|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-464 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 896.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 1 MNTLFDKIWDAHVVTTVEDGPTQLYIDRLYCHEVTSPQAFAGLRARGIGCLRPEKIICMPDHNTPTHDQDKPIEDEVSKT 80
Cdd:PRK05478 2 GKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLPIADPVSRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 81 QVDTLTKNAADFGLTHYGMMHPKNGIIHVVGPERGLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQS 160
Cdd:PRK05478 82 QVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 161 KPQTMRITIDGKLGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTFA 240
Cdd:PRK05478 162 KPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 241 YIRGREKAPAGDDWDTALAYWKTLKSDEDAVFDCEVTFCAEEIEPMITYGTNPGMGMGITQHIPTTEQMS-EAGKTSFIK 319
Cdd:PRK05478 242 YLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFAdPVKRASAER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 320 SLEYMGFAPGESLLGKKIDYVFIGSCTNGRIEDFRDFASIVKGKQKADHVVAWIVPGSWEVDRQLREEGLDALFIEAGFE 399
Cdd:PRK05478 322 ALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFE 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2676602106 400 IRQPGCSACLAMNDDKIPAGKYAVSTSNRNFEGRQGPGARTLLASPLVAAAAAVTGVITDPRTFL 464
Cdd:PRK05478 402 WREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
3-463 |
0e+00 |
|
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: 661.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 3 TLFDKIWDAHVVTTVEDG-PTQLYIDRLYCHEVTSPQAFAGLRARGIGCL-RPEKIICMPDHNTPTHDqdkpiedEVSKT 80
Cdd:COG0065 4 TLAEKILARHAGREVEPGeIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVwDPDRIVAVFDHNVPTKD-------PKSAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 81 QVDTLTKNAADFGLTHYGMMHPknGIIHVVGPERGLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQS 160
Cdd:COG0065 77 QVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWFK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 161 KPQTMRITIDGKLGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTFA 240
Cdd:COG0065 155 VPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 241 YIRGREKAPagddwdtalayWKTLKSDEDAVFDCEVTFCAEEIEPMITYGTNPGMGMGITQhiptteqmseagktsfiks 320
Cdd:COG0065 235 YLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE------------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 321 leymgfapgesLLGKKIDYVFIGSCTNGRIEDFRDFASIVKGKQKADHVVAWIVPGSWEVDRQLREEGLDALFIEAGFEI 400
Cdd:COG0065 285 -----------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEW 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2676602106 401 RQPGCSACLAMNDDKIPAGKYAVSTSNRNFEGRQG-PGARTLLASPLVAAAAAVTGVITDPRTF 463
Cdd:COG0065 354 REPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
6-445 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 634.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 6 DKIWDAHVVTTVEDgpTQLYI-DRLYCHEVTSPQAFAGLRARGIGCLRPEKIICMPDHNTPTHD--------QDKPIEDE 76
Cdd:pfam00330 1 EKIWDAHLVEELDG--SLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLvidhapdaLDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 77 VS--KTQVDTLTKNAADFGLTHYGmmhPKNGIIHVVGPERGLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLAS 154
Cdd:pfam00330 79 ISrnKEQYDFLEWNAKKFGIRFVP---PGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 155 QCILQSKPQTMRITIDGKLGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAP 234
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 235 DETTFAYIR--GREKAPAGDDWDTALAyWKTLKSDEDAVFDCEVTFCAEEIEPMITYGTNPGMGMGITQHIPTTEQmSEA 312
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDPFA-DAV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 313 GKTSFIKSLEYMGFAPGESLLGKKIDYVFIGSCTNGRIEDFRDFASIVK-----GKQKADHVVAWIVPGSWEVDRQLREE 387
Cdd:pfam00330 314 KRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEAE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2676602106 388 GLDALFIEAGFEIRQPGCSACLAmNDDKIPAGKYAVSTSNRNFEGRQGPGARTLLASP 445
Cdd:pfam00330 394 GLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASP 450
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
3-463 |
0e+00 |
|
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: 626.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 3 TLFDKIWDAHVVTTVEDGPTQLYIDRLYCHEVTSPQAFAGLRARGIGCLRPEKIICMPDHNTPTHDQDKPIEDEVSKTQV 82
Cdd:TIGR00170 4 TLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFNIKDEVAKIQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 83 DTLTKNAADFGLTHYGMMHPKNGIIHVVGPERGLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQSKP 162
Cdd:TIGR00170 84 TELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 163 QTMRITIDGKLGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTFAYI 242
Cdd:TIGR00170 164 KTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTFEYC 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 243 RGREKAPAGDDWDTALAYWKTLKSDEDAVFDCEVTFCAEEIEPMITYGTNPGMGMGITQHIPTTEQMS-EAGKTSFIKSL 321
Cdd:TIGR00170 244 KGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFAdPVDKASAERAL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 322 EYMGFAPGESLLGKKIDYVFIGSCTNGRIEDFRDFASIVKGKQKADHVVAWIVPGSWEVDRQLREEGLDALFIEAGFEIR 401
Cdd:TIGR00170 324 AYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGFEWR 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2676602106 402 QPGCSACLAMNDDKIPAGKYAVSTSNRNFEGRQGPGARTLLASPLVAAAAAVTGVITDPRTF 463
Cdd:TIGR00170 404 EPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
28-457 |
0e+00 |
|
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: 557.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 28 RLYCHEVTSPQAFAGLRARGI-GCLRPEKIICMPDHNTPTHDqdkpiedEVSKTQVDTLTKNAADFGLTHYGMMhpKNGI 106
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPTPD-------IKAAEQVKTLRKFAKEFGINFFDVG--RQGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 107 IHVVGPERGLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQSKPQTMRITIDGKLGKGVTAKDVALYI 186
Cdd:cd01583 72 CHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 187 IAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTFAYIRGREKapagddwdtalAYWKTLKS 266
Cdd:cd01583 152 IGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGK-----------AYWKELKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 267 DEDAVFDCEVTFCAEEIEPMITYGTNPGMGMGITQHIPTteqmseagktsfiksleymgfapgesllgkKIDYVFIGSCT 346
Cdd:cd01583 221 DEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEGI------------------------------KIDQVFIGSCT 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 347 NGRIEDFRDFASIVKGKQKADHVVAWIVPGSWEVDRQLREEGLDALFIEAGFEIRQPGCSACLAMNDDKIPAGKYAVSTS 426
Cdd:cd01583 271 NGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTS 350
|
410 420 430
....*....|....*....|....*....|..
gi 2676602106 427 NRNFEGRQG-PGARTLLASPLVAAAAAVTGVI 457
Cdd:cd01583 351 NRNFKGRMGsPGARIYLASPATAAASAITGEI 382
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
3-460 |
2.43e-75 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 242.36 E-value: 2.43e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 3 TLFDKIWDAHVVTTVEDGPT-QLYIDRLYCHEVTSPQAFAGLRARGIGCLRPEKIICMPDHNTPThdqdkpieDEVSKTQ 81
Cdd:NF040615 2 TLAEKILSKKLGKEVYAGDTvEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPA--------NTVKAAN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 82 VDTLTKN-AADFGLTHYgmmHPK-NGIIHVVGPERGLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQ 159
Cdd:NF040615 74 MQKITREfVKEQGIKNF---YLGgEGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 160 SKPQTMRITIDGKlGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTF 239
Cdd:NF040615 151 KVPKTIRVNIVGK-NENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 240 AYIRgreKAPAGDDWDTALAYWKTLKSDEDAVFDCEVTFCAEEIEPMITYGTNPGMGMGITQhiptteqmseagktsfik 319
Cdd:NF040615 230 EYLR---KEGVSEEEIAELKKNRITVNEKEENYYKEIEIDITDMEEQVACPHHPDNVKPVSE------------------ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 320 sleymgfapgesLLGKKIDYVFIGSCTNGRIEDFRDFASIVKGKQKADHVVAWIVPGSWEVDRQLREEGLDALFIEAGFE 399
Cdd:NF040615 289 ------------VEGTEIDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAM 356
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2676602106 400 IRQPGCSACLAMNDDKIPAGKYAVSTSNRNFEGRQG-PGARTLLASPLVAAAAAVTGVITDP 460
Cdd:NF040615 357 ICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGnINSYIYLSSPKIAAKSAVKGYITNE 418
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-464 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 896.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 1 MNTLFDKIWDAHVVTTVEDGPTQLYIDRLYCHEVTSPQAFAGLRARGIGCLRPEKIICMPDHNTPTHDQDKPIEDEVSKT 80
Cdd:PRK05478 2 GKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLPIADPVSRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 81 QVDTLTKNAADFGLTHYGMMHPKNGIIHVVGPERGLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQS 160
Cdd:PRK05478 82 QVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 161 KPQTMRITIDGKLGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTFA 240
Cdd:PRK05478 162 KPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 241 YIRGREKAPAGDDWDTALAYWKTLKSDEDAVFDCEVTFCAEEIEPMITYGTNPGMGMGITQHIPTTEQMS-EAGKTSFIK 319
Cdd:PRK05478 242 YLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFAdPVKRASAER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 320 SLEYMGFAPGESLLGKKIDYVFIGSCTNGRIEDFRDFASIVKGKQKADHVVAWIVPGSWEVDRQLREEGLDALFIEAGFE 399
Cdd:PRK05478 322 ALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFE 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2676602106 400 IRQPGCSACLAMNDDKIPAGKYAVSTSNRNFEGRQGPGARTLLASPLVAAAAAVTGVITDPRTFL 464
Cdd:PRK05478 402 WREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
3-464 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 713.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 3 TLFDKIWDAHVVTTVEDGPTQLYIDRLYCHEVTSPQAFAGLRARGIGCLRPEKIICMPDHNTPTHDQ-DKPIEDEVSKTQ 81
Cdd:PRK12466 5 TLYDKLWDSHTVARLDDGHVLLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPTRPGrDRGITDPGGALQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 82 VDTLTKNAADFGLTHYGMMHPKNGIIHVVGPERGLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQSK 161
Cdd:PRK12466 85 VDYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQTLVYRK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 162 PQTMRITIDGKLGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTFAY 241
Cdd:PRK12466 165 PKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETTFDY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 242 IRGREKAPAGDDWDTALAYWKTLKSDEDAVFDCEVTFCAEEIEPMITYGTNPGMGMGITQHIPTTEQMSEAGK-TSFIKS 320
Cdd:PRK12466 245 LRGRPRAPKGALWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAAEADPARrAAMERA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 321 LEYMGFAPGESLLGKKIDYVFIGSCTNGRIEDFRDFASIVKGKQKADHVVAWIVPGSWEVDRQLREEGLDALFIEAGFEI 400
Cdd:PRK12466 325 LDYMGLTPGTPLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAGFEW 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2676602106 401 RQPGCSACLAMNDDKIPAGKYAVSTSNRNFEGRQGPGARTLLASPLVAAAAAVTGVITDPRTFL 464
Cdd:PRK12466 405 REPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHITDVRSLL 468
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
3-463 |
0e+00 |
|
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: 661.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 3 TLFDKIWDAHVVTTVEDG-PTQLYIDRLYCHEVTSPQAFAGLRARGIGCL-RPEKIICMPDHNTPTHDqdkpiedEVSKT 80
Cdd:COG0065 4 TLAEKILARHAGREVEPGeIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVwDPDRIVAVFDHNVPTKD-------PKSAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 81 QVDTLTKNAADFGLTHYGMMHPknGIIHVVGPERGLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQS 160
Cdd:COG0065 77 QVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWFK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 161 KPQTMRITIDGKLGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTFA 240
Cdd:COG0065 155 VPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 241 YIRGREKAPagddwdtalayWKTLKSDEDAVFDCEVTFCAEEIEPMITYGTNPGMGMGITQhiptteqmseagktsfiks 320
Cdd:COG0065 235 YLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE------------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 321 leymgfapgesLLGKKIDYVFIGSCTNGRIEDFRDFASIVKGKQKADHVVAWIVPGSWEVDRQLREEGLDALFIEAGFEI 400
Cdd:COG0065 285 -----------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEW 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2676602106 401 RQPGCSACLAMNDDKIPAGKYAVSTSNRNFEGRQG-PGARTLLASPLVAAAAAVTGVITDPRTF 463
Cdd:COG0065 354 REPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
6-445 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 634.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 6 DKIWDAHVVTTVEDgpTQLYI-DRLYCHEVTSPQAFAGLRARGIGCLRPEKIICMPDHNTPTHD--------QDKPIEDE 76
Cdd:pfam00330 1 EKIWDAHLVEELDG--SLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLvidhapdaLDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 77 VS--KTQVDTLTKNAADFGLTHYGmmhPKNGIIHVVGPERGLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLAS 154
Cdd:pfam00330 79 ISrnKEQYDFLEWNAKKFGIRFVP---PGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 155 QCILQSKPQTMRITIDGKLGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAP 234
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 235 DETTFAYIR--GREKAPAGDDWDTALAyWKTLKSDEDAVFDCEVTFCAEEIEPMITYGTNPGMGMGITQHIPTTEQmSEA 312
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDPFA-DAV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 313 GKTSFIKSLEYMGFAPGESLLGKKIDYVFIGSCTNGRIEDFRDFASIVK-----GKQKADHVVAWIVPGSWEVDRQLREE 387
Cdd:pfam00330 314 KRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEAE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2676602106 388 GLDALFIEAGFEIRQPGCSACLAmNDDKIPAGKYAVSTSNRNFEGRQGPGARTLLASP 445
Cdd:pfam00330 394 GLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASP 450
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
3-463 |
0e+00 |
|
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: 626.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 3 TLFDKIWDAHVVTTVEDGPTQLYIDRLYCHEVTSPQAFAGLRARGIGCLRPEKIICMPDHNTPTHDQDKPIEDEVSKTQV 82
Cdd:TIGR00170 4 TLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFNIKDEVAKIQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 83 DTLTKNAADFGLTHYGMMHPKNGIIHVVGPERGLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQSKP 162
Cdd:TIGR00170 84 TELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 163 QTMRITIDGKLGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTFAYI 242
Cdd:TIGR00170 164 KTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTFEYC 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 243 RGREKAPAGDDWDTALAYWKTLKSDEDAVFDCEVTFCAEEIEPMITYGTNPGMGMGITQHIPTTEQMS-EAGKTSFIKSL 321
Cdd:TIGR00170 244 KGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFAdPVDKASAERAL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 322 EYMGFAPGESLLGKKIDYVFIGSCTNGRIEDFRDFASIVKGKQKADHVVAWIVPGSWEVDRQLREEGLDALFIEAGFEIR 401
Cdd:TIGR00170 324 AYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGFEWR 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2676602106 402 QPGCSACLAMNDDKIPAGKYAVSTSNRNFEGRQGPGARTLLASPLVAAAAAVTGVITDPRTF 463
Cdd:TIGR00170 404 EPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
28-457 |
0e+00 |
|
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: 557.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 28 RLYCHEVTSPQAFAGLRARGI-GCLRPEKIICMPDHNTPTHDqdkpiedEVSKTQVDTLTKNAADFGLTHYGMMhpKNGI 106
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPTPD-------IKAAEQVKTLRKFAKEFGINFFDVG--RQGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 107 IHVVGPERGLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQSKPQTMRITIDGKLGKGVTAKDVALYI 186
Cdd:cd01583 72 CHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 187 IAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTFAYIRGREKapagddwdtalAYWKTLKS 266
Cdd:cd01583 152 IGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGK-----------AYWKELKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 267 DEDAVFDCEVTFCAEEIEPMITYGTNPGMGMGITQHIPTteqmseagktsfiksleymgfapgesllgkKIDYVFIGSCT 346
Cdd:cd01583 221 DEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEGI------------------------------KIDQVFIGSCT 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 347 NGRIEDFRDFASIVKGKQKADHVVAWIVPGSWEVDRQLREEGLDALFIEAGFEIRQPGCSACLAMNDDKIPAGKYAVSTS 426
Cdd:cd01583 271 NGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTS 350
|
410 420 430
....*....|....*....|....*....|..
gi 2676602106 427 NRNFEGRQG-PGARTLLASPLVAAAAAVTGVI 457
Cdd:cd01583 351 NRNFKGRMGsPGARIYLASPATAAASAITGEI 382
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
3-464 |
4.45e-128 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 377.60 E-value: 4.45e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 3 TLFDKIWDAHVVTTVEdgPTQLY---IDRLYCHEVTSPQAFAGLRARGIGCLR-PEKIICMPDHNTPTHDQDkpiedevS 78
Cdd:PRK00402 4 TLAEKILARHSGRDVS--PGDIVeakVDLVMAHDITGPLAIKEFEKIGGDKVFdPSKIVIVFDHFVPAKDIK-------S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 79 KTQVDTLTKNAADFGLTHYgmMHPKNGIIHVVGPERGLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLAS-QCI 157
Cdd:PRK00402 75 AEQQKILREFAKEQGIPNF--FDVGEGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATgKTW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 158 LQsKPQTMRITIDGKLGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDET 237
Cdd:PRK00402 153 FK-VPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 238 TFAYIRGREKAPagddwdtalayWKTLKSDEDAVFDCEVTFCAEEIEPMITYGtnpgmgmgitqHIP-TTEQMSEAGkts 316
Cdd:PRK00402 232 TLEYLKERAGRD-----------YKPWKSDEDAEYEEVYEIDLSKLEPQVAAP-----------HLPdNVKPVSEVE--- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 317 fiksleymgfapgesllGKKIDYVFIGSCTNGRIEDFRDFASIVKGKQKADHVVAWIVPGSWEVDRQLREEGLDALFIEA 396
Cdd:PRK00402 287 -----------------GTKVDQVFIGSCTNGRLEDLRIAAEILKGRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDA 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2676602106 397 GFEIRQPGCSACLAMNDDKIPAGKYAVSTSNRNFEGRQG-PGARTLLASPLVAAAAAVTGVITDPRTFL 464
Cdd:PRK00402 350 GAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGsPESEVYLASPAVAAASAVTGKITDPREVL 418
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
3-461 |
1.57e-101 |
|
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: 309.38 E-value: 1.57e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 3 TLFDKIWDAHVVTTVEDGP-TQLYIDRLYCHEVTSPQAFAGLRARGIGCLR-PEKIICMPDHNTPTHDQdkpiedEVSKT 80
Cdd:TIGR01343 1 TIAEKILSKKSGKEVYAGDlIEAEIDLAMVHDITAPLAIKTLEEYGIDKVWnPEKIVIVFDHQVPADTI------KAAEM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 81 QVdTLTKNAADFGLTHYgmMHPKNGIIHVVGPERGLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQS 160
Cdd:TIGR01343 75 QK-LAREFVKKQGIKYF--YDVGEGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 161 KPQTMRITIDGKLGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTFA 240
Cdd:TIGR01343 152 VPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 241 YIRGREKAPagddwdtalayWKTLKSDEDAVFDCEVTFCAEEIEPMITYGTNPGMGmgitqhiptteqmseagktsfiks 320
Cdd:TIGR01343 232 YLKERRKEP-----------FRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNV------------------------ 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 321 leymgfAPGESLLGKKIDYVFIGSCTNGRIEDFRDFASIVKGKQKADHVVAWIVPGSWEVDRQLREEGLDALFIEAGFEI 400
Cdd:TIGR01343 277 ------KPVSEVEGTEIDQVFIGSCTNGRLEDLRVAAKILKGRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVV 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2676602106 401 RQPGCSACLAMNDDKIPAGKYAVSTSNRNFEGRQG-PGARTLLASPLVAAAAAVTGVITDPR 461
Cdd:TIGR01343 351 STPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMGhPNAEIYLASPATAAASAVKGYIADPR 412
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
3-461 |
1.58e-92 |
|
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: 286.27 E-value: 1.58e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 3 TLFDKIWDAHVVTTVEDGPT-QLYIDRLYCHEVTSPQAFAGLRARGIGCLR-PEKIICMPDHNTPthdqdkPIEDEVSKT 80
Cdd:TIGR02086 2 TLAEKILSEKVGRPVCAGEIvEVEVDLAMTHDGTGPLAIKALRELGVARVWdPEKIVIAFDHNVP------PPTVEAAEM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 81 QVDTLtKNAADFGLTHYgmmHPKNGIIHVVGPERGLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQS 160
Cdd:TIGR02086 76 QKEIR-EFAKRHGIKNF---DVGEGICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTWIK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 161 KPQTMRITIDGKLGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTFA 240
Cdd:TIGR02086 152 VPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEETYE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 241 YIRGRekapAGDDWdtalaywKTLKSDEDAVFDCEVTFCAEEIEPMITYGTNPGMGMGITQhiptteqmseagktsfiks 320
Cdd:TIGR02086 232 YLKKR----RGLEF-------RILVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVSD------------------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 321 leymgfapgesLLGKKIDYVFIGSCTNGRIEDFRDFASIVKGKQKADHVVAWIVPGSWEVDRQLREEGLDALFIEAGFEI 400
Cdd:TIGR02086 282 -----------VEGTEIDQVFIGSCTNGRLEDLRIAAEILKGRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAGAMI 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2676602106 401 RQPGCSACLAMNDDKIPAGKYAVSTSNRNFEGRQG-PGARTLLASPLVAAAAAVTGVITDPR 461
Cdd:TIGR02086 351 CPPGCGPCLGAHMGVLGDGEVCLSTTNRNFKGRMGsPNAEIYLASPATAAASAVEGYITDPE 412
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
3-460 |
2.43e-75 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 242.36 E-value: 2.43e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 3 TLFDKIWDAHVVTTVEDGPT-QLYIDRLYCHEVTSPQAFAGLRARGIGCLRPEKIICMPDHNTPThdqdkpieDEVSKTQ 81
Cdd:NF040615 2 TLAEKILSKKLGKEVYAGDTvEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPA--------NTVKAAN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 82 VDTLTKN-AADFGLTHYgmmHPK-NGIIHVVGPERGLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQ 159
Cdd:NF040615 74 MQKITREfVKEQGIKNF---YLGgEGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 160 SKPQTMRITIDGKlGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTF 239
Cdd:NF040615 151 KVPKTIRVNIVGK-NENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 240 AYIRgreKAPAGDDWDTALAYWKTLKSDEDAVFDCEVTFCAEEIEPMITYGTNPGMGMGITQhiptteqmseagktsfik 319
Cdd:NF040615 230 EYLR---KEGVSEEEIAELKKNRITVNEKEENYYKEIEIDITDMEEQVACPHHPDNVKPVSE------------------ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 320 sleymgfapgesLLGKKIDYVFIGSCTNGRIEDFRDFASIVKGKQKADHVVAWIVPGSWEVDRQLREEGLDALFIEAGFE 399
Cdd:NF040615 289 ------------VEGTEIDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAM 356
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2676602106 400 IRQPGCSACLAMNDDKIPAGKYAVSTSNRNFEGRQG-PGARTLLASPLVAAAAAVTGVITDP 460
Cdd:NF040615 357 ICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGnINSYIYLSSPKIAAKSAVKGYITNE 418
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
66-445 |
1.13e-64 |
|
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: 213.51 E-value: 1.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 66 THDQDKPIEDEVSKTQVDTLTKNAADFGLTHYgmmHPKNGIIHVVGPERGLtLPGMTIVCGDSHTSTHGAMGAVAFGIGT 145
Cdd:cd01351 34 VHDHAVQLEKPVNNEGHKFLSFFAALQGIAFY---RPGVGIIHQIMVENLA-LPGDLLVGSDSHTTSYGGLGAISTGAGG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 146 SEVEMVLASQCILQSKPQTMRITIDGKLGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEM 225
Cdd:cd01351 110 GDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 226 GARGGMIAPDETTFAYIRGREKAPAGDDWDtalAYWKTLKSDEDAVFDCEVTFCAEEIEPMITYGTNPGMGMGITQhipt 305
Cdd:cd01351 190 GATTGIFPEDKTTLKWLEATGRPLLKNLWL---AFPEELLADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSE---- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 306 teqmseagktsfiksleymgfapgesLLGKKIDYVFIGSCTNGRIEDFRDFASIVKGKQKADHVVAWIVPGSWEVDRQLR 385
Cdd:cd01351 263 --------------------------VEGTKIDQVLIGSCTNNRYSDMLAAAKLLKGAKVAPGVRLIVTPGSRMVYATLS 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2676602106 386 EEGLDALFIEAGFEIRQPGCSACLAMNDDKIPAGKYAVSTSNRNFEGRQG-PGARTLLASP 445
Cdd:cd01351 317 REGYYEILVDSGARILPPGCGPCMGNGARLVADGEVGVSSGNRNFPGRLGtYERHVYLASP 377
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
3-463 |
3.05e-63 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 216.17 E-value: 3.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 3 TLFDKIWDAHVVT-TVEDG-PTQLYIDRLYCHEVTSPQAFAGLRARGIGCLRPEKIICMPDHNTPTHDQDKPiEDEvskt 80
Cdd:PRK07229 4 TLTEKILYAHLVEgELEPGeEIAIRIDQTLTQDATGTMAYLQFEAMGLDRVKTELSVQYVDHNLLQADFENA-DDH---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 81 qvDTLTKNAADFGLthyGMMHPKNGIIHVVGPERgLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQS 160
Cdd:PRK07229 79 --RFLQSVAAKYGI---YFSKPGNGICHQVHLER-FAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGGPYYLK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 161 KPQTMRITIDGKLGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTFA 240
Cdd:PRK07229 153 MPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPSDERTRE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 241 YIR--GREkapagDDWDTalaywktLKSDEDAVFDCEVTFCAEEIEPMITYGTNPGMGMGItqhiptteqmSEAGktsfi 318
Cdd:PRK07229 233 FLKaqGRE-----DDWVE-------LLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPV----------SEVA----- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 319 ksleymgfapgesllGKKIDYVFIGSCTNGRIEDFRDFASIVKGKQKADHVVAWIVPGSWEVDRQLREEGLDALFIEAGF 398
Cdd:PRK07229 286 ---------------GIKVDQVLIGSCTNSSYEDLMRAASILKGKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGA 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2676602106 399 EIRQPGCSACLAMNDDKiPAGKYAVSTSNRNFEGRQG-PGARTLLASPLVAAAAAVTGVITDPRTF 463
Cdd:PRK07229 351 RILENACGPCIGMGQAP-ATGNVSLRTFNRNFPGRSGtKDAQVYLASPETAAASALTGVITDPRTL 415
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
27-457 |
3.13e-59 |
|
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: 198.83 E-value: 3.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 27 DRLYCHEVTSPQAFAGLRARGIGCLRPEKIICMPDHNTPTHDQDKPIEDEVsktqvdtLTKNAADFGLtHYGmmHPKNGI 106
Cdd:cd01585 1 DQTLTQDATGTMAYLQFEAMGVDRVRTELSVSYVDHNTLQTDFENADDHRF-------LQTVAARYGI-YFS--RPGNGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 107 IHVVGPERgLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQSKPQTMRITIDGKLGKGVTAKDVALYI 186
Cdd:cd01585 71 CHQVHLER-FAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 187 IAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTFAYIR--GREkapagDDwdtalayWKTL 264
Cdd:cd01585 150 LRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAaqGRE-----DD-------WVEL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 265 KSDEDAVFDCEVTFCAEEIEPMITYGTNPGmgmgitqhiptteqmseagktsfiksleymGFAPGESLLGKKIDYVFIGS 344
Cdd:cd01585 218 AADADAEYDEEIEIDLSELEPLIARPHSPD------------------------------NVVPVREVAGIKVDQVAIGS 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 345 CTNGRIEDFRDFASIVKGKQKADHVVAWIVPGSWEVDRQLREEGLDALFIEAGFEIRQPGCSACLAMNDDKiPAGKYAVS 424
Cdd:cd01585 268 CTNSSYEDLMTVAAILKGRRVHPHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQAP-PTGGVSVR 346
|
410 420 430
....*....|....*....|....*....|....
gi 2676602106 425 TSNRNFEGRQG-PGARTLLASPLVAAAAAVTGVI 457
Cdd:cd01585 347 TFNRNFEGRSGtKDDLVYLASPEVAAAAALTGVI 380
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
68-445 |
9.00e-34 |
|
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: 131.41 E-value: 9.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 68 DQDKPIEDEVSKTQVDTLTKNAADFGLthyGMMHPKNGIIHVVGPErGLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSE 147
Cdd:cd01584 43 EKDLKRAKDINKEVYDFLASAGAKYGI---GFWKPGSGIIHQIVLE-NYAFPGLLMIGTDSHTPNAGGLGGIAIGVGGAD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 148 VEMVLASQCILQSKPQTMRITIDGKLGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGA 227
Cdd:cd01584 119 AVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 228 RGGMIAPDETTFAYIRGREKAPAGDDWDtaLAYWKTLKSDEDAVFDCEVTFCAEEIEPMITYGTNPGMGmgitqhIPTTE 307
Cdd:cd01584 199 TTSVFPYNERMKKYLKATGRAEIADLAD--EFKDDLLVADEGAEYDQLIEINLSELEPHINGPFTPDLA------TPVSK 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 308 QMSEAGKTSFiksleymgfaPGESLLGkkidyvFIGSCTNGRIEDFRDFASIVkgKQKADHVVA-----WIVPGSWEVDR 382
Cdd:cd01584 271 FKEVAEKNGW----------PLDLRVG------LIGSCTNSSYEDMGRAASIA--KQALAHGLKcksifTITPGSEQIRA 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2676602106 383 QLREEGLDALFIEAGFEIRQPGCSACLAMNDDK-IPAG-KYAVSTS-NRNFEGRQ--GPGARTLLASP 445
Cdd:cd01584 333 TIERDGLLQTFRDAGGIVLANACGPCIGQWDRKdIKKGeKNTIVTSyNRNFTGRNdaNPATHAFVASP 400
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
98-444 |
2.74e-30 |
|
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: 121.84 E-value: 2.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 98 GMMHPKNGIIHVVGPErgLTLPGMTIVCGDSHTSThgAMGaVAFGIGTSEVEMVLASQCILQSKPQTMRITIDGKLGKGV 177
Cdd:cd01581 87 VALRPGDGVIHSWLNR--MLLPDTVGTGGDSHTRF--PIG-ISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 178 TAKDVALYIIAKMTTSGATGyfVEYAG------------EAIRSLSMEGRLTLCNLSIEMGARGGMI-APDETTFAYIRG 244
Cdd:cd01581 162 TLRDLVNAIPYYAIQQGLLT--VEKKGkknvfngrileiEGLPDLKVEQAFELTDASAERSAAACTVrLDKEPVIEYLES 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 245 REK------APAGDDWDT------ALAYW----KTLKSDEDAVFDCEVTFCAEEI-EPMITYGTNPgmgmgitqhiptte 307
Cdd:cd01581 240 NVVlmkimiANGYDDARTllrriiAMEEWlanpPLLEPDADAEYAAVIEIDLDDIkEPILACPNDP-------------- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 308 qmseagktSFIKSLEYMgfapgeslLGKKIDYVFIGSC-TNgrIEDFRDFASIVKGKQKADhVVAWIVPGSWEVDRQLRE 386
Cdd:cd01581 306 --------DDVKLLSEV--------AGKKIDEVFIGSCmTN--IGHFRAAAKILRGKEFKP-TRLWVAPPTRMDWAILQE 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2676602106 387 EGLDALFIEAGFEIRQPGCSACLAmNDDKIPAGKYAVSTSNRNFEGRQGPGARTLLAS 444
Cdd:cd01581 367 EGYYSIFGDAGARTEMPGCSLCMG-NQARVADGATVFSTSTRNFDNRVGKGAEVYLGS 423
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
32-445 |
3.88e-27 |
|
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: 111.94 E-value: 3.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 32 HEVTSPQAfagLRARGIGCLR---PEKIICMPDHNTpthdQDKPIEDEVSKTQVDTLTKNAadfGLTHYGmmhPKNGIIH 108
Cdd:cd01582 5 HDNSWPVA---LKFMSIGATKihnPDQIVMTLDHDV----QNKSEKNLKKYKNIESFAKKH---GIDFYP---AGRGIGH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 109 VVGPERGLTLPGMTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQSKPQTMRITIDGKLGKGVTAKDVALYIIA 188
Cdd:cd01582 72 QIMIEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 189 KMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTFAYirgrekapagdDWDTALAYwktlKSDE 268
Cdd:cd01582 152 LFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAKHLIL-----------DLSTLSPY----VSGP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 269 DAVfdcEVTFCAEEIEpmitygtnpgmgmgiTQHIptteqmseagktsfiksleymgfapgesllgkKIDYVFIGSCTNG 348
Cdd:cd01582 217 NSV---KVSTPLKELE---------------AQNI--------------------------------KINKAYLVSCTNS 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 349 RIEDFRDFASIVKGK-------QKADHVVAWIVPGSWEVDRQLREEGLDALFIEAGFEIRQPGCSACLAMNDDKIPAGKY 421
Cdd:cd01582 247 RASDIAAAADVVKGKkekngkiPVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQGLLEPGEV 326
|
410 420
....*....|....*....|....*
gi 2676602106 422 AVSTSNRNFEGRQG-PGARTLLASP 445
Cdd:cd01582 327 GISATNRNFKGRMGsTEALAYLASP 351
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
102-445 |
1.86e-26 |
|
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: 112.89 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 102 PKNGIIH---------VV--GPERGLTL--PGmTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQcilqskPQTMRI- 167
Cdd:COG1048 173 PGTGIVHqvnleylafVVwtREEDGETVayPD-TLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQ------PVSMLIp 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 168 -----TIDGKLGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTFAYI 242
Cdd:COG1048 246 evvgvKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 243 R--GRekapagDDWDTAL--AYWKTLK-----SDEDAVFDCEVTFCAEEIEPmitygtnpgmgmgitqHI--PTTEQ--- 308
Cdd:COG1048 326 RltGR------SEEQIELveAYAKAQGlwrdpDAPEPYYSDVLELDLSTVEP----------------SLagPKRPQdri 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 309 -MSEAgKTSFIKSLEYMGFAPGESLLGKKID---------YVF---IGSCTN--------GriedfrdfASIV------K 361
Cdd:COG1048 384 pLSDL-KEAFRAALAAPVGEELDKPVRVEVDgeefelghgAVViaaITSCTNtsnpsvmiA--------AGLLakkaveK 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 362 GKQKADHVVAWIVPGSWEVDRQLREEGLDALFIEAGFEIRQPGCSACL------------AMNDDKIPAGkyAVSTSNRN 429
Cdd:COG1048 455 GLKVKPWVKTSLAPGSKVVTDYLERAGLLPYLEALGFNVVGYGCTTCIgnsgplppeiseAIEENDLVVA--AVLSGNRN 532
|
410
....*....|....*..
gi 2676602106 430 FEGRQGPGART-LLASP 445
Cdd:COG1048 533 FEGRIHPDVKAnFLASP 549
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
101-444 |
6.18e-26 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 111.42 E-value: 6.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 101 HPKNGIIHVVGpERgLTLPGMTIVCGDSHT------STHGAMGAVAFGIGTSEVEMVLasqcilqskPQTMRITIDGKLG 174
Cdd:PRK09238 462 RPGDGVIHSWL-NR-MLLPDTVGTGGDSHTrfpigiSFPAGSGLVAFAAATGVMPLDM---------PESVLVRFKGEMQ 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 175 KGVTAKDVA----LYIIAK-MTTSGATGYFVEYAG-----EAIRSLSMEGRLTLCNLSIEMGARGGMIA-PDETTFAYIR 243
Cdd:PRK09238 531 PGITLRDLVhaipYYAIKQgLLTVEKKGKKNIFSGrileiEGLPDLKVEQAFELTDASAERSAAGCTIKlSKEPIIEYLR 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 244 ------------GREKAP-------AGDDWdtaLAYWKTLKSDEDAVFDCEVTFCAEEI-EPMITygtNPgmgmgitqHI 303
Cdd:PRK09238 611 snivllkwmiaeGYGDARtlerriaAMEEW---LANPELLEADADAEYAAVIEIDLAEIkEPILA---CP--------ND 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 304 PTTeqmseagktsfIKSLEYmgfapgesLLGKKIDYVFIGSC-TNgrIEDFRDFASIVKGKQKADHVVAWIVPGSWEVDR 382
Cdd:PRK09238 677 PDD-----------VRLLSE--------VAGTKIDEVFIGSCmTN--IGHFRAAGKLLEGKKGQLPTRLWVAPPTKMDAD 735
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2676602106 383 QLREEGLDALFIEAGFEIRQPGCSACLAmNDDKIPAGKYAVSTSNRNFEGRQGPGARTLLAS 444
Cdd:PRK09238 736 QLTEEGYYSIFGKAGARIEMPGCSLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYLGS 796
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
102-445 |
4.28e-25 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 108.95 E-value: 4.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 102 PKNGIIH---------VVGPERGLTLPGmTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQSKPQTMRITIDGK 172
Cdd:PTZ00092 182 PGSGIVHqvnleylarVVFNKDGLLYPD-SVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTGK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 173 LGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTFAYIR--GR--EKA 248
Cdd:PTZ00092 261 LSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKqtGRseEKV 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 249 PAGDDWDTALAYWKTlkSDEDAVFDCEVTFCAEEIEPMITYGTNPgmgmgiTQHIPTTEQmseagKTSFIKSLE----YM 324
Cdd:PTZ00092 341 ELIEKYLKANGLFRT--YAEQIEYSDVLELDLSTVVPSVAGPKRP------HDRVPLSDL-----KKDFTACLSapvgFK 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 325 GFAPGESLLGKKIDYVF----------------IGSCTNGRIEDFRDFASIV--KGKQKADHVVAWIV----PGSWEVDR 382
Cdd:PTZ00092 408 GFGIPEEKHEKKVKFTYkgkeytlthgsvviaaITSCTNTSNPSVMLAAGLLakKAVEKGLKVPPYIKtslsPGSKVVTK 487
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2676602106 383 QLREEGLDALFIEAGFEIRQPGCSACL------------AMNDDKIPAGkyAVSTSNRNFEGRQGPGAR-TLLASP 445
Cdd:PTZ00092 488 YLEASGLLKYLEKLGFYTAGYGCMTCIgnsgdldpevseAITNNDLVAA--AVLSGNRNFEGRVHPLTRaNYLASP 561
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
102-445 |
5.58e-25 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 108.74 E-value: 5.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 102 PKNGIIHVVGPE---------RGLTLPGmTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQSKPQTMRITIDGK 172
Cdd:PLN00070 214 PGSGIVHQVNLEylgrvvfntDGILYPD-SVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 173 LGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTFAYIR--GREkapa 250
Cdd:PLN00070 293 LRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKltGRS---- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 251 GDDWDTALAYWKTLK-------SDEDAVFDCEVTFCAEEIEPMITYGTNPgmgmgiTQHIPTTEqMSEAGKTSFIKSLEY 323
Cdd:PLN00070 369 DETVAMIEAYLRANKmfvdynePQQERVYSSYLELDLEDVEPCISGPKRP------HDRVPLKE-MKADWHSCLDNKVGF 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 324 MGFAPGESLLGKKIDYVF----------------IGSCTNGRIEDFRDFASIV--KGKQKADHVVAWI----VPGSWEVD 381
Cdd:PLN00070 442 KGFAVPKEAQSKVAKFSFhgqpaelrhgsvviaaITSCTNTSNPSVMLGAGLVakKACELGLEVKPWIktslAPGSGVVT 521
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2676602106 382 RQLREEGLDALFIEAGFEIRQPGCSACL------------AMNDDKIPAGkyAVSTSNRNFEGRQGPGAR-TLLASP 445
Cdd:PLN00070 522 KYLLKSGLQKYLNQQGFHIVGYGCTTCIgnsgeldesvasAITENDIVAA--AVLSGNRNFEGRVHPLTRaNYLASP 596
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
102-445 |
1.94e-24 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 106.94 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 102 PKNGIIHVVGPE-------------RGLTLPGmTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQSKPQTMRIT 168
Cdd:PRK12881 175 PGTGIMHQVNLEylarvvhtkeddgDTVAYPD-TLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIPDVVGVE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 169 IDGKLGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTFAYIR--GRE 246
Cdd:PRK12881 254 LTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLRltGRT 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 247 KApagddwDTAL--AYWKTLK----SDEDAVFDCEVTFCAEEIEPMITYGTNPgmgmgitQH-IPTTEqMSEAGKTSFIK 319
Cdd:PRK12881 334 EA------QIALveAYAKAQGlwgdPKAEPRYTRTLELDLSTVAPSLAGPKRP-------QDrIALGN-VKSAFSDLFSK 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 320 SLEYMGF-APGESLLGKKIDY--VFIG---SCTNgrIEDFRDF--ASIV------KGKQKADHVVAWIVPGSWEVDRQLR 385
Cdd:PRK12881 400 PVAENGFaKKAQTSNGVDLPDgaVAIAaitSCTN--TSNPSVLiaAGLLakkaveRGLTVKPWVKTSLAPGSKVVTEYLE 477
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2676602106 386 EEG----LDALfieaGFEIRQPGCSACLAMNDDKIPA--------GKYAVS--TSNRNFEGRQGPGART-LLASP 445
Cdd:PRK12881 478 RAGllpyLEKL----GFGIVGYGCTTCIGNSGPLTPEieqaitknDLVAAAvlSGNRNFEGRIHPNIKAnFLASP 548
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
102-445 |
1.11e-19 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 92.11 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 102 PKNGIIHVVGPER----------GLTL--PGmTIVCGDSHTsTH-GAMGAVAFGIGTSEVEMVLASQcilqskPQTMRI- 167
Cdd:PRK09277 176 PGTGICHQVNLEYlapvvwtredGELVayPD-TLVGTDSHT-TMiNGLGVLGWGVGGIEAEAAMLGQ------PSSMLIp 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 168 -----TIDGKLGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTFAYI 242
Cdd:PRK09277 248 evvgvKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 243 R--GRekapagDDWDTAL--AYWKT----LKSDEDAVFDCEVTFCAEEIEPMITYGTNPgmgmgiTQHIPTTEQmseagK 314
Cdd:PRK09277 328 RltGR------DEEQVALveAYAKAqglwRDPLEEPVYTDVLELDLSTVEPSLAGPKRP------QDRIPLSDV-----K 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 315 TSFIKSLEYMGFAPGESLLGKKIDYVF---------IGSCTN--------GriedfrdfASIV------KGKQKADHVVA 371
Cdd:PRK09277 391 EAFAKSAELGVQGFGLDEAEEGEDYELpdgavviaaITSCTNtsnpsvmiA--------AGLLakkaveKGLKVKPWVKT 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 372 WIVPGSWEVDRQLREEG----LDALfieaGFEIRQPGCSACL------------AMNDDKIPAGkyAVSTSNRNFEGRQG 435
Cdd:PRK09277 463 SLAPGSKVVTDYLEKAGllpyLEAL----GFNLVGYGCTTCIgnsgplppeiekAINDNDLVVT--AVLSGNRNFEGRIH 536
|
410
....*....|.
gi 2676602106 436 PGART-LLASP 445
Cdd:PRK09277 537 PLVKAnYLASP 547
|
|
| AcnB |
COG1049 |
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ... |
333-444 |
4.38e-19 |
|
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: 90.30 E-value: 4.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 333 LGKKIDYVFIGSC-TNgrIEDFRDFASIVKGKQKADhVVAWIVPGSWEVDRQLREEGLDALFIEAGFEIRQPGCSACLAm 411
Cdd:COG1049 687 AGTKIDEVFIGSCmTN--IGHFRAAGKLLEGKGNLP-TRLWIAPPTKMDEAQLTEEGYYSIFGAAGARTEMPGCSLCMG- 762
|
90 100 110
....*....|....*....|....*....|...
gi 2676602106 412 NDDKIPAGKYAVSTSNRNFEGRQGPGARTLLAS 444
Cdd:COG1049 763 NQARVADGATVFSTSTRNFPNRLGKGANVYLGS 795
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
102-445 |
2.29e-18 |
|
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: 86.59 E-value: 2.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 102 PKNGIIHVVGPE-------------RGLTLPGmTIVCGDSHTSTHGAMGAVAFGIGTSEVEMVLASQCILQSKPQTMRIT 168
Cdd:cd01586 91 PGTGIIHQVNLEylarvvftseedgDGVAYPD-SVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 169 IDGKLGKGVTAKDVALYIIAKMTTSGATGYFVEYAGEAIRSLSMEGRLTLCNLSIEMGARGGMIAPDETTfayirgreka 248
Cdd:cd01586 170 LTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVDTQV---------- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 249 pagddwdtalaywktlksdedavfdceVTFCAEEIEPMITYGTNPgmgmgiTQHIPtteqmseagktsfiksleymgfap 328
Cdd:cd01586 240 ---------------------------VELDLSTVEPSVSGPKRP------QDRVP------------------------ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 329 geslLGKKIDYVFIGSCTNGRIEDFRDFASIV--KGKQKADHVVAWI----VPGSWEVDRQLREEGLDALFIEAGFEIRQ 402
Cdd:cd01586 263 ----LHGSVVIAAITSCTNTSNPSVMLAAGLLakKAVELGLKVKPYVktslAPGSRVVTKYLEASGLLPYLEKLGFHVVG 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2676602106 403 PGCSACL------------AMNDDKIPAgkYAVSTSNRNFEGRQGPGAR-TLLASP 445
Cdd:cd01586 339 YGCTTCIgnsgplpeeveeAIKENDLVV--AAVLSGNRNFEGRIHPLVRaNYLASP 392
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
82-444 |
3.11e-16 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 81.51 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 82 VDTLTKNA-ADFGLTHYGM-MHPKNGIIHVvGPERGLtLPGMTIVCGDSHT------STHGAMGAVAFGIGTSEVEMVLa 153
Cdd:PLN00094 515 VDVVTHHTlPDFIRNRGGVsLRPGDGVIHS-WLNRML-LPDTVGTGGDSHTrfpigiSFPAGSGLVAFGAATGVIPLDM- 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 154 sqcilqskPQTMRITIDGKLGKGVTAKD----VALYII-AKMTTSGATGYFVEYAG-----EAIRSLSMEGRLTLCNLSI 223
Cdd:PLN00094 592 --------PESVLVRFTGTMQPGITLRDlvhaIPYTAIqDGLLTVEKKGKKNVFSGrileiEGLPHLKCEQAFELSDASA 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 224 EMGARGGMIAPDETTFA-YI------------------RGREKAPAG-DDWdtaLAYWKTLKSDEDAVFDCEVTFCAEEI 283
Cdd:PLN00094 664 ERSAAGCTIKLDKEPIIeYLnsnvvmlkwmiaegygdrRTLERRIARmQQW---LADPELLEADPDAEYAAVIEIDMDEI 740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 284 -EPMITYGTNPGmgmgitqhipTTEQMSEagktsfiksleymgfapgesLLGKKIDYVFIGSC-TNgrIEDFRDFASIVK 361
Cdd:PLN00094 741 kEPILCAPNDPD----------DARLLSE--------------------VTGDKIDEVFIGSCmTN--IGHFRAAGKLLN 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 362 GKQKADHVVAWIVPGSWEVDRQLREEGLDALFIEAGFEIRQPGCSACLAmNDDKIPAGKYAVSTSNRNFEGRQGPGARTL 441
Cdd:PLN00094 789 DNLSQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPGCSLCMG-NQARVAEKSTVVSTSTRNFPNRLGKGANVY 867
|
...
gi 2676602106 442 LAS 444
Cdd:PLN00094 868 LAS 870
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
86-437 |
6.01e-15 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 77.36 E-value: 6.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 86 TKNAAD--FGLT---HYGMMH--PKNGIIHVVGPERgLTLPGMTIVCGDSHTStHGAMGAVAFGIGTSEVEMVLASQCIL 158
Cdd:PRK11413 102 TINEDDhvFGLSaaqKYGGIFvpPHIAVIHQYMREM-MAGGGKMILGSDSHTR-YGALGTMAVGEGGGELVKQLLNDTYD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 159 QSKPQTMRITIDGKLGKGVTAKDVALYIIAKMTTSGatgyFV-----EYAGEAIRSLSMEGRL--------TLCNLSIem 225
Cdd:PRK11413 180 IDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNG----YVknkvmEFVGPGVSALSTDFRNgvdvmtteTTCLSSI-- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 226 garggmIAPDETTFAY--IRGREKApagddwdtalayWKTLKSDEDAVFDCEVTFCAEEIEPMITYGTNPGM-------- 295
Cdd:PRK11413 254 ------WQTDEEVHNWlaLHGRGQD------------YCELNPQPMAYYDGCISVDLSAIKPMIALPFHPSNvyeideln 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2676602106 296 --GMGITQHIPTTEQMSEAGKTSFiksleymgfapgeSLLGKKID---YV---FIGSCTNGRIEDFRDFASIVKGKQKAD 367
Cdd:PRK11413 316 qnLTDILREVEIESERVAHGKAKL-------------SLLDKIENgrlKVqqgIIAGCSGGNYENVIAAANALRGQSCGN 382
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2676602106 368 HVVAWIV-PGSWEVDRQLREEGLDALFIEAGFEIRQPGCSACLAMNDdkIPA-GKYAVSTSNRNFEGRQG--PG 437
Cdd:PRK11413 383 DTFSLSVyPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFGAGD--TPAnNGLSIRHTTRNFPNREGskPA 454
|
|
| |
