|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
12-476 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 921.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 12 PRTLFDKIWDAHVVCERPAAPPLVYIDLQLLHEVTSPQAFEGLRLAERPVRRPDLCLATVDHAVPTEGRAKPWADALAVE 91
Cdd:PRK05478 2 GKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLPIADPVSRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 92 QVETLRRNCAEAGITLYDIDDPRQGIVHVVAPEQGLTQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALATQTLAQA 171
Cdd:PRK05478 82 QVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 172 RPKTLAVEVEGQLRPGVEAKDLALAVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFA 251
Cdd:PRK05478 162 KPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 252 YLRDRPHAPAGPDWERATAHWRSLKTDPGARFDRTVRVDASAIAPRVTWGTNPAQSCGVDGRVPDPDALPEGPAREQARR 331
Cdd:PRK05478 242 YLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVKRASAER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 332 ALAYMALEPGTPIRDIRIDRVFIGSCTNARIEDLRAAARVVEGRRVAEGVAAMVVPGSGLVKAAAEAEGLDRVFQAAGFS 411
Cdd:PRK05478 322 ALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFE 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494034330 412 WREPGCSMCLAMNPDVLEAGQRCASTSNRNFEGRQGAGGRTHLVGPAMAAAAALAGRFVDVREVM 476
Cdd:PRK05478 402 WREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
12-475 |
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: 727.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 12 PRTLFDKIWDAHVVCERPAAPPLVYIDLQLLHEVTSPQAFEGLRLAERPVRRPDLCLATVDHAVPTEGRAKPWADALAVE 91
Cdd:TIGR00170 2 PRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFNIKDEVAKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 92 QVETLRRNCAEAGITLYDIDDPRQGIVHVVAPEQGLTQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALATQTLAQA 171
Cdd:TIGR00170 82 QVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 172 RPKTLAVEVEGQLRPGVEAKDLALAVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFA 251
Cdd:TIGR00170 162 RAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTFE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 252 YLRDRPHAPAGPDWERATAHWRSLKTDPGARFDRTVRVDASAIAPRVTWGTNPAQSCGVDGRVPDPDALPEGPAREQARR 331
Cdd:TIGR00170 242 YCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKASAER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 332 ALAYMALEPGTPIRDIRIDRVFIGSCTNARIEDLRAAARVVEGRRVAEGVAAMVVPGSGLVKAAAEAEGLDRVFQAAGFS 411
Cdd:TIGR00170 322 ALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGFE 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494034330 412 WREPGCSMCLAMNPDVLEAGQRCASTSNRNFEGRQGAGGRTHLVGPAMAAAAALAGRFVDVREV 475
Cdd:TIGR00170 402 WREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
12-475 |
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: 672.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 12 PRTLFDKIWDAHVVCE-RPAAPPLVYIDLQLLHEVTSPQAFEGLRLA-ERPVRRPDLCLATVDHAVPTegrakpwADALA 89
Cdd:COG0065 2 GMTLAEKILARHAGREvEPGEIVLLYIDLHLVHDVTSPQAFEGLREAgGRKVWDPDRIVAVFDHNVPT-------KDPKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 90 VEQVETLRRNCAEAGITLYDIDDPrqGIVHVVAPEQGLTQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALATQTLA 169
Cdd:COG0065 75 AEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 170 QARPKTLAVEVEGQLRPGVEAKDLALAVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETT 249
Cdd:COG0065 153 FKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 250 FAYLRDRPHAPagpdweratahWRSLKTDPGARFDRTVRVDASAIAPRVTWGTNPAQSCGVDGrvpdpdalpegpareqa 329
Cdd:COG0065 233 FEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE----------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 330 rralaymalepgtpIRDIRIDRVFIGSCTNARIEDLRAAARVVEGRRVAEGVAAMVVPGSGLVKAAAEAEGLDRVFQAAG 409
Cdd:COG0065 285 --------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAG 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494034330 410 FSWREPGCSMCLAMNPDVLEAGQRCASTSNRNFEGRQG-AGGRTHLVGPAMAAAAALAGRFVDVREV 475
Cdd:COG0065 351 AEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
17-457 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 654.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 17 DKIWDAHVVceRPAAPPLVYI-DLQLLHEVTSPQAFEGLRLAERPVRRPDLCLATVDHAVPT--------EGRAKPWADA 87
Cdd:pfam00330 1 EKIWDAHLV--EELDGSLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTdlvidhapDALDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 88 LA--VEQVETLRRNCAEAGITLYDiddPRQGIVHVVAPEQGLTQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALAT 165
Cdd:pfam00330 79 ISrnKEQYDFLEWNAKKFGIRFVP---PGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 166 QTLAQARPKTLAVEVEGQLRPGVEAKDLALAVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAP 245
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 246 DETTFAYLR--DRPHAPAGPDWERATAhWRSLKTDPGARFDRTVRVDASAIAPRVTWGTNPAQSCGVDGRVPDPdaLPEG 323
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDP--FADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 324 PAREQARRALAYMALEPGTPIRDIRIDRVFIGSCTNARIEDLRAAARVVE-----GRRVAEGVAAMVVPGSGLVKAAAEA 398
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 494034330 399 EGLDRVFQAAGFSWREPGCSMCLAmNPDVLEAGQRCASTSNRNFEGRQGAGGRTHLVGP 457
Cdd:pfam00330 393 EGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASP 450
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
39-457 |
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: 555.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 39 LQLLHEVTSPQAFEGLRLAERP-VRRPDLCLATVDHAVPTegrakpwADALAVEQVETLRRNCAEAGITLYDIDdpRQGI 117
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREkVWDPEKIVAVFDHNVPT-------PDIKAAEQVKTLRKFAKEFGINFFDVG--RQGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 118 VHVVAPEQGLTQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALATQTLAQARPKTLAVEVEGQLRPGVEAKDLALAV 197
Cdd:cd01583 72 CHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 198 IDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFAYLRDRPHAPagpdweratahWRSLKT 277
Cdd:cd01583 152 IGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAY-----------WKELKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 278 DPGARFDRTVRVDASAIAPRVTWGTNPAQSCGVDGRVPdpdalpegpareqarralaymalepgtpirdIRIDRVFIGSC 357
Cdd:cd01583 221 DEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQVFIGSC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 358 TNARIEDLRAAARVVEGRRVAEGVAAMVVPGSGLVKAAAEAEGLDRVFQAAGFSWREPGCSMCLAMNPDVLEAGQRCAST 437
Cdd:cd01583 270 TNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVST 349
|
410 420
....*....|....*....|.
gi 494034330 438 SNRNFEGRQGAGG-RTHLVGP 457
Cdd:cd01583 350 SNRNFKGRMGSPGaRIYLASP 370
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
35-447 |
1.74e-75 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 243.13 E-value: 1.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 35 VYIDLQLLHEVTSPQAFEGLRLAERPVRRPDLCLATVDHAVPtegrakpwADALAVEQVETLRRN-CAEAGITLYDIDDp 113
Cdd:NF040615 24 VDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVP--------ANTVKAANMQKITREfVKEQGIKNFYLGG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 114 rQGIVHVVAPEQGLTQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALATQTLAQARPKTLAVEVEGqLRPGVEAKDL 193
Cdd:NF040615 95 -EGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVNIVG-KNENISGKDI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 194 ALAVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFAYLRDRPHApagpDWERAT-AHW 272
Cdd:NF040615 173 ILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEGVS----EEEIAElKKN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 273 RSLKTDPGARFDRTVRVDASAIAPRVtwgtnpaqscgvdgrvpdpdALPEGPAReqarralaymaLEPGTPIRDIRIDRV 352
Cdd:NF040615 249 RITVNEKEENYYKEIEIDITDMEEQV--------------------ACPHHPDN-----------VKPVSEVEGTEIDQV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 353 FIGSCTNARIEDLRAAARVVEGRRVAEGVAAMVVPGSGLVKAAAEAEGLDRVFQAAGFSWREPGCSMCLAMNPDVLEAGQ 432
Cdd:NF040615 298 FIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGE 377
|
410
....*....|....*
gi 494034330 433 RCASTSNRNFEGRQG 447
Cdd:NF040615 378 VCLSTTNRNFKGRMG 392
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
12-476 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 921.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 12 PRTLFDKIWDAHVVCERPAAPPLVYIDLQLLHEVTSPQAFEGLRLAERPVRRPDLCLATVDHAVPTEGRAKPWADALAVE 91
Cdd:PRK05478 2 GKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLPIADPVSRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 92 QVETLRRNCAEAGITLYDIDDPRQGIVHVVAPEQGLTQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALATQTLAQA 171
Cdd:PRK05478 82 QVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 172 RPKTLAVEVEGQLRPGVEAKDLALAVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFA 251
Cdd:PRK05478 162 KPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 252 YLRDRPHAPAGPDWERATAHWRSLKTDPGARFDRTVRVDASAIAPRVTWGTNPAQSCGVDGRVPDPDALPEGPAREQARR 331
Cdd:PRK05478 242 YLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVKRASAER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 332 ALAYMALEPGTPIRDIRIDRVFIGSCTNARIEDLRAAARVVEGRRVAEGVAAMVVPGSGLVKAAAEAEGLDRVFQAAGFS 411
Cdd:PRK05478 322 ALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFE 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494034330 412 WREPGCSMCLAMNPDVLEAGQRCASTSNRNFEGRQGAGGRTHLVGPAMAAAAALAGRFVDVREVM 476
Cdd:PRK05478 402 WREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
11-474 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 778.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 11 PPRTLFDKIWDAHVVCERPAAPPLVYIDLQLLHEVTSPQAFEGLRLAERPVRRPDLCLATVDHAVPT-EGRAKPWADALA 89
Cdd:PRK12466 2 MPRTLYDKLWDSHTVARLDDGHVLLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPTrPGRDRGITDPGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 90 VEQVETLRRNCAEAGITLYDIDDPRQGIVHVVAPEQGLTQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALATQTLA 169
Cdd:PRK12466 82 ALQVDYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQTLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 170 QARPKTLAVEVEGQLRPGVEAKDLALAVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETT 249
Cdd:PRK12466 162 YRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 250 FAYLRDRPHAPAGPDWERATAHWRSLKTDPGARFDRTVRVDASAIAPRVTWGTNPAQSCGVDGRVPDPDALPEGPAREQA 329
Cdd:PRK12466 242 FDYLRGRPRAPKGALWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAAEADPARRAAM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 330 RRALAYMALEPGTPIRDIRIDRVFIGSCTNARIEDLRAAARVVEGRRVAEGVAAMVVPGSGLVKAAAEAEGLDRVFQAAG 409
Cdd:PRK12466 322 ERALDYMGLTPGTPLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAG 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494034330 410 FSWREPGCSMCLAMNPDVLEAGQRCASTSNRNFEGRQGAGGRTHLVGPAMAAAAALAGRFVDVRE 474
Cdd:PRK12466 402 FEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHITDVRS 466
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
12-475 |
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: 727.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 12 PRTLFDKIWDAHVVCERPAAPPLVYIDLQLLHEVTSPQAFEGLRLAERPVRRPDLCLATVDHAVPTEGRAKPWADALAVE 91
Cdd:TIGR00170 2 PRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFNIKDEVAKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 92 QVETLRRNCAEAGITLYDIDDPRQGIVHVVAPEQGLTQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALATQTLAQA 171
Cdd:TIGR00170 82 QVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 172 RPKTLAVEVEGQLRPGVEAKDLALAVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFA 251
Cdd:TIGR00170 162 RAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTFE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 252 YLRDRPHAPAGPDWERATAHWRSLKTDPGARFDRTVRVDASAIAPRVTWGTNPAQSCGVDGRVPDPDALPEGPAREQARR 331
Cdd:TIGR00170 242 YCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKASAER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 332 ALAYMALEPGTPIRDIRIDRVFIGSCTNARIEDLRAAARVVEGRRVAEGVAAMVVPGSGLVKAAAEAEGLDRVFQAAGFS 411
Cdd:TIGR00170 322 ALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGFE 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494034330 412 WREPGCSMCLAMNPDVLEAGQRCASTSNRNFEGRQGAGGRTHLVGPAMAAAAALAGRFVDVREV 475
Cdd:TIGR00170 402 WREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
12-475 |
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: 672.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 12 PRTLFDKIWDAHVVCE-RPAAPPLVYIDLQLLHEVTSPQAFEGLRLA-ERPVRRPDLCLATVDHAVPTegrakpwADALA 89
Cdd:COG0065 2 GMTLAEKILARHAGREvEPGEIVLLYIDLHLVHDVTSPQAFEGLREAgGRKVWDPDRIVAVFDHNVPT-------KDPKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 90 VEQVETLRRNCAEAGITLYDIDDPrqGIVHVVAPEQGLTQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALATQTLA 169
Cdd:COG0065 75 AEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 170 QARPKTLAVEVEGQLRPGVEAKDLALAVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETT 249
Cdd:COG0065 153 FKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 250 FAYLRDRPHAPagpdweratahWRSLKTDPGARFDRTVRVDASAIAPRVTWGTNPAQSCGVDGrvpdpdalpegpareqa 329
Cdd:COG0065 233 FEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE----------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 330 rralaymalepgtpIRDIRIDRVFIGSCTNARIEDLRAAARVVEGRRVAEGVAAMVVPGSGLVKAAAEAEGLDRVFQAAG 409
Cdd:COG0065 285 --------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAG 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494034330 410 FSWREPGCSMCLAMNPDVLEAGQRCASTSNRNFEGRQG-AGGRTHLVGPAMAAAAALAGRFVDVREV 475
Cdd:COG0065 351 AEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
17-457 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 654.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 17 DKIWDAHVVceRPAAPPLVYI-DLQLLHEVTSPQAFEGLRLAERPVRRPDLCLATVDHAVPT--------EGRAKPWADA 87
Cdd:pfam00330 1 EKIWDAHLV--EELDGSLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTdlvidhapDALDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 88 LA--VEQVETLRRNCAEAGITLYDiddPRQGIVHVVAPEQGLTQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALAT 165
Cdd:pfam00330 79 ISrnKEQYDFLEWNAKKFGIRFVP---PGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 166 QTLAQARPKTLAVEVEGQLRPGVEAKDLALAVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAP 245
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 246 DETTFAYLR--DRPHAPAGPDWERATAhWRSLKTDPGARFDRTVRVDASAIAPRVTWGTNPAQSCGVDGRVPDPdaLPEG 323
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDP--FADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 324 PAREQARRALAYMALEPGTPIRDIRIDRVFIGSCTNARIEDLRAAARVVE-----GRRVAEGVAAMVVPGSGLVKAAAEA 398
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 494034330 399 EGLDRVFQAAGFSWREPGCSMCLAmNPDVLEAGQRCASTSNRNFEGRQGAGGRTHLVGP 457
Cdd:pfam00330 393 EGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASP 450
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
39-457 |
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: 555.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 39 LQLLHEVTSPQAFEGLRLAERP-VRRPDLCLATVDHAVPTegrakpwADALAVEQVETLRRNCAEAGITLYDIDdpRQGI 117
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREkVWDPEKIVAVFDHNVPT-------PDIKAAEQVKTLRKFAKEFGINFFDVG--RQGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 118 VHVVAPEQGLTQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALATQTLAQARPKTLAVEVEGQLRPGVEAKDLALAV 197
Cdd:cd01583 72 CHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 198 IDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFAYLRDRPHAPagpdweratahWRSLKT 277
Cdd:cd01583 152 IGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAY-----------WKELKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 278 DPGARFDRTVRVDASAIAPRVTWGTNPAQSCGVDGRVPdpdalpegpareqarralaymalepgtpirdIRIDRVFIGSC 357
Cdd:cd01583 221 DEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQVFIGSC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 358 TNARIEDLRAAARVVEGRRVAEGVAAMVVPGSGLVKAAAEAEGLDRVFQAAGFSWREPGCSMCLAMNPDVLEAGQRCAST 437
Cdd:cd01583 270 TNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVST 349
|
410 420
....*....|....*....|.
gi 494034330 438 SNRNFEGRQGAGG-RTHLVGP 457
Cdd:cd01583 350 SNRNFKGRMGSPGaRIYLASP 370
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
12-476 |
1.53e-121 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 361.42 E-value: 1.53e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 12 PRTLFDKIWDAHVVceRPAAPP---LVYIDLQLLHEVTSPQAFEGLR--LAERpVRRPDLCLATVDHAVPtegrAKpwaD 86
Cdd:PRK00402 2 GMTLAEKILARHSG--RDVSPGdivEAKVDLVMAHDITGPLAIKEFEkiGGDK-VFDPSKIVIVFDHFVP----AK---D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 87 ALAVEQVETLRRNCAEAGIT-LYDIddpRQGIVHVVAPEQGLTQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALAT 165
Cdd:PRK00402 72 IKSAEQQKILREFAKEQGIPnFFDV---GEGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 166 QTLAQARPKTLAVEVEGQLRPGVEAKDLALAVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAP 245
Cdd:PRK00402 149 GKTWFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 246 DETTFAYLrdrphapagpdWERATAHWRSLKTDPGARFDRTVRVDASAIAPRVTWGTNPAQSCgvdgrvpdpdalpegPA 325
Cdd:PRK00402 229 DEKTLEYL-----------KERAGRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVK---------------PV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 326 REqarralaymalepgtpIRDIRIDRVFIGSCTNARIEDLRAAARVVEGRRVAEGVAAMVVPGSGLVKAAAEAEGLDRVF 405
Cdd:PRK00402 283 SE----------------VEGTKVDQVFIGSCTNGRLEDLRIAAEILKGRKVAPGVRLIVIPASQKIYLQALKEGLIEIF 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494034330 406 QAAGFSWREPGCSMCLAMNPDVLEAGQRCASTSNRNFEGRQG-AGGRTHLVGPAMAAAAALAGRFVDVREVM 476
Cdd:PRK00402 347 VDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGsPESEVYLASPAVAAASAVTGKITDPREVL 418
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
14-473 |
3.34e-105 |
|
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: 319.39 E-value: 3.34e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 14 TLFDKIWDAHVVCE-RPAAPPLVYIDLQLLHEVTSPQAFEGL-RLAERPVRRPDLCLATVDHAVPTEGRAkpwadalAVE 91
Cdd:TIGR01343 1 TIAEKILSKKSGKEvYAGDLIEAEIDLAMVHDITAPLAIKTLeEYGIDKVWNPEKIVIVFDHQVPADTIK-------AAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 92 QVETLRRNCAEAGITLYDidDPRQGIVHVVAPEQGLTQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALATQTLAQA 171
Cdd:TIGR01343 74 MQKLAREFVKKQGIKYFY--DVGEGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 172 RPKTLAVEVEGQLRPGVEAKDLALAVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFA 251
Cdd:TIGR01343 152 VPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 252 YLRDRPHAPagpdweratahWRSLKTDPGARFDRTVRVDASAIAPRVTWGTNPAQScgvdgrvpdpdalpeGPAREQARr 331
Cdd:TIGR01343 232 YLKERRKEP-----------FRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNV---------------KPVSEVEG- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 332 alaymalepgtpirdIRIDRVFIGSCTNARIEDLRAAARVVEGRRVAEGVAAMVVPGSGLVKAAAEAEGLDRVFQAAGFS 411
Cdd:TIGR01343 285 ---------------TEIDQVFIGSCTNGRLEDLRVAAKILKGRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAV 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494034330 412 WREPGCSMCLAMNPDVLEAGQRCASTSNRNFEGRQG-AGGRTHLVGPAMAAAAALAGRFVDVR 473
Cdd:TIGR01343 350 VSTPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMGhPNAEIYLASPATAAASAVKGYIADPR 412
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
14-474 |
3.49e-86 |
|
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: 270.48 E-value: 3.49e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 14 TLFDKIWDAHVVCE-RPAAPPLVYIDLQLLHEVTSPQAFEGLR-LAERPVRRPDLCLATVDHAVPTegrakpwADALAVE 91
Cdd:TIGR02086 2 TLAEKILSEKVGRPvCAGEIVEVEVDLAMTHDGTGPLAIKALReLGVARVWDPEKIVIAFDHNVPP-------PTVEAAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 92 QVETLRRNCAEAGITLYDIDDprqGIVHVVAPEQGLTQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALATQTLAQA 171
Cdd:TIGR02086 75 MQKEIREFAKRHGIKNFDVGE---GICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTWIK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 172 RPKTLAVEVEGQLRPGVEAKDLALAVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFA 251
Cdd:TIGR02086 152 VPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEETYE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 252 YLRDRphapaGPDWERAtahwrsLKTDPGARFDRTVRVDASAIAPRVtwgtnpaqscgvdgrvpdpdALPEGPAReqarr 331
Cdd:TIGR02086 232 YLKKR-----RGLEFRI------LVPDPGANYYKEIEIDLSDLEPQV--------------------AVPHSVDN----- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 332 alaymaLEPGTPIRDIRIDRVFIGSCTNARIEDLRAAARVVEGRRVAEGVAAMVVPGSGLVKAAAEAEGLDRVFQAAGFS 411
Cdd:TIGR02086 276 ------VKPVSDVEGTEIDQVFIGSCTNGRLEDLRIAAEILKGRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAGAM 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494034330 412 WREPGCSMCLAMNPDVLEAGQRCASTSNRNFEGRQGA-GGRTHLVGPAMAAAAALAGRFVDVRE 474
Cdd:TIGR02086 350 ICPPGCGPCLGAHMGVLGDGEVCLSTTNRNFKGRMGSpNAEIYLASPATAAASAVEGYITDPED 413
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
35-447 |
1.74e-75 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 243.13 E-value: 1.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 35 VYIDLQLLHEVTSPQAFEGLRLAERPVRRPDLCLATVDHAVPtegrakpwADALAVEQVETLRRN-CAEAGITLYDIDDp 113
Cdd:NF040615 24 VDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVP--------ANTVKAANMQKITREfVKEQGIKNFYLGG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 114 rQGIVHVVAPEQGLTQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALATQTLAQARPKTLAVEVEGqLRPGVEAKDL 193
Cdd:NF040615 95 -EGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVNIVG-KNENISGKDI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 194 ALAVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFAYLRDRPHApagpDWERAT-AHW 272
Cdd:NF040615 173 ILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEGVS----EEEIAElKKN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 273 RSLKTDPGARFDRTVRVDASAIAPRVtwgtnpaqscgvdgrvpdpdALPEGPAReqarralaymaLEPGTPIRDIRIDRV 352
Cdd:NF040615 249 RITVNEKEENYYKEIEIDITDMEEQV--------------------ACPHHPDN-----------VKPVSEVEGTEIDQV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 353 FIGSCTNARIEDLRAAARVVEGRRVAEGVAAMVVPGSGLVKAAAEAEGLDRVFQAAGFSWREPGCSMCLAMNPDVLEAGQ 432
Cdd:NF040615 298 FIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGE 377
|
410
....*....|....*
gi 494034330 433 RCASTSNRNFEGRQG 447
Cdd:NF040615 378 VCLSTTNRNFKGRMG 392
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
41-457 |
2.86e-61 |
|
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: 205.04 E-value: 2.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 41 LLHEVTSPQA---FEGLRLAERpVRRPDLCLATVDHAVPTEgrakpwaDALAVEQVETLRRNCAEAGITLYDIDDprqGI 117
Cdd:cd01351 3 MLQDATGPMAmkaFEILAALGK-VADPSQIACVHDHAVQLE-------KPVNNEGHKFLSFFAALQGIAFYRPGV---GI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 118 VHVVAPEQGLtQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALATQTLAQARPKTLAVEVEGQLRPGVEAKDLALAV 197
Cdd:cd01351 72 IHQIMVENLA-LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 198 IDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFAYLRDRPHAPAGPDWERATAHwrsLKT 277
Cdd:cd01351 151 GGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWLAFPEE---LLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 278 DPGARFDRTVRVDASAIAPRVTwgtnpaqscgvdgrvpdpdalpeGPAREQARRALAYMAlepgtpirDIRIDRVFIGSC 357
Cdd:cd01351 228 DEGAEYDQVIEIDLSELEPDIS-----------------------GPNRPDDAVSVSEVE--------GTKIDQVLIGSC 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 358 TNARIEDLRAAARVVEGRRVAEGVAAMVVPGSGLVKAAAEAEGLDRVFQAAGFSWREPGCSMCLAMNPDVLEAGQRCAST 437
Cdd:cd01351 277 TNNRYSDMLAAAKLLKGAKVAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLVADGEVGVSS 356
|
410 420
....*....|....*....|.
gi 494034330 438 SNRNFEGRQGAG-GRTHLVGP 457
Cdd:cd01351 357 GNRNFPGRLGTYeRHVYLASP 377
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
113-447 |
1.40e-48 |
|
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: 171.09 E-value: 1.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 113 PRQGIVHVVAPEQgLTQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALATQTLAQARPKTLAVEVEGQLRPGVEAKD 192
Cdd:cd01585 66 PGNGICHQVHLER-FAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKD 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 193 LALAVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFAYLR--DRPhapagpdweratA 270
Cdd:cd01585 145 VILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAaqGRE------------D 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 271 HWRSLKTDPGARFDRTVRVDASAIAPRVtwgtnpaqscgvdgrvpdpdALPEGPAREQARRALAymalepgtpirDIRID 350
Cdd:cd01585 213 DWVELAADADAEYDEEIEIDLSELEPLI--------------------ARPHSPDNVVPVREVA-----------GIKVD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 351 RVFIGSCTNARIEDLRAAARVVEGRRVAEGVAAMVVPGSGLVKAAAEAEGLDRVFQAAGFSWREPGCSMCLAMNpDVLEA 430
Cdd:cd01585 262 QVAIGSCTNSSYEDLMTVAAILKGRRVHPHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMG-QAPPT 340
|
330
....*....|....*..
gi 494034330 431 GQRCASTSNRNFEGRQG 447
Cdd:cd01585 341 GGVSVRTFNRNFEGRSG 357
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
116-474 |
1.41e-46 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 171.10 E-value: 1.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 116 GIVHVVAPEQgLTQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALATQTLAQARPKTLAVEVEGQLRPGVEAKDLAL 195
Cdd:PRK07229 98 GICHQVHLER-FAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVIL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 196 AVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFAYLR--DRPhapagpdweratAHWR 273
Cdd:PRK07229 177 ELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLKaqGRE------------DDWV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 274 SLKTDPGARFDRTVRVDASAIAPRVtwgtnpaqscgvdgrvpdpdALPEGPAReqarralaymalepGTPIRDIR---ID 350
Cdd:PRK07229 245 ELLADPDAEYDEVIEIDLSELEPLI--------------------AGPHSPDN--------------VVPVSEVAgikVD 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 351 RVFIGSCTNARIEDLRAAARVVEGRRVAEGVAAMVVPGSGLVKAAAEAEGLDRVFQAAGFSWREPGCSMCLAMnpdvlea 430
Cdd:PRK07229 291 QVLIGSCTNSSYEDLMRAASILKGKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGM------- 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 494034330 431 GQRCAS------TSNRNFEGRQG-AGGRTHLVGPAMAAAAALAGRFVDVRE 474
Cdd:PRK07229 364 GQAPATgnvslrTFNRNFPGRSGtKDAQVYLASPETAAASALTGVITDPRT 414
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
43-448 |
1.44e-32 |
|
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: 127.35 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 43 HEVTSPQAFEGLRLAERPVRRPDLCLATVDHAVptegRAKPWADALAVEQVETLRRncaEAGITLYDIDdprQGIVHVVA 122
Cdd:cd01582 5 HDNSWPVALKFMSIGATKIHNPDQIVMTLDHDV----QNKSEKNLKKYKNIESFAK---KHGIDFYPAG---RGIGHQIM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 123 PEQGLTQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALAT-QTLAQArPKTLAVEVEGQLRPGVEAKDLALAVIDAL 201
Cdd:cd01582 75 IEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATgQTWWQI-PPVAKVELKGQLPKGVTGKDVIVALCGLF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 202 GFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDEttfaylrdrphapagpdweratahwrslktdpga 281
Cdd:cd01582 154 NKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDA---------------------------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 282 rfdRTVRVDASAIAPRVTwgtnpaqscgvdgrvpdpdalpeGPAREQARRALAYMALEpgtpirDIRIDRVFIGSCTNAR 361
Cdd:cd01582 200 ---KHLILDLSTLSPYVS-----------------------GPNSVKVSTPLKELEAQ------NIKINKAYLVSCTNSR 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 362 IEDLRAAARVVEGRR-------VAEGVAAMVVPGSGLVKAAAEAEGLDRVFQAAGFSWREPGCSMCLAMNPDVLEAGQRC 434
Cdd:cd01582 248 ASDIAAAADVVKGKKekngkipVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQGLLEPGEVG 327
|
410
....*....|....
gi 494034330 435 ASTSNRNFEGRQGA 448
Cdd:cd01582 328 ISATNRNFKGRMGS 341
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
113-453 |
6.48e-31 |
|
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: 123.70 E-value: 6.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 113 PRQGIVHVVAPEQgLTQPGMVIVCGDSHTATHGAFGALAFGIGTSEVEHALATQTLAQARPKTLAVEVEGQLRPGVEAKD 192
Cdd:cd01584 74 PGSGIIHQIVLEN-YAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKD 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 193 LALAVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFAYLRDRPHAPAGPDWERatAHW 272
Cdd:cd01584 153 VILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEIADLADE--FKD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 273 RSLKTDPGARFDRTVRVDASAIAPRVtwgTNPAQscgvdgrvpdPD-ALPEGPAREQARralaymalEPGTPIrDIRIDr 351
Cdd:cd01584 231 DLLVADEGAEYDQLIEINLSELEPHI---NGPFT----------PDlATPVSKFKEVAE--------KNGWPL-DLRVG- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 352 vFIGSCTNARIEDLRAAARVVEgRRVAEGVAA----MVVPGSGLVKAAAEAEGLDRVFQAAGFSWREPGCSMCLAM--NP 425
Cdd:cd01584 288 -LIGSCTNSSYEDMGRAASIAK-QALAHGLKCksifTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQwdRK 365
|
330 340
....*....|....*....|....*....
gi 494034330 426 DVLEAGQRCASTS-NRNFEGRQGAGGRTH 453
Cdd:cd01584 366 DIKKGEKNTIVTSyNRNFTGRNDANPATH 394
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
113-445 |
1.64e-25 |
|
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: 110.19 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 113 PRQGIVH---------VV--APEQGLTQ--PGMVIvcG-DSHTATHGAFGALAFGIGTSEVEHALATQTLAQARPKTLAV 178
Cdd:COG1048 173 PGTGIVHqvnleylafVVwtREEDGETVayPDTLV--GtDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVVGV 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 179 EVEGQLRPGVEAKDLALAVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFAYLR--DR 256
Cdd:COG1048 251 KLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRltGR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 257 PhaPAGPDWERATAHWRSLKTDPGA---RFDRTVRVDASAIAPRVTWGTNPaqscgvDGRVPdpdaLPEgpAREQARRAL 333
Cdd:COG1048 331 S--EEQIELVEAYAKAQGLWRDPDApepYYSDVLELDLSTVEPSLAGPKRP------QDRIP----LSD--LKEAFRAAL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 334 AYMALEPGTPIRDIRIDRVF------------IGSCTNARIED-LRAA---AR--VVEGRRVAEGVAAMVVPGSGLVKAA 395
Cdd:COG1048 397 AAPVGEELDKPVRVEVDGEEfelghgavviaaITSCTNTSNPSvMIAAgllAKkaVEKGLKVKPWVKTSLAPGSKVVTDY 476
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 396 AEAEGLDRVFQAAGFSWREPGCSMCL--------AMNPDVLEAGQRCAS-TS-NRNFEGR 445
Cdd:COG1048 477 LERAGLLPYLEALGFNVVGYGCTTCIgnsgplppEISEAIEENDLVVAAvLSgNRNFEGR 536
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
138-445 |
1.07e-23 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 104.63 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 138 DSHTATHGAFGALAFGIGTSEVEHALATQTLAQARPKTLAVEVEGQLRPGVEAKDLALAVIDALGFGGGTGHVIEYRGAA 217
Cdd:PRK12881 212 DSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEG 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 218 VRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFAYL----RDRPHAPAGPDWERATAHWRSLKTDPgaRFDRTVRVDASA 293
Cdd:PRK12881 292 VASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLrltgRTEAQIALVEAYAKAQGLWGDPKAEP--RYTRTLELDLST 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 294 IAPRVTWGTNPAQscgvdgRVPDPDaLPEGPAREQARRALAYMALEPGTPIRDIRIDR--VFIG---SCTN--------- 359
Cdd:PRK12881 370 VAPSLAGPKRPQD------RIALGN-VKSAFSDLFSKPVAENGFAKKAQTSNGVDLPDgaVAIAaitSCTNtsnpsvlia 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 360 ----ARiedlRAAARvveGRRVAEGVAAMVVPGSGLVKAAAEAEGLDRVFQAAGFSWREPGCSMCLAMNPDVLEAGQR-- 433
Cdd:PRK12881 443 agllAK----KAVER---GLTVKPWVKTSLAPGSKVVTEYLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQai 515
|
330 340
....*....|....*....|
gi 494034330 434 ------CAS--TSNRNFEGR 445
Cdd:PRK12881 516 tkndlvAAAvlSGNRNFEGR 535
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
113-445 |
4.90e-23 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 102.78 E-value: 4.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 113 PRQGIVH---------VVAPEQGLTQPGMViVCGDSHTATHGAFGALAFGIGTSEVEHALATQTLAQARPKTLAVEVEGQ 183
Cdd:PTZ00092 182 PGSGIVHqvnleylarVVFNKDGLLYPDSV-VGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTGK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 184 LRPGVEAKDLALAVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFAYL----RDRPHA 259
Cdd:PTZ00092 261 LSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLkqtgRSEEKV 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 260 PAGPDWERATAHWRSLKTDPgaRFDRTVRVDASAIAPRVTwgtnpaqscgvdgrvpdpdalpeGPAREQARRALAYM--- 336
Cdd:PTZ00092 341 ELIEKYLKANGLFRTYAEQI--EYSDVLELDLSTVVPSVA-----------------------GPKRPHDRVPLSDLkkd 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 337 ---ALEP-------GTPIRDIRIDRVF------------------IGSCTNARIED------LRAAARVVEGRRVAEGVA 382
Cdd:PTZ00092 396 ftaCLSApvgfkgfGIPEEKHEKKVKFtykgkeytlthgsvviaaITSCTNTSNPSvmlaagLLAKKAVEKGLKVPPYIK 475
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494034330 383 AMVVPGSGLVKAAAEAEGLDRVFQAAGFSWREPGCSMCLA----MNPDVLEAGQR----CAS--TSNRNFEGR 445
Cdd:PTZ00092 476 TSLSPGSKVVTKYLEASGLLKYLEKLGFYTAGYGCMTCIGnsgdLDPEVSEAITNndlvAAAvlSGNRNFEGR 548
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
113-454 |
4.02e-19 |
|
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: 89.48 E-value: 4.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 113 PRQGIVHVVAPEqgLTQPGMVIVCGDSHTAThgAFGaLAFGIGTSEVEHALATQTLAQARPKTLAVEVEGQLRPGVEAKD 192
Cdd:cd01581 91 PGDGVIHSWLNR--MLLPDTVGTGGDSHTRF--PIG-ISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 193 LALAV--------IDALGFGGG----TGHVIEYRGaaVRGLSMEGRMTLCNMSIEAGARAGMV-APDETTFAYLR----- 254
Cdd:cd01581 166 LVNAIpyyaiqqgLLTVEKKGKknvfNGRILEIEG--LPDLKVEQAFELTDASAERSAAACTVrLDKEPVIEYLEsnvvl 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 255 -----DRPHAPAGPDWER--ATAHWRS----LKTDPGARFDRTVRVDASAIaprvtwgTNPAQSCGVDgrvPDPDALpeg 323
Cdd:cd01581 244 mkimiANGYDDARTLLRRiiAMEEWLAnpplLEPDADAEYAAVIEIDLDDI-------KEPILACPND---PDDVKL--- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 324 pareqarraLAYMAlepgtpirDIRIDRVFIGSC-TNarIEDLRAAARVVEGRRVAEgVAAMVVPGSGLVKAAAEAEGLD 402
Cdd:cd01581 311 ---------LSEVA--------GKKIDEVFIGSCmTN--IGHFRAAAKILRGKEFKP-TRLWVAPPTRMDWAILQEEGYY 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 494034330 403 RVFQAAGFSWREPGCSMCLAmNPDVLEAGQRCASTSNRNFEGRQGAGGRTHL 454
Cdd:cd01581 371 SIFGDAGARTEMPGCSLCMG-NQARVADGATVFSTSTRNFDNRVGKGAEVYL 421
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
113-445 |
8.10e-19 |
|
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: 88.13 E-value: 8.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 113 PRQGIVHVVAPE-------------QGLTQPGMViVCGDSHTATHGAFGALAFGIGTSEVEHALATQTLAQARPKTLAVE 179
Cdd:cd01586 91 PGTGIIHQVNLEylarvvftseedgDGVAYPDSV-VGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 180 VEGQLRPGVEAKDLALAVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDettfaylrdrpha 259
Cdd:cd01586 170 LTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD------------- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 260 pagpdweratahwrslktdpgarfDRTVRVDASAIAPRVTwgtnpaqscgvdgrvpdpdalpeGPAREQARRALAymale 339
Cdd:cd01586 237 ------------------------TQVVELDLSTVEPSVS-----------------------GPKRPQDRVPLH----- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 340 pgtpiRDIRIdrVFIGSCTNARIEDLRAAA-----RVVE-GRRVAEGVAAMVVPGSGLVKAAAEAEGLDRVFQAAGFSWR 413
Cdd:cd01586 265 -----GSVVI--AAITSCTNTSNPSVMLAAgllakKAVElGLKVKPYVKTSLAPGSRVVTKYLEASGLLPYLEKLGFHVV 337
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 494034330 414 EPGCSMCLA----MNPDVLEAGQR-----CASTS-NRNFEGR 445
Cdd:cd01586 338 GYGCTTCIGnsgpLPEEVEEAIKEndlvvAAVLSgNRNFEGR 379
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
113-445 |
1.02e-18 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 89.48 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 113 PRQGIVH---------VVAPEQGLTQPGMViVCGDSHTATHGAFGALAFGIGTSEVEHALATQTLAQARPKTLAVEVEGQ 183
Cdd:PLN00070 214 PGSGIVHqvnleylgrVVFNTDGILYPDSV-VGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 184 LRPGVEAKDLALAVIDALGFGGGTGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFAYLRdrphaPAGP 263
Cdd:PLN00070 293 LRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLK-----LTGR 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 264 DWERAT---AHWRSLK-------TDPGARFDRTVRVDASAIAPRVTWGTNPA------------QSCgVDGRVPDPD-AL 320
Cdd:PLN00070 368 SDETVAmieAYLRANKmfvdynePQQERVYSSYLELDLEDVEPCISGPKRPHdrvplkemkadwHSC-LDNKVGFKGfAV 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 321 PegparEQARRALAYMALEpGTPIrDIRIDRVFIG---SCTNARIEDLRAAARVVE------GRRVAEGVAAMVVPGSGL 391
Cdd:PLN00070 447 P-----KEAQSKVAKFSFH-GQPA-ELRHGSVVIAaitSCTNTSNPSVMLGAGLVAkkacelGLEVKPWIKTSLAPGSGV 519
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494034330 392 VKAAAEAEGLDRVFQAAGFSWREPGCSMCLAMNPDVLEAGQRCAS----------TSNRNFEGR 445
Cdd:PLN00070 520 VTKYLLKSGLQKYLNQQGFHIVGYGCTTCIGNSGELDESVASAITendivaaavlSGNRNFEGR 583
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
138-445 |
1.46e-16 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 82.48 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 138 DSHTaTH-GAFGALAFGIGTSEVEHALATQTLAQARPKTLAVEVEGQLRPGVEAKDLALAVIDALGFGGGTGHVIEYRGA 216
Cdd:PRK09277 212 DSHT-TMiNGLGVLGWGVGGIEAEAAMLGQPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 217 AVRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFAYL----RDRPHAPAGPDWERATAHWRSlkTDPGARFDRTVRVDAS 292
Cdd:PRK09277 291 GLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLrltgRDEEQVALVEAYAKAQGLWRD--PLEEPVYTDVLELDLS 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 293 AIAPRVTWGTNPaqscgvDGRVPdpdaLPEGPA--REQARRALAYMALEPGTPIRDIRIDR--VFIG---SCTN------ 359
Cdd:PRK09277 369 TVEPSLAGPKRP------QDRIP----LSDVKEafAKSAELGVQGFGLDEAEEGEDYELPDgaVVIAaitSCTNtsnpsv 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 360 -------ARiedlRAAARvveGRRVAEGVAAMVVPGSGLVKAAAEAEGLDRVFQAAGFSWREPGCSMCLAM----NPDVL 428
Cdd:PRK09277 439 miaagllAK----KAVEK---GLKVKPWVKTSLAPGSKVVTDYLEKAGLLPYLEALGFNLVGYGCTTCIGNsgplPPEIE 511
|
330 340
....*....|....*....|...
gi 494034330 429 EA----GQRCAS--TSNRNFEGR 445
Cdd:PRK09277 512 KAindnDLVVTAvlSGNRNFEGR 534
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
113-447 |
1.56e-16 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 82.36 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 113 PRQGIVHVVAPEQgLTQPGMVIVCGDSHTaTHGAFGALAFGIGTSEVEHALATQTLAQARPKTLAVEVEGQLRPGVEAKD 192
Cdd:PRK11413 125 PHIAVIHQYMREM-MAGGGKMILGSDSHT-RYGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 193 LALAVIDALgFGGG--TGHVIEYRGAAVRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFAYLR--DRPHApagpdwera 268
Cdd:PRK11413 203 VALAIIGAV-FKNGyvKNKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLAlhGRGQD--------- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 269 tahWRSLKTDPGARFDRTVRVDASAIAPRVTWGTNPAQSCGVD---GRVPDPDALPEGPAREQARRALAYMALEpgtPIR 345
Cdd:PRK11413 273 ---YCELNPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDelnQNLTDILREVEIESERVAHGKAKLSLLD---KIE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 346 D--IRIDRVFIGSCTNARIEDLRAAARVVEGRRVAEGVAAM-VVPGS-----GLVKAAAEAEgldrvFQAAGFSWREPGC 417
Cdd:PRK11413 347 NgrLKVQQGIIAGCSGGNYENVIAAANALRGQSCGNDTFSLsVYPSSqpvfmDLAKKGVVAD-----LMGAGAIIRTAFC 421
|
330 340 350
....*....|....*....|....*....|
gi 494034330 418 SMCLAMNpDVLEAGQRCASTSNRNFEGRQG 447
Cdd:PRK11413 422 GPCFGAG-DTPANNGLSIRHTTRNFPNREG 450
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
104-454 |
4.66e-13 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 71.36 E-value: 4.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 104 GITLYDIDdprqGIVHVVAPEqgLTQPGMVIVCGDSHTAThgAFGaLAFGIGTSEVEHALATQTLAQARPKTLAVEVEGQ 183
Cdd:PRK09238 458 GVSLRPGD----GVIHSWLNR--MLLPDTVGTGGDSHTRF--PIG-ISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGE 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 184 LRPGVEAKDLALAV-IDALGFGGGT-----------GHVIEYRGaaVRGLSMEGRMTLCNMSIEAGARAGMVA-PDETTF 250
Cdd:PRK09238 529 MQPGITLRDLVHAIpYYAIKQGLLTvekkgkknifsGRILEIEG--LPDLKVEQAFELTDASAERSAAGCTIKlSKEPII 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 251 AYLR---------------DRPHApagpdwERATAHWRS-------LKTDPGARFDRTVRVDASAIaprvtwgTNPAQSC 308
Cdd:PRK09238 607 EYLRsnivllkwmiaegygDARTL------ERRIAAMEEwlanpelLEADADAEYAAVIEIDLAEI-------KEPILAC 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 309 gvdgrvP-DPDALpegpareqarRALAYMAlepGTPIrdiriDRVFIGSC-TNarIEDLRAAARVVEGRRVAEGVAAMVV 386
Cdd:PRK09238 674 ------PnDPDDV----------RLLSEVA---GTKI-----DEVFIGSCmTN--IGHFRAAGKLLEGKKGQLPTRLWVA 727
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494034330 387 PGSGLVKAAAEAEGLDRVFQAAGFSWREPGCSMCLAmNPDVLEAGQRCASTSNRNFEGRQGAGGRTHL 454
Cdd:PRK09238 728 PPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYL 794
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
113-476 |
1.20e-11 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 67.26 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 113 PRQGIVHVVAPEQGLtqPGMVIVCGDSHTAthgaFG-ALAFGIGTSEVEHALATQTLAQARPKTLAVEVEGQLRPGVEAK 191
Cdd:PLN00094 537 PGDGVIHSWLNRMLL--PDTVGTGGDSHTR----FPiGISFPAGSGLVAFGAATGVIPLDMPESVLVRFTGTMQPGITLR 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 192 DLALAV-IDALGFGGGT-----------GHVIEYRGaaVRGLSMEGRMTLCNMSIEAGARAGMVAPDETTFA-YLRDRPh 258
Cdd:PLN00094 611 DLVHAIpYTAIQDGLLTvekkgkknvfsGRILEIEG--LPHLKCEQAFELSDASAERSAAGCTIKLDKEPIIeYLNSNV- 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 259 apAGPDW------------ERATAHWRS-------LKTDPGARFDRTVRVDASAIAPRVTWGTNpaqscgvdgrvpDPDA 319
Cdd:PLN00094 688 --VMLKWmiaegygdrrtlERRIARMQQwladpelLEADPDAEYAAVIEIDMDEIKEPILCAPN------------DPDD 753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 320 lpegpareqaRRALAYMALEpgtpirdiRIDRVFIGSC-TNarIEDLRAAARVVEGRRVAEGVAAMVVPGSGLVKAAAEA 398
Cdd:PLN00094 754 ----------ARLLSEVTGD--------KIDEVFIGSCmTN--IGHFRAAGKLLNDNLSQLPTRLWVAPPTKMDEAQLKA 813
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494034330 399 EGLDRVFQAAGFSWREPGCSMCLAMNPDVLEaGQRCASTSNRNFEGRQGAGGRTHLVGPAMAAAAALAGRFVDVREVM 476
Cdd:PLN00094 814 EGYYSTFGTVGARTEMPGCSLCMGNQARVAE-KSTVVSTSTRNFPNRLGKGANVYLASAELAAVAAILGRLPTVEEYL 890
|
|
| AcnB |
COG1049 |
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ... |
348-454 |
4.14e-09 |
|
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: 59.10 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494034330 348 RIDRVFIGSC-TNarIEDLRAAARVVEGRRVAEgVAAMVVPGSGLVKAAAEAEGLDRVFQAAGFSWREPGCSMCLAmNPD 426
Cdd:COG1049 690 KIDEVFIGSCmTN--IGHFRAAGKLLEGKGNLP-TRLWIAPPTKMDEAQLTEEGYYSIFGAAGARTEMPGCSLCMG-NQA 765
|
90 100
....*....|....*....|....*...
gi 494034330 427 VLEAGQRCASTSNRNFEGRQGAGGRTHL 454
Cdd:COG1049 766 RVADGATVFSTSTRNFPNRLGKGANVYL 793
|
|
| |
