVKNKVMEFVGPgvsalstDFRNGvDVMTTETTCLssiwqtDEEVHNWLALHGRG--QDY-----CELNP 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 250 DEGATYVQSIEIDLATLNPRMSAPSEVDNVFDVAQLREELRD-----------------------------QHVDQVFIG 300
Cdd:PRK11413 279 QPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDELNQNLTDilreveieservahgkaklslldkiengrLKVQQGIIA 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 301 TCTNGRIEDLHAAAEVLRGRRVAPGT-RLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGrhQG-VLAPGEV 378
Cdd:PRK11413 359 GCSGGNYENVIAAANALRGQSCGNDTfSLSVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFG--AGdTPANNGL 436
|
330
....*....|....*.
gi 1906333327 379 CVSTSNRNFIGRMGDK 394
Cdd:PRK11413 437 SIRHTTRNFPNREGSK 452
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
65-390 |
1.54e-18 |
|
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: 88.24 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 65 VSIVIDHvapastvSVaQAQKEAREYAAQTGVRL---------------------FDV---GRGICHQVLMEEgLARPGW 120
Cdd:COG1048 121 VDLVIDH-------SV-QVDYFGTPDALEKNLELefernreryqflkwgqqafdnFRVvppGTGIVHQVNLEY-LAFVVW 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 121 I-------------VLGSDSHSTTYGAVAAFGSGMGATDiALAAASGKTW-LKVPDSVKVTFTGDLRPGVTAKDVAL--- 183
Cdd:COG1048 192 TreedgetvaypdtLVGTDSHTTMINGLGVLGWGVGGIE-AEAAMLGQPVsMLIPEVVGVKLTGKLPEGVTATDLVLtvt 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 184 EMIRRLGA---------DGATYQSIemhagdrftrGERMTLANLCVEAGAKAGL-------------------VVpggEI 235
Cdd:COG1048 271 EMLRKKGVvgkfveffgPGLASLSL----------ADRATIANMAPEYGATCGFfpvdeetldylrltgrseeQI---EL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 236 LTAYGYDIPEWVYPDEG-ATYVQSIEIDLATLNPRMSAP---------SEVDNVFDvAQLREELRDQHVDQVF------- 298
Cdd:COG1048 338 VEAYAKAQGLWRDPDAPePYYSDVLELDLSTVEPSLAGPkrpqdriplSDLKEAFR-AALAAPVGEELDKPVRvevdgee 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 299 ------------IGTCTNGRIEDLHAAAEVL------RGRRVAPGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVLGTP 360
Cdd:COG1048 417 felghgavviaaITSCTNTSNPSVMIAAGLLakkaveKGLKVKPWVKTSLAPGSKVVTDYLERAGLLPYLEALGFNVVGY 496
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1906333327 361 GCGPCMGR--------HQGVLAPGEVCVS-TS-NRNFIGR 390
Cdd:COG1048 497 GCTTCIGNsgplppeiSEAIEENDLVVAAvLSgNRNFEGR 536
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
59-400 |
2.12e-16 |
|
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: 80.43 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 59 PKYPerVSIVIDH---VAPASTvSVAQAQKEAREY--------------AAQTGVRLFDVGRGICHQVLME--------- 112
Cdd:cd01586 35 PLIP--VDLVIDHsvqVDFYGT-ADALAKNMKLEFernreryeflkwgqKAFKNLRVVPPGTGIIHQVNLEylarvvfts 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 113 ----EGLARPGwIVLGSDSHSTTYGAVAAFGSGMGATDiALAAASGKTW-LKVPDSVKVTFTGDLRPGVTAKDVALEMIR 187
Cdd:cd01586 112 eedgDGVAYPD-SVVGTDSHTTMINGLGVLGWGVGGIE-AEAVMLGQPIsMLLPEVVGVKLTGKLRPGVTATDLVLTVTQ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 188 RLGADGATYQSIEMH--AGDRFTRGERMTLANLCVEAGAKAGLvvpggeiltaYGYDipewvypdegatyVQSIEIDLAT 265
Cdd:cd01586 190 MLRKVGVVGKFVEFFgpGVAKLSVADRATIANMAPEYGATCGF----------FPVD-------------TQVVELDLST 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 266 LNPRMSAPSEvdnvfdvAQLREELrdqHVDQVF--IGTCTN----------GriedLHAAAEVLRGRRVAPGTRLLVIPA 333
Cdd:cd01586 247 VEPSVSGPKR-------PQDRVPL---HGSVVIaaITSCTNtsnpsvmlaaG----LLAKKAVELGLKVKPYVKTSLAPG 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1906333327 334 SSQVMEDAMADGTLLTLQRAGAVLGTPGCGPCMGrHQGVLAP---------GEVCVS--TSNRNFIGRMGDKDARIYL 400
Cdd:cd01586 313 SRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIG-NSGPLPEeveeaikenDLVVAAvlSGNRNFEGRIHPLVRANYL 389
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
92-390 |
4.63e-16 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 80.75 E-value: 4.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 92 AQTGVRLFDVGRGICHQVLMEEgLAR---------PGWIV----LGSDSHSTTYGAVAAFGSGMGATDiALAAASGK-TW 157
Cdd:PRK12881 166 AFDNFRVVPPGTGIMHQVNLEY-LARvvhtkeddgDTVAYpdtlVGTDSHTTMINGIGVLGWGVGGIE-AEAVMLGQpVY 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 158 LKVPDSVKVTFTGDLRPGVTAKDVAL---EMIRRLGADGATyqsIEMHaGD---RFTRGERMTLANLCVEAGAKAGLvVP 231
Cdd:PRK12881 244 MLIPDVVGVELTGKLREGVTATDLVLtvtEMLRKEGVVGKF---VEFF-GEgvaSLTLGDRATIANMAPEYGATMGF-FP 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 232 GGEILTAY----GYDIPE-------------WVYPDEGATYVQSIEIDLATLNPRMSAP---------SEVDNVFD---- 281
Cdd:PRK12881 319 VDEQTLDYlrltGRTEAQialveayakaqglWGDPKAEPRYTRTLELDLSTVAPSLAGPkrpqdrialGNVKSAFSdlfs 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 282 ------------VAQLREELRDQHVDQVFIGTCTNGRIEDLHAAAEVL------RGRRVAPGTRLLVIPASSQVMEDAMA 343
Cdd:PRK12881 399 kpvaengfakkaQTSNGVDLPDGAVAIAAITSCTNTSNPSVLIAAGLLakkaveRGLTVKPWVKTSLAPGSKVVTEYLER 478
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1906333327 344 DGTLLTLQRAGAVLGTPGCGPCMGR--------HQGVLAPGEVCVS--TSNRNFIGR 390
Cdd:PRK12881 479 AGLLPYLEKLGFGIVGYGCTTCIGNsgpltpeiEQAITKNDLVAAAvlSGNRNFEGR 535
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
65-274 |
2.50e-12 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 69.00 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 65 VSIVIDHvapasTVSV-------AQAQKEAREYA-----------AQTGVRLFDV---GRGICHQVLME----------- 112
Cdd:PRK09277 124 VDLVIDH-----SVQVdyfgtpdAFEKNVELEFErneeryqflkwGQKAFDNFRVvppGTGICHQVNLEylapvvwtred 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 113 -EGLARPGWIVlGSDSHSTTYGAVAAFGSGMGATDiALAAASGK-TWLKVPDSVKVTFTGDLRPGVTAKDVAL---EMIR 187
Cdd:PRK09277 199 gELVAYPDTLV-GTDSHTTMINGLGVLGWGVGGIE-AEAAMLGQpSSMLIPEVVGVKLTGKLPEGVTATDLVLtvtEMLR 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 188 RLGA---------DGATYQSIemhagdrftrGERMTLANLCVEAGAKAGLvVPGGEILTAY----GYDIPE--------- 245
Cdd:PRK09277 277 KKGVvgkfveffgEGLASLSL----------ADRATIANMAPEYGATCGF-FPIDEETLDYlrltGRDEEQvalveayak 345
|
250 260 270
....*....|....*....|....*....|...
gi 1906333327 246 ----WVYPDEGATYVQSIEIDLATLNPRMSAPS 274
Cdd:PRK09277 346 aqglWRDPLEEPVYTDVLELDLSTVEPSLAGPK 378
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
47-390 |
2.58e-09 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 59.26 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 47 FIQRMQQDLNA-TPKYPerVSIVIDHVAPA--STVSVAQAQKEAREYAAQT--------GVRLFD------VGRGICHQV 109
Cdd:PTZ00092 113 AMKRLGGDPAKiNPLVP--VDLVIDHSVQVdfSRSPDALELNQEIEFERNLerfeflkwGSKAFKnllivpPGSGIVHQV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 110 LME---------EGLARPGWIVlGSDSHSTTYGAVAAFGSGMGATDiALAAASGKTWLKV-PDSVKVTFTGDLRPGVTAK 179
Cdd:PTZ00092 191 NLEylarvvfnkDGLLYPDSVV-GTDSHTTMINGLGVLGWGVGGIE-AEAVMLGQPISMVlPEVVGFKLTGKLSEHVTAT 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 180 DVAL---EMIRRLGADGatyQSIEMHAG--DRFTRGERMTLANLCVEAGAKAG-----------LVVPGG-----EILTA 238
Cdd:PTZ00092 269 DLVLtvtSMLRKRGVVG---KFVEFYGPgvKTLSLADRATIANMAPEYGATMGffpidektldyLKQTGRseekvELIEK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 239 YGYDIPEWVYPDEGATYVQSIEIDLATLNPRMSAPSEV-DNVF--DVAQ----------------LREELRDQHVDQVF- 298
Cdd:PTZ00092 346 YLKANGLFRTYAEQIEYSDVLELDLSTVVPSVAGPKRPhDRVPlsDLKKdftaclsapvgfkgfgIPEEKHEKKVKFTYk 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 299 ---------------IGTCTNGRIEDLHAAAEVL------RGRRVAPGTRLLVIPASSQVMEDAMADGTLLTLQRAGAVL 357
Cdd:PTZ00092 426 gkeytlthgsvviaaITSCTNTSNPSVMLAAGLLakkaveKGLKVPPYIKTSLSPGSKVVTKYLEASGLLKYLEKLGFYT 505
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1906333327 358 GTPGCGPCMGrHQGVLAPgEV--CVS----------TSNRNFIGR 390
Cdd:PTZ00092 506 AGYGCMTCIG-NSGDLDP-EVseAITnndlvaaavlSGNRNFEGR 548
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
102-227 |
2.54e-08 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 56.35 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1906333327 102 GRGICHQVLME---------EGLARPGWIVlGSDSHSTTYGAVAAFGSGMGATDiALAAASGKTWLKV-PDSVKVTFTGD 171
Cdd:PLN00070 215 GSGIVHQVNLEylgrvvfntDGILYPDSVV-GTDSHTTMIDGLGVAGWGVGGIE-AEAAMLGQPMSMVlPGVVGFKLSGK 292
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1906333327 172 LRPGVTAKDVAL---EMIRRLGADGatyQSIEMHAG--DRFTRGERMTLANLCVEAGAKAG 227
Cdd:PLN00070 293 LRDGVTATDLVLtvtQMLRKHGVVG---KFVEFYGEgmSELSLADRATIANMSPEYGATMG 350
|
|
| |
