|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
1-422 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 699.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 1 MGKTIAEKIFDAHRVDMPFP-DTHVLKLDRVFCHEITTPIAITDLMARGMDRVYDPTKIKAVIDHVTPAKDSKTAEQGKI 79
Cdd:PRK00402 1 MGMTLAEKILARHSGRDVSPgDIVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVIVFDHFVPAKDIKSAEQQKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 80 LRDWAKRHGIKDFFDIGRnGVCHAIFPEKGFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCAFHFPKTI 159
Cdd:PRK00402 81 LREFAKEQGIPNFFDVGE-GICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKTWFKVPETI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 160 KIVLKGTLQPGVYAKDLILFIIKELTVNGATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGICYPDMTTVNYLWDF 239
Cdd:PRK00402 160 KVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLEYLKER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 240 ikdefstkeeALQEYSKWTSDADAAYEKVYEYDVTDLGPMATFGNKPDQVKTVAEMSGTAIDQVYIGSCTNGRIEDLRIA 319
Cdd:PRK00402 240 ----------AGRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVEGTKVDQVFIGSCTNGRLEDLRIA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 320 ASILKDKKISDDVRAIVSPATPAIFNMALKEGLIEIFQNAGFCVTNPTCGACLGMSNGVLASGEVCASTTNRNFNGRMGK 399
Cdd:PRK00402 310 AEILKGRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGS 389
|
410 420
....*....|....*....|....
gi 503951987 400 -GGTVHLMSPATAAASAIEGKITN 422
Cdd:PRK00402 390 pESEVYLASPAVAAASAVTGKITD 413
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-421 |
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: 666.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 1 MGKTIAEKIFDAHRVDMPFP-DTHVLKLDRVFCHEITTPIAITDLMARGMDRVYDPTKIKAVIDHVTPAKDSKTAEQGKI 79
Cdd:COG0065 1 MGMTLAEKILARHAGREVEPgEIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVAVFDHNVPTKDPKSAEQVKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 80 LRDWAKRHGIKdFFDIGRNGVCHAIFPEKGFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCAFHFPKTI 159
Cdd:COG0065 81 LREFAKEFGIT-FFDVGDPGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWFKVPETM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 160 KIVLKGTLQPGVYAKDLILFIIKELTVNGATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGICYPDMTTVNYLwdf 239
Cdd:COG0065 160 RIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFEYL--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 240 ikdefstKEEALQEYSKWTSDADAAYEKVYEYDVTDLGPMATFGNKPDQVKTVAEMSGTAIDQVYIGSCTNGRIEDLRIA 319
Cdd:COG0065 237 -------KGRPFAPWRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELEGIKIDQVFIGSCTNGRIEDLRAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 320 ASILKDKKISDDVRAIVSPATPAIFNMALKEGLIEIFQNAGFCVTNPTCGACLGMSNGVLASGEVCASTTNRNFNGRMG- 398
Cdd:COG0065 310 AEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGs 389
|
410 420
....*....|....*....|...
gi 503951987 399 KGGTVHLMSPATAAASAIEGKIT 421
Cdd:COG0065 390 PGSRTYLASPATAAASAIAGRIT 412
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
29-420 |
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: 579.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 29 RVFCHEITTPIAITDLMARGMDRVYDPTKIKAVIDHVTPAKDSKTAEQGKILRDWAKRHGIkDFFDIGRNGVCHAIFPEK 108
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAVFDHNVPTPDIKAAEQVKTLRKFAKEFGI-NFFDVGRQGICHVILPEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 109 GFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCAFHFPKTIKIVLKGTLQPGVYAKDLILFIIKELTVNG 188
Cdd:cd01583 80 GLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 189 ATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGICYPDMTTVNYLwdfikdefstKEEALQEYSKWTSDADAAYEKV 268
Cdd:cd01583 160 ATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYL----------KGRGKAYWKELKSDEDAEYDKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 269 YEYDVTDLGPMATFGNKPDQVKTVAEMSGTAIDQVYIGSCTNGRIEDLRIAASILKDKKISDDVRAIVSPATPAIFNMAL 348
Cdd:cd01583 230 VEIDASELEPQVAWPHSPDNVVPVSEVEGIKIDQVFIGSCTNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAE 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503951987 349 KEGLIEIFQNAGFCVTNPTCGACLGMSNGVLASGEVCASTTNRNFNGRMGKGGT-VHLMSPATAAASAIEGKI 420
Cdd:cd01583 310 KEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTSNRNFKGRMGSPGArIYLASPATAAASAITGEI 382
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
4-422 |
1.72e-176 |
|
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: 499.28 E-value: 1.72e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 4 TIAEKIFDAHRVDMPFP-DTHVLKLDRVFCHEITTPIAITDLMARGMDRVYDPTKIKAVIDHVTPAKDSKTAEQGKILRD 82
Cdd:TIGR01343 1 TIAEKILSKKSGKEVYAgDLIEAEIDLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIVFDHQVPADTIKAAEMQKLARE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 83 WAKRHGIKDFFDIGRnGVCHAIFPEKGFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCAFHFPKTIKIV 162
Cdd:TIGR01343 81 FVKKQGIKYFYDVGE-GICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFKVPETIRVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 163 LKGTLQPGVYAKDLILFIIKELTVNGATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGICYPDMTTVNYLwdfikd 242
Cdd:TIGR01343 160 ITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYL------ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 243 efstKEEALQEYSKWTSDADAAYEKVYEYDVTDLGPMATFGNKPDQVKTVAEMSGTAIDQVYIGSCTNGRIEDLRIAASI 322
Cdd:TIGR01343 234 ----KERRKEPFRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEVEGTEIDQVFIGSCTNGRLEDLRVAAKI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 323 LKDKKISDDVRAIVSPATPAIFNMALKEGLIEIFQNAGFCVTNPTCGACLGMSNGVLASGEVCASTTNRNFNGRMG-KGG 401
Cdd:TIGR01343 310 LKGRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMGhPNA 389
|
410 420
....*....|....*....|.
gi 503951987 402 TVHLMSPATAAASAIEGKITN 422
Cdd:TIGR01343 390 EIYLASPATAAASAVKGYIAD 410
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-418 |
4.85e-140 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 408.35 E-value: 4.85e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 7 EKIFDAHRVD-----MPFpdthvlKLDRVFCHEITTPIAITDLMARGmDRVYDPTKIKAVIDHVTPAKD----------- 70
Cdd:pfam00330 1 EKIWDAHLVEeldgsLLY------IPDRVLMHDVTSPQAFVDLRAAG-RAVRRPGGTPATIDHLVPTDLvidhapdaldk 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 71 ------SKTAEQGKILRDWAKRHGIKdFFDIGrNGVCHAIFPEKGFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEV 144
Cdd:pfam00330 74 niedeiSRNKEQYDFLEWNAKKFGIR-FVPPG-QGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 145 GILKGVCAFHFPKTIKIVLKGTLQPGVYAKDLILFIIKELTVNGATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCG 224
Cdd:pfam00330 152 VLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 225 ICYPDMTTVNYLwDFIKDEFSTKEEALQEYSKW---TSDADAAYEKVYEYDVTDLGPMATFGNKPDQVKTVAE------- 294
Cdd:pfam00330 232 LFPPDETTFEYL-RATGRPEAPKGEAYDKAVAWktlASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSElvpdpfa 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 295 ----------------------MSGTAIDQVYIGSCTNGRIEDLRIAASILKD-----KKISDDVRAIVSPATPAIFNMA 347
Cdd:pfam00330 311 davkrkaaeraleymglgpgtpLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKKavekgLKVAPGVKASVVPGSEVVRAYA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503951987 348 LKEGLIEIFQNAGFCVTNPTCGACLGMSnGVLASGEVCASTTNRNFNGRMGKGGTVHLMSPATAAASAIEG 418
Cdd:pfam00330 391 EAEGLDKILEEAGFEWRGPGCSMCIGNS-DRLPPGERCVSSSNRNFEGRQGPGGRTHLASPALVAAAAIAG 460
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
21-422 |
1.94e-139 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 405.29 E-value: 1.94e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 21 DTHVLKLDRVFCHEITTPIAITDLMARGmDRVYDPTKIKAVIDHVTPAKDSKTAEQGKILRDWAKRHGIKDFFDIGRnGV 100
Cdd:NF040615 20 DTVEVDVDLAMTHDGTTPLTYKAFKEIS-DKVWDNEKIVIVFDHNVPANTVKAANMQKITREFVKEQGIKNFYLGGE-GI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 101 CHAIFPEKGFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCAFHFPKTIKIVLKGtLQPGVYAKDLILFI 180
Cdd:NF040615 98 CHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVNIVG-KNENISGKDIILKV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 181 IKELTVNGATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGICYPDMTTVNYLwdfiKDEFSTKEE--ALQEYSKWT 258
Cdd:NF040615 177 CKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYL----RKEGVSEEEiaELKKNRITV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 259 SDADAAYEKVYEYDVTDLGPMATFGNKPDQVKTVAEMSGTAIDQVYIGSCTNGRIEDLRIAASILKDKKISDDVRAIVSP 338
Cdd:NF040615 253 NEKEENYYKEIEIDITDMEEQVACPHHPDNVKPVSEVEGTEIDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 339 ATPAIFNMALKEGLIEIFQNAGFCVTNPTCGACLGMSNGVLASGEVCASTTNRNFNGRMG-KGGTVHLMSPATAAASAIE 417
Cdd:NF040615 333 ASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGnINSYIYLSSPKIAAKSAVK 412
|
....*
gi 503951987 418 GKITN 422
Cdd:NF040615 413 GYITN 417
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
1-422 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 699.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 1 MGKTIAEKIFDAHRVDMPFP-DTHVLKLDRVFCHEITTPIAITDLMARGMDRVYDPTKIKAVIDHVTPAKDSKTAEQGKI 79
Cdd:PRK00402 1 MGMTLAEKILARHSGRDVSPgDIVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVIVFDHFVPAKDIKSAEQQKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 80 LRDWAKRHGIKDFFDIGRnGVCHAIFPEKGFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCAFHFPKTI 159
Cdd:PRK00402 81 LREFAKEQGIPNFFDVGE-GICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKTWFKVPETI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 160 KIVLKGTLQPGVYAKDLILFIIKELTVNGATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGICYPDMTTVNYLWDF 239
Cdd:PRK00402 160 KVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLEYLKER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 240 ikdefstkeeALQEYSKWTSDADAAYEKVYEYDVTDLGPMATFGNKPDQVKTVAEMSGTAIDQVYIGSCTNGRIEDLRIA 319
Cdd:PRK00402 240 ----------AGRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVEGTKVDQVFIGSCTNGRLEDLRIA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 320 ASILKDKKISDDVRAIVSPATPAIFNMALKEGLIEIFQNAGFCVTNPTCGACLGMSNGVLASGEVCASTTNRNFNGRMGK 399
Cdd:PRK00402 310 AEILKGRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGS 389
|
410 420
....*....|....*....|....
gi 503951987 400 -GGTVHLMSPATAAASAIEGKITN 422
Cdd:PRK00402 390 pESEVYLASPAVAAASAVTGKITD 413
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-421 |
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: 666.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 1 MGKTIAEKIFDAHRVDMPFP-DTHVLKLDRVFCHEITTPIAITDLMARGMDRVYDPTKIKAVIDHVTPAKDSKTAEQGKI 79
Cdd:COG0065 1 MGMTLAEKILARHAGREVEPgEIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVAVFDHNVPTKDPKSAEQVKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 80 LRDWAKRHGIKdFFDIGRNGVCHAIFPEKGFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCAFHFPKTI 159
Cdd:COG0065 81 LREFAKEFGIT-FFDVGDPGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWFKVPETM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 160 KIVLKGTLQPGVYAKDLILFIIKELTVNGATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGICYPDMTTVNYLwdf 239
Cdd:COG0065 160 RIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFEYL--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 240 ikdefstKEEALQEYSKWTSDADAAYEKVYEYDVTDLGPMATFGNKPDQVKTVAEMSGTAIDQVYIGSCTNGRIEDLRIA 319
Cdd:COG0065 237 -------KGRPFAPWRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELEGIKIDQVFIGSCTNGRIEDLRAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 320 ASILKDKKISDDVRAIVSPATPAIFNMALKEGLIEIFQNAGFCVTNPTCGACLGMSNGVLASGEVCASTTNRNFNGRMG- 398
Cdd:COG0065 310 AEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGs 389
|
410 420
....*....|....*....|...
gi 503951987 399 KGGTVHLMSPATAAASAIEGKIT 421
Cdd:COG0065 390 PGSRTYLASPATAAASAIAGRIT 412
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
29-420 |
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: 579.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 29 RVFCHEITTPIAITDLMARGMDRVYDPTKIKAVIDHVTPAKDSKTAEQGKILRDWAKRHGIkDFFDIGRNGVCHAIFPEK 108
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAVFDHNVPTPDIKAAEQVKTLRKFAKEFGI-NFFDVGRQGICHVILPEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 109 GFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCAFHFPKTIKIVLKGTLQPGVYAKDLILFIIKELTVNG 188
Cdd:cd01583 80 GLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 189 ATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGICYPDMTTVNYLwdfikdefstKEEALQEYSKWTSDADAAYEKV 268
Cdd:cd01583 160 ATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYL----------KGRGKAYWKELKSDEDAEYDKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 269 YEYDVTDLGPMATFGNKPDQVKTVAEMSGTAIDQVYIGSCTNGRIEDLRIAASILKDKKISDDVRAIVSPATPAIFNMAL 348
Cdd:cd01583 230 VEIDASELEPQVAWPHSPDNVVPVSEVEGIKIDQVFIGSCTNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAE 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503951987 349 KEGLIEIFQNAGFCVTNPTCGACLGMSNGVLASGEVCASTTNRNFNGRMGKGGT-VHLMSPATAAASAIEGKI 420
Cdd:cd01583 310 KEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTSNRNFKGRMGSPGArIYLASPATAAASAITGEI 382
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
4-422 |
1.72e-176 |
|
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: 499.28 E-value: 1.72e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 4 TIAEKIFDAHRVDMPFP-DTHVLKLDRVFCHEITTPIAITDLMARGMDRVYDPTKIKAVIDHVTPAKDSKTAEQGKILRD 82
Cdd:TIGR01343 1 TIAEKILSKKSGKEVYAgDLIEAEIDLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIVFDHQVPADTIKAAEMQKLARE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 83 WAKRHGIKDFFDIGRnGVCHAIFPEKGFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCAFHFPKTIKIV 162
Cdd:TIGR01343 81 FVKKQGIKYFYDVGE-GICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFKVPETIRVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 163 LKGTLQPGVYAKDLILFIIKELTVNGATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGICYPDMTTVNYLwdfikd 242
Cdd:TIGR01343 160 ITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYL------ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 243 efstKEEALQEYSKWTSDADAAYEKVYEYDVTDLGPMATFGNKPDQVKTVAEMSGTAIDQVYIGSCTNGRIEDLRIAASI 322
Cdd:TIGR01343 234 ----KERRKEPFRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEVEGTEIDQVFIGSCTNGRLEDLRVAAKI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 323 LKDKKISDDVRAIVSPATPAIFNMALKEGLIEIFQNAGFCVTNPTCGACLGMSNGVLASGEVCASTTNRNFNGRMG-KGG 401
Cdd:TIGR01343 310 LKGRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMGhPNA 389
|
410 420
....*....|....*....|.
gi 503951987 402 TVHLMSPATAAASAIEGKITN 422
Cdd:TIGR01343 390 EIYLASPATAAASAVKGYIAD 410
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
3-424 |
3.50e-153 |
|
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: 439.97 E-value: 3.50e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 3 KTIAEKIFdAHRVDMPFP--DTHVLKLDRVFCHEITTPIAITDLMARGMDRVYDPTKIKAVIDHVTPAKDSKTAEQGKIL 80
Cdd:TIGR02086 1 MTLAEKIL-SEKVGRPVCagEIVEVEVDLAMTHDGTGPLAIKALRELGVARVWDPEKIVIAFDHNVPPPTVEAAEMQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 81 RDWAKRHGIKDFfDIGRnGVCHAIFPEKGFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCAFHFPKTIK 160
Cdd:TIGR02086 80 REFAKRHGIKNF-DVGE-GICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTWIKVPETIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 161 IVLKGTLQPGVYAKDLILFIIKELTVNGATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGICYPDMTTVNYLwdfi 240
Cdd:TIGR02086 158 VVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEETYEYL---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 241 kdefstKEEALQEYSKWTSDADAAYEKVYEYDVTDLGPMATFGNKPDQVKTVAEMSGTAIDQVYIGSCTNGRIEDLRIAA 320
Cdd:TIGR02086 234 ------KKRRGLEFRILVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVSDVEGTEIDQVFIGSCTNGRLEDLRIAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 321 SILKDKKISDDVRAIVSPATPAIFNMALKEGLIEIFQNAGFCVTNPTCGACLGMSNGVLASGEVCASTTNRNFNGRMG-K 399
Cdd:TIGR02086 308 EILKGRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAGAMICPPGCGPCLGAHMGVLGDGEVCLSTTNRNFKGRMGsP 387
|
410 420
....*....|....*....|....*
gi 503951987 400 GGTVHLMSPATAAASAIEGKITNSQ 424
Cdd:TIGR02086 388 NAEIYLASPATAAASAVEGYITDPE 412
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-421 |
3.05e-151 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 436.86 E-value: 3.05e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 1 MGKTIAEKIFDAHRVDMPFPDTHVLKLDRVFCHEITTPIAITDLMARGMdRVYDPTKIKAVIDHVTP-------AKDSKT 73
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGR-KVRRPDLTFATMDHNVPttdrdlpIADPVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 74 AEQGKILRDWAKRHGIKdFFDIG--RNGVCHAIFPEKGFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEvgilkgvc 151
Cdd:PRK05478 80 RIQVETLEKNCKEFGIT-LFDLGdpRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVE-------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 152 afHF----------PKTIKIVLKGTLQPGVYAKDLILFIIKELTVNGATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGG 221
Cdd:PRK05478 151 --HVlatqtllqkkPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 222 TCGICYPDMTTVNYLwdfiKD-EFSTK----EEALQEYSKWTSDADAAYEKVYEYDVTDLGPMATFGNKPDQVKTVAE-- 294
Cdd:PRK05478 229 RAGLVAPDETTFEYL----KGrPFAPKgedwDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGkv 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 295 -----------------------------MSGTAIDQVYIGSCTNGRIEDLRIAASILKDKKISDDVRAIVSPATPAIFN 345
Cdd:PRK05478 305 pdpedfadpvkrasaeralaymglkpgtpITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKA 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503951987 346 MALKEGLIEIFQNAGFCVTNPTCGACLGMSNGVLASGEVCASTTNRNFNGRMGKGGTVHLMSPATAAASAIEGKIT 421
Cdd:PRK05478 385 QAEAEGLDKIFIEAGFEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFV 460
|
|
| LEU2 |
TIGR02083 |
3-isopropylmalate dehydratase, large subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
4-424 |
2.91e-150 |
|
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: 432.70 E-value: 2.91e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 4 TIAEKIFDAH--RVDMPFPDTHVLKLDRVFCHEITTPIAITDLMARGMDRVYDPTKIKAVIDHVTPAKDSKTAEQGKILR 81
Cdd:TIGR02083 2 TMAEKILAQHagLESVEPGELILAKLDIVLGNDITTPLAIKAFKEYGGKKVFDPDRVALVPDHFTPNKDIKSAEQCKMMR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 82 DWAKRHGIKDFFDIGRNGVCHAIFPEKGFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCAFHFPKTIKI 161
Cdd:TIGR02083 82 EFAREQGIEKFFEIGNMGIEHALLPEEGIVKPGDLIIGADSHTCTYGALGAFATGVGSTDMAVGMATGKAWFRVPEAIKF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 162 VLKGTLQPGVYAKDLILFIIKELTVNGATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGICYPDMTTVNYLwdfik 241
Cdd:TIGR02083 162 VLKGKLKPWVTGKDLILHIIGIIGVDGALYKSMEFSGEGLKELSMDDRFTIANMAIEAGAKTGIFPVDEITIEYE----- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 242 defstKEEALQEYSKWTSDADAAYEKVYEYDVTDLGPMATFGNKPDQVKTV--AEMSGTAIDQVYIGSCTNGRIEDLRIA 319
Cdd:TIGR02083 237 -----KGRGKREEKIYKADEDAKYVRVIEIDLSELEPQVAFPHLPENTKDIseAGKEEIKIDQVVIGSCTNGRLEDLRLA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 320 ASILKDKKISDDVRAIVSPATPAIFNMALKEGLIEIFQNAGFCVTNPTCGACLGMSNGVLASGEVCASTTNRNFNGRMGK 399
Cdd:TIGR02083 312 AEILKGKTVAPDVRCIIIPGSQNVYLEAMKEGLLEIFIEAGAVVSTPTCGPCLGGHMGILAEGERAISTTNRNFVGRMGH 391
|
410 420
....*....|....*....|....*.
gi 503951987 400 GGT-VHLMSPATAAASAIEGKITNSQ 424
Cdd:TIGR02083 392 PKSeVYLASPAVAAASAIKGYIASPE 417
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
1-421 |
1.23e-145 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 422.78 E-value: 1.23e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 1 MGKTIAEKIFDAHRVdMPFPDTHVL-KLDRVFCHEITTPIAITDLMARGMdRVYDPTKIKAVIDHVTP--------AKDS 71
Cdd:PRK12466 2 MPRTLYDKLWDSHTV-ARLDDGHVLlYIDRHLLNEYTSPQAFSGLRARGR-TVRRPDLTLAVVDHVVPtrpgrdrgITDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 72 KTAEQGKILRDWAKRHGIKdFFDIG--RNGVCHAIFPEKGFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKG 149
Cdd:PRK12466 80 GGALQVDYLRENCADFGIR-LFDVDdpRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 150 VCAFHFPKTIKIVLKGTLQPGVYAKDLILFIIKELTVNGATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGICYPD 229
Cdd:PRK12466 159 TLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 230 MTTVNYLWDFIKD-EFSTKEEALQEYSKWTSDADAAYEKVYEYDVTDLGPMATFGNKPDQVKTVAE-------------- 294
Cdd:PRK12466 239 ETTFDYLRGRPRApKGALWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGrvpdpaaeadparr 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 295 -----------------MSGTAIDQVYIGSCTNGRIEDLRIAASILKDKKISDDVRAIVSPATPAIFNMALKEGLIEIFQ 357
Cdd:PRK12466 319 aameraldymgltpgtpLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFI 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503951987 358 NAGFCVTNPTCGACLGMSNGVLASGEVCASTTNRNFNGRMGKGGTVHLMSPATAAASAIEGKIT 421
Cdd:PRK12466 399 AAGFEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHIT 462
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-418 |
4.85e-140 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 408.35 E-value: 4.85e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 7 EKIFDAHRVD-----MPFpdthvlKLDRVFCHEITTPIAITDLMARGmDRVYDPTKIKAVIDHVTPAKD----------- 70
Cdd:pfam00330 1 EKIWDAHLVEeldgsLLY------IPDRVLMHDVTSPQAFVDLRAAG-RAVRRPGGTPATIDHLVPTDLvidhapdaldk 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 71 ------SKTAEQGKILRDWAKRHGIKdFFDIGrNGVCHAIFPEKGFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEV 144
Cdd:pfam00330 74 niedeiSRNKEQYDFLEWNAKKFGIR-FVPPG-QGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 145 GILKGVCAFHFPKTIKIVLKGTLQPGVYAKDLILFIIKELTVNGATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCG 224
Cdd:pfam00330 152 VLATQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 225 ICYPDMTTVNYLwDFIKDEFSTKEEALQEYSKW---TSDADAAYEKVYEYDVTDLGPMATFGNKPDQVKTVAE------- 294
Cdd:pfam00330 232 LFPPDETTFEYL-RATGRPEAPKGEAYDKAVAWktlASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSElvpdpfa 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 295 ----------------------MSGTAIDQVYIGSCTNGRIEDLRIAASILKD-----KKISDDVRAIVSPATPAIFNMA 347
Cdd:pfam00330 311 davkrkaaeraleymglgpgtpLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKKavekgLKVAPGVKASVVPGSEVVRAYA 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503951987 348 LKEGLIEIFQNAGFCVTNPTCGACLGMSnGVLASGEVCASTTNRNFNGRMGKGGTVHLMSPATAAASAIEG 418
Cdd:pfam00330 391 EAEGLDKILEEAGFEWRGPGCSMCIGNS-DRLPPGERCVSSSNRNFEGRQGPGGRTHLASPALVAAAAIAG 460
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
21-422 |
1.94e-139 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 405.29 E-value: 1.94e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 21 DTHVLKLDRVFCHEITTPIAITDLMARGmDRVYDPTKIKAVIDHVTPAKDSKTAEQGKILRDWAKRHGIKDFFDIGRnGV 100
Cdd:NF040615 20 DTVEVDVDLAMTHDGTTPLTYKAFKEIS-DKVWDNEKIVIVFDHNVPANTVKAANMQKITREFVKEQGIKNFYLGGE-GI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 101 CHAIFPEKGFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCAFHFPKTIKIVLKGtLQPGVYAKDLILFI 180
Cdd:NF040615 98 CHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVNIVG-KNENISGKDIILKV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 181 IKELTVNGATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGICYPDMTTVNYLwdfiKDEFSTKEE--ALQEYSKWT 258
Cdd:NF040615 177 CKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYL----RKEGVSEEEiaELKKNRITV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 259 SDADAAYEKVYEYDVTDLGPMATFGNKPDQVKTVAEMSGTAIDQVYIGSCTNGRIEDLRIAASILKDKKISDDVRAIVSP 338
Cdd:NF040615 253 NEKEENYYKEIEIDITDMEEQVACPHHPDNVKPVSEVEGTEIDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 339 ATPAIFNMALKEGLIEIFQNAGFCVTNPTCGACLGMSNGVLASGEVCASTTNRNFNGRMG-KGGTVHLMSPATAAASAIE 417
Cdd:NF040615 333 ASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGnINSYIYLSSPKIAAKSAVK 412
|
....*
gi 503951987 418 GKITN 422
Cdd:NF040615 413 GYITN 417
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
1-419 |
3.64e-123 |
|
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: 365.33 E-value: 3.64e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 1 MGKTIAEKIFDAHRVDMPFPDTHVLKLDRVFCHEITTPIAITDLMARGMdRVYDPTKIKAVIDHVTP-------AKDSKT 73
Cdd:TIGR00170 1 MPRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGR-KVRRPQKTFATMDHNIPtqnrdfnIKDEVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 74 AEQGKILRDWAKRHGIKdFFDIG--RNGVCHAIFPEKGFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVC 151
Cdd:TIGR00170 80 KIQVTELEKNCKEFGVR-LFDLHsvDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 152 AFHFPKTIKIVLKGTLQPGVYAKDLILFIIKELTVNGATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGICYPDMT 231
Cdd:TIGR00170 159 KQARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDET 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 232 TVNYLwdfiKDEFSTK-----EEALQEYSKWTSDADAAYEKVYEYDVTDLGPMATFGNKPDQVKTVAE------------ 294
Cdd:TIGR00170 239 TFEYC----KGRPHAPkgkefDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSevpdpesfadpv 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 295 -------------------MSGTAIDQVYIGSCTNGRIEDLRIAASILKDKKISDDVRAIVSPATPAIFNMALKEGLIEI 355
Cdd:TIGR00170 315 dkasaeralaymglepgtpLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKI 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503951987 356 FQNAGFCVTNPTCGACLGMSNGVLASGEVCASTTNRNFNGRMGKGGTVHLMSPATAAASAIEGK 419
Cdd:TIGR00170 395 FIEAGFEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGH 458
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
1-422 |
4.93e-95 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 298.60 E-value: 4.93e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 1 MGKTIAEKIFDAHRVDMPF-PDTHV-LKLDRVFCHEITTPIAITDLMARGMDRVYDPTKIkAVIDHVTPAKDSKTAEQGK 78
Cdd:PRK07229 1 MGLTLTEKILYAHLVEGELePGEEIaIRIDQTLTQDATGTMAYLQFEAMGLDRVKTELSV-QYVDHNLLQADFENADDHR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 79 ILRDWAKRHGIkDFFDIGrNGVCHAIFPEKgFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGvcAFH--FP 156
Cdd:PRK07229 80 FLQSVAAKYGI-YFSKPG-NGICHQVHLER-FAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGG--PYYlkMP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 157 KTIKIVLKGTLQPGVYAKDLILFIIKELTVNGATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGIcypdmttvnyl 236
Cdd:PRK07229 155 KVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSI----------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 237 wdFIKDEfSTKE--EAL---QEYSKWTSDADAAYEKVYEYDVTDLGPMATFGNKPDQVKTVAEMSGTAIDQVYIGSCTNG 311
Cdd:PRK07229 224 --FPSDE-RTREflKAQgreDDWVELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVAGIKVDQVLIGSCTNS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 312 RIEDLRIAASILKDKKISDDVRAIVSPATPAIFNMALKEGLIEIFQNAGFCVTNPTCGACLGMSnGVLASGEVCASTTNR 391
Cdd:PRK07229 301 SYEDLMRAASILKGKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMG-QAPATGNVSLRTFNR 379
|
410 420 430
....*....|....*....|....*....|..
gi 503951987 392 NFNGRMG-KGGTVHLMSPATAAASAIEGKITN 422
Cdd:PRK07229 380 NFPGRSGtKDAQVYLASPETAAASALTGVITD 411
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
29-420 |
2.11e-91 |
|
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: 281.31 E-value: 2.11e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 29 RVFCHEITTPIAITDLMA-RGMDRVYDPTKIKAVIDHVTPAKDSKTAEQGKILRDWAKRHGIkDFFDIGrNGVCHAIFPE 107
Cdd:cd01351 1 RVMLQDATGPMAMKAFEIlAALGKVADPSQIACVHDHAVQLEKPVNNEGHKFLSFFAALQGI-AFYRPG-VGIIHQIMVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 108 KgFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCAFHFPKTIKIVLKGTLQPGVYAKDLILFIIKELTVN 187
Cdd:cd01351 79 N-LALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 188 GATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGICYPDMTTVNYLWDFIKdeFSTKEEALQEYSKWTSDADAAYEK 267
Cdd:cd01351 158 GVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGR--PLLKNLWLAFPEELLADEGAEYDQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 268 VYEYDVTDLGPMATFGNKPDQVKTVAEMSGTAIDQVYIGSCTNGRIEDLRIAASILKDKKISDDVRAIVSPATPAIFNMA 347
Cdd:cd01351 236 VIEIDLSELEPDISGPNRPDDAVSVSEVEGTKIDQVLIGSCTNNRYSDMLAAAKLLKGAKVAPGVRLIVTPGSRMVYATL 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503951987 348 LKEGLIEIFQNAGFCVTNPTCGACLGMSNGVLASGEVCASTTNRNFNGRMGKG-GTVHLMSPATAAASAIEGKI 420
Cdd:cd01351 316 SREGYYEILVDSGARILPPGCGPCMGNGARLVADGEVGVSSGNRNFPGRLGTYeRHVYLASPELAAATAIAGKI 389
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
28-420 |
7.50e-85 |
|
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: 264.31 E-value: 7.50e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 28 DRVFCHEITTPIAITDLMARGMDRVYDPTKIkAVIDHVTPAKDSKTAEQGKILRDWAKRHGIkdFFDIGRNGVCHAIFPE 107
Cdd:cd01585 1 DQTLTQDATGTMAYLQFEAMGVDRVRTELSV-SYVDHNTLQTDFENADDHRFLQTVAARYGI--YFSRPGNGICHQVHLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 108 KgFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCAFHFPKTIKIVLKGTLQPGVYAKDLILFIIKELTVN 187
Cdd:cd01585 78 R-FAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 188 GATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGICYPDMTTVNYLwdfikdEFSTKEEALQEYSkwtSDADAAYEK 267
Cdd:cd01585 157 GGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFL------AAQGREDDWVELA---ADADAEYDE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 268 VYEYDVTDLGPMATFGNKPDQVKTVAEMSGTAIDQVYIGSCTNGRIEDLRIAASILKDKKISDDVRAIVSPATPAIFNMA 347
Cdd:cd01585 228 EIEIDLSELEPLIARPHSPDNVVPVREVAGIKVDQVAIGSCTNSSYEDLMTVAAILKGRRVHPHVSMVVAPGSKQVLEML 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503951987 348 LKEGLIEIFQNAGFCVTNPTCGACLGMSnGVLASGEVCASTTNRNFNGRMG-KGGTVHLMSPATAAASAIEGKI 420
Cdd:cd01585 308 ARNGALADLLAAGARILESACGPCIGMG-QAPPTGGVSVRTFNRNFEGRSGtKDDLVYLASPEVAAAAALTGVI 380
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
29-420 |
5.69e-55 |
|
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: 186.28 E-value: 5.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 29 RVFCHEITTPIAITdLMARGMDRVYDPTKIKAVIDHVTPAKDSKTAEQGKILRDWAKRHGIkDFFDIGRnGVCHAIFPEK 108
Cdd:cd01582 1 HCMTHDNSWPVALK-FMSIGATKIHNPDQIVMTLDHDVQNKSEKNLKKYKNIESFAKKHGI-DFYPAGR-GIGHQIMIEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 109 GFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCAFHFPKTIKIVLKGTLQPGVYAKDLILFIIKELTVNG 188
Cdd:cd01582 78 GYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 189 ATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGIcypdmttvnylwdfikdeFSTKEEALqeyskwtsdadaayekv 268
Cdd:cd01582 158 VLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGL------------------FPTDAKHL----------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 269 yeydVTDLGPMATFGNKPDQVK---TVAEMSGT--AIDQVYIGSCTNGRIEDLRIAASILKDKK-------ISDDVRAIV 336
Cdd:cd01582 203 ----ILDLSTLSPYVSGPNSVKvstPLKELEAQniKINKAYLVSCTNSRASDIAAAADVVKGKKekngkipVAPGVEFYV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 337 SPATPAIFNMALKEGLIEIFQNAGfCVTNPT-CGACLGMSNGVLASGEVCASTTNRNFNGRMG-KGGTVHLMSPATAAAS 414
Cdd:cd01582 279 AAASSEVQAAAEKNGDWQTLLEAG-ATPLPAgCGPCIGLGQGLLEPGEVGISATNRNFKGRMGsTEALAYLASPAVVAAS 357
|
....*.
gi 503951987 415 AIEGKI 420
Cdd:cd01582 358 AISGKI 363
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
29-420 |
4.39e-37 |
|
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: 139.88 E-value: 4.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 29 RVFCHEITTPIAITDLMARGMDRVYDPTKIKAviDHVTPA-----KDSKTA-----EQGKILRDWAKRHGIkDFFDIGrN 98
Cdd:cd01584 1 RVAMQDATAQMALLQFMSSGLPKVAVPSTIHC--DHLIEAqvggeKDLKRAkdinkEVYDFLASAGAKYGI-GFWKPG-S 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 99 GVCHAIFPEKgFVRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDlEVGILKGV-CAFHFPKTIKIVLKGTLQPGVYAKDLI 177
Cdd:cd01584 77 GIIHQIVLEN-YAFPGLLMIGTDSHTPNAGGLGGIAIGVGGAD-AVDVMAGIpWELKCPKVIGVKLTGKLSGWTSPKDVI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 178 LFIIKELTVNGATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGICYPDMTTVNYLWDFIKDEFSTKEEALQEySKW 257
Cdd:cd01584 155 LKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEIADLADEFKD-DLL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 258 TSDADAAYEKVYEYDVTDLGPMATFGNKPDQVKTVAEMSGTAIDQVY--------IGSCTNGRIEDLRIAASILK---DK 326
Cdd:cd01584 234 VADEGAEYDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAEKNGWpldlrvglIGSCTNSSYEDMGRAASIAKqalAH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 327 KISDDVRAIVSPATPAIFNMALKEGLIEIFQNAGFCVTNPTCGACLGMSNGV-LASGEVCASTT--NRNFNGRMGKGGTV 403
Cdd:cd01584 314 GLKCKSIFTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQWDRKdIKKGEKNTIVTsyNRNFTGRNDANPAT 393
|
410
....*....|....*....
gi 503951987 404 H--LMSPATAAASAIEGKI 420
Cdd:cd01584 394 HafVASPEIVTAMAIAGTL 412
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
116-427 |
2.40e-34 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 135.69 E-value: 2.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 116 TVIMG-DSHTCTH-G-AFG------AFAAGVGTTDLEVgilkgvcafhfPKTIKIVLKGTLQPGVYAKDLI----LFIIK 182
Cdd:PRK09238 480 TVGTGgDSHTRFPiGiSFPagsglvAFAAATGVMPLDM-----------PESVLVRFKGEMQPGITLRDLVhaipYYAIK 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 183 E--LTVN--GATNM----VIEFTGpvVDAMSMESRMTLCNMAIE---AGGTCGIcyPDMTTVNYLWDFIK---------- 241
Cdd:PRK09238 549 QglLTVEkkGKKNIfsgrILEIEG--LPDLKVEQAFELTDASAErsaAGCTIKL--SKEPIIEYLRSNIVllkwmiaegy 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 242 DEFSTKEEALQEYSKW-------TSDADAAYEKVYEYDVTDLG-PMATFGNKPDQVKTVAEMSGTAIDQVYIGSC-TNgr 312
Cdd:PRK09238 625 GDARTLERRIAAMEEWlanpellEADADAEYAAVIEIDLAEIKePILACPNDPDDVRLLSEVAGTKIDEVFIGSCmTN-- 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 313 IEDLRIAASILKDKKISDDVRAIVSPATPAIFNMALKEGLIEIFQNAGFCVTNPTCGACLGMSNGVlASGEVCASTTNRN 392
Cdd:PRK09238 703 IGHFRAAGKLLEGKKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMGNQARV-ADGATVFSTSTRN 781
|
330 340 350
....*....|....*....|....*....|....*
gi 503951987 393 FNGRMGKGGTVHLMSPATAAASAIEGKITNSQLYK 427
Cdd:PRK09238 782 FPNRLGKGANVYLGSAELAAVCALLGRIPTVEEYQ 816
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
120-420 |
3.19e-33 |
|
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: 129.54 E-value: 3.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 120 GDSHTctHGAFG-AFAAGVGTTDLEVGIlkGVCAFHFPKTIKIVLKGTLQPGVYAKDLI----LFIIKE--LTVNGATNM 192
Cdd:cd01581 113 GDSHT--RFPIGiSFPAGSGLVAFAAAT--GVMPLDMPESVLVRFKGKMQPGITLRDLVnaipYYAIQQglLTVEKKGKK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 193 VIeFTGPVVDA-----MSMESRMTLCNMAIEAGGTCGICYPDMTTV-NYLWDFIK----------DEFSTKEEALQEYSK 256
Cdd:cd01581 189 NV-FNGRILEIeglpdLKVEQAFELTDASAERSAAACTVRLDKEPViEYLESNVVlmkimiangyDDARTLLRRIIAMEE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 257 W-------TSDADAAYEKVYEYDVTDLG-PMATFGNKPDQVKTVAEMSGTAIDQVYIGSC-TNgrIEDLRIAASILKDKK 327
Cdd:cd01581 268 WlanppllEPDADAEYAAVIEIDLDDIKePILACPNDPDDVKLLSEVAGKKIDEVFIGSCmTN--IGHFRAAAKILRGKE 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 328 ISDdVRAIVSPATPAIFNMALKEGLIEIFQNAGFCVTNPTCGACLGMSNGVlASGEVCASTTNRNFNGRMGKGGTVHLMS 407
Cdd:cd01581 346 FKP-TRLWVAPPTRMDWAILQEEGYYSIFGDAGARTEMPGCSLCMGNQARV-ADGATVFSTSTRNFDNRVGKGAEVYLGS 423
|
330
....*....|...
gi 503951987 408 PATAAASAIEGKI 420
Cdd:cd01581 424 AELAAVCALLGRI 436
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
120-426 |
7.04e-28 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 116.56 E-value: 7.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 120 GDSHTctHGAFG-AFAAGVGTtdLEVGILKGVCAFHFPKTIKIVLKGTLQPGVYAKDLI----LFIIKE--LTV--NGAT 190
Cdd:PLN00094 559 GDSHT--RFPIGiSFPAGSGL--VAFGAATGVIPLDMPESVLVRFTGTMQPGITLRDLVhaipYTAIQDglLTVekKGKK 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 191 NMvieFTGPVVDAMSMESRMtlCNMAIE---------AGGtCGICYPDMTTVNYL--------WdFIKDEFS---TKEEA 250
Cdd:PLN00094 635 NV---FSGRILEIEGLPHLK--CEQAFElsdasaersAAG-CTIKLDKEPIIEYLnsnvvmlkW-MIAEGYGdrrTLERR 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 251 LQEYSKW-------TSDADAAYEKVYEYDVTDLG-PMATFGNKPDQVKTVAEMSGTAIDQVYIGSC-TNgrIEDLRIAAS 321
Cdd:PLN00094 708 IARMQQWladpellEADPDAEYAAVIEIDMDEIKePILCAPNDPDDARLLSEVTGDKIDEVFIGSCmTN--IGHFRAAGK 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 322 ILKDKKISDDVRAIVSPATPAIFNMALKEGLIEIFQNAGFCVTNPTCGACLGMSNGVlASGEVCASTTNRNFNGRMGKGG 401
Cdd:PLN00094 786 LLNDNLSQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPGCSLCMGNQARV-AEKSTVVSTSTRNFPNRLGKGA 864
|
330 340
....*....|....*....|....*
gi 503951987 402 TVHLMSPATAAASAIEGKITNSQLY 426
Cdd:PLN00094 865 NVYLASAELAAVAAILGRLPTVEEY 889
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
28-421 |
3.06e-25 |
|
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle
Pssm-ID: 440669 [Multi-domain] Cd Length: 891 Bit Score: 108.65 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 28 DRVFCHEIT-TPiAITDLMA--RGMDRV-YDPTKIKA------VIDHVTPAKDSKTAEQGKI---------------LRd 82
Cdd:COG1048 82 ARVLMQDFTgVP-AVVDLAAmrDAVARLgGDPKKINPlvpvdlVIDHSVQVDYFGTPDALEKnlelefernreryqfLK- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 83 WAKrhgiKDFFDIG----RNGVCHAIFPEK-GFV-----RPGYTVIMG------DSHTCTHGAFGAFAAGVGTTDLEVGI 146
Cdd:COG1048 160 WGQ----QAFDNFRvvppGTGIVHQVNLEYlAFVvwtreEDGETVAYPdtlvgtDSHTTMINGLGVLGWGVGGIEAEAAM 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 147 LKGVCAFHFPKTIKIVLKGTLQPGVYAKDLILFIIKELTVNGATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGIC 226
Cdd:COG1048 236 LGQPVSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFF 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 227 YPDMTTVNYLwdfikdEFSTKEEAL----QEYSK----W--TSDADAAYEKVYEYDVTDL-----GP------------- 278
Cdd:COG1048 316 PVDEETLDYL------RLTGRSEEQielvEAYAKaqglWrdPDAPEPYYSDVLELDLSTVepslaGPkrpqdriplsdlk 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 279 -------MATFGNKPDQVKTVA-EMSGTAIDQVY-----IGSCTNGRIEDLRIAASIL------KDKKISDDVRAIVSPA 339
Cdd:COG1048 390 eafraalAAPVGEELDKPVRVEvDGEEFELGHGAvviaaITSCTNTSNPSVMIAAGLLakkaveKGLKVKPWVKTSLAPG 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 340 TPAIFNMALKEGLIEIFQNAGFCVTNPTCGACLGMS--------NGVLASGEVCASTT--NRNFNGRmgkggtVH----- 404
Cdd:COG1048 470 SKVVTDYLERAGLLPYLEALGFNVVGYGCTTCIGNSgplppeisEAIEENDLVVAAVLsgNRNFEGR------IHpdvka 543
|
490
....*....|....*....
gi 503951987 405 --LMSPATAAASAIEGKIT 421
Cdd:COG1048 544 nfLASPPLVVAYALAGTVD 562
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
29-421 |
1.15e-23 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 103.86 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 29 RVFCHEITTPIAITDLMA-RG-MDRV-YDPTKIKA------VIDH-----VTPAKDS----------KTAEQGKILRdWA 84
Cdd:PRK12881 85 RVVMQDFTGVPALVDLAAmRDaAAEAgGDPAKINPlvpvdlVVDHsvavdYFGQKDAldlnmkiefqRNAERYQFLK-WG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 85 KRHgikdfFDIGR-----NGVCHAIFPEK-------------GFVRPGyTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGI 146
Cdd:PRK12881 164 MQA-----FDNFRvvppgTGIMHQVNLEYlarvvhtkeddgdTVAYPD-TLVGTDSHTTMINGIGVLGWGVGGIEAEAVM 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 147 LKGVCAFHFPKTIKIVLKGTLQPGVYAKDLILFIIKELTVNGATNMVIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGIC 226
Cdd:PRK12881 238 LGQPVYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFF 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 227 YPDMTTVNYLwdfikdEFSTKEEA----LQEYSK----W-TSDADAAYEKVYEYDVTDLGP-MA---------------- 280
Cdd:PRK12881 318 PVDEQTLDYL------RLTGRTEAqialVEAYAKaqglWgDPKAEPRYTRTLELDLSTVAPsLAgpkrpqdrialgnvks 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 281 TFG------------NKPDQVKTVAEMSGTAIDQVYIGSCTNGRIEDLRIAASILKDK------KISDDVRAIVSPATPA 342
Cdd:PRK12881 392 AFSdlfskpvaengfAKKAQTSNGVDLPDGAVAIAAITSCTNTSNPSVLIAAGLLAKKaverglTVKPWVKTSLAPGSKV 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 343 IFNMALKEGLIEIFQNAGFCVTNPTCGACLGMS--------NGVLASGEVCAS--TTNRNFNGRmgkggtVH-------L 405
Cdd:PRK12881 472 VTEYLERAGLLPYLEKLGFGIVGYGCTTCIGNSgpltpeieQAITKNDLVAAAvlSGNRNFEGR------IHpnikanfL 545
|
490
....*....|....*.
gi 503951987 406 MSPATAAASAIEGKIT 421
Cdd:PRK12881 546 ASPPLVVAYALAGTVR 561
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
7-421 |
1.71e-23 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 103.55 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 7 EKIFD-----AHRVDMPFpdthvlKLDRVFCHEITTPIAITDL--MARGMDRV-YDPTKIKA------VIDHVTPAKDSK 72
Cdd:PTZ00092 71 ENILNweensKKQIEIPF------KPARVLLQDFTGVPAVVDLaaMRDAMKRLgGDPAKINPlvpvdlVIDHSVQVDFSR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 73 T---------------AEQGKILRdWakrhGIKDF--FDIGRNG-----------VCHAIFPEKGFVRPGyTVIMGDSHT 124
Cdd:PTZ00092 145 SpdalelnqeiefernLERFEFLK-W----GSKAFknLLIVPPGsgivhqvnleyLARVVFNKDGLLYPD-SVVGTDSHT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 125 CTHGAFGAFAAGVGTTDLEVGILKGVCAFHFPKTIKIVLKGTLQPGVYAKDLILFIIKELTVNGATNMVIEFTGPVVDAM 204
Cdd:PTZ00092 219 TMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 205 SMESRMTLCNMAIEAGGTCGICYPDMTTVNYLWDFIKDEfsTKEEALQEYSK-----WTSDADAAYEKVYEYDVTDLGPM 279
Cdd:PTZ00092 299 SLADRATIANMAPEYGATMGFFPIDEKTLDYLKQTGRSE--EKVELIEKYLKanglfRTYAEQIEYSDVLELDLSTVVPS 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 280 A------------------------------TFGNKPDQVKTVAEMsgTAIDQVY-----------IGSCTNGRIEDLRI 318
Cdd:PTZ00092 377 VagpkrphdrvplsdlkkdftaclsapvgfkGFGIPEEKHEKKVKF--TYKGKEYtlthgsvviaaITSCTNTSNPSVML 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 319 AASILKDK------KISDDVRAIVSPATPAIFNMALKEGLIEIFQNAGFCVTNPTCGACLG--------MSNGVLASGEV 384
Cdd:PTZ00092 455 AAGLLAKKavekglKVPPYIKTSLSPGSKVVTKYLEASGLLKYLEKLGFYTAGYGCMTCIGnsgdldpeVSEAITNNDLV 534
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 503951987 385 CAS--TTNRNFNGRmgkggtVH-------LMSPATAAASAIEGKIT 421
Cdd:PTZ00092 535 AAAvlSGNRNFEGR------VHpltranyLASPPLVVAYALAGRVN 574
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
118-418 |
5.33e-22 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 98.54 E-value: 5.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 118 IMG-DSHTcTHGAFGAFAAGVGTTDLEVGILKGVCAFHFPKTIKIVLKGTLQPGVYAKDLILFIIKELTVNGAT-NMVIE 195
Cdd:PRK11413 145 ILGsDSHT-RYGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVME 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 196 FTGPVVDAMSMESRMTLCNMAIEAggTC--GICYPDMTTVNYLwdfikdEFSTKEEAlqeYSKWTSDADAAYEKVYEYDV 273
Cdd:PRK11413 224 FVGPGVSALSTDFRNGVDVMTTET--TClsSIWQTDEEVHNWL------ALHGRGQD---YCELNPQPMAYYDGCISVDL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 274 TDLGPMATFGNKPDQVKTVAEM-------------------SGTA--------------IDQVYIGSCTNGRIEDLRIAA 320
Cdd:PRK11413 293 SAIKPMIALPFHPSNVYEIDELnqnltdilreveieservaHGKAklslldkiengrlkVQQGIIAGCSGGNYENVIAAA 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 321 SILKDKKISDDVRAI-VSPATPAIFnMAL-KEGLIEIFQNAGFCVTNPTCGACLGMSNgVLASGEVCASTTNRNFNGRMG 398
Cdd:PRK11413 373 NALRGQSCGNDTFSLsVYPSSQPVF-MDLaKKGVVADLMGAGAIIRTAFCGPCFGAGD-TPANNGLSIRHTTRNFPNREG 450
|
330 340
....*....|....*....|....*.
gi 503951987 399 -KGG-----TVHLMSPATAAASAIEG 418
Cdd:PRK11413 451 sKPAngqmsAVALMDARSIAATAANG 476
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
116-420 |
1.37e-20 |
|
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: 93.14 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 116 TVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCAFHFPKTIKIVLKGTLQPGVYAKDLILFIIKELTVNGATNMVIE 195
Cdd:cd01586 123 SVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 196 FTGPVVDAMSMESRMTLCNMAIEAGGTCGICYPDMTTVnylwdfikdefstkeealqeyskwtsdadaayekvyEYDVTD 275
Cdd:cd01586 203 FFGPGVAKLSVADRATIANMAPEYGATCGFFPVDTQVV------------------------------------ELDLST 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 276 LGPMATFGNKPDQvkTVAEMSGTAIdqVYIGSCTNGRIEDLRIAASILKDK------KISDDVRAIVSPATPAIFNMALK 349
Cdd:cd01586 247 VEPSVSGPKRPQD--RVPLHGSVVI--AAITSCTNTSNPSVMLAAGLLAKKavelglKVKPYVKTSLAPGSRVVTKYLEA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 350 EGLIEIFQNAGFCVTNPTCGACLGMS--------NGVLASGEVCAS--TTNRNFNGRmgkggtVH-------LMSPATAA 412
Cdd:cd01586 323 SGLLPYLEKLGFHVVGYGCTTCIGNSgplpeeveEAIKENDLVVAAvlSGNRNFEGR------IHplvranyLASPPLVV 396
|
....*...
gi 503951987 413 ASAIEGKI 420
Cdd:cd01586 397 AYALAGTV 404
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
7-420 |
2.46e-15 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 78.31 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 7 EKIFD-----AHRVDMPFpdthvlKLDRVFCHEITTPIAITDL--MARGMDRV-YDPTKIKA------VIDH---VTPAK 69
Cdd:PLN00070 103 EKIIDwentsPKQVEIPF------KPARVLLQDFTGVPAVVDLacMRDAMNNLgGDPNKINPlvpvdlVIDHsvqVDVAR 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 70 dSKTAEQGKILRDWAKRHGIKDFFDIGRN------------GVCH---------AIFPEKGFVRPGyTVIMGDSHTCTHG 128
Cdd:PLN00070 177 -SENAVQANMELEFQRNKERFAFLKWGSTafqnmlvvppgsGIVHqvnleylgrVVFNTDGILYPD-SVVGTDSHTTMID 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 129 AFGAFAAGVGTTDLEVGILKGVCAFHFPKTIKIVLKGTLQPGVYAKDLILFIIKELTVNGATNMVIEFTGPVVDAMSMES 208
Cdd:PLN00070 255 GLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLAD 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 209 RMTLCNMAIEAGGTCGICYPDMTTVNYLWDFIKDEFSTKE-EALQEYSKWTSD-----ADAAYEKVYEYDVTDLGPMATF 282
Cdd:PLN00070 335 RATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETVAMiEAYLRANKMFVDynepqQERVYSSYLELDLEDVEPCISG 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 283 GNKPDQVKTVAEM--------------SGTAI-----DQVY--------------------IGSCTNGRIEDLRIAASIL 323
Cdd:PLN00070 415 PKRPHDRVPLKEMkadwhscldnkvgfKGFAVpkeaqSKVAkfsfhgqpaelrhgsvviaaITSCTNTSNPSVMLGAGLV 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 324 KDK------KISDDVRAIVSPATPAIFNMALKEGLIEIFQNAGFCVTNPTCGACLGMSNGV-------LASGEVCASTT- 389
Cdd:PLN00070 495 AKKacelglEVKPWIKTSLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIGNSGELdesvasaITENDIVAAAVl 574
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 503951987 390 --NRNFNGRmgkggtVH-------LMSPATAAASAIEGKI 420
Cdd:PLN00070 575 sgNRNFEGR------VHpltranyLASPPLVVAYALAGTV 608
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
3-421 |
4.57e-15 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 77.47 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 3 KTIAEKIFDAHR-VDMPFpdthvlKLDRVFCHEITTPIAITDL--MARGMDRV-YDPTKIKA------VIDH---V---- 65
Cdd:PRK09277 65 EALAEWLPKAKPdREIPF------RPARVVMQDFTGVPAVVDLaaMRDAIADLgGDPAKINPlvpvdlVIDHsvqVdyfg 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 66 TP---AK-----DSKTAEQGKILRdWAKrhgiKDF--FDI---GrNGVCHAI-------------------FPEkgfvrp 113
Cdd:PRK09277 139 TPdafEKnveleFERNEERYQFLK-WGQ----KAFdnFRVvppG-TGICHQVnleylapvvwtredgelvaYPD------ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 114 gyTVIMGDSHTcTH-GAFGAFAAGVGTTDLEVGILKGVCAFHFPKTIKIVLKGTLQPGVYAKDLILFIIKELTVNGATNM 192
Cdd:PRK09277 207 --TLVGTDSHT-TMiNGLGVLGWGVGGIEAEAAMLGQPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGK 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 193 VIEFTGPVVDAMSMESRMTLCNMAIEAGGTCGICYPDMTTVNYLwdfikdEFSTKEEAL----QEYSK----W-TSDADA 263
Cdd:PRK09277 284 FVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYL------RLTGRDEEQvalvEAYAKaqglWrDPLEEP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 264 AYEKVYEYDVTDLGP-MA----------------TFGNKPDQVKTVAEMSGTAIDQVY-----------IGSCTNGRIED 315
Cdd:PRK09277 358 VYTDVLELDLSTVEPsLAgpkrpqdriplsdvkeAFAKSAELGVQGFGLDEAEEGEDYelpdgavviaaITSCTNTSNPS 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503951987 316 LRIAASILKDK------KISDDVRAIVSPATPAIfNMALKE-GLIEIFQNAGFCVTNPTCGACLGMS------------- 375
Cdd:PRK09277 438 VMIAAGLLAKKavekglKVKPWVKTSLAPGSKVV-TDYLEKaGLLPYLEALGFNLVGYGCTTCIGNSgplppeiekaind 516
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 503951987 376 NGVLA----SGevcasttNRNFNGRmgkggtVH-------LMSPATAAASAIEGKIT 421
Cdd:PRK09277 517 NDLVVtavlSG-------NRNFEGR------IHplvkanyLASPPLVVAYALAGTVD 560
|
|
| |
