|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
7-478 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 973.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 7 SPKTLYDKVWDSHVVDLQEDGTCLLYIDRHLIHEVTSPQAFEGLRTAGRKVRHPELALATVDHNIPTDPRKdmKDIASfi 86
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRD--LPIAD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 87 hqPDSRTQVLALENNIKEFGLTYYGMNDRRQGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLA 166
Cdd:PRK05478 77 --PVSRIQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 167 TQTILQRKSKNMRIRVNGKLPEGIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIA 246
Cdd:PRK05478 155 TQTLLQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 247 PDATTFEYVKNRPLAPKGDDWEQAVAYWKTLRSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPINGNIPDPAHVKDNV 326
Cdd:PRK05478 235 PDETTFEYLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 327 RAASIQRSLEYMGLKPNTSIVSYPIDKVFIGSCTNSRIEDLRLAAAVVKGRKVAANVKdAMIVPGSGLVKKMAEAEGLDQ 406
Cdd:PRK05478 315 KRASAERALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVR-ALVVPGSGLVKAQAEAEGLDK 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115488 407 IFIEAGFDWREAGCSMCLGMNPDQLKPYERCASTSNRNFEGRQGAKGRTHLVSPAMAAAAAIKGHLCNVREF 478
Cdd:PRK05478 394 IFIEAGFEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVREL 465
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
8-478 |
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: 805.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 8 PKTLYDKVWDSHVVDLQEDGTCLLYIDRHLIHEVTSPQAFEGLRTAGRKVRHPELALATVDHNIPTDPRkdmkDIasFIH 87
Cdd:TIGR00170 2 PRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNR----DF--NIK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 88 QPDSRTQVLALENNIKEFGLTYYGMNDRRQGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLAT 167
Cdd:TIGR00170 76 DEVAKIQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 168 QTILQRKSKNMRIRVNGKLPEGIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAP 247
Cdd:TIGR00170 156 QTLKQARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 248 DATTFEYVKNRPLAPKGDDWEQAVAYWKTLRSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPINGNIPDPAHVKDNVR 327
Cdd:TIGR00170 236 DETTFEYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 328 AASIQRSLEYMGLKPNTSIVSYPIDKVFIGSCTNSRIEDLRLAAAVVKGRKVAANVKdAMIVPGSGLVKKMAEAEGLDQI 407
Cdd:TIGR00170 316 KASAERALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVK-ALVVPGSGLVKLQAEKEGLDKI 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115488 408 FIEAGFDWREAGCSMCLGMNPDQLKPYERCASTSNRNFEGRQGAKGRTHLVSPAMAAAAAIKGHLCNVREF 478
Cdd:TIGR00170 395 FIEAGFEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
13-460 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 708.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 13 DKVWDSHVVDlqEDGTCLLYI-DRHLIHEVTSPQAFEGLRTAGRKVRHPELALATVDHNIPTDPRKDMKDIASFIHQPDS 91
Cdd:pfam00330 1 EKIWDAHLVE--ELDGSLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDHAPDALDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 92 ----RTQVLALENNIKEFGLTYYGMNdrrQGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLAT 167
Cdd:pfam00330 79 isrnKEQYDFLEWNAKKFGIRFVPPG---QGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 168 QTILQRKSKNMRIRVNGKLPEGIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAP 247
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 248 DATTFEYVK--NRPLAPKGDDWEQAVAyWKTLRSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPINGNIPDPAhvKDN 325
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDPF--ADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 326 VRAASIQRSLEYMGLKPNTSIVSYPIDKVFIGSCTNSRIEDLRLAAAVVK-----GRKVAANVKdAMIVPGSGLVKKMAE 400
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVK-ASVVPGSEVVRAYAE 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 401 AEGLDQIFIEAGFDWREAGCSMCLGmNPDQLKPYERCASTSNRNFEGRQGAKGRTHLVSP 460
Cdd:pfam00330 392 AEGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASP 450
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
8-478 |
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: 700.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 8 PKTLYDKVWDSHVV-DLQEDGTCLLYIDRHLIHEVTSPQAFEGLRTAG-RKVRHPELALATVDHNIPTDPrkdmkdiasf 85
Cdd:COG0065 2 GMTLAEKILARHAGrEVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPTKD---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 86 ihqPDSRTQVLALENNIKEFGLTYYGMNDRrqGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVL 165
Cdd:COG0065 72 ---PKSAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 166 ATQTILQRKSKNMRIRVNGKLPEGIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMI 245
Cdd:COG0065 147 ATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGII 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 246 APDATTFEYVKNRPLAPkgddweqavayWKTLRSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPINGnipdpahvkdn 325
Cdd:COG0065 227 APDETTFEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE----------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 326 vraasiqrsleymglkpntsIVSYPIDKVFIGSCTNSRIEDLRLAAAVVKGRKVAANVKdAMIVPGSGLVKKMAEAEGLD 405
Cdd:COG0065 285 --------------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVR-AIVVPGSQEVYRQAEAEGLD 343
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115488 406 QIFIEAGFDWREAGCSMCLGMNPDQLKPYERCASTSNRNFEGRQGAKG-RTHLVSPAMAAAAAIKGHLCNVREF 478
Cdd:COG0065 344 EIFIEAGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGSPGsRTYLASPATAAASAIAGRITDPREL 417
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
35-472 |
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: 621.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 35 RHLIHEVTSPQAFEGLRTAGR-KVRHPELALATVDHNIPTDprkdmkdiasfihQPDSRTQVLALENNIKEFGLTYYGMN 113
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPTP-------------DIKAAEQVKTLRKFAKEFGINFFDVG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 114 drRQGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNGKLPEGIASK 193
Cdd:cd01583 68 --RQGICHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 194 DLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAPDATTFEYVKNRPlapkgddweqaVAY 273
Cdd:cd01583 146 DVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRG-----------KAY 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 274 WKTLRSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPINGNIPdpahvkdnvraasiqrsleymglkpntsivsYPIDK 353
Cdd:cd01583 215 WKELKSDEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 354 VFIGSCTNSRIEDLRLAAAVVKGRKVAANVKdAMIVPGSGLVKKMAEAEGLDQIFIEAGFDWREAGCSMCLGMNPDQLKP 433
Cdd:cd01583 264 VFIGSCTNGRLEDLRAAAEILKGRKVADGVR-LIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAP 342
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 19115488 434 YERCASTSNRNFEGRQGAKG-RTHLVSPAMAAAAAIKGHL 472
Cdd:cd01583 343 GERCVSTSNRNFKGRMGSPGaRIYLASPATAAASAITGEI 382
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
539-734 |
7.45e-120 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 357.90 E-value: 7.45e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 539 KFTVVEGIAAPLPMANVDTDKIIPKQFLKTIKRTGLGQFAFYEIRYDADGKEIPDFVLNREPYRHATVLVAHDNFGCGSS 618
Cdd:PRK01641 3 KFTTHTGLAVPLDRANVDTDQIIPKQFLKRITRTGFGKGLFDDWRYLDDGQPNPDFVLNQPRYQGASILLAGDNFGCGSS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 619 REHAPWALNDFGIRVIIAPSFADIFFNNCFKNGMLPIPTPIEQVNDMMKAAEN--QVKFSVDLVNQTITYGDKQVKFDVE 696
Cdd:PRK01641 83 REHAPWALADYGFRAVIAPSFADIFYNNCFKNGLLPIVLPEEDVDELFKLVEAnpGAELTVDLEAQTVTAPDKTFPFEID 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 19115488 697 PFRKHCLVNGLDDIGLTLQKETMIDAFEAAREENFPWM 734
Cdd:PRK01641 163 PFRRHCLLNGLDDIGLTLQHEDAIAAYEAKRPAFRPWL 200
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
539-734 |
2.89e-103 |
|
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; 3-isopropylmalate dehydratase small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439836 [Multi-domain] Cd Length: 195 Bit Score: 314.80 E-value: 2.89e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 539 KFTVVEGIAAPLPMANVDTDKIIPKQFLKTIKRTGLGQFAFYEIRYDAdgKEIPDFVLNREPYRHATVLVAHDNFGCGSS 618
Cdd:COG0066 2 KFTTLTGRAVPLDGDNIDTDQIIPARFLKTIDREGLGKHLFEDWRYDR--SPDPDFVLNQPRYQGADILVAGRNFGCGSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 619 REHAPWALNDFGIRVIIAPSFADIFFNNCFKNGMLPIPTPIEQVNDMMKAAENQ--VKFSVDLVNQTITYGDKQV-KFDV 695
Cdd:COG0066 80 REHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEAVDALFAAIEANpgDELTVDLEAGTVTNGTGETyPFEI 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 19115488 696 EPFRKHCLVNGLDDIGLTLQKETMIDAFEAAREenfPWM 734
Cdd:COG0066 160 DPFRRECLLNGLDDIGLTLKHADAIAAFEAKRP---AWL 195
|
|
| leuD |
TIGR00171 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
540-720 |
2.62e-86 |
|
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The candidate archaeal leuD proteins are not included in the seed alignment for this model and score below the trusted cutoff. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 129275 [Multi-domain] Cd Length: 188 Bit Score: 270.53 E-value: 2.62e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 540 FTVVEGIAAPLPMANVDTDKIIPKQFLKTIKRTGLGQFAFYEIRY-DADGKEI-PDFVLNREPYRHATVLVAHDNFGCGS 617
Cdd:TIGR00171 4 FKSHTGLVAPLDAANVDTDAIIPKQFLKRITRTGFGKHLFFDWRFlDANGKEPnPDFVLNQPQYQGASILLARENFGCGS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 618 SREHAPWALNDFGIRVIIAPSFADIFFNNCFKNGMLPIPTPIEQVNDMMKAAENQ-VKFSVDLVNQTITYGD-KQVKFDV 695
Cdd:TIGR00171 84 SREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPIRLSYDEVKELFGQVENQgLQMTVDLENQLIHDSEgKVYSFEI 163
|
170 180
....*....|....*....|....*
gi 19115488 696 EPFRKHCLVNGLDDIGLTLQKETMI 720
Cdd:TIGR00171 164 DPFRKHCLINGLDEIGLTLQHEDEI 188
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
33-474 |
1.42e-85 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 277.02 E-value: 1.42e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 33 IDRHLIHEVTSPQAFEGLRTAGRKVRHPELALATVDHNIPTDPRKdmkdIASFihqpdsrtQVLALENnIKEFGLTYYGM 112
Cdd:NF040615 26 VDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPANTVK----AANM--------QKITREF-VKEQGIKNFYL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 113 NDrrQGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNGKlPEGIAS 192
Cdd:NF040615 93 GG--EGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVNIVGK-NENISG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 193 KDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAPDATTFEYVKNRPLApkgddwEQAVA 272
Cdd:NF040615 170 KDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEGVS------EEEIA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 273 YWKTLR---SDENAKYDIEVEINAADVlptvtwgtSPQDVIPingnipdpaHVKDNVraasiqrsleymglKPNTSIVSY 349
Cdd:NF040615 244 ELKKNRitvNEKEENYYKEIEIDITDM--------EEQVACP---------HHPDNV--------------KPVSEVEGT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 350 PIDKVFIGSCTNSRIEDLRLAAAVVKGRKVAANVKdAMIVPGSGLVKKMAEAEGLDQIFIEAGFDWREAGCSMCLGMNPD 429
Cdd:NF040615 293 EIDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVR-LIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQG 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 19115488 430 QLKPYERCASTSNRNFEGRQG-AKGRTHLVSPAMAAAAAIKGHLCN 474
Cdd:NF040615 372 VLGDGEVCLSTTNRNFKGRMGnINSYIYLSSPKIAAKSAVKGYITN 417
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
538-655 |
3.08e-45 |
|
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This domain undergoes conformational change in the enzyme mechanism.
Pssm-ID: 459908 [Multi-domain] Cd Length: 131 Bit Score: 158.30 E-value: 3.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 538 PKFTVVEGIAAPLPMANVDTDKIIPKQFLKTIKRTGLGQFAFYEIRY----DADGKEIPDFVLNREPYRHAT---VLVAH 610
Cdd:pfam00694 2 PVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYgkvrYLPDGENPDFYDAAMRYKQHGapiVVIGG 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 19115488 611 DNFGCGSSREHAPWALNDFGIRVIIAPSFADIFFNNCFKNGMLPI 655
Cdd:pfam00694 82 KNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPL 126
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
550-679 |
1.04e-38 |
|
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238809 [Multi-domain] Cd Length: 91 Bit Score: 138.49 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 550 LPMANVDTDKIIPKQFLktikrtglgqfafyeirydadgkeipdfvlnrepyrhATVLVAHDNFGCGSSREHAPWALNDF 629
Cdd:cd01577 1 LFGDNIDTDQIIPARFL-------------------------------------GDIIVAGKNFGCGSSREHAPWALKDA 43
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 19115488 630 GIRVIIAPSFADIFFNNCFKNGMLPIPTPIEQVNDmmKAAENQVKFSVDL 679
Cdd:cd01577 44 GIRAVIAESFARIFFRNAINNGLLPVTLADEDVEE--VEAKPGDEVEVDL 91
|
|
| HacB2_Meth |
NF040625 |
homoaconitase small subunit; |
554-712 |
1.72e-19 |
|
homoaconitase small subunit;
Pssm-ID: 468597 [Multi-domain] Cd Length: 161 Bit Score: 85.92 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 554 NVDTDKIIPKQFLKTIKRTGLGQFAFYEIRydadgkeiPDFVLNrepYRHATVLVAHDNFGCGSSREHAPWALNDFGIRV 633
Cdd:NF040625 14 NIDTDVIIPGRYLRTFNPDDLASHVMEGER--------PDFTKN---VQKGDIIVAGWNFGCGSSREQAPVAIKHAGVSA 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19115488 634 IIAPSFADIFFNNCFKNGMLPIPTPIEqvndmmkaAENQVKFSVDLVNQTITYGDKQVKFDVEPFRKHCLvNGLDDIGL 712
Cdd:NF040625 83 IIAKSFARIFYRNAINIGLPVIVADIE--------ADDGDILSIDLEKGIIKNKTTGEEFKIQPFKEFML-EILEDGGL 152
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
7-478 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 973.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 7 SPKTLYDKVWDSHVVDLQEDGTCLLYIDRHLIHEVTSPQAFEGLRTAGRKVRHPELALATVDHNIPTDPRKdmKDIASfi 86
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRD--LPIAD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 87 hqPDSRTQVLALENNIKEFGLTYYGMNDRRQGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLA 166
Cdd:PRK05478 77 --PVSRIQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 167 TQTILQRKSKNMRIRVNGKLPEGIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIA 246
Cdd:PRK05478 155 TQTLLQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 247 PDATTFEYVKNRPLAPKGDDWEQAVAYWKTLRSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPINGNIPDPAHVKDNV 326
Cdd:PRK05478 235 PDETTFEYLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 327 RAASIQRSLEYMGLKPNTSIVSYPIDKVFIGSCTNSRIEDLRLAAAVVKGRKVAANVKdAMIVPGSGLVKKMAEAEGLDQ 406
Cdd:PRK05478 315 KRASAERALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVR-ALVVPGSGLVKAQAEAEGLDK 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115488 407 IFIEAGFDWREAGCSMCLGMNPDQLKPYERCASTSNRNFEGRQGAKGRTHLVSPAMAAAAAIKGHLCNVREF 478
Cdd:PRK05478 394 IFIEAGFEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVREL 465
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
6-480 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 828.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 6 ASPKTLYDKVWDSHVVDLQEDGTCLLYIDRHLIHEVTSPQAFEGLRTAGRKVRHPELALATVDHNIPTDPRKDMKdiasf 85
Cdd:PRK12466 1 MMPRTLYDKLWDSHTVARLDDGHVLLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPTRPGRDRG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 86 IHQPDSRTQVLALENNIKEFGLTYYGMNDRRQGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVL 165
Cdd:PRK12466 76 ITDPGGALQVDYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 166 ATQTILQRKSKNMRIRVNGKLPEGIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMI 245
Cdd:PRK12466 156 ATQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 246 APDATTFEYVKNRPLAPKGDDWEQAVAYWKTLRSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPINGNIPDPAHVKDN 325
Cdd:PRK12466 236 APDETTFDYLRGRPRAPKGALWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAAEADP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 326 VRAASIQRSLEYMGLKPNTSIVSYPIDKVFIGSCTNSRIEDLRLAAAVVKGRKVAANVkDAMIVPGSGLVKKMAEAEGLD 405
Cdd:PRK12466 316 ARRAAMERALDYMGLTPGTPLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGV-RAMVVPGSGAVRRQAEAEGLA 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115488 406 QIFIEAGFDWREAGCSMCLGMNPDQLKPYERCASTSNRNFEGRQGAKGRTHLVSPAMAAAAAIKGHLCNVREFFG 480
Cdd:PRK12466 395 RIFIAAGFEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHITDVRSLLQ 469
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
8-478 |
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: 805.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 8 PKTLYDKVWDSHVVDLQEDGTCLLYIDRHLIHEVTSPQAFEGLRTAGRKVRHPELALATVDHNIPTDPRkdmkDIasFIH 87
Cdd:TIGR00170 2 PRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNR----DF--NIK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 88 QPDSRTQVLALENNIKEFGLTYYGMNDRRQGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLAT 167
Cdd:TIGR00170 76 DEVAKIQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 168 QTILQRKSKNMRIRVNGKLPEGIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAP 247
Cdd:TIGR00170 156 QTLKQARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 248 DATTFEYVKNRPLAPKGDDWEQAVAYWKTLRSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPINGNIPDPAHVKDNVR 327
Cdd:TIGR00170 236 DETTFEYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 328 AASIQRSLEYMGLKPNTSIVSYPIDKVFIGSCTNSRIEDLRLAAAVVKGRKVAANVKdAMIVPGSGLVKKMAEAEGLDQI 407
Cdd:TIGR00170 316 KASAERALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVK-ALVVPGSGLVKLQAEKEGLDKI 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115488 408 FIEAGFDWREAGCSMCLGMNPDQLKPYERCASTSNRNFEGRQGAKGRTHLVSPAMAAAAAIKGHLCNVREF 478
Cdd:TIGR00170 395 FIEAGFEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
13-460 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 708.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 13 DKVWDSHVVDlqEDGTCLLYI-DRHLIHEVTSPQAFEGLRTAGRKVRHPELALATVDHNIPTDPRKDMKDIASFIHQPDS 91
Cdd:pfam00330 1 EKIWDAHLVE--ELDGSLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVIDHAPDALDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 92 ----RTQVLALENNIKEFGLTYYGMNdrrQGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLAT 167
Cdd:pfam00330 79 isrnKEQYDFLEWNAKKFGIRFVPPG---QGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 168 QTILQRKSKNMRIRVNGKLPEGIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAP 247
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 248 DATTFEYVK--NRPLAPKGDDWEQAVAyWKTLRSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPINGNIPDPAhvKDN 325
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDPF--ADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 326 VRAASIQRSLEYMGLKPNTSIVSYPIDKVFIGSCTNSRIEDLRLAAAVVK-----GRKVAANVKdAMIVPGSGLVKKMAE 400
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVK-ASVVPGSEVVRAYAE 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 401 AEGLDQIFIEAGFDWREAGCSMCLGmNPDQLKPYERCASTSNRNFEGRQGAKGRTHLVSP 460
Cdd:pfam00330 392 AEGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASP 450
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
8-478 |
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: 700.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 8 PKTLYDKVWDSHVV-DLQEDGTCLLYIDRHLIHEVTSPQAFEGLRTAG-RKVRHPELALATVDHNIPTDPrkdmkdiasf 85
Cdd:COG0065 2 GMTLAEKILARHAGrEVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPTKD---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 86 ihqPDSRTQVLALENNIKEFGLTYYGMNDRrqGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVL 165
Cdd:COG0065 72 ---PKSAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 166 ATQTILQRKSKNMRIRVNGKLPEGIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMI 245
Cdd:COG0065 147 ATGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGII 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 246 APDATTFEYVKNRPLAPkgddweqavayWKTLRSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPINGnipdpahvkdn 325
Cdd:COG0065 227 APDETTFEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE----------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 326 vraasiqrsleymglkpntsIVSYPIDKVFIGSCTNSRIEDLRLAAAVVKGRKVAANVKdAMIVPGSGLVKKMAEAEGLD 405
Cdd:COG0065 285 --------------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVR-AIVVPGSQEVYRQAEAEGLD 343
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115488 406 QIFIEAGFDWREAGCSMCLGMNPDQLKPYERCASTSNRNFEGRQGAKG-RTHLVSPAMAAAAAIKGHLCNVREF 478
Cdd:COG0065 344 EIFIEAGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGSPGsRTYLASPATAAASAIAGRITDPREL 417
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
35-472 |
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: 621.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 35 RHLIHEVTSPQAFEGLRTAGR-KVRHPELALATVDHNIPTDprkdmkdiasfihQPDSRTQVLALENNIKEFGLTYYGMN 113
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPTP-------------DIKAAEQVKTLRKFAKEFGINFFDVG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 114 drRQGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNGKLPEGIASK 193
Cdd:cd01583 68 --RQGICHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 194 DLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAPDATTFEYVKNRPlapkgddweqaVAY 273
Cdd:cd01583 146 DVILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRG-----------KAY 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 274 WKTLRSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPINGNIPdpahvkdnvraasiqrsleymglkpntsivsYPIDK 353
Cdd:cd01583 215 WKELKSDEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 354 VFIGSCTNSRIEDLRLAAAVVKGRKVAANVKdAMIVPGSGLVKKMAEAEGLDQIFIEAGFDWREAGCSMCLGMNPDQLKP 433
Cdd:cd01583 264 VFIGSCTNGRLEDLRAAAEILKGRKVADGVR-LIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAP 342
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 19115488 434 YERCASTSNRNFEGRQGAKG-RTHLVSPAMAAAAAIKGHL 472
Cdd:cd01583 343 GERCVSTSNRNFKGRMGSPGaRIYLASPATAAASAITGEI 382
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
8-478 |
6.15e-124 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 376.82 E-value: 6.15e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 8 PKTLYDKVWDSHVVDLQEDGTCLLY-IDRHLIHEVTSPQAFEGLRTAG-RKVRHPELALATVDHNIPTdprkdmKDIasf 85
Cdd:PRK00402 2 GMTLAEKILARHSGRDVSPGDIVEAkVDLVMAHDITGPLAIKEFEKIGgDKVFDPSKIVIVFDHFVPA------KDI--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 86 ihqpDSRTQVLALENNIKEFGLTYYgmNDRRQGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVL 165
Cdd:PRK00402 73 ----KSAEQQKILREFAKEQGIPNF--FDVGEGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 166 ATQTILQRKSKNMRIRVNGKLPEGIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMI 245
Cdd:PRK00402 147 ATGKTWFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 246 APDATTFEYVKNRPLAPkgddweqavayWKTLRSDENAKYDIEVEINAADVLPTVTWGTSPqdvipingnipdpahvkDN 325
Cdd:PRK00402 227 APDEKTLEYLKERAGRD-----------YKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLP-----------------DN 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 326 VRAASiqrslEYMGLKpntsivsypIDKVFIGSCTNSRIEDLRLAAAVVKGRKVAANVKdAMIVPGSGLVKKMAEAEGLD 405
Cdd:PRK00402 279 VKPVS-----EVEGTK---------VDQVFIGSCTNGRLEDLRIAAEILKGRKVAPGVR-LIVIPASQKIYLQALKEGLI 343
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115488 406 QIFIEAGFDWREAGCSMCLGMNPDQLKPYERCASTSNRNFEGRQG-AKGRTHLVSPAMAAAAAIKGHLCNVREF 478
Cdd:PRK00402 344 EIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGsPESEVYLASPAVAAASAVTGKITDPREV 417
|
|
| leuD |
PRK01641 |
3-isopropylmalate dehydratase small subunit; |
539-734 |
7.45e-120 |
|
3-isopropylmalate dehydratase small subunit;
Pssm-ID: 179314 [Multi-domain] Cd Length: 200 Bit Score: 357.90 E-value: 7.45e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 539 KFTVVEGIAAPLPMANVDTDKIIPKQFLKTIKRTGLGQFAFYEIRYDADGKEIPDFVLNREPYRHATVLVAHDNFGCGSS 618
Cdd:PRK01641 3 KFTTHTGLAVPLDRANVDTDQIIPKQFLKRITRTGFGKGLFDDWRYLDDGQPNPDFVLNQPRYQGASILLAGDNFGCGSS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 619 REHAPWALNDFGIRVIIAPSFADIFFNNCFKNGMLPIPTPIEQVNDMMKAAEN--QVKFSVDLVNQTITYGDKQVKFDVE 696
Cdd:PRK01641 83 REHAPWALADYGFRAVIAPSFADIFYNNCFKNGLLPIVLPEEDVDELFKLVEAnpGAELTVDLEAQTVTAPDKTFPFEID 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 19115488 697 PFRKHCLVNGLDDIGLTLQKETMIDAFEAAREENFPWM 734
Cdd:PRK01641 163 PFRRHCLLNGLDDIGLTLQHEDAIAAYEAKRPAFRPWL 200
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
33-476 |
6.39e-106 |
|
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: 330.18 E-value: 6.39e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 33 IDRHLIHEVTSPQAFEGL-RTAGRKVRHPELALATVDHNIPTDPRKDMKDiasfihqpdsrtQVLALENnIKEFGLTYYg 111
Cdd:TIGR01343 25 IDLAMVHDITAPLAIKTLeEYGIDKVWNPEKIVIVFDHQVPADTIKAAEM------------QKLAREF-VKKQGIKYF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 112 mNDRRQGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNGKLPEGIA 191
Cdd:TIGR01343 91 -YDVGEGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFKVPETIRVNITGKLNPGVT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 192 SKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAPDATTFEYVKNRPLAPkgddweqav 271
Cdd:TIGR01343 170 AKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYLKERRKEP--------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 272 ayWKTLRSDENAKYDIEVEINAADVLPTVTWgtspqdvipingnipdPAHVkDNVRAASiqrslEYMGLkpntsivsyPI 351
Cdd:TIGR01343 241 --FRVYKSDEDAEYAKEIEIDASQIEPVVAC----------------PHNV-DNVKPVS-----EVEGT---------EI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 352 DKVFIGSCTNSRIEDLRLAAAVVKGRKVAANVKdAMIVPGSGLVKKMAEAEGLDQIFIEAGFDWREAGCSMCLGMNPDQL 431
Cdd:TIGR01343 288 DQVFIGSCTNGRLEDLRVAAKILKGRKVAPDVR-LIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLGSHQGVL 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 19115488 432 KPYERCASTSNRNFEGRQGAK-GRTHLVSPAMAAAAAIKGHLCNVR 476
Cdd:TIGR01343 367 APGEVCISTSNRNFKGRMGHPnAEIYLASPATAAASAVKGYIADPR 412
|
|
| LeuD |
COG0066 |
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; ... |
539-734 |
2.89e-103 |
|
3-isopropylmalate dehydratase small subunit [Amino acid transport and metabolism]; 3-isopropylmalate dehydratase small subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439836 [Multi-domain] Cd Length: 195 Bit Score: 314.80 E-value: 2.89e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 539 KFTVVEGIAAPLPMANVDTDKIIPKQFLKTIKRTGLGQFAFYEIRYDAdgKEIPDFVLNREPYRHATVLVAHDNFGCGSS 618
Cdd:COG0066 2 KFTTLTGRAVPLDGDNIDTDQIIPARFLKTIDREGLGKHLFEDWRYDR--SPDPDFVLNQPRYQGADILVAGRNFGCGSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 619 REHAPWALNDFGIRVIIAPSFADIFFNNCFKNGMLPIPTPIEQVNDMMKAAENQ--VKFSVDLVNQTITYGDKQV-KFDV 695
Cdd:COG0066 80 REHAPWALKDYGFRAVIAPSFADIFYRNAINNGLLPIELPEEAVDALFAAIEANpgDELTVDLEAGTVTNGTGETyPFEI 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 19115488 696 EPFRKHCLVNGLDDIGLTLQKETMIDAFEAAREenfPWM 734
Cdd:COG0066 160 DPFRRECLLNGLDDIGLTLKHADAIAAFEAKRP---AWL 195
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
9-477 |
1.70e-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: 279.34 E-value: 1.70e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 9 KTLYDKVWDSHVVDLQEDG-TCLLYIDRHLIHEVTSPQAFEGLRTAGR-KVRHPELALATVDHNIPTdPRKDMKDIasfi 86
Cdd:TIGR02086 1 MTLAEKILSEKVGRPVCAGeIVEVEVDLAMTHDGTGPLAIKALRELGVaRVWDPEKIVIAFDHNVPP-PTVEAAEM---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 87 hqpdsrtQVLALENnIKEFGLTYYGMNDrrqGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLA 166
Cdd:TIGR02086 76 -------QKEIREF-AKRHGIKNFDVGE---GICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 167 TQTILQRKSKNMRIRVNGKLPEGIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIA 246
Cdd:TIGR02086 145 TGKTWIKVPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 247 PDATTFEYVKNRplapKGDDWeqavaywKTLRSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPINgnipdpahvkdnv 326
Cdd:TIGR02086 225 PDEETYEYLKKR----RGLEF-------RILVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVS------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 327 raasiqrslEYMGLKpntsivsypIDKVFIGSCTNSRIEDLRLAAAVVKGRKVAANVKdAMIVPGSGLVKKMAEAEGLDQ 406
Cdd:TIGR02086 281 ---------DVEGTE---------IDQVFIGSCTNGRLEDLRIAAEILKGRRVHPDVR-LIVIPASRKVYLRALEEGIIL 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115488 407 IFIEAGFDWREAGCSMCLGMNPDQLKPYERCASTSNRNFEGRQGA-KGRTHLVSPAMAAAAAIKGHLCNVRE 477
Cdd:TIGR02086 342 TLVRAGAMICPPGCGPCLGAHMGVLGDGEVCLSTTNRNFKGRMGSpNAEIYLASPATAAASAVEGYITDPED 413
|
|
| leuD |
TIGR00171 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
540-720 |
2.62e-86 |
|
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The candidate archaeal leuD proteins are not included in the seed alignment for this model and score below the trusted cutoff. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 129275 [Multi-domain] Cd Length: 188 Bit Score: 270.53 E-value: 2.62e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 540 FTVVEGIAAPLPMANVDTDKIIPKQFLKTIKRTGLGQFAFYEIRY-DADGKEI-PDFVLNREPYRHATVLVAHDNFGCGS 617
Cdd:TIGR00171 4 FKSHTGLVAPLDAANVDTDAIIPKQFLKRITRTGFGKHLFFDWRFlDANGKEPnPDFVLNQPQYQGASILLARENFGCGS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 618 SREHAPWALNDFGIRVIIAPSFADIFFNNCFKNGMLPIPTPIEQVNDMMKAAENQ-VKFSVDLVNQTITYGD-KQVKFDV 695
Cdd:TIGR00171 84 SREHAPWALDDYGFKVIIAPSFADIFYNNSFKNGLLPIRLSYDEVKELFGQVENQgLQMTVDLENQLIHDSEgKVYSFEI 163
|
170 180
....*....|....*....|....*
gi 19115488 696 EPFRKHCLVNGLDDIGLTLQKETMI 720
Cdd:TIGR00171 164 DPFRKHCLINGLDEIGLTLQHEDEI 188
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
33-474 |
1.42e-85 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 277.02 E-value: 1.42e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 33 IDRHLIHEVTSPQAFEGLRTAGRKVRHPELALATVDHNIPTDPRKdmkdIASFihqpdsrtQVLALENnIKEFGLTYYGM 112
Cdd:NF040615 26 VDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPANTVK----AANM--------QKITREF-VKEQGIKNFYL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 113 NDrrQGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNGKlPEGIAS 192
Cdd:NF040615 93 GG--EGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVNIVGK-NENISG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 193 KDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAPDATTFEYVKNRPLApkgddwEQAVA 272
Cdd:NF040615 170 KDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEGVS------EEEIA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 273 YWKTLR---SDENAKYDIEVEINAADVlptvtwgtSPQDVIPingnipdpaHVKDNVraasiqrsleymglKPNTSIVSY 349
Cdd:NF040615 244 ELKKNRitvNEKEENYYKEIEIDITDM--------EEQVACP---------HHPDNV--------------KPVSEVEGT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 350 PIDKVFIGSCTNSRIEDLRLAAAVVKGRKVAANVKdAMIVPGSGLVKKMAEAEGLDQIFIEAGFDWREAGCSMCLGMNPD 429
Cdd:NF040615 293 EIDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVR-LIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQG 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 19115488 430 QLKPYERCASTSNRNFEGRQG-AKGRTHLVSPAMAAAAAIKGHLCN 474
Cdd:NF040615 372 VLGDGEVCLSTTNRNFKGRMGnINSYIYLSSPKIAAKSAVKGYITN 417
|
|
| LEU2 |
TIGR02083 |
3-isopropylmalate dehydratase, large subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
30-477 |
9.31e-80 |
|
3-isopropylmalate dehydratase, large subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. These homologs are described by a separate model of subfamily (rather than equivalog) homology type (TIGR01343). This model along with TIGR00170 describe clades which consist only of LeuC sequences. Here, the genes from Pyrococcus furiosus, Clostridium acetobutylicum, Thermotoga maritima and others are gene clustered with related genes from the leucine biosynthesis pathway. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 131138 Cd Length: 419 Bit Score: 261.67 E-value: 9.31e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 30 LLYIDRHLIHEVTSPQAFEGLRTAG-RKVRHPELALATVDHnipTDPRKDMKdiasfihqpdSRTQVLALENNIKEFGLT 108
Cdd:TIGR02083 24 LAKLDIVLGNDITTPLAIKAFKEYGgKKVFDPDRVALVPDH---FTPNKDIK----------SAEQCKMMREFAREQGIE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 109 YYgMNDRRQGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNGKLPE 188
Cdd:TIGR02083 91 KF-FEIGNMGIEHALLPEEGIVKPGDLIIGADSHTCTYGALGAFATGVGSTDMAVGMATGKAWFRVPEAIKFVLKGKLKP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 189 GIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAPDATTFEYVKNRplapkgddwe 268
Cdd:TIGR02083 170 WVTGKDLILHIIGIIGVDGALYKSMEFSGEGLKELSMDDRFTIANMAIEAGAKTGIFPVDEITIEYEKGR---------- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 269 qAVAYWKTLRSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPIngnipdpahvkDNVRAASIQrsleymglkpntsivs 348
Cdd:TIGR02083 240 -GKREEKIYKADEDAKYVRVIEIDLSELEPQVAFPHLPENTKDI-----------SEAGKEEIK---------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 349 ypIDKVFIGSCTNSRIEDLRLAAAVVKGRKVAANVKdAMIVPGSGLVKKMAEAEGLDQIFIEAGFDWREAGCSMCLGMNP 428
Cdd:TIGR02083 292 --IDQVVIGSCTNGRLEDLRLAAEILKGKTVAPDVR-CIIIPGSQNVYLEAMKEGLLEIFIEAGAVVSTPTCGPCLGGHM 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 19115488 429 DQLKPYERCASTSNRNFEGRQG-AKGRTHLVSPAMAAAAAIKGHLCNVRE 477
Cdd:TIGR02083 369 GILAEGERAISTTNRNFVGRMGhPKSEVYLASPAVAAASAIKGYIASPEE 418
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
8-655 |
1.03e-66 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 232.73 E-value: 1.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 8 PKTLYDKVWDSHVVDLQ-EDGTCL-LYIDRHLIHEVTSPQAFEGLRTAGR-KVRhPELALATVDHNIP-TDPRKdmKDIA 83
Cdd:PRK07229 2 GLTLTEKILYAHLVEGElEPGEEIaIRIDQTLTQDATGTMAYLQFEAMGLdRVK-TELSVQYVDHNLLqADFEN--ADDH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 84 SFIhqpdsrtQVLAlenniKEFGLTYY--GmndrrQGIVHVIGPEQgFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEV 161
Cdd:PRK07229 79 RFL-------QSVA-----AKYGIYFSkpG-----NGICHQVHLER-FAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 162 EHVLATQTILQRKSKNMRIRVNGKLPEGIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGAR 241
Cdd:PRK07229 141 ALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGAT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 242 AGMIAPDATTFEYVK--NRplapkGDDWEQavaywktLRSDENAKYDIEVEINAADVLPTVTWGTSPqdvipingnipdp 319
Cdd:PRK07229 221 TSIFPSDERTREFLKaqGR-----EDDWVE-------LLADPDAEYDEVIEIDLSELEPLIAGPHSP------------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 320 ahvkDNVRAASiqrslEYMGLKpntsivsypIDKVFIGSCTNSRIEDLRLAAAVVKGRKVAANVkDAMIVPGSGLVKKMA 399
Cdd:PRK07229 276 ----DNVVPVS-----EVAGIK---------VDQVLIGSCTNSSYEDLMRAASILKGKKVHPKV-SLVINPGSRQVLEML 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 400 EAEGLDQIFIEAGFDWREAGCSMCLGMnpDQlKPYERCAS--TSNRNFEGRQGAK-GRTHLVSPAMAAAAAIKGHLCNVR 476
Cdd:PRK07229 337 ARDGALADLIAAGARILENACGPCIGM--GQ-APATGNVSlrTFNRNFPGRSGTKdAQVYLASPETAAASALTGVITDPR 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 477 EFfgDVSNGSPSiitnknydpshDVEGDIGLSVDDATDAVTDADGIATNVAgsVSSGSAGIPKFT-VVEGIAAPLPMA-- 553
Cdd:PRK07229 414 TL--ALENGEYP-----------KLEEPEGFAVDDAGIIAPAEDGSDVEVV--RGPNIKPLPLLEpLPDLLEGKVLLKvg 478
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 554 -NVDTDKIIP--KQFLK---TIKRtgLGQFAFyeIRYDADgkeIPDFVLNREPyrhaTVLVAHDNFGCGSSREHAPWALN 627
Cdd:PRK07229 479 dNITTDHIMPagAKWLPyrsNIPN--ISEFVF--EGVDNT---FPERAKEQGG----GIVVGGENYGQGSSREHAALAPR 547
|
650 660
....*....|....*....|....*...
gi 19115488 628 DFGIRVIIAPSFADIFFNNCFKNGMLPI 655
Cdd:PRK07229 548 YLGVKAVLAKSFARIHKANLINFGILPL 575
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
37-470 |
8.78e-63 |
|
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: 215.44 E-value: 8.78e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 37 LIHEVTSPQA---FEGLRTAGrKVRHPELALATVDHNIPTDPRKDMKDiasfihqpdsrtqvlalENNIKEFGLTYYGMN 113
Cdd:cd01351 3 MLQDATGPMAmkaFEILAALG-KVADPSQIACVHDHAVQLEKPVNNEG-----------------HKFLSFFAALQGIAF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 114 DR-RQGIVHVIGPEQgFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNGKLPEGIAS 192
Cdd:cd01351 65 YRpGVGIIHQIMVEN-LALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 193 KDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAPDATTFEYVKN--RPLAPKGDDweqa 270
Cdd:cd01351 144 KDVVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEAtgRPLLKNLWL---- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 271 vAYWKTLRSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPIngnipdpahvkdnvraasiqrsleymglkpnTSIVSYP 350
Cdd:cd01351 220 -AFPEELLADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSV-------------------------------SEVEGTK 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 351 IDKVFIGSCTNSRIEDLRLAAAVVKGRKVAANVkDAMIVPGSGLVKKMAEAEGLDQIFIEAGFDWREAGCSMCLGMNPDQ 430
Cdd:cd01351 268 IDQVLIGSCTNNRYSDMLAAAKLLKGAKVAPGV-RLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARL 346
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 19115488 431 LKPYERCASTSNRNFEGRQGAK-GRTHLVSPAMAAAAAIKG 470
Cdd:cd01351 347 VADGEVGVSSGNRNFPGRLGTYeRHVYLASPELAAATAIAG 387
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
118-472 |
4.82e-54 |
|
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: 191.12 E-value: 4.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 118 GIVHVIGPEQgFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNGKLPEGIASKDLIL 197
Cdd:cd01585 69 GICHQVHLER-FAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVIL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 198 HIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAPDATTFEYVKNRPlapKGDDWEQavaywktL 277
Cdd:cd01585 148 ELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQG---REDDWVE-------L 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 278 RSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPIngnipdpahvkdnvraasiqRSLEymGLKpntsivsypIDKVFIG 357
Cdd:cd01585 218 AADADAEYDEEIEIDLSELEPLIARPHSPDNVVPV--------------------REVA--GIK---------VDQVAIG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 358 SCTNSRIEDLRLAAAVVKGRKVAANVkDAMIVPGSGLVKKMAEAEGLDQIFIEAGFDWREAGCSMCLGMNpdQLKPYERC 437
Cdd:cd01585 267 SCTNSSYEDLMTVAAILKGRRVHPHV-SMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMG--QAPPTGGV 343
|
330 340 350
....*....|....*....|....*....|....*..
gi 19115488 438 A-STSNRNFEGRQGAK-GRTHLVSPAMAAAAAIKGHL 472
Cdd:cd01585 344 SvRTFNRNFEGRSGTKdDLVYLASPEVAAAAALTGVI 380
|
|
| Aconitase_C |
pfam00694 |
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This ... |
538-655 |
3.08e-45 |
|
Aconitase C-terminal domain; Members of this family usually also match to pfam00330. This domain undergoes conformational change in the enzyme mechanism.
Pssm-ID: 459908 [Multi-domain] Cd Length: 131 Bit Score: 158.30 E-value: 3.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 538 PKFTVVEGIAAPLPMANVDTDKIIPKQFLKTIKRTGLGQFAFYEIRY----DADGKEIPDFVLNREPYRHAT---VLVAH 610
Cdd:pfam00694 2 PVFLKLKGKTTPDFNSNVDTDLIIPKQFLGTIANIGIGNINFEGWRYgkvrYLPDGENPDFYDAAMRYKQHGapiVVIGG 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 19115488 611 DNFGCGSSREHAPWALNDFGIRVIIAPSFADIFFNNCFKNGMLPI 655
Cdd:pfam00694 82 KNFGCGSSREHAAWALRDLGIKAVIAESFARIHRNNLIKNGLLPL 126
|
|
| IPMI_Swivel |
cd01577 |
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized ... |
550-679 |
1.04e-38 |
|
Aconatase-like swivel domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238809 [Multi-domain] Cd Length: 91 Bit Score: 138.49 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 550 LPMANVDTDKIIPKQFLktikrtglgqfafyeirydadgkeipdfvlnrepyrhATVLVAHDNFGCGSSREHAPWALNDF 629
Cdd:cd01577 1 LFGDNIDTDQIIPARFL-------------------------------------GDIIVAGKNFGCGSSREHAPWALKDA 43
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 19115488 630 GIRVIIAPSFADIFFNNCFKNGMLPIPTPIEQVNDmmKAAENQVKFSVDL 679
Cdd:cd01577 44 GIRAVIAESFARIFFRNAINNGLLPVTLADEDVEE--VEAKPGDEVEVDL 91
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
39-472 |
2.28e-35 |
|
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: 137.75 E-value: 2.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 39 HEVTSPQAFEGLRTAGRKVRHPELALATVDHNIPTDPRKDMKDIASfihqpdsrtqvlaLENNIKEFGLTYYGMNdrrQG 118
Cdd:cd01582 5 HDNSWPVALKFMSIGATKIHNPDQIVMTLDHDVQNKSEKNLKKYKN-------------IESFAKKHGIDFYPAG---RG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 119 IVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNGKLPEGIASKDLILH 198
Cdd:cd01582 69 IGHQIMIEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 199 IIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAPDATtfeyvknrplapkgddweqavaywktlr 278
Cdd:cd01582 149 LCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAK---------------------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 279 sdenakydiEVEINAADVLPTVTWGTSpqdvipingnipdpahvkdnVRAASIQRSLEYMGLKpntsivsypIDKVFIGS 358
Cdd:cd01582 201 ---------HLILDLSTLSPYVSGPNS--------------------VKVSTPLKELEAQNIK---------INKAYLVS 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 359 CTNSRIEDLRLAAAVVKGRK-------VAANVKdAMIVPGSGLVKKMAEAEGLDQIFIEAGFDWREAGCSMCLGMNPDQL 431
Cdd:cd01582 243 CTNSRASDIAAAADVVKGKKekngkipVAPGVE-FYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQGLL 321
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 19115488 432 KPYERCASTSNRNFEGRQGAK-GRTHLVSPAMAAAAAIKGHL 472
Cdd:cd01582 322 EPGEVGISATNRNFKGRMGSTeALAYLASPAVVAASAISGKI 363
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
118-472 |
8.59e-35 |
|
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: 137.57 E-value: 8.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 118 GIVHVIGPEQgFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNGKLPEGIASKDLIL 197
Cdd:cd01584 77 GIIHQIVLEN-YAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVIL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 198 HIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAPDATTFEYVK--NRP-LAPKGDDWEQavayw 274
Cdd:cd01584 156 KVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKatGRAeIADLADEFKD----- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 275 KTLRSDENAKYDIEVEINAADVLPTvtwgtspqdvipINGNI-PDPAHVKDNVRAASIQRsleymglkpntsivSYPID- 352
Cdd:cd01584 231 DLLVADEGAEYDQLIEINLSELEPH------------INGPFtPDLATPVSKFKEVAEKN--------------GWPLDl 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 353 KV-FIGSCTNSRIEDLRLAAAVVKgRKVAANVK---DAMIVPGSGLVKKMAEAEGLDQIFIEAGFDWREAGCSMCLGM-N 427
Cdd:cd01584 285 RVgLIGSCTNSSYEDMGRAASIAK-QALAHGLKcksIFTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQwD 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 19115488 428 PDQLKPYERCA--STSNRNFEGRQGAKGRTH--LVSPAMAAAAAIKGHL 472
Cdd:cd01584 364 RKDIKKGEKNTivTSYNRNFTGRNDANPATHafVASPEIVTAMAIAGTL 412
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
118-448 |
3.69e-29 |
|
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: 124.45 E-value: 3.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 118 GIVH----------VIGPEQGFTL---PGTtLVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTIlqrkskNMRI---- 180
Cdd:COG1048 176 GIVHqvnleylafvVWTREEDGETvayPDT-LVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPV------SMLIpevv 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 181 --RVNGKLPEGIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAPDATTFEYVK-- 256
Cdd:COG1048 249 gvKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRlt 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 257 NRplapkgDDWEQAV--AYWKT--LRSDENAK---YDIEVEINAADVLPTVTWGTSPQDVIPIngnipdpAHVKDNVRAA 329
Cdd:COG1048 329 GR------SEEQIELveAYAKAqgLWRDPDAPepyYSDVLELDLSTVEPSLAGPKRPQDRIPL-------SDLKEAFRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 330 siqrsLEYMGLKPNTSIVSYPIDKVF------------IGSCTNSRIEDLRLAA------AVVKGRKVAANVKdAMIVPG 391
Cdd:COG1048 396 -----LAAPVGEELDKPVRVEVDGEEfelghgavviaaITSCTNTSNPSVMIAAgllakkAVEKGLKVKPWVK-TSLAPG 469
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 392 SGLVKKMAEAEGLDQIFIEAGFDWREAGCSMCLGM------------NPDQLKPyerCASTS-NRNFEGR 448
Cdd:COG1048 470 SKVVTDYLERAGLLPYLEALGFNVVGYGCTTCIGNsgplppeiseaiEENDLVV---AAVLSgNRNFEGR 536
|
|
| leuD |
PRK00439 |
3-isopropylmalate dehydratase small subunit; Reviewed |
554-698 |
1.29e-27 |
|
3-isopropylmalate dehydratase small subunit; Reviewed
Pssm-ID: 234762 [Multi-domain] Cd Length: 163 Bit Score: 109.53 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 554 NVDTDKIIPKQFLKTIKRTGLGQFAFYEIRydadgkeiPDFVLNREPyrhATVLVAHDNFGCGSSREHAPWALNDFGIRV 633
Cdd:PRK00439 10 NIDTDVIIPARYLNTSDPQELAKHCMEDLD--------PEFAKKVKP---GDIIVAGKNFGCGSSREHAPIALKAAGVSA 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115488 634 IIAPSFADIFFNNCFKNGmLPI---PTPIEQVNDmmkaaENQVkfSVDLVNQTITYGDKQVKFDVEPF 698
Cdd:PRK00439 79 VIAKSFARIFYRNAINIG-LPVlecDEAVDKIED-----GDEV--EVDLETGVITNLTTGEEYKFKPI 138
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
118-448 |
2.23e-26 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 115.88 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 118 GIVH---------VIGPEQGFTLPgTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNGKLPE 188
Cdd:PTZ00092 185 GIVHqvnleylarVVFNKDGLLYP-DSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTGKLSE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 189 GIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAPDATTFEYVK--NRPlAPKGDD 266
Cdd:PTZ00092 264 HVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKqtGRS-EEKVEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 267 WEQAVAYWKTLRSD-ENAKYDIEVEINAADVLPTVTWGTSPQDVIPING------------------NIPDPAHVKDnvr 327
Cdd:PTZ00092 343 IEKYLKANGLFRTYaEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDlkkdftaclsapvgfkgfGIPEEKHEKK--- 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 328 aasiqRSLEYMGLKPNTSIVSYPIDKvfIGSCTNSRIEDLRLAA------AVVKGRKVAANVKDAMiVPGSGLVKKMAEA 401
Cdd:PTZ00092 420 -----VKFTYKGKEYTLTHGSVVIAA--ITSCTNTSNPSVMLAAgllakkAVEKGLKVPPYIKTSL-SPGSKVVTKYLEA 491
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 19115488 402 EGLDQIFIEAGFDWREAGCSMCLGMNPDQLKPYERCAS----------TSNRNFEGR 448
Cdd:PTZ00092 492 SGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITnndlvaaavlSGNRNFEGR 548
|
|
| PRK14812 |
PRK14812 |
hypothetical protein; Provisional |
616-727 |
1.91e-25 |
|
hypothetical protein; Provisional
Pssm-ID: 173273 [Multi-domain] Cd Length: 119 Bit Score: 101.72 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 616 GSSREHAPWALNDFGIRVIIAPSFADIFFNNCFKNGMLPIPTPIEqVNDMMKAAENQVKFSVDLVNQTITYGDKQVKFDV 695
Cdd:PRK14812 3 GSSREHAAWALADYGFKVVIAGSFGDIHYNNELNNGMLPIVQPRE-VREKLAQLKPTDQVTVDLEQQKIISPVEEFTFEI 81
|
90 100 110
....*....|....*....|....*....|..
gi 19115488 696 EPFRKHCLVNGLDDIGLTLQKETMIDAFEAAR 727
Cdd:PRK14812 82 DSEWKHKLLNSLDDIGITLQYEELIAAYEKQR 113
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
118-448 |
1.47e-23 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 106.56 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 118 GIVHVIGPEQ-------------GFTLPgTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNG 184
Cdd:PRK12881 178 GIMHQVNLEYlarvvhtkeddgdTVAYP-DTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIPDVVGVELTG 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 185 KLPEGIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAPDATTFEYvknrpLAPKG 264
Cdd:PRK12881 257 KLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDY-----LRLTG 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 265 DDWEQ--AV-AYWKT----LRSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPIngnipdpAHVKDNVRAASIQRSLEY 337
Cdd:PRK12881 332 RTEAQiaLVeAYAKAqglwGDPKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIAL-------GNVKSAFSDLFSKPVAEN 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 338 MGLKPNTSIVSYPIDK--VFIG---SCTNSRIEDLRLAA------AVVKGRKVAANVKDAMiVPGSGLVKKMAEAEGLDQ 406
Cdd:PRK12881 405 GFAKKAQTSNGVDLPDgaVAIAaitSCTNTSNPSVLIAAgllakkAVERGLTVKPWVKTSL-APGSKVVTEYLERAGLLP 483
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 19115488 407 IFIEAGFDWREAGCSMCLGMNPDQLKPYER--------CAS--TSNRNFEGR 448
Cdd:PRK12881 484 YLEKLGFGIVGYGCTTCIGNSGPLTPEIEQaitkndlvAAAvlSGNRNFEGR 535
|
|
| LEUD_arch |
TIGR02087 |
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the ... |
554-664 |
3.09e-23 |
|
3-isopropylmalate dehydratase, small subunit; This subfamily is most closely related to the 3-isopropylmalate dehydratase, small subunits which form TIGR00171. This subfamily includes the members of TIGR02084 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities.
Pssm-ID: 273961 [Multi-domain] Cd Length: 154 Bit Score: 96.72 E-value: 3.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 554 NVDTDKIIPKQFLKTIKRTGLGQFAFYEIRydadgkeiPDFVlnrEPYRHATVLVAHDNFGCGSSREHAPWALNDFGIRV 633
Cdd:TIGR02087 9 DIDTDEIIPGRYLRTTDPDELASHAMEGID--------PEFA---KKVRPGDVIVAGKNFGCGSSREQAALALKAAGIAA 77
|
90 100 110
....*....|....*....|....*....|.
gi 19115488 634 IIAPSFADIFFNNCFKNGMLPIPTPIEQVND 664
Cdd:TIGR02087 78 VIAESFARIFYRNAINIGLPLIEAKTEGIKD 108
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
119-460 |
3.28e-23 |
|
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: 102.77 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 119 IVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNGKLPEGIASKDLILH 198
Cdd:cd01586 107 VVFTSEEDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTGKLRPGVTATDLVLT 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 199 IIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAPDATTfeyvknrplapkgddweqavaywktlr 278
Cdd:cd01586 187 VTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVDTQV--------------------------- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 279 sdenakydieVEINAADVLPTVTWGTSPQDVIPINGNIpdpahvkdnVRAAsiqrsleymglkpntsivsypidkvfIGS 358
Cdd:cd01586 240 ----------VELDLSTVEPSVSGPKRPQDRVPLHGSV---------VIAA--------------------------ITS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 359 CTNSRIEDLRLAA------AVVKGRKVAANVKDAMiVPGSGLVKKMAEAEGLDQIFIEAGFDWREAGCSMCLGmNPDQLK 432
Cdd:cd01586 275 CTNTSNPSVMLAAgllakkAVELGLKVKPYVKTSL-APGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIG-NSGPLP 352
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 19115488 433 P----------YERCASTS-NRNFEGRQGAKGR-THLVSP 460
Cdd:cd01586 353 EeveeaikendLVVAAVLSgNRNFEGRIHPLVRaNYLASP 392
|
|
| leud |
TIGR02084 |
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
554-698 |
4.09e-22 |
|
3-isopropylmalate dehydratase, small subunit; Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. The members of the seed for this model are those sequences which are gene clustered with other genes involved in leucine biosynthesis and include some archaea. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 131139 [Multi-domain] Cd Length: 156 Bit Score: 93.32 E-value: 4.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 554 NVDTDKIIPKQFLKTIKRTGLGQFAFYEIRydadgkeiPDFvlnREPYRHATVLVAHDNFGCGSSREHAPWALNDFGIRV 633
Cdd:TIGR02084 9 NVDTDVIIPARYLNTSDPKELAKHCMEDLD--------KDF---VKKVKEGDIIVAGENFGCGSSREHAPIAIKASGISC 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115488 634 IIAPSFADIFFNNCFKNGmLPIPTPIEQVNDmmkaAENQVKFSVDLVNQTITYGDKQVKFDVEPF 698
Cdd:TIGR02084 78 VIAKSFARIFYRNAINIG-LPIVESEEAVDE----IEEGDEVEVDLEKGIIKNLTKGKEYKATPF 137
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
118-460 |
3.77e-21 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 99.11 E-value: 3.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 118 GIVHVIGPE---------QGFTLPgTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNGKLPE 188
Cdd:PLN00070 217 GIVHQVNLEylgrvvfntDGILYP-DSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRD 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 189 GIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAPDATTFEYVKnrpLAPKGDDWE 268
Cdd:PLN00070 296 GVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLK---LTGRSDETV 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 269 QAV-AYwktLRSD----------ENAKYDIEVEINAADVLPTVTWGTSPQDVIPINGNIPDPAHVKDNV----------R 327
Cdd:PLN00070 373 AMIeAY---LRANkmfvdynepqQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHSCLDNKvgfkgfavpkE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 328 AASIQRSLEYMG----LKPNTSIVSYpidkvfIGSCTNSRIEDLRLAAAVVK------GRKVAANVKDAMiVPGSGLVKK 397
Cdd:PLN00070 450 AQSKVAKFSFHGqpaeLRHGSVVIAA------ITSCTNTSNPSVMLGAGLVAkkacelGLEVKPWIKTSL-APGSGVVTK 522
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115488 398 MAEAEGLDQIFIEAGFDWREAGCSMCLGmNPDQLKPYERCASTS-----------NRNFEGRQGAKGR-THLVSP 460
Cdd:PLN00070 523 YLLKSGLQKYLNQQGFHIVGYGCTTCIG-NSGELDESVASAITEndivaaavlsgNRNFEGRVHPLTRaNYLASP 596
|
|
| PLN00072 |
PLN00072 |
3-isopropylmalate isomerase/dehydratase small subunit; Provisional |
554-657 |
1.04e-19 |
|
3-isopropylmalate isomerase/dehydratase small subunit; Provisional
Pssm-ID: 177701 [Multi-domain] Cd Length: 246 Bit Score: 89.15 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 554 NVDTDKIIPKQFLKTI-----KRTGLGQFA------FYEIRYDADGKeipdfvlNREPYrhaTVLVAHDNFGCGSSREHA 622
Cdd:PLN00072 79 NIDTDQIIPAEYLTLVpskpdEYEKLGSYAliglpaFYKTRFVEPGE-------MKTKY---SIIIGGENFGCGSSREHA 148
|
90 100 110
....*....|....*....|....*....|....*.
gi 19115488 623 PWALNDFGIRVIIAPSFADIFFNNCFKNG-MLPIPT 657
Cdd:PLN00072 149 PVALGAAGAKAVVAESYARIFFRNSVATGeVYPLES 184
|
|
| HacB2_Meth |
NF040625 |
homoaconitase small subunit; |
554-712 |
1.72e-19 |
|
homoaconitase small subunit;
Pssm-ID: 468597 [Multi-domain] Cd Length: 161 Bit Score: 85.92 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 554 NVDTDKIIPKQFLKTIKRTGLGQFAFYEIRydadgkeiPDFVLNrepYRHATVLVAHDNFGCGSSREHAPWALNDFGIRV 633
Cdd:NF040625 14 NIDTDVIIPGRYLRTFNPDDLASHVMEGER--------PDFTKN---VQKGDIIVAGWNFGCGSSREQAPVAIKHAGVSA 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19115488 634 IIAPSFADIFFNNCFKNGMLPIPTPIEqvndmmkaAENQVKFSVDLVNQTITYGDKQVKFDVEPFRKHCLvNGLDDIGL 712
Cdd:NF040625 83 IIAKSFARIFYRNAINIGLPVIVADIE--------ADDGDILSIDLEKGIIKNKTTGEEFKIQPFKEFML-EILEDGGL 152
|
|
| PRK14023 |
PRK14023 |
homoaconitate hydratase small subunit; Provisional |
553-697 |
1.10e-18 |
|
homoaconitate hydratase small subunit; Provisional
Pssm-ID: 184460 [Multi-domain] Cd Length: 166 Bit Score: 84.08 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 553 ANVDTDKIIPKQFLK-TIKRTGLGQFAFYEIRydadgkeiPDFVlnrEPYRHATVLVAHDNFGCGSSREHAPWALNDFGI 631
Cdd:PRK14023 9 DNINTDDILPGKYAPfMVGEDRFHNYAFAHLR--------PEFA---STVRPGDILVAGRNFGLGSSREYAPEALKMLGI 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115488 632 RVIIAPSFADIFFNNCFKNGMLPIPTPieqvnDMMKAAENQVKFSVDLVNQTITYGDKQVKFDVEP 697
Cdd:PRK14023 78 GAIIAKSYARIFYRNLVNLGIPPFESE-----EVVDALEDGDEVELDLETGVLTRGGETFQLRPPP 138
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
135-448 |
9.56e-18 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 87.87 E-value: 9.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 135 TLVCGDSHTsTH-GAFGALAFGIGTSEVEHVLATQTIlqrkskNMRI------RVNGKLPEGIASKDLILHI------IG 201
Cdd:PRK09277 207 TLVGTDSHT-TMiNGLGVLGWGVGGIEAEAAMLGQPS------SMLIpevvgvKLTGKLPEGVTATDLVLTVtemlrkKG 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 202 VIGtaggtgSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAPDATTFEYVK--NRplapkgDDWEQAV--AYWKT- 276
Cdd:PRK09277 280 VVG------KFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRltGR------DEEQVALveAYAKAq 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 277 ---LRSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPIngnipdpAHVKDNVRAAsIQRSLEYMGLKPNTSIVSYPIDK 353
Cdd:PRK09277 348 glwRDPLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPL-------SDVKEAFAKS-AELGVQGFGLDEAEEGEDYELPD 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 354 --VFIG---SCTNSRIEDLRLAA------AVVKGRKVAANVKDAMiVPGSGLVKKMAEAEGLdQIFIEA-GFDWREAGCS 421
Cdd:PRK09277 420 gaVVIAaitSCTNTSNPSVMIAAgllakkAVEKGLKVKPWVKTSL-APGSKVVTDYLEKAGL-LPYLEAlGFNLVGYGCT 497
|
330 340 350
....*....|....*....|....*....|....*..
gi 19115488 422 MCLGMNPDQLKPYERC------ASTS----NRNFEGR 448
Cdd:PRK09277 498 TCIGNSGPLPPEIEKAindndlVVTAvlsgNRNFEGR 534
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
130-472 |
4.42e-17 |
|
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: 84.47 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 130 TLPGTTLVCGDSHTSthgaFG-ALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNGKLPEGIASKDLILHI--------I 200
Cdd:cd01581 104 LLPDTVGTGGDSHTR----FPiGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVNAIpyyaiqqgL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 201 GVIGTAGG----TGSVIEFcgEAIEGLSMEARMSMCNMSIEAGARAGMI-APDATTFEYVKN----------------RP 259
Cdd:cd01581 180 LTVEKKGKknvfNGRILEI--EGLPDLKVEQAFELTDASAERSAAACTVrLDKEPVIEYLESnvvlmkimiangyddaRT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 260 LAPKGDDWEQAVAYWKTLRSDENAKYDIEVEINAADVLPtvtwgtspqdviPIngnIPDPaHVKDNVRAASiqrsleymg 339
Cdd:cd01581 258 LLRRIIAMEEWLANPPLLEPDADAEYAAVIEIDLDDIKE------------PI---LACP-NDPDDVKLLS--------- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 340 lkpntSIVSYPIDKVFIGSC-TNsrIEDLRLAAAVVKGRKVAANVkdAMIVPGSGLVKKMAEAEGLDQIFIEAGFDWREA 418
Cdd:cd01581 313 -----EVAGKKIDEVFIGSCmTN--IGHFRAAAKILRGKEFKPTR--LWVAPPTRMDWAILQEEGYYSIFGDAGARTEMP 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 19115488 419 GCSMCLGmNPDQLKPYERCASTSNRNFEGRQGAKGRTHLVSPAMAAAAAIKGHL 472
Cdd:cd01581 384 GCSLCMG-NQARVADGATVFSTSTRNFDNRVGKGAEVYLGSAELAAVCALLGRI 436
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
129-484 |
2.80e-16 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 83.30 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 129 FTLPGTTLVCGDSHTSTH-G-AFGA----LAFGIGTSEV-----EHVLatqtilqrksknmrIRVNGKLPEGIASKDLIl 197
Cdd:PRK09238 475 MLLPDTVGTGGDSHTRFPiGiSFPAgsglVAFAAATGVMpldmpESVL--------------VRFKGEMQPGITLRDLV- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 198 HII-------GVIgTAGGTGSVIEFCG-----EAIEGLSMEARMSMCNMSIEAGARAGMIA-PDATTFEYVKN------- 257
Cdd:PRK09238 540 HAIpyyaikqGLL-TVEKKGKKNIFSGrileiEGLPDLKVEQAFELTDASAERSAAGCTIKlSKEPIIEYLRSnivllkw 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 258 ---------RPLAPKGDDWEQAVAYWKTLRSDENAKYDIEVEINAADVlptvtwgtspqdVIPIngnIPDPAHvKDNVRA 328
Cdd:PRK09238 619 miaegygdaRTLERRIAAMEEWLANPELLEADADAEYAAVIEIDLAEI------------KEPI---LACPND-PDDVRL 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 329 ASiqrslEYMGLKpntsivsypIDKVFIGSC-TNsrIEDLRLAAAVVKGRKVAANVKdAMIVPGSGLVKKMAEAEGLDQI 407
Cdd:PRK09238 683 LS-----EVAGTK---------IDEVFIGSCmTN--IGHFRAAGKLLEGKKGQLPTR-LWVAPPTKMDADQLTEEGYYSI 745
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115488 408 FIEAGFDWREAGCSMCLGmNPDQLKPYERCASTSNRNFEGRQGAKGRTHLVSPAMAAAAAIKGHLCNVREFFGDVSN 484
Cdd:PRK09238 746 FGKAGARIEMPGCSLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYLGSAELAAVCALLGRIPTVEEYQEYVAE 821
|
|
| Aconitase_swivel |
cd00404 |
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible ... |
606-655 |
1.88e-13 |
|
Aconitase swivel domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. The aconitase family contains the following proteins: - Iron-responsive element binding protein (IRE-BP). IRE-BP is a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid.
Pssm-ID: 238236 [Multi-domain] Cd Length: 88 Bit Score: 66.34 E-value: 1.88e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 19115488 606 VLVAHDNFGCGSSREHAPWALNDFGIRVIIAPSFADIFFNNCFKNGMLPI 655
Cdd:cd00404 18 VVIGDENYGTGSSREHAALELRLLGGRAVIAKSFARIFFRNLVDQGLLPL 67
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
131-478 |
6.73e-13 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 72.26 E-value: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 131 LPGTTLVCGDSHTSthgaFG-ALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNGKLPEGIASKDLIlHIIGVIGTAGG- 208
Cdd:PLN00094 551 LPDTVGTGGDSHTR----FPiGISFPAGSGLVAFGAATGVIPLDMPESVLVRFTGTMQPGITLRDLV-HAIPYTAIQDGl 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 209 ------------TGSVIEFcgEAIEGLSMEARMSMCNMSIEAGARAGMIAPD-ATTFEYVKN----------------RP 259
Cdd:PLN00094 626 ltvekkgkknvfSGRILEI--EGLPHLKCEQAFELSDASAERSAAGCTIKLDkEPIIEYLNSnvvmlkwmiaegygdrRT 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 260 LAPKGDDWEQAVAYWKTLRSDENAKYDIEVEINAADVlptvtwgTSPQDVIPingNIPDPAhvkdnvraasiqRSLeymg 339
Cdd:PLN00094 704 LERRIARMQQWLADPELLEADPDAEYAAVIEIDMDEI-------KEPILCAP---NDPDDA------------RLL---- 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 340 lkpnTSIVSYPIDKVFIGSC-TNsrIEDLRLAAAVVKGRKVAANVKdAMIVPGSGLVKKMAEAEGLDQIFIEAGFDWREA 418
Cdd:PLN00094 758 ----SEVTGDKIDEVFIGSCmTN--IGHFRAAGKLLNDNLSQLPTR-LWVAPPTKMDEAQLKAEGYYSTFGTVGARTEMP 830
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 419 GCSMCLGmNPDQLKPYERCASTSNRNFEGRQGAKGRTHLVSPAMAAAAAIKGHLCNVREF 478
Cdd:PLN00094 831 GCSLCMG-NQARVAEKSTVVSTSTRNFPNRLGKGANVYLASAELAAVAAILGRLPTVEEY 889
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
140-452 |
1.82e-09 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 61.18 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 140 DSHTStHGAFGALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNGKLPEGIASKDLILHIIG-VIGTAGGTGSVIEFCGE 218
Cdd:PRK11413 149 DSHTR-YGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGaVFKNGYVKNKVMEFVGP 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 219 AIEGLSMEARMSMCNMSIEAGARAGMIAPDATTFEYVK--NRPLApkgddweqavayWKTLRSDENAKYDIEVEINAADV 296
Cdd:PRK11413 228 GVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLAlhGRGQD------------YCELNPQPMAYYDGCISVDLSAI 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 297 LPTVTWGTSPQDVIPI---NGNIPDpahVKDNVRAASIQRSLEYMGLKPNTSIVS--YPIDKVFIGSCTNSRIEDLRLAA 371
Cdd:PRK11413 296 KPMIALPFHPSNVYEIdelNQNLTD---ILREVEIESERVAHGKAKLSLLDKIENgrLKVQQGIIAGCSGGNYENVIAAA 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 372 AVVKGRKVAANVKDAMIVPGS-----GLVKKMAEAEgldqiFIEAGFDWREAGCSMCLGMNPdqlKPYERCAST--SNRN 444
Cdd:PRK11413 373 NALRGQSCGNDTFSLSVYPSSqpvfmDLAKKGVVAD-----LMGAGAIIRTAFCGPCFGAGD---TPANNGLSIrhTTRN 444
|
....*...
gi 19115488 445 FEGRQGAK 452
Cdd:PRK11413 445 FPNREGSK 452
|
|
| AcnB |
COG1049 |
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ... |
277-483 |
2.49e-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: 60.64 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 277 LRSDENAKYDIEVEINAADVlptvtwgTSPQDVIPingNipDPahvkDNVRAASiqrslEYMGLKpntsivsypIDKVFI 356
Cdd:COG1049 647 LEADADAEYAAVIEIDLNEI-------KEPILACP---N--DP----DDVKLLS-----EVAGTK---------IDEVFI 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 357 GSC-TNsrIEDLRLAAAVVKGrkvAANVKDAM-IVPGSGLVKKMAEAEGLDQIFIEAGFDWREAGCSMCLGmNPDQLKPY 434
Cdd:COG1049 697 GSCmTN--IGHFRAAGKLLEG---KGNLPTRLwIAPPTKMDEAQLTEEGYYSIFGAAGARTEMPGCSLCMG-NQARVADG 770
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 19115488 435 ERCASTSNRNFEGRQGAKGRTHLVSPAMAAAAAIKGHLCNVREFFGDVS 483
Cdd:COG1049 771 ATVFSTSTRNFPNRLGKGANVYLGSAELAAVCALLGRLPTVEEYMEYVK 819
|
|
| AcnA_Bact_Swivel |
cd01579 |
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) ... |
554-655 |
1.88e-08 |
|
Bacterial Aconitase-like swivel domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This is the aconitase-like swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism. This distinct subfamily is found only in bacteria and archea. Its exact characteristics are not known.
Pssm-ID: 238811 [Multi-domain] Cd Length: 121 Bit Score: 53.21 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 554 NVDTDKIIPK-----QFLKTIKRtgLGQFAFYeiRYDadgkeiPDFVlNREPYRHATVLVAHDNFGCGSSREHAPWALND 628
Cdd:cd01579 5 NITTDHIMPAgakvlPLRSNIPA--ISEFVFH--RVD------PTFA-ERAKAAGPGFIVGGENYGQGSSREHAALAPMY 73
|
90 100
....*....|....*....|....*..
gi 19115488 629 FGIRVIIAPSFADIFFNNCFKNGMLPI 655
Cdd:cd01579 74 LGVRAVLAKSFARIHRANLINFGILPL 100
|
|
| Homoaconitase_Swivel |
cd01674 |
Homoaconitase swivel domain. This family includes homoaconitase and other uncharacterized ... |
551-658 |
2.40e-07 |
|
Homoaconitase swivel domain. This family includes 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. This is the swivel domain, which is believed to undergo swivelling conformational change in the enzyme mechanism.
Pssm-ID: 238837 [Multi-domain] Cd Length: 129 Bit Score: 50.36 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115488 551 PMANVDTDKIIPKQFLKTIKRTGLGQFAFYEIRYDADgkeipdfvlNREPYRHATVLVAHDNFGCGSSREHAPWALNDFG 630
Cdd:cd01674 2 DADNLNTDGIYPGKYTYQDDITPEKMAEVCMENYDSE---------FSTKTKQGDILVSGFNFGTGSSREQAATALLAKG 72
|
90 100
....*....|....*....|....*...
gi 19115488 631 IRVIIAPSFADIFFNNCFKNGMLPIPTP 658
Cdd:cd01674 73 IPLVVSGSFGNIFSRNSINNALLSIELP 100
|
|
| AcnA_Mitochon_Swivel |
cd01578 |
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and ... |
606-655 |
5.89e-07 |
|
Mitochondrial aconitase A swivel domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. This is the aconitase swivel domain, which undergoes swivelling conformational change in the enzyme mechanism. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 238810 [Multi-domain] Cd Length: 149 Bit Score: 49.77 E-value: 5.89e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 19115488 606 VLVAHDNFGCGSSREHAPWALNDFGIRVIIAPSFADIFFNNCFKNGMLPI 655
Cdd:cd01578 72 VVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPL 121
|
|
| |
