|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-465 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 994.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 1 MKTMFEKIWEDHLVGELDAGSYLIYIDRHLIHEVTSPQAFEGLKLAGRKVRRPEATFATMDHNVSTRTRDLSLADPISAI 80
Cdd:PRK05478 2 GKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLPIADPVSRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 81 QMQTLKKNCDENGIRVYDFQNPDQGIIHVIAPEMGLTHPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLVQK 160
Cdd:PRK05478 82 QVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 161 KAKTMEIRVDGKLSDKVTAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEITFN 240
Cdd:PRK05478 162 KPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 241 YIQGKDFSPKGAEWDLAVKKWKHYVTDEGAKFDRTVILHADEIAPMVTWGTSPSQVISIKGVVPDPKDANDPVEKIGIES 320
Cdd:PRK05478 242 YLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVKRASAER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 321 ALKYMDLKSGQKIEDISINKVFIGSCTNSRIEDLRAAAATVKGKKVSSKVQAIVVPGSGRVKRQAEQEGLDKIFTAAGFE 400
Cdd:PRK05478 322 ALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFE 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523628383 401 WRNPGCSMCLAMNDDVLEPGDRCASTSNRNFEGRQGKGGRTHLVGPEMAAAAAIEGHFVDIRNWK 465
Cdd:PRK05478 402 WREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
2-463 |
0e+00 |
|
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate dehydratase, large subunit, or the large subunit domain of single-chain forms. Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. These homologs are now described by a separate model of subfamily (rather than equivalog) homology type, and the priors and cutoffs for this model have been changed to focus this equivalog family more narrowly. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 272940 Cd Length: 465 Bit Score: 784.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 2 KTMFEKIWEDHLVGELDAGSYLIYIDRHLIHEVTSPQAFEGLKLAGRKVRRPEATFATMDHNVSTRTRDLSLADPISAIQ 81
Cdd:TIGR00170 3 RTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFNIKDEVAKIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 82 MQTLKKNCDENGIRVYDFQNPDQGIIHVIAPEMGLTHPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLVQKK 161
Cdd:TIGR00170 83 VTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 162 AKTMEIRVDGKLSDKVTAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEITFNY 241
Cdd:TIGR00170 163 AKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTFEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 242 IQGKDFSPKGAEWDLAVKKWKHYVTDEGAKFDRTVILHADEIAPMVTWGTSPSQVISIKGVVPDPKDANDPVEKIGIESA 321
Cdd:TIGR00170 243 CKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKASAERA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 322 LKYMDLKSGQKIEDISINKVFIGSCTNSRIEDLRAAAATVKGKKVSSKVQAIVVPGSGRVKRQAEQEGLDKIFTAAGFEW 401
Cdd:TIGR00170 323 LAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGFEW 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523628383 402 RNPGCSMCLAMNDDVLEPGDRCASTSNRNFEGRQGKGGRTHLVGPEMAAAAAIEGHFVDIRN 463
Cdd:TIGR00170 403 REPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRK 464
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
2-464 |
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: 720.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 2 KTMFEKIWEDHLVGELDAGSY-LIYIDRHLIHEVTSPQAFEGLKLAG-RKVRRPEATFATMDHNVSTrtrdlslADPISA 79
Cdd:COG0065 3 MTLAEKILARHAGREVEPGEIvLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPT-------KDPKSA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 80 IQMQTLKKNCDENGIRVYDFQnpDQGIIHVIAPEMGLTHPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLVQ 159
Cdd:COG0065 76 EQVKTLREFAKEFGITFFDVG--DPGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 160 KKAKTMEIRVDGKLSDKVTAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEITF 239
Cdd:COG0065 154 KVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 240 NYIQGKDFSPkgaewdlavkkWKHYVTDEGAKFDRTVILHADEIAPMVTWGTSPSQVISIKGVvpdpkdandpvekigie 319
Cdd:COG0065 234 EYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSEL----------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 320 salkymdlksgqkiEDISINKVFIGSCTNSRIEDLRAAAATVKGKKVSSKVQAIVVPGSGRVKRQAEQEGLDKIFTAAGF 399
Cdd:COG0065 286 --------------EGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGA 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523628383 400 EWRNPGCSMCLAMNDDVLEPGDRCASTSNRNFEGRQG-KGGRTHLVGPEMAAAAAIEGHFVDIRNW 464
Cdd:COG0065 352 EWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
6-456 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 708.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 6 EKIWEDHLVGELDagSYLIYI-DRHLIHEVTSPQAFEGLKLAGRKVRRPEATFATMDHNVST--------RTRDLSLADP 76
Cdd:pfam00330 1 EKIWDAHLVEELD--GSLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTdlvidhapDALDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 77 IS--AIQMQTLKKNCDENGIRVYDfqnPDQGIIHVIAPEMGLTHPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAT 154
Cdd:pfam00330 79 ISrnKEQYDFLEWNAKKFGIRFVP---PGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 155 QTLVQKKAKTMEIRVDGKLSDKVTAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAP 234
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 235 DEITFNYIQ--GKDFSPKGAEWDLAVkKWKHYVTDEGAKFDRTVILHADEIAPMVTWGTSPSQVISIKGVVPDPkdANDP 312
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAV-AWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDP--FADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 313 VEKIGIESALKYMDLKSGQKIEDISINKVFIGSCTNSRIEDLRAAAATVK-----GKKVSSKVQAIVVPGSGRVKRQAEQ 387
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523628383 388 EGLDKIFTAAGFEWRNPGCSMCLAmNDDVLEPGDRCASTSNRNFEGRQGKGGRTHLVGPEMAAAAAIEG 456
Cdd:pfam00330 393 EGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASPALVAAAAIAG 460
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
28-458 |
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 523628383 28 RHLIHEVTSPQAFEGLKLAGR-KVRRPEATFATMDHNVSTrtrdlslADPISAIQMQTLKKNCDENGIRVYDFQNpdQGI 106
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPT-------PDIKAAEQVKTLRKFAKEFGINFFDVGR--QGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 107 IHVIAPEMGLTHPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLVQKKAKTMEIRVDGKLSDKVTAKDVILAI 186
Cdd:cd01583 72 CHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 187 IGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEITFNYIQGKDFSPkgaewdlavkkWKHYVT 266
Cdd:cd01583 152 IGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAY-----------WKELKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 267 DEGAKFDRTVILHADEIAPMVTWGTSPSQVISIKGVVPdpkdandpvekigiesalkymdlksgqkiedISINKVFIGSC 346
Cdd:cd01583 221 DEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQVFIGSC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 347 TNSRIEDLRAAAATVKGKKVSSKVQAIVVPGSGRVKRQAEQEGLDKIFTAAGFEWRNPGCSMCLAMNDDVLEPGDRCAST 426
Cdd:cd01583 270 TNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVST 349
|
410 420 430
....*....|....*....|....*....|...
gi 523628383 427 SNRNFEGRQG-KGGRTHLVGPEMAAAAAIEGHF 458
Cdd:cd01583 350 SNRNFKGRMGsPGARIYLASPATAAASAITGEI 382
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
3-457 |
8.28e-93 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 287.42 E-value: 8.28e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 3 TMFEKIWEDHLVGELDAGSYL-IYIDRHLIHEVTSPQAFEGLKLAGRKVRRPEATFATMDHNVSTRTrdlsladpISAIQ 81
Cdd:NF040615 2 TLAEKILSKKLGKEVYAGDTVeVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPANT--------VKAAN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 82 MQTLKKN-CDENGIRvyDFQNPDQGIIHVIAPEMGLTHPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLVQK 160
Cdd:NF040615 74 MQKITREfVKEQGIK--NFYLGGEGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 161 KAKTMEIRVDGKlSDKVTAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEITFN 240
Cdd:NF040615 152 VPKTIRVNIVGK-NENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 241 YIQGKDFSpkgAEWDLAVKKWKHYVTDEGAKFDRTVILHADEIAPMVTWGTSPSQVisiKGVvpdpkdandpvekigies 320
Cdd:NF040615 231 YLRKEGVS---EEEIAELKKNRITVNEKEENYYKEIEIDITDMEEQVACPHHPDNV---KPV------------------ 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 321 alkymdlksgQKIEDISINKVFIGSCTNSRIEDLRAAAATVKGKKVSSKVQAIVVPGSGRVKRQAEQEGLDKIFTAAGFE 400
Cdd:NF040615 287 ----------SEVEGTEIDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAM 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 523628383 401 WRNPGCSMCLAMNDDVLEPGDRCASTSNRNFEGRQG-KGGRTHLVGPEMAAAAAIEGH 457
Cdd:NF040615 357 ICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGnINSYIYLSSPKIAAKSAVKGY 414
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-465 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 994.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 1 MKTMFEKIWEDHLVGELDAGSYLIYIDRHLIHEVTSPQAFEGLKLAGRKVRRPEATFATMDHNVSTRTRDLSLADPISAI 80
Cdd:PRK05478 2 GKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLPIADPVSRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 81 QMQTLKKNCDENGIRVYDFQNPDQGIIHVIAPEMGLTHPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLVQK 160
Cdd:PRK05478 82 QVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 161 KAKTMEIRVDGKLSDKVTAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEITFN 240
Cdd:PRK05478 162 KPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 241 YIQGKDFSPKGAEWDLAVKKWKHYVTDEGAKFDRTVILHADEIAPMVTWGTSPSQVISIKGVVPDPKDANDPVEKIGIES 320
Cdd:PRK05478 242 YLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVKRASAER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 321 ALKYMDLKSGQKIEDISINKVFIGSCTNSRIEDLRAAAATVKGKKVSSKVQAIVVPGSGRVKRQAEQEGLDKIFTAAGFE 400
Cdd:PRK05478 322 ALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFE 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523628383 401 WRNPGCSMCLAMNDDVLEPGDRCASTSNRNFEGRQGKGGRTHLVGPEMAAAAAIEGHFVDIRNWK 465
Cdd:PRK05478 402 WREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
1-463 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 833.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 1 MKTMFEKIWEDHLVGELDAGSYLIYIDRHLIHEVTSPQAFEGLKLAGRKVRRPEATFATMDHNVSTR-TRDLSLADPISA 79
Cdd:PRK12466 3 PRTLYDKLWDSHTVARLDDGHVLLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPTRpGRDRGITDPGGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 80 IQMQTLKKNCDENGIRVYDFQNPDQGIIHVIAPEMGLTHPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLVQ 159
Cdd:PRK12466 83 LQVDYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQTLVY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 160 KKAKTMEIRVDGKLSDKVTAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEITF 239
Cdd:PRK12466 163 RKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETTF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 240 NYIQGKDFSPKGAEWDLAVKKWKHYVTDEGAKFDRTVILHADEIAPMVTWGTSPSQVISIKGVVPDPKDANDPVEKIGIE 319
Cdd:PRK12466 243 DYLRGRPRAPKGALWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAAEADPARRAAME 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 320 SALKYMDLKSGQKIEDISINKVFIGSCTNSRIEDLRAAAATVKGKKVSSKVQAIVVPGSGRVKRQAEQEGLDKIFTAAGF 399
Cdd:PRK12466 323 RALDYMGLTPGTPLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAGF 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523628383 400 EWRNPGCSMCLAMNDDVLEPGDRCASTSNRNFEGRQGKGGRTHLVGPEMAAAAAIEGHFVDIRN 463
Cdd:PRK12466 403 EWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHITDVRS 466
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
2-463 |
0e+00 |
|
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate dehydratase, large subunit, or the large subunit domain of single-chain forms. Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. These homologs are now described by a separate model of subfamily (rather than equivalog) homology type, and the priors and cutoffs for this model have been changed to focus this equivalog family more narrowly. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 272940 Cd Length: 465 Bit Score: 784.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 2 KTMFEKIWEDHLVGELDAGSYLIYIDRHLIHEVTSPQAFEGLKLAGRKVRRPEATFATMDHNVSTRTRDLSLADPISAIQ 81
Cdd:TIGR00170 3 RTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFNIKDEVAKIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 82 MQTLKKNCDENGIRVYDFQNPDQGIIHVIAPEMGLTHPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLVQKK 161
Cdd:TIGR00170 83 VTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 162 AKTMEIRVDGKLSDKVTAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEITFNY 241
Cdd:TIGR00170 163 AKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTFEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 242 IQGKDFSPKGAEWDLAVKKWKHYVTDEGAKFDRTVILHADEIAPMVTWGTSPSQVISIKGVVPDPKDANDPVEKIGIESA 321
Cdd:TIGR00170 243 CKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKASAERA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 322 LKYMDLKSGQKIEDISINKVFIGSCTNSRIEDLRAAAATVKGKKVSSKVQAIVVPGSGRVKRQAEQEGLDKIFTAAGFEW 401
Cdd:TIGR00170 323 LAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGFEW 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523628383 402 RNPGCSMCLAMNDDVLEPGDRCASTSNRNFEGRQGKGGRTHLVGPEMAAAAAIEGHFVDIRN 463
Cdd:TIGR00170 403 REPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRK 464
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
2-464 |
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: 720.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 2 KTMFEKIWEDHLVGELDAGSY-LIYIDRHLIHEVTSPQAFEGLKLAG-RKVRRPEATFATMDHNVSTrtrdlslADPISA 79
Cdd:COG0065 3 MTLAEKILARHAGREVEPGEIvLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPT-------KDPKSA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 80 IQMQTLKKNCDENGIRVYDFQnpDQGIIHVIAPEMGLTHPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLVQ 159
Cdd:COG0065 76 EQVKTLREFAKEFGITFFDVG--DPGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 160 KKAKTMEIRVDGKLSDKVTAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEITF 239
Cdd:COG0065 154 KVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 240 NYIQGKDFSPkgaewdlavkkWKHYVTDEGAKFDRTVILHADEIAPMVTWGTSPSQVISIKGVvpdpkdandpvekigie 319
Cdd:COG0065 234 EYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSEL----------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 320 salkymdlksgqkiEDISINKVFIGSCTNSRIEDLRAAAATVKGKKVSSKVQAIVVPGSGRVKRQAEQEGLDKIFTAAGF 399
Cdd:COG0065 286 --------------EGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGA 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523628383 400 EWRNPGCSMCLAMNDDVLEPGDRCASTSNRNFEGRQG-KGGRTHLVGPEMAAAAAIEGHFVDIRNW 464
Cdd:COG0065 352 EWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
6-456 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 708.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 6 EKIWEDHLVGELDagSYLIYI-DRHLIHEVTSPQAFEGLKLAGRKVRRPEATFATMDHNVST--------RTRDLSLADP 76
Cdd:pfam00330 1 EKIWDAHLVEELD--GSLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTdlvidhapDALDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 77 IS--AIQMQTLKKNCDENGIRVYDfqnPDQGIIHVIAPEMGLTHPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAT 154
Cdd:pfam00330 79 ISrnKEQYDFLEWNAKKFGIRFVP---PGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 155 QTLVQKKAKTMEIRVDGKLSDKVTAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAP 234
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 235 DEITFNYIQ--GKDFSPKGAEWDLAVkKWKHYVTDEGAKFDRTVILHADEIAPMVTWGTSPSQVISIKGVVPDPkdANDP 312
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAV-AWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDP--FADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 313 VEKIGIESALKYMDLKSGQKIEDISINKVFIGSCTNSRIEDLRAAAATVK-----GKKVSSKVQAIVVPGSGRVKRQAEQ 387
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523628383 388 EGLDKIFTAAGFEWRNPGCSMCLAmNDDVLEPGDRCASTSNRNFEGRQGKGGRTHLVGPEMAAAAAIEG 456
Cdd:pfam00330 393 EGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASPALVAAAAIAG 460
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
28-458 |
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 523628383 28 RHLIHEVTSPQAFEGLKLAGR-KVRRPEATFATMDHNVSTrtrdlslADPISAIQMQTLKKNCDENGIRVYDFQNpdQGI 106
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPT-------PDIKAAEQVKTLRKFAKEFGINFFDVGR--QGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 107 IHVIAPEMGLTHPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLVQKKAKTMEIRVDGKLSDKVTAKDVILAI 186
Cdd:cd01583 72 CHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 187 IGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEITFNYIQGKDFSPkgaewdlavkkWKHYVT 266
Cdd:cd01583 152 IGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAY-----------WKELKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 267 DEGAKFDRTVILHADEIAPMVTWGTSPSQVISIKGVVPdpkdandpvekigiesalkymdlksgqkiedISINKVFIGSC 346
Cdd:cd01583 221 DEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQVFIGSC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 347 TNSRIEDLRAAAATVKGKKVSSKVQAIVVPGSGRVKRQAEQEGLDKIFTAAGFEWRNPGCSMCLAMNDDVLEPGDRCAST 426
Cdd:cd01583 270 TNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVST 349
|
410 420 430
....*....|....*....|....*....|...
gi 523628383 427 SNRNFEGRQG-KGGRTHLVGPEMAAAAAIEGHF 458
Cdd:cd01583 350 SNRNFKGRMGsPGARIYLASPATAAASAITGEI 382
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
1-462 |
2.07e-134 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 393.77 E-value: 2.07e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 1 MKTMFEKIWEDHLVGELDAGSYLIY-IDRHLIHEVTSPQAFEGL-KLAGRKVRRPEATFATMDHNVSTrtrdlslADPIS 78
Cdd:PRK00402 2 GMTLAEKILARHSGRDVSPGDIVEAkVDLVMAHDITGPLAIKEFeKIGGDKVFDPSKIVIVFDHFVPA-------KDIKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 79 AIQMQTLKKNCDENGIR-VYDFQnpdQGIIHVIAPEMGLTHPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTL 157
Cdd:PRK00402 75 AEQQKILREFAKEQGIPnFFDVG---EGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 158 VQKKAKTMEIRVDGKLSDKVTAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEI 237
Cdd:PRK00402 152 WFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 238 TFNYIqgkdfspkgaeWDLAVKKWKHYVTDEGAKFDRTVILHADEIAPMVTWGTSPSQVisikgvvpdpkdandpvekig 317
Cdd:PRK00402 232 TLEYL-----------KERAGRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNV--------------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 318 iesalkymdlKSGQKIEDISINKVFIGSCTNSRIEDLRAAAATVKGKKVSSKVQAIVVPGSGRVKRQAEQEGLDKIFTAA 397
Cdd:PRK00402 280 ----------KPVSEVEGTKVDQVFIGSCTNGRLEDLRIAAEILKGRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDA 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 523628383 398 GFEWRNPGCSMCLAMNDDVLEPGDRCASTSNRNFEGRQGK-GGRTHLVGPEMAAAAAIEGHFVDIR 462
Cdd:PRK00402 350 GAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGSpESEVYLASPAVAAASAVTGKITDPR 415
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
3-462 |
1.94e-115 |
|
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: 345.20 E-value: 1.94e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 3 TMFEKIWEDHLVGELDAG-SYLIYIDRHLIHEVTSPQAFEGLK-LAGRKVRRPEATFATMDHNVStrtrdlslADPISAI 80
Cdd:TIGR01343 1 TIAEKILSKKSGKEVYAGdLIEAEIDLAMVHDITAPLAIKTLEeYGIDKVWNPEKIVIVFDHQVP--------ADTIKAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 81 QMQTL-KKNCDENGIRvyDFQNPDQGIIHVIAPEMGLTHPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLVQ 159
Cdd:TIGR01343 73 EMQKLaREFVKKQGIK--YFYDVGEGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 160 KKAKTMEIRVDGKLSDKVTAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEITF 239
Cdd:TIGR01343 151 KVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 240 NYIQgkdfspkgaewDLAVKKWKHYVTDEGAKFDRTVILHADEIAPMVTWGTSPSQVISIKGVvpdpkdandpvekigie 319
Cdd:TIGR01343 231 QYLK-----------ERRKEPFRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEV----------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 320 salkymdlksgqkiEDISINKVFIGSCTNSRIEDLRAAAATVKGKKVSSKVQAIVVPGSGRVKRQAEQEGLDKIFTAAGF 399
Cdd:TIGR01343 283 --------------EGTEIDQVFIGSCTNGRLEDLRVAAKILKGRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGA 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523628383 400 EWRNPGCSMCLAMNDDVLEPGDRCASTSNRNFEGRQG-KGGRTHLVGPEMAAAAAIEGHFVDIR 462
Cdd:TIGR01343 349 VVSTPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMGhPNAEIYLASPATAAASAVKGYIADPR 412
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
2-460 |
1.13e-98 |
|
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: 302.07 E-value: 1.13e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 2 KTMFEKIWEDHLVGELDAG-SYLIYIDRHLIHEVTSPQAFEGLKLAGR-KVRRPEATFATMDHNVSTRTrdlsladpISA 79
Cdd:TIGR02086 1 MTLAEKILSEKVGRPVCAGeIVEVEVDLAMTHDGTGPLAIKALRELGVaRVWDPEKIVIAFDHNVPPPT--------VEA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 80 IQMQT-LKKNCDENGIRVYDFqnpDQGIIHVIAPEMGLTHPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLV 158
Cdd:TIGR02086 73 AEMQKeIREFAKRHGIKNFDV---GEGICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 159 QKKAKTMEIRVDGKLSDKVTAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEIT 238
Cdd:TIGR02086 150 IKVPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEET 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 239 FNYIQGKdfspkgaewdlAVKKWKHYVTDEGAKFDRTVILHADEIAPMVTwgtspsqvisikgvVPDPKDANDPVEkigi 318
Cdd:TIGR02086 230 YEYLKKR-----------RGLEFRILVPDPGANYYKEIEIDLSDLEPQVA--------------VPHSVDNVKPVS---- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 319 esalkymdlksgqKIEDISINKVFIGSCTNSRIEDLRAAAATVKGKKVSSKVQAIVVPGSGRVKRQAEQEGLDKIFTAAG 398
Cdd:TIGR02086 281 -------------DVEGTEIDQVFIGSCTNGRLEDLRIAAEILKGRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAG 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523628383 399 FEWRNPGCSMCLAMNDDVLEPGDRCASTSNRNFEGRQG-KGGRTHLVGPEMAAAAAIEGHFVD 460
Cdd:TIGR02086 348 AMICPPGCGPCLGAHMGVLGDGEVCLSTTNRNFKGRMGsPNAEIYLASPATAAASAVEGYITD 410
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
3-457 |
8.28e-93 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 287.42 E-value: 8.28e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 3 TMFEKIWEDHLVGELDAGSYL-IYIDRHLIHEVTSPQAFEGLKLAGRKVRRPEATFATMDHNVSTRTrdlsladpISAIQ 81
Cdd:NF040615 2 TLAEKILSKKLGKEVYAGDTVeVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPANT--------VKAAN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 82 MQTLKKN-CDENGIRvyDFQNPDQGIIHVIAPEMGLTHPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLVQK 160
Cdd:NF040615 74 MQKITREfVKEQGIK--NFYLGGEGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 161 KAKTMEIRVDGKlSDKVTAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEITFN 240
Cdd:NF040615 152 VPKTIRVNIVGK-NENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 241 YIQGKDFSpkgAEWDLAVKKWKHYVTDEGAKFDRTVILHADEIAPMVTWGTSPSQVisiKGVvpdpkdandpvekigies 320
Cdd:NF040615 231 YLRKEGVS---EEEIAELKKNRITVNEKEENYYKEIEIDITDMEEQVACPHHPDNV---KPV------------------ 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 321 alkymdlksgQKIEDISINKVFIGSCTNSRIEDLRAAAATVKGKKVSSKVQAIVVPGSGRVKRQAEQEGLDKIFTAAGFE 400
Cdd:NF040615 287 ----------SEVEGTEIDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAM 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 523628383 401 WRNPGCSMCLAMNDDVLEPGDRCASTSNRNFEGRQG-KGGRTHLVGPEMAAAAAIEGH 457
Cdd:NF040615 357 ICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGnINSYIYLSSPKIAAKSAVKGY 414
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
30-456 |
1.13e-72 |
|
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: 234.31 E-value: 1.13e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 30 LIHEVTSPQA---FEGLKLAGrKVRRPEATFATMDHnvstrtrDLSLADPISAIQMQTLKKNCDENGIRVYDfqnPDQGI 106
Cdd:cd01351 3 MLQDATGPMAmkaFEILAALG-KVADPSQIACVHDH-------AVQLEKPVNNEGHKFLSFFAALQGIAFYR---PGVGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 107 IHVIAPEMGLtHPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLVQKKAKTMEIRVDGKLSDKVTAKDVILAI 186
Cdd:cd01351 72 IHQIMVENLA-LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 187 IGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEITFNYIQGKDFSPKGAEWDLavkKWKHYVT 266
Cdd:cd01351 151 GGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWLA---FPEELLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 267 DEGAKFDRTVILHADEIAPmvtwgtspsqviSIKGvVPDPKDANDPVEkigiesalkymdlksgqkIEDISINKVFIGSC 346
Cdd:cd01351 228 DEGAEYDQVIEIDLSELEP------------DISG-PNRPDDAVSVSE------------------VEGTKIDQVLIGSC 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 347 TNSRIEDLRAAAATVKGKKVSSKVQAIVVPGSGRVKRQAEQEGLDKIFTAAGFEWRNPGCSMCLAMNDDVLEPGDRCAST 426
Cdd:cd01351 277 TNNRYSDMLAAAKLLKGAKVAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLVADGEVGVSS 356
|
410 420 430
....*....|....*....|....*....|.
gi 523628383 427 SNRNFEGRQGKG-GRTHLVGPEMAAAAAIEG 456
Cdd:cd01351 357 GNRNFPGRLGTYeRHVYLASPELAAATAIAG 387
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
2-465 |
1.21e-61 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 211.93 E-value: 1.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 2 KTMFEKIWEDHLV-GELDAGSYL-IYIDRHLIHEVTSPQA---FEGLKLAGRKVrrpEATFATMDHNVstrtrdlsladp 76
Cdd:PRK07229 3 LTLTEKILYAHLVeGELEPGEEIaIRIDQTLTQDATGTMAylqFEAMGLDRVKT---ELSVQYVDHNL------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 77 isaiqMQTLKKNCDengirVYDF------------QNPDQGIIHVIapemgltH------PGMTIVCGDSHTSTHGAFGA 138
Cdd:PRK07229 68 -----LQADFENAD-----DHRFlqsvaakygiyfSKPGNGICHQV-------HlerfafPGKTLLGSDSHTPTAGGLGM 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 139 LAFGIGTSEVEHVLATQTLVQKKAKTMEIRVDGKLSDKVTAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTV 218
Cdd:PRK07229 131 LAIGAGGLDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 219 CNMSIEAGARAGLIAPDEITFNYIQ----GKDFSPKGAewdlavkkwkhyvtDEGAKFDRTVILHADEIAPMVTWGTSPS 294
Cdd:PRK07229 211 TNMGAELGATTSIFPSDERTREFLKaqgrEDDWVELLA--------------DPDAEYDEVIEIDLSELEPLIAGPHSPD 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 295 QVISIKgvvpdpkdandpvekigiesalkymdlksgqKIEDISINKVFIGSCTNSRIEDLRAAAATVKGKKVSSKVQAIV 374
Cdd:PRK07229 277 NVVPVS-------------------------------EVAGIKVDQVLIGSCTNSSYEDLMRAASILKGKKVHPKVSLVI 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 375 VPGSGRVKRQAEQEGLDKIFTAAG---FEwrnPGCSMCLAMNDDvlePGDRCAS--TSNRNFEGRQG-KGGRTHLVGPEM 448
Cdd:PRK07229 326 NPGSRQVLEMLARDGALADLIAAGariLE---NACGPCIGMGQA---PATGNVSlrTFNRNFPGRSGtKDAQVYLASPET 399
|
490
....*....|....*..
gi 523628383 449 AAAAAIEGHFVDIRNWK 465
Cdd:PRK07229 400 AAASALTGVITDPRTLA 416
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
89-458 |
2.73e-58 |
|
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: 196.52 E-value: 2.73e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 89 CDENGIRVyDFQNPD-----QGI-----IHVIAPEMGLTH---------PGMTIVCGDSHTSTHGAFGALAFGIGTSEVE 149
Cdd:cd01585 34 VDHNTLQT-DFENADdhrflQTVaarygIYFSRPGNGICHqvhlerfavPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 150 HVLATQTLVQKKAKTMEIRVDGKLSDKVTAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARA 229
Cdd:cd01585 113 LAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 230 GLIAPDEITFNYIQGKDfspKGAEW-DLAvkkwkhyvTDEGAKFDRTVILHADEIAPMVTWGTSPSQVISIKgvvpdpkd 308
Cdd:cd01585 193 SIFPSDERTREFLAAQG---REDDWvELA--------ADADAEYDEEIEIDLSELEPLIARPHSPDNVVPVR-------- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 309 andpvekigiesalkymdlksgqKIEDISINKVFIGSCTNSRIEDLRAAAATVKGKKVSSKVQAIVVPGSGRVKRQAEQE 388
Cdd:cd01585 254 -----------------------EVAGIKVDQVAIGSCTNSSYEDLMTVAAILKGRRVHPHVSMVVAPGSKQVLEMLARN 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523628383 389 GLDKIFTAAGFEWRNPGCSMCLAMNDdvlEPGDRCAS--TSNRNFEGRQG-KGGRTHLVGPEMAAAAAIEGHF 458
Cdd:cd01585 311 GALADLLAAGARILESACGPCIGMGQ---APPTGGVSvrTFNRNFEGRSGtKDDLVYLASPEVAAAAALTGVI 380
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
98-456 |
3.80e-41 |
|
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: 151.82 E-value: 3.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 98 DFQNPDQGIIHVIAPEmGLTHPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLVQKKAKTMEIRVDGKLSDKV 177
Cdd:cd01584 70 GFWKPGSGIIHQIVLE-NYAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWT 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 178 TAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEITFNYIQGkdfSPKGAEWDLA 257
Cdd:cd01584 149 SPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKA---TGRAEIADLA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 258 VK-KWKHYVTDEGAKFDRTVILHADEIAPMVTWGTSPsqvisikgvvpdpkDANDPVEKIGiESALKY---MDLKSGqki 333
Cdd:cd01584 226 DEfKDDLLVADEGAEYDQLIEINLSELEPHINGPFTP--------------DLATPVSKFK-EVAEKNgwpLDLRVG--- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 334 edisinkvFIGSCTNSRIEDLRAAAATVK---GKKVSSKVQAIVVPGSGRVKRQAEQEGLDKIFTAAGFEWRNPGCSMCL 410
Cdd:cd01584 288 --------LIGSCTNSSYEDMGRAASIAKqalAHGLKCKSIFTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCI 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 523628383 411 AMNDDV-LEPGDRCA--STSNRNFEGRQGKGGRTH--LVGPEMAAAAAIEG 456
Cdd:cd01584 360 GQWDRKdIKKGEKNTivTSYNRNFTGRNDANPATHafVASPEIVTAMAIAG 410
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
32-456 |
2.86e-39 |
|
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: 145.45 E-value: 2.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 32 HEVTSPQAFEGLKLAGRKVRRPEATFATMDHNVSTRT-RDLSLADPISAIQMQtlkkncdeNGIrvyDFQNPDQGIIHVI 110
Cdd:cd01582 5 HDNSWPVALKFMSIGATKIHNPDQIVMTLDHDVQNKSeKNLKKYKNIESFAKK--------HGI---DFYPAGRGIGHQI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 111 APEMGLTHPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLVQKKAKTMEIRVDGKLSDKVTAKDVILAIIGKI 190
Cdd:cd01582 74 MIEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCGLF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 191 GTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEitfnyiqgkdfspkgaewdlavkkwKHYVTDega 270
Cdd:cd01582 154 NKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDA-------------------------KHLILD--- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 271 kfdrtvilhadeIAPMVTWGTSPSqviSIKgvVPDPKDandpvekigiesalkymDLKSgqkiEDISINKVFIGSCTNSR 350
Cdd:cd01582 206 ------------LSTLSPYVSGPN---SVK--VSTPLK-----------------ELEA----QNIKINKAYLVSCTNSR 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 351 IEDLRAAAATVKGKKVSSKVQAiVVPG--------SGRVKRQAEQEGLDKIFTAAGFEWRNPGCSMCLAMNDDVLEPGDR 422
Cdd:cd01582 248 ASDIAAAADVVKGKKEKNGKIP-VAPGvefyvaaaSSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQGLLEPGEV 326
|
410 420 430
....*....|....*....|....*....|....*
gi 523628383 423 CASTSNRNFEGRQG-KGGRTHLVGPEMAAAAAIEG 456
Cdd:cd01582 327 GISATNRNFKGRMGsTEALAYLASPAVVAASAISG 361
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
99-461 |
3.96e-25 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 109.12 E-value: 3.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 99 FQN-----PDQGIIHVIAPEM---------GLTHPGmTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLVQKKAKT 164
Cdd:PLN00070 206 FQNmlvvpPGSGIVHQVNLEYlgrvvfntdGILYPD-SVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGV 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 165 MEIRVDGKLSDKVTAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEITFNYIQ- 243
Cdd:PLN00070 285 VGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKl 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 244 -GKDfSPKGAEWDLAVKKWKHYVTDEGAKFDRT----VILHADEIAPMVTWGTSPSQVISIKGVVPD------------- 305
Cdd:PLN00070 365 tGRS-DETVAMIEAYLRANKMFVDYNEPQQERVyssyLELDLEDVEPCISGPKRPHDRVPLKEMKADwhscldnkvgfkg 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 306 ---PKDANDPVEKIGIESalKYMDLKSGqkieDISINKvfIGSCTNSRIEDLRAAAATVKGK------KVSSKVQAIVVP 376
Cdd:PLN00070 444 favPKEAQSKVAKFSFHG--QPAELRHG----SVVIAA--ITSCTNTSNPSVMLGAGLVAKKacelglEVKPWIKTSLAP 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 377 GSGRVKRQAEQEGLDKIFTAAGFEWRNPGCSMCLAMNDDVLEP-------GDRCAS---TSNRNFEGRQGKGGR-THLVG 445
Cdd:PLN00070 516 GSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIGNSGELDESvasaiteNDIVAAavlSGNRNFEGRVHPLTRaNYLAS 595
|
410
....*....|....*.
gi 523628383 446 PEMAAAAAIEGHfVDI 461
Cdd:PLN00070 596 PPLVVAYALAGT-VDI 610
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
102-434 |
3.43e-22 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 100.09 E-value: 3.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 102 PDQGIIH---------VIAPEMGLTHPGmTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLVQKKAKTMEIRVDGK 172
Cdd:PTZ00092 182 PGSGIVHqvnleylarVVFNKDGLLYPD-SVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTGK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 173 LSDKVTAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEITFNYIQ--GKDfSPK 250
Cdd:PTZ00092 261 LSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKqtGRS-EEK 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 251 GAEWDLAVKKWK-HYVTDEGAKFDRTVILHADEIAPMVTWGTSPSQVISIKGVVPDPKDA----------NDPVEKIGIE 319
Cdd:PTZ00092 340 VELIEKYLKANGlFRTYAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTAClsapvgfkgfGIPEEKHEKK 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 320 SALKYmdlkSGQK--IEDISINKVFIGSCTNSRIED------LRAAAATVKGKKVSSKVQAIVVPGSGRVKRQAEQEGLD 391
Cdd:PTZ00092 420 VKFTY----KGKEytLTHGSVVIAAITSCTNTSNPSvmlaagLLAKKAVEKGLKVPPYIKTSLSPGSKVVTKYLEASGLL 495
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 523628383 392 KIFTAAGFEWRNPGCSMCLAMNDDVLEPGDRCAS----------TSNRNFEGR 434
Cdd:PTZ00092 496 KYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITnndlvaaavlSGNRNFEGR 548
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
99-434 |
3.68e-22 |
|
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: 99.79 E-value: 3.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 99 FQN-----PDQGIIH----------VIAPEMG---LTHPGmTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLvqk 160
Cdd:COG1048 165 FDNfrvvpPGTGIVHqvnleylafvVWTREEDgetVAYPD-TLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPV--- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 161 kakTMEI------RVDGKLSDKVTAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAP 234
Cdd:COG1048 241 ---SMLIpevvgvKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPV 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 235 DEITFNYIQ--GKDfspkgaEWDLAV--------KKWKHYVTDEgAKFDRTVILHADEIAPMVTWGTSPSQVISIKGVvp 304
Cdd:COG1048 318 DEETLDYLRltGRS------EEQIELveayakaqGLWRDPDAPE-PYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDL-- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 305 dPKDANDPVEKIGIESALKYMDLKSGQKIEDISINKVF---IGSCTNSRIED-LRAAA-----ATVKGKKVSSKVQAIVV 375
Cdd:COG1048 389 -KEAFRAALAAPVGEELDKPVRVEVDGEEFELGHGAVViaaITSCTNTSNPSvMIAAGllakkAVEKGLKVKPWVKTSLA 467
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523628383 376 PGSGRVKRQAEQEGLDKIFTAAGFewrNP---GCSMCL--------AMNDDVLEPGDRCAS-TS-NRNFEGR 434
Cdd:COG1048 468 PGSKVVTDYLERAGLLPYLEALGF---NVvgyGCTTCIgnsgplppEISEAIEENDLVVAAvLSgNRNFEGR 536
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
101-457 |
4.95e-21 |
|
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: 95.26 E-value: 4.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 101 NPDQGIIHVIAPEMGLthPGMTIVCGDSHTSthgaFG-ALAFGIGTSEVEHVLATQTLVQKKAKTMEIRVDGKLSDKVTA 179
Cdd:cd01581 90 RPGDGVIHSWLNRMLL--PDTVGTGGDSHTR----FPiGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 180 KDVILAI-----------IGKIGTAGA-TGYVIEYRGsaIQALSMEARMTVCNMSIEAGARAGLIAPDEITFnyiqgkdf 247
Cdd:cd01581 164 RDLVNAIpyyaiqqglltVEKKGKKNVfNGRILEIEG--LPDLKVEQAFELTDASAERSAAACTVRLDKEPV-------- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 248 spkgAEWDLAVKKWKHYVTDEGAKFDRTVIlhaDEIAPMVTWGTSPS-----------QVISI------KGVVPDPKDAN 310
Cdd:cd01581 234 ----IEYLESNVVLMKIMIANGYDDARTLL---RRIIAMEEWLANPPllepdadaeyaAVIEIdlddikEPILACPNDPD 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 311 DpvekigiesaLKYMDLKSGQKIEDisinkVFIGSC-TNsrIEDLRAAAATVKGKKvSSKVQAIVVPGSGRVKRQAEQEG 389
Cdd:cd01581 307 D----------VKLLSEVAGKKIDE-----VFIGSCmTN--IGHFRAAAKILRGKE-FKPTRLWVAPPTRMDWAILQEEG 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523628383 390 LDKIFTAAGFEWRNPGCSMCLAmNDDVLEPGDRCASTSNRNFEGRQGKGGRTHLVGPEMAAAAAIEGH 457
Cdd:cd01581 369 YYSIFGDAGARTEMPGCSLCMG-NQARVADGATVFSTSTRNFDNRVGKGAEVYLGSAELAAVCALLGR 435
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
122-434 |
6.24e-19 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 89.99 E-value: 6.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 122 TIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLVQKKAKTMEIRVDGKLSDKVTAKDVILAI---IGKIGTAGAtgY 198
Cdd:PRK12881 207 TLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIPDVVGVELTGKLREGVTATDLVLTVtemLRKEGVVGK--F 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 199 ViEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEITFNYIQGKDFSPkgAEWDL------AVKKWkhYVTDEGAKF 272
Cdd:PRK12881 285 V-EFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLRLTGRTE--AQIALveayakAQGLW--GDPKAEPRY 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 273 DRTVILHADEIAPMVTWGTSPSQVISI-------KGVVPDPKDANDPVEKIGIESAlkyMDLKSGqkieDISINKvfIGS 345
Cdd:PRK12881 360 TRTLELDLSTVAPSLAGPKRPQDRIALgnvksafSDLFSKPVAENGFAKKAQTSNG---VDLPDG----AVAIAA--ITS 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 346 CTN-SRIEDLRAAA-----ATVKGKKVSSKVQAIVVPGSGRVKRQAEQEGLDKIFTAAGFEWRNPGCSMCLAMNDDVLEP 419
Cdd:PRK12881 431 CTNtSNPSVLIAAGllakkAVERGLTVKPWVKTSLAPGSKVVTEYLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPE 510
|
330 340
....*....|....*....|....*
gi 523628383 420 -------GD-RCAS--TSNRNFEGR 434
Cdd:PRK12881 511 ieqaitkNDlVAAAvlSGNRNFEGR 535
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
338-457 |
2.86e-18 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 87.93 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 338 INKVFIGSC-TNsrIEDLRAAAATVKGKKVSSKVQAIVVPGSGRVKRQAEQEGLDKIFTAAGFEWRNPGCSMCLAmNDDV 416
Cdd:PRK09238 691 IDEVFIGSCmTN--IGHFRAAGKLLEGKKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMG-NQAR 767
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 523628383 417 LEPGDRCASTSNRNFEGRQGKGGRTHLVGPEMAAAAAIEGH 457
Cdd:PRK09238 768 VADGATVFSTSTRNFPNRLGKGANVYLGSAELAAVCALLGR 808
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
99-456 |
5.88e-18 |
|
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydrolyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes.
Pssm-ID: 153136 Cd Length: 404 Bit Score: 85.43 E-value: 5.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 99 FQN-----PDQGIIHVIAPEM-------------GLTHPGmTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLVQK 160
Cdd:cd01586 83 FKNlrvvpPGTGIIHQVNLEYlarvvftseedgdGVAYPD-SVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISML 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 161 KAKTMEIRVDGKLSDKVTAKDVILAIIGKIGTAGATGYVIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDeitfn 240
Cdd:cd01586 162 LPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD----- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 241 yiqgkdfspkgaewdlavkkwkhyvtdegakfDRTVILHADEIAPMVTWGTSPSQVISIKGVVpdpkdandpvekiGIES 320
Cdd:cd01586 237 --------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPLHGSV-------------VIAA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 321 alkymdlksgqkiedisinkvfIGSCTNSRIEDLRAAAATV------KGKKVSSKVQAIVVPGSGRVKRQAEQEGLDKIF 394
Cdd:cd01586 272 ----------------------ITSCTNTSNPSVMLAAGLLakkaveLGLKVKPYVKTSLAPGSRVVTKYLEASGLLPYL 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523628383 395 TAAGFEWRNPGCSMCL--------AMNDDVLEPGDRCAS--TSNRNFEGRQGKGGR-THLVGPEMAAAAAIEG 456
Cdd:cd01586 330 EKLGFHVVGYGCTTCIgnsgplpeEVEEAIKENDLVVAAvlSGNRNFEGRIHPLVRaNYLASPPLVVAYALAG 402
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
102-456 |
2.21e-17 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 84.97 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 102 PDQGIIHVIAPEMGLthPGMTIVCGDSHT------STHGAFGALAFGIGTSEVEHVLATQTLVqkkaktmeiRVDGKLSD 175
Cdd:PLN00094 537 PGDGVIHSWLNRMLL--PDTVGTGGDSHTrfpigiSFPAGSGLVAFGAATGVIPLDMPESVLV---------RFTGTMQP 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 176 KVTAKDVILAI-----------IGKIGTAGA-TGYVIEYRGsaIQALSMEARMTVCNMSIEAGARAGLIAPDEITF-NYI 242
Cdd:PLN00094 606 GITLRDLVHAIpytaiqdglltVEKKGKKNVfSGRILEIEG--LPHLKCEQAFELSDASAERSAAGCTIKLDKEPIiEYL 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 243 QGkdfspkgaewDLAVKKWkhyVTDEGAKFDRTVilhADEIAPMVTWGTSP-----------SQVISIK-GVVPDPKDA- 309
Cdd:PLN00094 684 NS----------NVVMLKW---MIAEGYGDRRTL---ERRIARMQQWLADPelleadpdaeyAAVIEIDmDEIKEPILCa 747
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 310 -NDPvekigieSALKYMDLKSGQKIEDisinkVFIGSC-TNsrIEDLRAAAATVKGKKVSSKVQAIVVPGSGRVKRQAEQ 387
Cdd:PLN00094 748 pNDP-------DDARLLSEVTGDKIDE-----VFIGSCmTN--IGHFRAAGKLLNDNLSQLPTRLWVAPPTKMDEAQLKA 813
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523628383 388 EGLDKIFTAAGFEWRNPGCSMCLAmNDDVLEPGDRCASTSNRNFEGRQGKGGRTHLVGPEMAAAAAIEG 456
Cdd:PLN00094 814 EGYYSTFGTVGARTEMPGCSLCMG-NQARVAEKSTVVSTSTRNFPNRLGKGANVYLASAELAAVAAILG 881
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
102-436 |
7.06e-16 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 80.44 E-value: 7.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 102 PDQGIIHVIAPEMgLTHPGMTIVCGDSHTStHGAFGALAFGIGTSEVEHVLATQTLVQKKAKTMEIRVDGKLSDKVTAKD 181
Cdd:PRK11413 125 PHIAVIHQYMREM-MAGGGKMILGSDSHTR-YGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 182 VILAIIGKIgtaGATGY----VIEYRGSAIQALSMEARMTVCNMSIEAGARAGLIAPDEITFNY--IQGKdfspkgaewd 255
Cdd:PRK11413 203 VALAIIGAV---FKNGYvknkVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWlaLHGR---------- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 256 laVKKWKHYVTDEGAKFDRTVILHADEIAPMVTWGTSPSQVISIKGVVPDPKDANDPVEKIGIESALKYMDLKSGQKIED 335
Cdd:PRK11413 270 --GQDYCELNPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDELNQNLTDILREVEIESERVAHGKAKLSLLDKIEN 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 336 --ISINKVFIGSCTNSRIEDLRAAAATVKGKKVSSKVQAI-VVPGSGRVKRQAEQEGLDKIFTAAGFEWRNPGCSMCLAM 412
Cdd:PRK11413 348 grLKVQQGIIAGCSGGNYENVIAAANALRGQSCGNDTFSLsVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFGA 427
|
330 340
....*....|....*....|....*.
gi 523628383 413 NDdvlEPGDRCAST--SNRNFEGRQG 436
Cdd:PRK11413 428 GD---TPANNGLSIrhTTRNFPNREG 450
|
|
| AcnB |
COG1049 |
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ... |
338-457 |
3.44e-14 |
|
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: 74.89 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 338 INKVFIGSC-TNsrIEDLRAAAATVKGKKvSSKVQAIVVPGSGRVKRQAEQEGLDKIFTAAGFEWRNPGCSMCLAmNDDV 416
Cdd:COG1049 691 IDEVFIGSCmTN--IGHFRAAGKLLEGKG-NLPTRLWIAPPTKMDEAQLTEEGYYSIFGAAGARTEMPGCSLCMG-NQAR 766
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 523628383 417 LEPGDRCASTSNRNFEGRQGKGGRTHLVGPEMAAAAAIEGH 457
Cdd:COG1049 767 VADGATVFSTSTRNFPNRLGKGANVYLGSAELAAVCALLGR 807
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
99-434 |
2.14e-10 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 63.22 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 99 FQN-----PDQGIIHVI-----APEMGLTHPGM------TIVCGDSHTsTH-GAFGALAFGIGTSEVEHVLATQtlvqkk 161
Cdd:PRK09277 168 FDNfrvvpPGTGICHQVnleylAPVVWTREDGElvaypdTLVGTDSHT-TMiNGLGVLGWGVGGIEAEAAMLGQ------ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 162 AKTMEI------RVDGKLSDKVTAKDVILAI---IGKIGTAGAtgYViEYRGSAIQALSMEARMTVCNMSIEAGARAGLI 232
Cdd:PRK09277 241 PSSMLIpevvgvKLTGKLPEGVTATDLVLTVtemLRKKGVVGK--FV-EFFGEGLASLSLADRATIANMAPEYGATCGFF 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 233 APDEITFNYIQ--GKDfspkgaEWDLA-VKKW-KH----YVTDEGAKFDRTVILHADEIAPmvtwgtspsqviSIKGvvp 304
Cdd:PRK09277 318 PIDEETLDYLRltGRD------EEQVAlVEAYaKAqglwRDPLEEPVYTDVLELDLSTVEP------------SLAG--- 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 305 dPKDANDPVE--------KIGIESALKYMDLKSGQKIEDISI--NKVFIG---SCTN-SRIEDLRAAA-----ATVKGKK 365
Cdd:PRK09277 377 -PKRPQDRIPlsdvkeafAKSAELGVQGFGLDEAEEGEDYELpdGAVVIAaitSCTNtSNPSVMIAAGllakkAVEKGLK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523628383 366 VSSKVQAIVVPGSGRVKRQAEQEG----LDKI-FTAAGFewrnpGCSMCLAMNDDVLEP-------GDRCAST--S-NRN 430
Cdd:PRK09277 456 VKPWVKTSLAPGSKVVTDYLEKAGllpyLEALgFNLVGY-----GCTTCIGNSGPLPPEiekaindNDLVVTAvlSgNRN 530
|
....
gi 523628383 431 FEGR 434
Cdd:PRK09277 531 FEGR 534
|
|
| |
