|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
1-427 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 678.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 1 MGKTIAQKIFDAHLRDTPTP-ENMVLDLDVVLCHEITTPIAIMDLMEKGMDRVFDPNKIKAVIDHVTPAKDSKTAAQGKI 79
Cdd:PRK00402 1 MGMTLAEKILARHSGRDVSPgDIVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVIVFDHFVPAKDIKSAEQQKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 80 MREWAKRQNIKDFFDVGEnGVCHALFPEKGFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCTFRAPVSM 159
Cdd:PRK00402 81 LREFAKEQGIPNFFDVGE-GICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKTWFKVPETI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 160 KVSISGILQNGVSAKDVILAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDRVTAEYLWQF 239
Cdd:PRK00402 160 KVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLEYLKER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 240 IKDDYttidaavakfEKWHSDADAEYASVIELDVSELEPQVTYGYKPDHVKNIREMEGTPVDQIYIGSCTNGRIEDLRQA 319
Cdd:PRK00402 240 AGRDY----------KPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVEGTKVDQVFIGSCTNGRLEDLRIA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 320 AAILKGKRLASGVRGIVTPATPGIYSQALEEGIIKIFMDAGFCVLNPTCGACLGMSSGVLAEGEVCASTTNRNFNGRMGK 399
Cdd:PRK00402 310 AEILKGRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGS 389
|
410 420
....*....|....*....|....*....
gi 505217943 400 -GGMVHLMSPASAAAAAITGTISDPRQFL 427
Cdd:PRK00402 390 pESEVYLASPAVAAASAVTGKITDPREVL 418
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-426 |
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: 639.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 1 MGKTIAQKIFDAHLRDTPTP-ENMVLDLDVVLCHEITTPIAIMDLMEKGMDRVFDPNKIKAVIDHVTPAKDSKTAAQGKI 79
Cdd:COG0065 1 MGMTLAEKILARHAGREVEPgEIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVAVFDHNVPTKDPKSAEQVKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 80 MREWAKRQNIKdFFDVGENGVCHALFPEKGFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCTFRAPVSM 159
Cdd:COG0065 81 LREFAKEFGIT-FFDVGDPGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWFKVPETM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 160 KVSISGILQNGVSAKDVILAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDRVTAEYLWqf 239
Cdd:COG0065 160 RIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFEYLK-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 240 ikddyttiDAAVAKFEKWHSDADAEYASVIELDVSELEPQVTYGYKPDHVKNIREMEGTPVDQIYIGSCTNGRIEDLRQA 319
Cdd:COG0065 238 --------GRPFAPWRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELEGIKIDQVFIGSCTNGRIEDLRAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 320 AAILKGKRLASGVRGIVTPATPGIYSQALEEGIIKIFMDAGFCVLNPTCGACLGMSSGVLAEGEVCASTTNRNFNGRMG- 398
Cdd:COG0065 310 AEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGs 389
|
410 420
....*....|....*....|....*...
gi 505217943 399 KGGMVHLMSPASAAAAAITGTISDPRQF 426
Cdd:COG0065 390 PGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| 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: 551.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 29 VVLCHEITTPIAIMDLMEKGMDRVFDPNKIKAVIDHVTPAKDSKTAAQGKIMREWAKRQNIkDFFDVGENGVCHALFPEK 108
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAVFDHNVPTPDIKAAEQVKTLRKFAKEFGI-NFFDVGRQGICHVILPEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 109 GFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCTFRAPVSMKVSISGILQNGVSAKDVILAVIKKLTVNG 188
Cdd:cd01583 80 GLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 189 ATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDRVTAEYLWQfikddyttidAAVAKFEKWHSDADAEYASV 268
Cdd:cd01583 160 ATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKG----------RGKAYWKELKSDEDAEYDKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 269 IELDVSELEPQVTYGYKPDHVKNIREMEGTPVDQIYIGSCTNGRIEDLRQAAAILKGKRLASGVRGIVTPATPGIYSQAL 348
Cdd:cd01583 230 VEIDASELEPQVAWPHSPDNVVPVSEVEGIKIDQVFIGSCTNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAE 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505217943 349 EEGIIKIFMDAGFCVLNPTCGACLGMSSGVLAEGEVCASTTNRNFNGRMG-KGGMVHLMSPASAAAAAITGTI 420
Cdd:cd01583 310 KEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTSNRNFKGRMGsPGARIYLASPATAAASAITGEI 382
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
4-424 |
1.79e-173 |
|
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: 491.58 E-value: 1.79e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 4 TIAQKIFDAHLRDTPTP-ENMVLDLDVVLCHEITTPIAIMDLMEKGMDRVFDPNKIKAVIDHVTPAKDSKTAAQGKIMRE 82
Cdd:TIGR01343 1 TIAEKILSKKSGKEVYAgDLIEAEIDLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIVFDHQVPADTIKAAEMQKLARE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 83 WAKRQNIKDFFDVGEnGVCHALFPEKGFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCTFRAPVSMKVS 162
Cdd:TIGR01343 81 FVKKQGIKYFYDVGE-GICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFKVPETIRVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 163 ISGILQNGVSAKDVILAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDRVTAEYLWQFIKD 242
Cdd:TIGR01343 160 ITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYLKERRKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 243 DYTTIdaavakfekwHSDADAEYASVIELDVSELEPQVTYGYKPDHVKNIREMEGTPVDQIYIGSCTNGRIEDLRQAAAI 322
Cdd:TIGR01343 240 PFRVY----------KSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEVEGTEIDQVFIGSCTNGRLEDLRVAAKI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 323 LKGKRLASGVRGIVTPATPGIYSQALEEGIIKIFMDAGFCVLNPTCGACLGMSSGVLAEGEVCASTTNRNFNGRMG-KGG 401
Cdd:TIGR01343 310 LKGRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMGhPNA 389
|
410 420
....*....|....*....|...
gi 505217943 402 MVHLMSPASAAAAAITGTISDPR 424
Cdd:TIGR01343 390 EIYLASPATAAASAVKGYIADPR 412
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
4-423 |
1.21e-134 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 392.97 E-value: 1.21e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 4 TIAQKIFDAHL-RDTPTPENMVLDLDVVLCHEITTPIAIMDLMEKGmDRVFDPNKIKAVIDHVTPAKDSKTAAQGKIMRE 82
Cdd:NF040615 2 TLAEKILSKKLgKEVYAGDTVEVDVDLAMTHDGTTPLTYKAFKEIS-DKVWDNEKIVIVFDHNVPANTVKAANMQKITRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 83 WAKRQNIKDFFDVGEnGVCHALFPEKGFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCTFRAPVSMKVS 162
Cdd:NF040615 81 FVKEQGIKNFYLGGE-GICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 163 ISGILQNgVSAKDVILAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDRVTAEYLWQFIKD 242
Cdd:NF040615 160 IVGKNEN-ISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEGVS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 243 DYTTidAAVAKFEKWHSDADAEYASVIELDVSELEPQVTYGYKPDHVKNIREMEGTPVDQIYIGSCTNGRIEDLRQAAAI 322
Cdd:NF040615 239 EEEI--AELKKNRITVNEKEENYYKEIEIDITDMEEQVACPHHPDNVKPVSEVEGTEIDQVFIGSCTNGRLSDLRIAAKY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 323 LKGKRLASGVRGIVTPATPGIYSQALEEGIIKIFMDAGFCVLNPTCGACLGMSSGVLAEGEVCASTTNRNFNGRMG-KGG 401
Cdd:NF040615 317 LKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGnINS 396
|
410 420
....*....|....*....|..
gi 505217943 402 MVHLMSPASAAAAAITGTISDP 423
Cdd:NF040615 397 YIYLSSPKIAAKSAVKGYITNE 418
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-408 |
1.67e-134 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 394.09 E-value: 1.67e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 7 QKIFDAHLrDTPTPENMVLDLDVVLCHEITTPIAIMDLMEKGmDRVFDPNKIKAVIDHVTPAKD----SKTAAQGKIMRE 82
Cdd:pfam00330 1 EKIWDAHL-VEELDGSLLYIPDRVLMHDVTSPQAFVDLRAAG-RAVRRPGGTPATIDHLVPTDLvidhAPDALDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 83 WAK--------RQNIKDF----FDVGeNGVCHALFPEKGFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGV 150
Cdd:pfam00330 79 ISRnkeqydflEWNAKKFgirfVPPG-QGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLATQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 151 CTFRAPVSMKVSISGILQNGVSAKDVILAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDR 230
Cdd:pfam00330 158 LEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPPDE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 231 VTAEYLwQFIKDDYTTIDAAVAKFEKW---HSDADAEYASVIELDVSELEPQVTYGYKPDHVKNIRE------------- 294
Cdd:pfam00330 238 TTFEYL-RATGRPEAPKGEAYDKAVAWktlASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSElvpdpfadavkrk 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 295 ----------------MEGTPVDQIYIGSCTNGRIEDLRQAAAILK-----GKRLASGVRGIVTPATPGIYSQALEEGII 353
Cdd:pfam00330 317 aaeraleymglgpgtpLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEAEGLD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 505217943 354 KIFMDAGFCVLNPTCGACLGMsSGVLAEGEVCASTTNRNFNGRMGKGGMVHLMSP 408
Cdd:pfam00330 397 KILEEAGFEWRGPGCSMCIGN-SDRLPPGERCVSSSNRNFEGRQGPGGRTHLASP 450
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
1-427 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 678.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 1 MGKTIAQKIFDAHLRDTPTP-ENMVLDLDVVLCHEITTPIAIMDLMEKGMDRVFDPNKIKAVIDHVTPAKDSKTAAQGKI 79
Cdd:PRK00402 1 MGMTLAEKILARHSGRDVSPgDIVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVIVFDHFVPAKDIKSAEQQKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 80 MREWAKRQNIKDFFDVGEnGVCHALFPEKGFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCTFRAPVSM 159
Cdd:PRK00402 81 LREFAKEQGIPNFFDVGE-GICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKTWFKVPETI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 160 KVSISGILQNGVSAKDVILAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDRVTAEYLWQF 239
Cdd:PRK00402 160 KVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLEYLKER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 240 IKDDYttidaavakfEKWHSDADAEYASVIELDVSELEPQVTYGYKPDHVKNIREMEGTPVDQIYIGSCTNGRIEDLRQA 319
Cdd:PRK00402 240 AGRDY----------KPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVEGTKVDQVFIGSCTNGRLEDLRIA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 320 AAILKGKRLASGVRGIVTPATPGIYSQALEEGIIKIFMDAGFCVLNPTCGACLGMSSGVLAEGEVCASTTNRNFNGRMGK 399
Cdd:PRK00402 310 AEILKGRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGS 389
|
410 420
....*....|....*....|....*....
gi 505217943 400 -GGMVHLMSPASAAAAAITGTISDPRQFL 427
Cdd:PRK00402 390 pESEVYLASPAVAAASAVTGKITDPREVL 418
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-426 |
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: 639.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 1 MGKTIAQKIFDAHLRDTPTP-ENMVLDLDVVLCHEITTPIAIMDLMEKGMDRVFDPNKIKAVIDHVTPAKDSKTAAQGKI 79
Cdd:COG0065 1 MGMTLAEKILARHAGREVEPgEIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVAVFDHNVPTKDPKSAEQVKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 80 MREWAKRQNIKdFFDVGENGVCHALFPEKGFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCTFRAPVSM 159
Cdd:COG0065 81 LREFAKEFGIT-FFDVGDPGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWFKVPETM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 160 KVSISGILQNGVSAKDVILAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDRVTAEYLWqf 239
Cdd:COG0065 160 RIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFEYLK-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 240 ikddyttiDAAVAKFEKWHSDADAEYASVIELDVSELEPQVTYGYKPDHVKNIREMEGTPVDQIYIGSCTNGRIEDLRQA 319
Cdd:COG0065 238 --------GRPFAPWRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSELEGIKIDQVFIGSCTNGRIEDLRAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 320 AAILKGKRLASGVRGIVTPATPGIYSQALEEGIIKIFMDAGFCVLNPTCGACLGMSSGVLAEGEVCASTTNRNFNGRMG- 398
Cdd:COG0065 310 AEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGs 389
|
410 420
....*....|....*....|....*...
gi 505217943 399 KGGMVHLMSPASAAAAAITGTISDPRQF 426
Cdd:COG0065 390 PGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| 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: 551.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 29 VVLCHEITTPIAIMDLMEKGMDRVFDPNKIKAVIDHVTPAKDSKTAAQGKIMREWAKRQNIkDFFDVGENGVCHALFPEK 108
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAVFDHNVPTPDIKAAEQVKTLRKFAKEFGI-NFFDVGRQGICHVILPEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 109 GFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCTFRAPVSMKVSISGILQNGVSAKDVILAVIKKLTVNG 188
Cdd:cd01583 80 GLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 189 ATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDRVTAEYLWQfikddyttidAAVAKFEKWHSDADAEYASV 268
Cdd:cd01583 160 ATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKG----------RGKAYWKELKSDEDAEYDKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 269 IELDVSELEPQVTYGYKPDHVKNIREMEGTPVDQIYIGSCTNGRIEDLRQAAAILKGKRLASGVRGIVTPATPGIYSQAL 348
Cdd:cd01583 230 VEIDASELEPQVAWPHSPDNVVPVSEVEGIKIDQVFIGSCTNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAE 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505217943 349 EEGIIKIFMDAGFCVLNPTCGACLGMSSGVLAEGEVCASTTNRNFNGRMG-KGGMVHLMSPASAAAAAITGTI 420
Cdd:cd01583 310 KEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTSNRNFKGRMGsPGARIYLASPATAAASAITGEI 382
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
4-424 |
1.79e-173 |
|
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: 491.58 E-value: 1.79e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 4 TIAQKIFDAHLRDTPTP-ENMVLDLDVVLCHEITTPIAIMDLMEKGMDRVFDPNKIKAVIDHVTPAKDSKTAAQGKIMRE 82
Cdd:TIGR01343 1 TIAEKILSKKSGKEVYAgDLIEAEIDLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIVFDHQVPADTIKAAEMQKLARE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 83 WAKRQNIKDFFDVGEnGVCHALFPEKGFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCTFRAPVSMKVS 162
Cdd:TIGR01343 81 FVKKQGIKYFYDVGE-GICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFKVPETIRVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 163 ISGILQNGVSAKDVILAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDRVTAEYLWQFIKD 242
Cdd:TIGR01343 160 ITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYLKERRKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 243 DYTTIdaavakfekwHSDADAEYASVIELDVSELEPQVTYGYKPDHVKNIREMEGTPVDQIYIGSCTNGRIEDLRQAAAI 322
Cdd:TIGR01343 240 PFRVY----------KSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEVEGTEIDQVFIGSCTNGRLEDLRVAAKI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 323 LKGKRLASGVRGIVTPATPGIYSQALEEGIIKIFMDAGFCVLNPTCGACLGMSSGVLAEGEVCASTTNRNFNGRMG-KGG 401
Cdd:TIGR01343 310 LKGRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMGhPNA 389
|
410 420
....*....|....*....|...
gi 505217943 402 MVHLMSPASAAAAAITGTISDPR 424
Cdd:TIGR01343 390 EIYLASPATAAASAVKGYIADPR 412
|
|
| LEU2 |
TIGR02083 |
3-isopropylmalate dehydratase, large subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
4-425 |
2.09e-148 |
|
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: 428.08 E-value: 2.09e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 4 TIAQKIFDAHL-RDTPTPENMVL-DLDVVLCHEITTPIAIMDLMEKGMDRVFDPNKIKAVIDHVTPAKDSKTAAQGKIMR 81
Cdd:TIGR02083 2 TMAEKILAQHAgLESVEPGELILaKLDIVLGNDITTPLAIKAFKEYGGKKVFDPDRVALVPDHFTPNKDIKSAEQCKMMR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 82 EWAKRQNIKDFFDVGENGVCHALFPEKGFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCTFRAPVSMKV 161
Cdd:TIGR02083 82 EFAREQGIEKFFEIGNMGIEHALLPEEGIVKPGDLIIGADSHTCTYGALGAFATGVGSTDMAVGMATGKAWFRVPEAIKF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 162 SISGILQNGVSAKDVILAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDRVTAEYLWQFIK 241
Cdd:TIGR02083 162 VLKGKLKPWVTGKDLILHIIGIIGVDGALYKSMEFSGEGLKELSMDDRFTIANMAIEAGAKTGIFPVDEITIEYEKGRGK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 242 DDYttidaavakfEKWHSDADAEYASVIELDVSELEPQVTYGYKPDHVKNIREMEGT--PVDQIYIGSCTNGRIEDLRQA 319
Cdd:TIGR02083 242 REE----------KIYKADEDAKYVRVIEIDLSELEPQVAFPHLPENTKDISEAGKEeiKIDQVVIGSCTNGRLEDLRLA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 320 AAILKGKRLASGVRGIVTPATPGIYSQALEEGIIKIFMDAGFCVLNPTCGACLGMSSGVLAEGEVCASTTNRNFNGRMGK 399
Cdd:TIGR02083 312 AEILKGKTVAPDVRCIIIPGSQNVYLEAMKEGLLEIFIEAGAVVSTPTCGPCLGGHMGILAEGERAISTTNRNFVGRMGH 391
|
410 420
....*....|....*....|....*..
gi 505217943 400 -GGMVHLMSPASAAAAAITGTISDPRQ 425
Cdd:TIGR02083 392 pKSEVYLASPAVAAASAIKGYIASPEE 418
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
3-425 |
9.64e-146 |
|
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: 421.09 E-value: 9.64e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 3 KTIAQKIFDAHLRDTPTP-ENMVLDLDVVLCHEITTPIAIMDLMEKGMDRVFDPNKIKAVIDHVTPAKDSKTAAQGKIMR 81
Cdd:TIGR02086 1 MTLAEKILSEKVGRPVCAgEIVEVEVDLAMTHDGTGPLAIKALRELGVARVWDPEKIVIAFDHNVPPPTVEAAEMQKEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 82 EWAKRQNIKDFfDVGEnGVCHALFPEKGFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCTFRAPVSMKV 161
Cdd:TIGR02086 81 EFAKRHGIKNF-DVGE-GICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTWIKVPETIRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 162 SISGILQNGVSAKDVILAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDRVTAEYLWQFIK 241
Cdd:TIGR02086 159 VVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEETYEYLKKRRG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 242 DDyttidaavakFEKWHSDADAEYASVIELDVSELEPQVTYGYKPDHVKNIREMEGTPVDQIYIGSCTNGRIEDLRQAAA 321
Cdd:TIGR02086 239 LE----------FRILVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVSDVEGTEIDQVFIGSCTNGRLEDLRIAAE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 322 ILKGKRLASGVRGIVTPATPGIYSQALEEGIIKIFMDAGFCVLNPTCGACLGMSSGVLAEGEVCASTTNRNFNGRMG-KG 400
Cdd:TIGR02086 309 ILKGRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAGAMICPPGCGPCLGAHMGVLGDGEVCLSTTNRNFKGRMGsPN 388
|
410 420
....*....|....*....|....*
gi 505217943 401 GMVHLMSPASAAAAAITGTISDPRQ 425
Cdd:TIGR02086 389 AEIYLASPATAAASAVEGYITDPED 413
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-427 |
2.84e-143 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 416.83 E-value: 2.84e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 1 MGKTIAQKIFDAHLRDTPTPENMVLDLDVVLCHEITTPIAIMDLMEKGMdRVFDPNKIKAVIDHVTPAKDSKTAAQGKIM 80
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGR-KVRRPDLTFATMDHNVPTTDRDLPIADPVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 81 REW--AKRQNIKDF----FDVG--ENGVCHALFPEKGFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTdlEVG------- 145
Cdd:PRK05478 80 RIQveTLEKNCKEFgitlFDLGdpRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTS--EVEhvlatqt 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 146 ILKgvctfRAPVSMKVSISGILQNGVSAKDVILAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGL 225
Cdd:PRK05478 158 LLQ-----KKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 226 CYPDRVTAEYL-----------WqfikddyttiDAAVAKFEKWHSDADAEYASVIELDVSELEPQVTYGYKPDHV----- 289
Cdd:PRK05478 233 VAPDETTFEYLkgrpfapkgedW----------DKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVisidg 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 290 --------------KNIRE------------MEGTPVDQIYIGSCTNGRIEDLRQAAAILKGKRLASGVRGIVTPATPGI 343
Cdd:PRK05478 303 kvpdpedfadpvkrASAERalaymglkpgtpITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 344 YSQALEEGIIKIFMDAGFCVLNPTCGACLGMSSGVLAEGEVCASTTNRNFNGRMGKGGMVHLMSPASAAAAAITGTISDP 423
Cdd:PRK05478 383 KAQAEAEGLDKIFIEAGFEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDV 462
|
....
gi 505217943 424 RQFL 427
Cdd:PRK05478 463 RELL 466
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
1-429 |
5.24e-140 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 408.52 E-value: 5.24e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 1 MGKTIAQKIFDAHLRDTPTPENMVLDLDVVLCHEITTPIAIMDLMEKGMdRVFDPNKIKAVIDHVTP--------AKDSK 72
Cdd:PRK12466 2 MPRTLYDKLWDSHTVARLDDGHVLLYIDRHLLNEYTSPQAFSGLRARGR-TVRRPDLTLAVVDHVVPtrpgrdrgITDPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 73 TAAQGKIMREWAKRQNIKdFFDVGE--NGVCHALFPEKGFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGV 150
Cdd:PRK12466 81 GALQVDYLRENCADFGIR-LFDVDDprQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 151 CTFRAPVSMKVSISGILQNGVSAKDVILAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDR 230
Cdd:PRK12466 160 LVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 231 VTAEYLWQFIKD-DYTTIDAAVAKFEKWHSDADAEYASVIELDVSELEPQVTYGYKPDHVKNIRE--------------- 294
Cdd:PRK12466 240 TTFDYLRGRPRApKGALWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGrvpdpaaeadparra 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 295 ----------------MEGTPVDQIYIGSCTNGRIEDLRQAAAILKGKRLASGVRGIVTPATPGIYSQALEEGIIKIFMD 358
Cdd:PRK12466 320 ameraldymgltpgtpLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505217943 359 AGFCVLNPTCGACLGMSSGVLAEGEVCASTTNRNFNGRMGKGGMVHLMSPASAAAAAITGTISDPRQFLAQ 429
Cdd:PRK12466 400 AGFEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHITDVRSLLQA 470
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
4-423 |
1.21e-134 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 392.97 E-value: 1.21e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 4 TIAQKIFDAHL-RDTPTPENMVLDLDVVLCHEITTPIAIMDLMEKGmDRVFDPNKIKAVIDHVTPAKDSKTAAQGKIMRE 82
Cdd:NF040615 2 TLAEKILSKKLgKEVYAGDTVEVDVDLAMTHDGTTPLTYKAFKEIS-DKVWDNEKIVIVFDHNVPANTVKAANMQKITRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 83 WAKRQNIKDFFDVGEnGVCHALFPEKGFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCTFRAPVSMKVS 162
Cdd:NF040615 81 FVKEQGIKNFYLGGE-GICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 163 ISGILQNgVSAKDVILAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDRVTAEYLWQFIKD 242
Cdd:NF040615 160 IVGKNEN-ISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEGVS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 243 DYTTidAAVAKFEKWHSDADAEYASVIELDVSELEPQVTYGYKPDHVKNIREMEGTPVDQIYIGSCTNGRIEDLRQAAAI 322
Cdd:NF040615 239 EEEI--AELKKNRITVNEKEENYYKEIEIDITDMEEQVACPHHPDNVKPVSEVEGTEIDQVFIGSCTNGRLSDLRIAAKY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 323 LKGKRLASGVRGIVTPATPGIYSQALEEGIIKIFMDAGFCVLNPTCGACLGMSSGVLAEGEVCASTTNRNFNGRMG-KGG 401
Cdd:NF040615 317 LKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGnINS 396
|
410 420
....*....|....*....|..
gi 505217943 402 MVHLMSPASAAAAAITGTISDP 423
Cdd:NF040615 397 YIYLSSPKIAAKSAVKGYITNE 418
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-408 |
1.67e-134 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 394.09 E-value: 1.67e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 7 QKIFDAHLrDTPTPENMVLDLDVVLCHEITTPIAIMDLMEKGmDRVFDPNKIKAVIDHVTPAKD----SKTAAQGKIMRE 82
Cdd:pfam00330 1 EKIWDAHL-VEELDGSLLYIPDRVLMHDVTSPQAFVDLRAAG-RAVRRPGGTPATIDHLVPTDLvidhAPDALDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 83 WAK--------RQNIKDF----FDVGeNGVCHALFPEKGFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGV 150
Cdd:pfam00330 79 ISRnkeqydflEWNAKKFgirfVPPG-QGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLATQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 151 CTFRAPVSMKVSISGILQNGVSAKDVILAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDR 230
Cdd:pfam00330 158 LEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPPDE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 231 VTAEYLwQFIKDDYTTIDAAVAKFEKW---HSDADAEYASVIELDVSELEPQVTYGYKPDHVKNIRE------------- 294
Cdd:pfam00330 238 TTFEYL-RATGRPEAPKGEAYDKAVAWktlASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSElvpdpfadavkrk 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 295 ----------------MEGTPVDQIYIGSCTNGRIEDLRQAAAILK-----GKRLASGVRGIVTPATPGIYSQALEEGII 353
Cdd:pfam00330 317 aaeraleymglgpgtpLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEAEGLD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 505217943 354 KIFMDAGFCVLNPTCGACLGMsSGVLAEGEVCASTTNRNFNGRMGKGGMVHLMSP 408
Cdd:pfam00330 397 KILEEAGFEWRGPGCSMCIGN-SDRLPPGERCVSSSNRNFEGRQGPGGRTHLASP 450
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
1-426 |
7.25e-121 |
|
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: 359.55 E-value: 7.25e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 1 MGKTIAQKIFDAHLRDTPTPENMVLDLDVVLCHEITTPIAIMDLMEKGMdRVFDPNKIKAVIDHVTPAKDSKTAAQGkim 80
Cdd:TIGR00170 1 MPRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGR-KVRRPQKTFATMDHNIPTQNRDFNIKD--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 81 rEWAKRQ------NIKDF----FDVG--ENGVCHALFPEKGFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILK 148
Cdd:TIGR00170 77 -EVAKIQvtelekNCKEFgvrlFDLHsvDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 149 GVCTFRAPVSMKVSISGILQNGVSAKDVILAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYP 228
Cdd:TIGR00170 156 QTLKQARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 229 DRVTAEYLwqfiKDDYTT-----IDAAVAKFEKWHSDADAEYASVIELDVSELEPQVTYGYKPDHVKNI----------- 292
Cdd:TIGR00170 236 DETTFEYC----KGRPHApkgkeFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVnsevpdpesfa 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 293 -----REME----------GTP-----VDQIYIGSCTNGRIEDLRQAAAILKGKRLASGVRGIVTPATPGIYSQALEEGI 352
Cdd:TIGR00170 312 dpvdkASAEralaymglepGTPlkdikVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGL 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505217943 353 IKIFMDAGFCVLNPTCGACLGMSSGVLAEGEVCASTTNRNFNGRMGKGGMVHLMSPASAAAAAITGTISDPRQF 426
Cdd:TIGR00170 392 DKIFIEAGFEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
30-420 |
3.57e-90 |
|
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: 278.23 E-value: 3.57e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 30 VLCHEITTPIAIMDLMEKG-MDRVFDPNKIKAVIDHVTPAKDSKTAAQGKIMREWAKRQNIkDFFDVGeNGVCHALFPEK 108
Cdd:cd01351 2 VMLQDATGPMAMKAFEILAaLGKVADPSQIACVHDHAVQLEKPVNNEGHKFLSFFAALQGI-AFYRPG-VGIIHQIMVEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 109 gFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCTFRAPVSMKVSISGILQNGVSAKDVILAVIKKLTVNG 188
Cdd:cd01351 80 -LALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVDG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 189 ATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDRVTAEYLWQFIKDDYTTIDAAvaKFEKWHSDADAEYASV 268
Cdd:cd01351 159 VLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWLA--FPEELLADEGAEYDQV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 269 IELDVSELEPQVTYGYKPDHVKNIREMEGTPVDQIYIGSCTNGRIEDLRQAAAILKGKRLASGVRGIVTPATPGIYSQAL 348
Cdd:cd01351 237 IEIDLSELEPDISGPNRPDDAVSVSEVEGTKIDQVLIGSCTNNRYSDMLAAAKLLKGAKVAPGVRLIVTPGSRMVYATLS 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505217943 349 EEGIIKIFMDAGFCVLNPTCGACLGMSSGVLAEGEVCASTTNRNFNGRMGKG-GMVHLMSPASAAAAAITGTI 420
Cdd:cd01351 317 REGYYEILVDSGARILPPGCGPCMGNGARLVADGEVGVSSGNRNFPGRLGTYeRHVYLASPELAAATAIAGKI 389
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
1-424 |
5.59e-89 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 282.81 E-value: 5.59e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 1 MGKTIAQKIFDAHLRD-TPTP-ENMVLDLDVVLCHEITTPIAIMDLMEKGMDRVFDPnkiKAV--IDHVTPAKDSKTAAQ 76
Cdd:PRK07229 1 MGLTLTEKILYAHLVEgELEPgEEIAIRIDQTLTQDATGTMAYLQFEAMGLDRVKTE---LSVqyVDHNLLQADFENADD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 77 GKIMREWAKRQNIkDFFDVGeNGVCHALFPEKgFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCTFRAP 156
Cdd:PRK07229 78 HRFLQSVAAKYGI-YFSKPG-NGICHQVHLER-FAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGGPYYLKMP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 157 VSMKVSISGILQNGVSAKDVILAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLcYP-DRVTAEY 235
Cdd:PRK07229 155 KVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSI-FPsDERTREF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 236 L-WQFIKDDyttidaavakFEKWHSDADAEYASVIELDVSELEPQVTYGYKPDHVKNIREMEGTPVDQIYIGSCTNGRIE 314
Cdd:PRK07229 234 LkAQGREDD----------WVELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEVAGIKVDQVLIGSCTNSSYE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 315 DLRQAAAILKGKRLASGVRGIVTPATPGIYSQALEEGIIKIFMDAGFCVLNPTCGACLGMsSGVLAEGEVCASTTNRNFN 394
Cdd:PRK07229 304 DLMRAASILKGKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGM-GQAPATGNVSLRTFNRNFP 382
|
410 420 430
....*....|....*....|....*....|.
gi 505217943 395 GRMG-KGGMVHLMSPASAAAAAITGTISDPR 424
Cdd:PRK07229 383 GRSGtKDAQVYLASPETAAASALTGVITDPR 413
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
28-420 |
1.42e-82 |
|
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: 258.53 E-value: 1.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 28 DVVLCHEITTPIAIMDLMEKGMDRVFDPNKIkAVIDHVTPAKDSKTAAQGKIMREWAKRQNIkdFFDVGENGVCHALFPE 107
Cdd:cd01585 1 DQTLTQDATGTMAYLQFEAMGVDRVRTELSV-SYVDHNTLQTDFENADDHRFLQTVAARYGI--YFSRPGNGICHQVHLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 108 KgFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCTFRAPVSMKVSISGILQNGVSAKDVILAVIKKLTVN 187
Cdd:cd01585 78 R-FAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 188 GATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDRVTAEYLWQFIKDDyttidaavaKFEKWHSDADAEYAS 267
Cdd:cd01585 157 GGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGRED---------DWVELAADADAEYDE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 268 VIELDVSELEPQVTYGYKPDHVKNIREMEGTPVDQIYIGSCTNGRIEDLRQAAAILKGKRLASGVRGIVTPATPGIYSQA 347
Cdd:cd01585 228 EIEIDLSELEPLIARPHSPDNVVPVREVAGIKVDQVAIGSCTNSSYEDLMTVAAILKGRRVHPHVSMVVAPGSKQVLEML 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505217943 348 LEEGIIKIFMDAGFCVLNPTCGACLGMsSGVLAEGEVCASTTNRNFNGRMG-KGGMVHLMSPASAAAAAITGTI 420
Cdd:cd01585 308 ARNGALADLLAAGARILESACGPCIGM-GQAPPTGGVSVRTFNRNFEGRSGtKDDLVYLASPEVAAAAALTGVI 380
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
30-420 |
7.56e-49 |
|
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: 170.10 E-value: 7.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 30 VLCHEITTPIAiMDLMEKGMDRVFDPNKIKAVIDHVTPAKDSKTAAQGKIMREWAKRQNIkDFFDVGEnGVCHALFPEKG 109
Cdd:cd01582 2 CMTHDNSWPVA-LKFMSIGATKIHNPDQIVMTLDHDVQNKSEKNLKKYKNIESFAKKHGI-DFYPAGR-GIGHQIMIEEG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 110 FIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCTFRAPVSMKVSISGILQNGVSAKDVILAVIKKLTVNGA 189
Cdd:cd01582 79 YAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 190 TDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLcYPdrvtaeylwqfikddyttidaavakfekwhsdADAEYasvI 269
Cdd:cd01582 159 LNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGL-FP--------------------------------TDAKH---L 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 270 ELDVSELEPQVTygyKPDHVK---NIREMEGT--PVDQIYIGSCTNGRIEDLRQAAAILKGKR-------LASGVRGIVT 337
Cdd:cd01582 203 ILDLSTLSPYVS---GPNSVKvstPLKELEAQniKINKAYLVSCTNSRASDIAAAADVVKGKKekngkipVAPGVEFYVA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 338 PATPGIYSQALEEGIIKIFMDAGFCVLNPTCGACLGMSSGVLAEGEVCASTTNRNFNGRMG-KGGMVHLMSPASAAAAAI 416
Cdd:cd01582 280 AASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQGLLEPGEVGISATNRNFKGRMGsTEALAYLASPAVVAASAI 359
|
....
gi 505217943 417 TGTI 420
Cdd:cd01582 360 SGKI 363
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
30-420 |
4.75e-45 |
|
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: 161.45 E-value: 4.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 30 VLCHEITTPIAIMDLMEKGMDRVFDPNKIKAviDHVTPAKDsktAAQGKIMREWAKRQNIKDF-------FDVG----EN 98
Cdd:cd01584 2 VAMQDATAQMALLQFMSSGLPKVAVPSTIHC--DHLIEAQV---GGEKDLKRAKDINKEVYDFlasagakYGIGfwkpGS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 99 GVCHALFPEKgFIRPGYTVIMGDSHTCTHGAFGAFAAGVGTTDlEVGILKGV-CTFRAPVSMKVSISGILQNGVSAKDVI 177
Cdd:cd01584 77 GIIHQIVLEN-YAFPGLLMIGTDSHTPNAGGLGGIAIGVGGAD-AVDVMAGIpWELKCPKVIGVKLTGKLSGWTSPKDVI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 178 LAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDRVTAEYLWQFIKDDYTTiDAAVAKFEKW 257
Cdd:cd01584 155 LKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEIAD-LADEFKDDLL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 258 HSDADAEYASVIELDVSELEPQVTYGYKPD------HVKNIREMEGTPVDQIY--IGSCTNGRIEDLRQAAAILKgKRLA 329
Cdd:cd01584 234 VADEGAEYDQLIEINLSELEPHINGPFTPDlatpvsKFKEVAEKNGWPLDLRVglIGSCTNSSYEDMGRAASIAK-QALA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 330 SGVRG----IVTPATPGIYSQALEEGIIKIFMDAGFCVLNPTCGACLGMSSGV-LAEGEVCASTT--NRNFNGRMGKGGM 402
Cdd:cd01584 313 HGLKCksifTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQWDRKdIKKGEKNTIVTsyNRNFTGRNDANPA 392
|
410 420
....*....|....*....|
gi 505217943 403 VH--LMSPASAAAAAITGTI 420
Cdd:cd01584 393 THafVASPEIVTAMAIAGTL 412
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
120-420 |
3.47e-35 |
|
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: 134.93 E-value: 3.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 120 GDSHTctHGAFG-AFAAGVGTTDLEVGIlkGVCTFRAPVSMKVSISGILQNGVSAKDVI------------LAVIKKLTV 186
Cdd:cd01581 113 GDSHT--RFPIGiSFPAGSGLVAFAAAT--GVMPLDMPESVLVRFKGKMQPGITLRDLVnaipyyaiqqglLTVEKKGKK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 187 NGATDKVIEFTGplVDSMNMSARMTLCNMAVEAGATSGLCYPDRVT-AEYLWQFIK----------DDYTTIDAAVAKFE 255
Cdd:cd01581 189 NVFNGRILEIEG--LPDLKVEQAFELTDASAERSAAACTVRLDKEPvIEYLESNVVlmkimiangyDDARTLLRRIIAME 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 256 KW-------HSDADAEYASVIELDVSEL-EPQVTYGYKPDHVKNIREMEGTPVDQIYIGSC-TNgrIEDLRQAAAILKGK 326
Cdd:cd01581 267 EWlanppllEPDADAEYAAVIEIDLDDIkEPILACPNDPDDVKLLSEVAGKKIDEVFIGSCmTN--IGHFRAAAKILRGK 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 327 RlASGVRGIVTPATPGIYSQALEEGIIKIFMDAGFCVLNPTCGACLGMSSGVlAEGEVCASTTNRNFNGRMGKGGMVHLM 406
Cdd:cd01581 345 E-FKPTRLWVAPPTRMDWAILQEEGYYSIFGDAGARTEMPGCSLCMGNQARV-ADGATVFSTSTRNFDNRVGKGAEVYLG 422
|
330
....*....|....
gi 505217943 407 SPASAAAAAITGTI 420
Cdd:cd01581 423 SAELAAVCALLGRI 436
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
116-407 |
2.26e-33 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 132.99 E-value: 2.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 116 TVIMG-DSHTCTH-G-AFG------AFAAGVGTTDLEVgilkgvctfraPVSMKVSISGILQNGVSAKDVILAV----IK 182
Cdd:PRK09238 480 TVGTGgDSHTRFPiGiSFPagsglvAFAAATGVMPLDM-----------PESVLVRFKGEMQPGITLRDLVHAIpyyaIK 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 183 K--LTV---------NGatdKVIEFTGplVDSMNMSARMTLCNMAVEAGATSGLCYPDRVT-AEYL--------WqFIKD 242
Cdd:PRK09238 549 QglLTVekkgkknifSG---RILEIEG--LPDLKVEQAFELTDASAERSAAGCTIKLSKEPiIEYLrsnivllkW-MIAE 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 243 DY---TTIDAAVAKFEKW-------HSDADAEYASVIELDVSEL-EPQVTYGYKPDHVKNIREMEGTPVDQIYIGSC-TN 310
Cdd:PRK09238 623 GYgdaRTLERRIAAMEEWlanpellEADADAEYAAVIEIDLAEIkEPILACPNDPDDVRLLSEVAGTKIDEVFIGSCmTN 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 311 grIEDLRQAAAILKGKRLASGVRGIVTPATPGIYSQALEEGIIKIFMDAGFCVLNPTCGACLGMSSGVlAEGEVCASTTN 390
Cdd:PRK09238 703 --IGHFRAAGKLLEGKKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMGNQARV-ADGATVFSTST 779
|
330
....*....|....*..
gi 505217943 391 RNFNGRMGKGGMVHLMS 407
Cdd:PRK09238 780 RNFPNRLGKGANVYLGS 796
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
116-408 |
1.21e-29 |
|
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle
Pssm-ID: 440669 [Multi-domain] Cd Length: 891 Bit Score: 121.75 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 116 TVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILkGVctfraPVSMK------VSISGILQNGVSAKDVILAVIKKLTVNGA 189
Cdd:COG1048 205 TLVGTDSHTTMINGLGVLGWGVGGIEAEAAML-GQ-----PVSMLipevvgVKLTGKLPEGVTATDLVLTVTEMLRKKGV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 190 TDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDRVTAEYL-------WQfikddyttiDAAVAKFEK----WH 258
Cdd:COG1048 279 VGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLrltgrseEQ---------IELVEAYAKaqglWR 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 259 SD--ADAEYASVIELDVSELEPQVTyGYK-P-DHV----------KNIREMEGTPVDQIY-------------------- 304
Cdd:COG1048 350 DPdaPEPYYSDVLELDLSTVEPSLA-GPKrPqDRIplsdlkeafrAALAAPVGEELDKPVrvevdgeefelghgavviaa 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 305 IGSCTNGRIEDLRQAAAIL------KGKRLASGVRgivTPATPGiySQA----LEE-GIIKIFMDAGFCVLNPTCGACLG 373
Cdd:COG1048 429 ITSCTNTSNPSVMIAAGLLakkaveKGLKVKPWVK---TSLAPG--SKVvtdyLERaGLLPYLEALGFNVVGYGCTTCIG 503
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 505217943 374 MS-------SGVLAEGE-VCASTT--NRNFNGRmgkggmVH-------LMSP 408
Cdd:COG1048 504 NSgplppeiSEAIEENDlVVAAVLsgNRNFEGR------IHpdvkanfLASP 549
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
120-428 |
6.07e-27 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 113.86 E-value: 6.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 120 GDSHTctHGAFG-AFAAGVGTtdLEVGILKGVCTFRAPVSMKVSISGILQNGVSAKDVI------------LAVIKKLTV 186
Cdd:PLN00094 559 GDSHT--RFPIGiSFPAGSGL--VAFGAATGVIPLDMPESVLVRFTGTMQPGITLRDLVhaipytaiqdglLTVEKKGKK 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 187 NGATDKVIEFTGplVDSMNMSARMTLCNMAVE---AGATSGLcyPDRVTAEYL--------WqFIKDDY---TTIDAAVA 252
Cdd:PLN00094 635 NVFSGRILEIEG--LPHLKCEQAFELSDASAErsaAGCTIKL--DKEPIIEYLnsnvvmlkW-MIAEGYgdrRTLERRIA 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 253 KFEKW-------HSDADAEYASVIELDVSEL-EPQVTYGYKPDHVKNIREMEGTPVDQIYIGSC-TNgrIEDLRQAAAIL 323
Cdd:PLN00094 710 RMQQWladpellEADPDAEYAAVIEIDMDEIkEPILCAPNDPDDARLLSEVTGDKIDEVFIGSCmTN--IGHFRAAGKLL 787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 324 KGKRLASGVRGIVTPATPGIYSQALEEGIIKIFMDAGFCVLNPTCGACLGMSSGVlAEGEVCASTTNRNFNGRMGKGGMV 403
Cdd:PLN00094 788 NDNLSQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPGCSLCMGNQARV-AEKSTVVSTSTRNFPNRLGKGANV 866
|
330 340
....*....|....*....|....*
gi 505217943 404 HLMSPASAAAAAITGTISDPRQFLA 428
Cdd:PLN00094 867 YLASAELAAVAAILGRLPTVEEYLS 891
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
30-420 |
7.65e-24 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 104.63 E-value: 7.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 30 VLCHEITTPIAIMDL--MEKGMDRV-FDPNKIKA------VIDH---VTPAKDSKTAAQG-KI-MR---------EWAkr 86
Cdd:PRK12881 86 VVMQDFTGVPALVDLaaMRDAAAEAgGDPAKINPlvpvdlVVDHsvaVDYFGQKDALDLNmKIeFQrnaeryqflKWG-- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 87 QNIKDFFDV---GeNGVCHALFPEK-------------GFIRPGyTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGV 150
Cdd:PRK12881 164 MQAFDNFRVvppG-TGIMHQVNLEYlarvvhtkeddgdTVAYPD-TLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 151 CTFRAPVSMKVSISGILQNGVSAKDVILAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDR 230
Cdd:PRK12881 242 VYMLIPDVVGVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDE 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 231 VTAEYLWQFIKDdyttiDAAVAKFEK-------WH-SDADAEYASVIELDVSELEPQV---------------------- 280
Cdd:PRK12881 322 QTLDYLRLTGRT-----EAQIALVEAyakaqglWGdPKAEPRYTRTLELDLSTVAPSLagpkrpqdrialgnvksafsdl 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 281 --------TYGYKPDHVKNIREMEGtPVDQIYIGSCTNGRIEDLRQAAAILKGKRLASGVRG---IVTPATPGiySQALE 349
Cdd:PRK12881 397 fskpvaenGFAKKAQTSNGVDLPDG-AVAIAAITSCTNTSNPSVLIAAGLLAKKAVERGLTVkpwVKTSLAPG--SKVVT 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 350 E-----GIIKIFMDAGFCVLNPTCGACLGMsSGVLAE---------GEVCAS--TTNRNFNGRmgkggmVH-------LM 406
Cdd:PRK12881 474 EyleraGLLPYLEKLGFGIVGYGCTTCIGN-SGPLTPeieqaitknDLVAAAvlSGNRNFEGR------IHpnikanfLA 546
|
490
....*....|....
gi 505217943 407 SPASAAAAAITGTI 420
Cdd:PRK12881 547 SPPLVVAYALAGTV 560
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
30-420 |
1.58e-23 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 103.73 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 30 VLCHEITTPIAIMDL--MEKGMDRV-FDPNKIKA------VIDH---VTPAKdSKTAAQGKIMREWAKRQNIKDFFDVGE 97
Cdd:PLN00070 125 VLLQDFTGVPAVVDLacMRDAMNNLgGDPNKINPlvpvdlVIDHsvqVDVAR-SENAVQANMELEFQRNKERFAFLKWGS 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 98 N------------GVCH---------ALFPEKGFIRPGyTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCTFRAP 156
Cdd:PLN00070 204 TafqnmlvvppgsGIVHqvnleylgrVVFNTDGILYPD-SVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLP 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 157 VSMKVSISGILQNGVSAKDVILAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDRVTAEYL 236
Cdd:PLN00070 283 GVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYL 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 237 WQFIKDDYTtidaaVAKFEKW---------HSDADAE--YASVIELDVSELEPQVTYGYKPDHVKNIREM---------- 295
Cdd:PLN00070 363 KLTGRSDET-----VAMIEAYlrankmfvdYNEPQQErvYSSYLELDLEDVEPCISGPKRPHDRVPLKEMkadwhscldn 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 296 ----------------------EGTPVDQIY-------IGSCTNGRIEDLRQAAAILKGKRLASGVR---GIVTPATPG- 342
Cdd:PLN00070 438 kvgfkgfavpkeaqskvakfsfHGQPAELRHgsvviaaITSCTNTSNPSVMLGAGLVAKKACELGLEvkpWIKTSLAPGs 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 343 --IYSQALEEGIIKIFMDAGFCVLNPTCGACLGMS-------SGVLAEGEVCASTT---NRNFNGRmgkggmVH------ 404
Cdd:PLN00070 518 gvVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIGNSgeldesvASAITENDIVAAAVlsgNRNFEGR------VHpltran 591
|
490
....*....|....*..
gi 505217943 405 -LMSPASAAAAAITGTI 420
Cdd:PLN00070 592 yLASPPLVVAYALAGTV 608
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
30-396 |
3.63e-23 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 102.40 E-value: 3.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 30 VLCHEITTPIAIMDL--MEKGMDRV-FDPNKIKA------VIDHVTPAKDSKTAA-----QGKIMREWAKR--------Q 87
Cdd:PTZ00092 93 VLLQDFTGVPAVVDLaaMRDAMKRLgGDPAKINPlvpvdlVIDHSVQVDFSRSPDalelnQEIEFERNLERfeflkwgsK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 88 NIKDFFDV--GeNGVCH---------ALFPEKGFIRPGyTVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKgvctfrAP 156
Cdd:PTZ00092 173 AFKNLLIVppG-SGIVHqvnleylarVVFNKDGLLYPD-SVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLG------QP 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 157 VSMKV------SISGILQNGVSAKDVILAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDR 230
Cdd:PTZ00092 245 ISMVLpevvgfKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 231 VTAEYLWQFIKDDYTtidaaVAKFEKW--------HSDADAEYASVIELDVSELEPQVTYGYKP-DHV------KNIREM 295
Cdd:PTZ00092 325 KTLDYLKQTGRSEEK-----VELIEKYlkanglfrTYAEQIEYSDVLELDLSTVVPSVAGPKRPhDRVplsdlkKDFTAC 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 296 EGTPV---------------------DQIY-----------IGSCTNGRIEDLRQAAAILKGKRLASGVR---GIVTPAT 340
Cdd:PTZ00092 400 LSAPVgfkgfgipeekhekkvkftykGKEYtlthgsvviaaITSCTNTSNPSVMLAAGLLAKKAVEKGLKvppYIKTSLS 479
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505217943 341 PG--IYSQALEEGIIKIFMDA-GFCVLNPTCGACLGMS-------SGVLAEGE-VCAS--TTNRNFNGR 396
Cdd:PTZ00092 480 PGskVVTKYLEASGLLKYLEKlGFYTAGYGCMTCIGNSgdldpevSEAITNNDlVAAAvlSGNRNFEGR 548
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
116-420 |
2.68e-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: 91.98 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 116 TVIMGDSHTCTHGAFGAFAAGVGTTDLEVGILKGVCTFRAPVSMKVSISGILQNGVSAKDVILAVIKKLTVNGATDKVIE 195
Cdd:cd01586 123 SVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 196 FTGPLVDSMNMSARMTLCNMAVEAGATSGLcYPdrvtaeylwqfikddyttIDaavakfekwhsdadaeyASVIELDVSE 275
Cdd:cd01586 203 FFGPGVAKLSVADRATIANMAPEYGATCGF-FP------------------VD-----------------TQVVELDLST 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 276 LEPQVTYGYKP-DHVkniremegtPVDQIY----IGSCTNGRIEDLRQAAAILKGKRLASGVR---GIVTPATPG--IYS 345
Cdd:cd01586 247 VEPSVSGPKRPqDRV---------PLHGSVviaaITSCTNTSNPSVMLAAGLLAKKAVELGLKvkpYVKTSLAPGsrVVT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 346 QALEEGIIKIFMDA-GFCVLNPTCGACLGmSSGVLAE---------GEVCAS--TTNRNFNGRmgkggmVH-------LM 406
Cdd:cd01586 318 KYLEASGLLPYLEKlGFHVVGYGCTTCIG-NSGPLPEeveeaikenDLVVAAvlSGNRNFEGR------IHplvranyLA 390
|
330
....*....|....
gi 505217943 407 SPASAAAAAITGTI 420
Cdd:cd01586 391 SPPLVVAYALAGTV 404
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
118-406 |
2.08e-19 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 90.84 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 118 IMG-DSHTcTHGAFGAFAAGVGTTDLEVGILKGVCTFRAPVSMKVSISGILQNGVSAKDVILAVIKKLTVNGAT-DKVIE 195
Cdd:PRK11413 145 ILGsDSHT-RYGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVkNKVME 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 196 FTGPLVDSMNMSARMTLCNMAVEAGATSGLCYPDRVTAEYLWQF-IKDDYTTIDAAvakfekwhsdADAEYASVIELDVS 274
Cdd:PRK11413 224 FVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLALHgRGQDYCELNPQ----------PMAYYDGCISVDLS 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 275 ELEPQVTYGYKPDHVKNIREMEGTP---------------------------------VDQIYIGSCTNGRIEDLRQAAA 321
Cdd:PRK11413 294 AIKPMIALPFHPSNVYEIDELNQNLtdilreveieservahgkaklslldkiengrlkVQQGIIAGCSGGNYENVIAAAN 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 322 ILKGKRLASGVRGI-VTPATPGIYSQALEEGIIKIFMDAGFCVLNPTCGACLGmSSGVLAEGEVCASTTNRNFNGRMG-- 398
Cdd:PRK11413 374 ALRGQSCGNDTFSLsVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFG-AGDTPANNGLSIRHTTRNFPNREGsk 452
|
330
....*....|..
gi 505217943 399 --KGGM--VHLM 406
Cdd:PRK11413 453 paNGQMsaVALM 464
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
30-278 |
5.91e-18 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 86.33 E-value: 5.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 30 VLCHEITTPIAIMDL--MEKGMDRV-FDPNKIKA------VIDH---VtpakD---SKTAAQGKIMRE------------ 82
Cdd:PRK09277 87 VVMQDFTGVPAVVDLaaMRDAIADLgGDPAKINPlvpvdlVIDHsvqV----DyfgTPDAFEKNVELEferneeryqflk 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 83 WAKrqniKDF--FDV---GeNGVCHA-------------------LFPEkgfirpgyTVIMGDSHTcTH-GAFGAFAAGV 137
Cdd:PRK09277 163 WGQ----KAFdnFRVvppG-TGICHQvnleylapvvwtredgelvAYPD--------TLVGTDSHT-TMiNGLGVLGWGV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505217943 138 GTTDLEVGILkGvctfrAPVSMK------VSISGILQNGVSAKDVILAVIKKLTVNGATDKVIEFTGPLVDSMNMSARMT 211
Cdd:PRK09277 229 GGIEAEAAML-G-----QPSSMLipevvgVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRAT 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505217943 212 LCNMAVEAGATSGLCYPDRVTAEYLWQFIKDdyttiDAAVAKFEK-------WH-SDADAEYASVIELDVSELEP 278
Cdd:PRK09277 303 IANMAPEYGATCGFFPIDEETLDYLRLTGRD-----EEQVALVEAyakaqglWRdPLEEPVYTDVLELDLSTVEP 372
|
|
| |
