|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
1-424 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 728.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 1 MGQTISEKIFSEHAGRPVKAGEIVRVDIDMVIGNDITTPISIRAFEESGAKELANPDGFAIVMDHYIPAKDIASANQAKI 80
Cdd:PRK00402 1 MGMTLAEKILARHSGRDVSPGDIVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVIVFDHFVPAKDIKSAEQQKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 81 SRDFALKHNLKYFFDEKDmGIEHALLPEKGLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISFAIITGGNWFKVPETI 160
Cdd:PRK00402 81 LREFAKEQGIPNFFDVGE-GICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKTWFKVPETI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 161 KVELVGKPGPHIYGKDIILEVIRILGVDGALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYLEER 240
Cdd:PRK00402 160 KVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLEYLKER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 241 kkvnggLRAEPKIHTSDPDAEYCQSITIDVEKLSPVIAYPFLPSNGKPVEQAVadRIKIDQVMIGSCTNGRLEDLRIAAE 320
Cdd:PRK00402 240 ------AGRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVE--GTKVDQVFIGSCTNGRLEDLRIAAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 321 IVRGKRVARHTRMIVTPATQRIFMQAEKEGLIDTLIEAGAVVSNPTCGACLGGYMGILGDGEKCVSTTNRNFVGRMGART 400
Cdd:PRK00402 312 ILKGRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGSPE 391
|
410 420
....*....|....*....|....
gi 503318543 401 SEIYLANSAVAAASAIEGYITDPR 424
Cdd:PRK00402 392 SEVYLASPAVAAASAVTGKITDPR 415
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-424 |
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: 657.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 1 MGQTISEKIFSEHAGRPVKAGEIVRVDIDMVIGNDITTPISIRAFEESGAKELANPDGFAIVMDHYIPAKDIASANQAKI 80
Cdd:COG0065 1 MGMTLAEKILARHAGREVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVAVFDHNVPTKDPKSAEQVKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 81 SRDFALKHNLKyFFDEKDMGIEHALLPEKGLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISFAIITGGNWFKVPETI 160
Cdd:COG0065 81 LREFAKEFGIT-FFDVGDPGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWFKVPETM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 161 KVELVGKPGPHIYGKDIILEVIRILGVDGALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYLEER 240
Cdd:COG0065 160 RIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFEYLKGR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 241 KkvngglRAEPKIHTSDPDAEYCQSITIDVEKLSPVIAYPFLPSNGKPVEQaVADrIKIDQVMIGSCTNGRLEDLRIAAE 320
Cdd:COG0065 240 P------FAPWRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE-LEG-IKIDQVFIGSCTNGRIEDLRAAAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 321 IVRGKRVARHTRMIVTPATQRIFMQAEKEGLIDTLIEAGAVVSNPTCGACLGGYMGILGDGEKCVSTTNRNFVGRMGART 400
Cdd:COG0065 312 ILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGSPG 391
|
410 420
....*....|....*....|....
gi 503318543 401 SEIYLANSAVAAASAIEGYITDPR 424
Cdd:COG0065 392 SRTYLASPATAAASAIAGRITDPR 415
|
|
| LEU2 |
TIGR02083 |
3-isopropylmalate dehydratase, large subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
4-424 |
0e+00 |
|
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: 565.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 4 TISEKIFSEHAGR-PVKAGEIVRVDIDMVIGNDITTPISIRAFEESGAKELANPDGFAIVMDHYIPAKDIASANQAKISR 82
Cdd:TIGR02083 2 TMAEKILAQHAGLeSVEPGELILAKLDIVLGNDITTPLAIKAFKEYGGKKVFDPDRVALVPDHFTPNKDIKSAEQCKMMR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 83 DFALKHNLKYFFDEKDMGIEHALLPEKGLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISFAIITGGNWFKVPETIKV 162
Cdd:TIGR02083 82 EFAREQGIEKFFEIGNMGIEHALLPEEGIVKPGDLIIGADSHTCTYGALGAFATGVGSTDMAVGMATGKAWFRVPEAIKF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 163 ELVGKPGPHIYGKDIILEVIRILGVDGALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYLEERKK 242
Cdd:TIGR02083 162 VLKGKLKPWVTGKDLILHIIGIIGVDGALYKSMEFSGEGLKELSMDDRFTIANMAIEAGAKTGIFPVDEITIEYEKGRGK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 243 vngglrAEPKIHTSDPDAEYCQSITIDVEKLSPVIAYPFLPSNGKPVEQAVADRIKIDQVMIGSCTNGRLEDLRIAAEIV 322
Cdd:TIGR02083 242 ------REEKIYKADEDAKYVRVIEIDLSELEPQVAFPHLPENTKDISEAGKEEIKIDQVVIGSCTNGRLEDLRLAAEIL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 323 RGKRVARHTRMIVTPATQRIFMQAEKEGLIDTLIEAGAVVSNPTCGACLGGYMGILGDGEKCVSTTNRNFVGRMGARTSE 402
Cdd:TIGR02083 316 KGKTVAPDVRCIIIPGSQNVYLEAMKEGLLEIFIEAGAVVSTPTCGPCLGGHMGILAEGERAISTTNRNFVGRMGHPKSE 395
|
410 420
....*....|....*....|..
gi 503318543 403 IYLANSAVAAASAIEGYITDPR 424
Cdd:TIGR02083 396 VYLASPAVAAASAIKGYIASPE 417
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
30-420 |
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: 547.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 30 MVIGNDITTPISIRAFEESGAKELANPDGFAIVMDHYIPAKDIASANQAKISRDFALKHNLKyFFDEKDMGIEHALLPEK 109
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAVFDHNVPTPDIKAAEQVKTLRKFAKEFGIN-FFDVGRQGICHVILPEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 110 GLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISFAIITGGNWFKVPETIKVELVGKPGPHIYGKDIILEVIRILGVDG 189
Cdd:cd01583 80 GLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 190 ALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYLEERkkvnggLRAEPKIHTSDPDAEYCQSITID 269
Cdd:cd01583 160 ATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGR------GKAYWKELKSDEDAEYDKVVEID 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 270 VEKLSPVIAYPFLPSNGKPVEQAVAdrIKIDQVMIGSCTNGRLEDLRIAAEIVRGKRVARHTRMIVTPATQRIFMQAEKE 349
Cdd:cd01583 234 ASELEPQVAWPHSPDNVVPVSEVEG--IKIDQVFIGSCTNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKE 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503318543 350 GLIDTLIEAGAVVSNPTCGACLGGYMGILGDGEKCVSTTNRNFVGRMGARTSEIYLANSAVAAASAIEGYI 420
Cdd:cd01583 312 GLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTSNRNFKGRMGSPGARIYLASPATAAASAITGEI 382
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
4-423 |
3.60e-157 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 450.36 E-value: 3.60e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 4 TISEKIFSEHAGRPVKAGEIVRVDIDMVIGNDITTPISIRAFEESGAKeLANPDGFAIVMDHYIPAKDIASANQAKISRD 83
Cdd:NF040615 2 TLAEKILSKKLGKEVYAGDTVEVDVDLAMTHDGTTPLTYKAFKEISDK-VWDNEKIVIVFDHNVPANTVKAANMQKITRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 84 FALKHNLKYFFDEKDmGIEHALLPEKGLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISFAIITGGNWFKVPETIKVE 163
Cdd:NF040615 81 FVKEQGIKNFYLGGE-GICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 164 LVGKpGPHIYGKDIILEVIRILGVDGALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYLEErKKV 243
Cdd:NF040615 160 IVGK-NENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRK-EGV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 244 NGGLRAEPK---IHTSDPDAEYCQSITIDVEKLSPVIAYPFLPSNGKPVEQAVAdrIKIDQVMIGSCTNGRLEDLRIAAE 320
Cdd:NF040615 238 SEEEIAELKknrITVNEKEENYYKEIEIDITDMEEQVACPHHPDNVKPVSEVEG--TEIDQVFIGSCTNGRLSDLRIAAK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 321 IVRGKRVARHTRMIVTPATQRIFMQAEKEGLIDTLIEAGAVVSNPTCGACLGGYMGILGDGEKCVSTTNRNFVGRMGART 400
Cdd:NF040615 316 YLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGNIN 395
|
410 420
....*....|....*....|...
gi 503318543 401 SEIYLANSAVAAASAIEGYITDP 423
Cdd:NF040615 396 SYIYLSSPKIAAKSAVKGYITNE 418
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-400 |
5.43e-112 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 336.31 E-value: 5.43e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 7 EKIFSEHAGRPvKAGEIVRVdIDMVIGNDITTPISIRAFEESGAKeLANPDGFAIVMDHYIP-------AKDIASANQAK 79
Cdd:pfam00330 1 EKIWDAHLVEE-LDGSLLYI-PDRVLMHDVTSPQAFVDLRAAGRA-VRRPGGTPATIDHLVPtdlvidhAPDALDKNIED 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 80 -ISRD---------FALKHNLKYFfdEKDMGIEHALLPEKGLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISFAIIT 149
Cdd:pfam00330 78 eISRNkeqydflewNAKKFGIRFV--PPGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 150 GGNWFKVPETIKVELVGKPGPHIYGKDIILEVIRILGVDGALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAV 229
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 230 DDITLEYLE-----ERKKVNGGLRA-EPKIHTSDPDAEYCQSITIDVEKLSPVIAYPFLPSNGKPVEQAVADR------- 296
Cdd:pfam00330 236 DETTFEYLRatgrpEAPKGEAYDKAvAWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDPfadavkr 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 297 --------------------IKIDQVMIGSCTNGRLEDLRIAAEIVR-----GKRVARHTRMIVTPATQRIFMQAEKEGL 351
Cdd:pfam00330 316 kaaeraleymglgpgtplsdGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEAEGL 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 503318543 352 IDTLIEAGAVVSNPTCGACLGGYmGILGDGEKCVSTTNRNFVGRMGART 400
Cdd:pfam00330 396 DKILEEAGFEWRGPGCSMCIGNS-DRLPPGERCVSSSNRNFEGRQGPGG 443
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
1-424 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 728.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 1 MGQTISEKIFSEHAGRPVKAGEIVRVDIDMVIGNDITTPISIRAFEESGAKELANPDGFAIVMDHYIPAKDIASANQAKI 80
Cdd:PRK00402 1 MGMTLAEKILARHSGRDVSPGDIVEAKVDLVMAHDITGPLAIKEFEKIGGDKVFDPSKIVIVFDHFVPAKDIKSAEQQKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 81 SRDFALKHNLKYFFDEKDmGIEHALLPEKGLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISFAIITGGNWFKVPETI 160
Cdd:PRK00402 81 LREFAKEQGIPNFFDVGE-GICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKTWFKVPETI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 161 KVELVGKPGPHIYGKDIILEVIRILGVDGALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYLEER 240
Cdd:PRK00402 160 KVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLEYLKER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 241 kkvnggLRAEPKIHTSDPDAEYCQSITIDVEKLSPVIAYPFLPSNGKPVEQAVadRIKIDQVMIGSCTNGRLEDLRIAAE 320
Cdd:PRK00402 240 ------AGRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEVE--GTKVDQVFIGSCTNGRLEDLRIAAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 321 IVRGKRVARHTRMIVTPATQRIFMQAEKEGLIDTLIEAGAVVSNPTCGACLGGYMGILGDGEKCVSTTNRNFVGRMGART 400
Cdd:PRK00402 312 ILKGRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGSPE 391
|
410 420
....*....|....*....|....
gi 503318543 401 SEIYLANSAVAAASAIEGYITDPR 424
Cdd:PRK00402 392 SEVYLASPAVAAASAVTGKITDPR 415
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-424 |
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: 657.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 1 MGQTISEKIFSEHAGRPVKAGEIVRVDIDMVIGNDITTPISIRAFEESGAKELANPDGFAIVMDHYIPAKDIASANQAKI 80
Cdd:COG0065 1 MGMTLAEKILARHAGREVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGGRKVWDPDRIVAVFDHNVPTKDPKSAEQVKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 81 SRDFALKHNLKyFFDEKDMGIEHALLPEKGLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISFAIITGGNWFKVPETI 160
Cdd:COG0065 81 LREFAKEFGIT-FFDVGDPGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWFKVPETM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 161 KVELVGKPGPHIYGKDIILEVIRILGVDGALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYLEER 240
Cdd:COG0065 160 RIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFEYLKGR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 241 KkvngglRAEPKIHTSDPDAEYCQSITIDVEKLSPVIAYPFLPSNGKPVEQaVADrIKIDQVMIGSCTNGRLEDLRIAAE 320
Cdd:COG0065 240 P------FAPWRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE-LEG-IKIDQVFIGSCTNGRIEDLRAAAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 321 IVRGKRVARHTRMIVTPATQRIFMQAEKEGLIDTLIEAGAVVSNPTCGACLGGYMGILGDGEKCVSTTNRNFVGRMGART 400
Cdd:COG0065 312 ILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGSPG 391
|
410 420
....*....|....*....|....
gi 503318543 401 SEIYLANSAVAAASAIEGYITDPR 424
Cdd:COG0065 392 SRTYLASPATAAASAIAGRITDPR 415
|
|
| LEU2 |
TIGR02083 |
3-isopropylmalate dehydratase, large subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
4-424 |
0e+00 |
|
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: 565.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 4 TISEKIFSEHAGR-PVKAGEIVRVDIDMVIGNDITTPISIRAFEESGAKELANPDGFAIVMDHYIPAKDIASANQAKISR 82
Cdd:TIGR02083 2 TMAEKILAQHAGLeSVEPGELILAKLDIVLGNDITTPLAIKAFKEYGGKKVFDPDRVALVPDHFTPNKDIKSAEQCKMMR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 83 DFALKHNLKYFFDEKDMGIEHALLPEKGLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISFAIITGGNWFKVPETIKV 162
Cdd:TIGR02083 82 EFAREQGIEKFFEIGNMGIEHALLPEEGIVKPGDLIIGADSHTCTYGALGAFATGVGSTDMAVGMATGKAWFRVPEAIKF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 163 ELVGKPGPHIYGKDIILEVIRILGVDGALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYLEERKK 242
Cdd:TIGR02083 162 VLKGKLKPWVTGKDLILHIIGIIGVDGALYKSMEFSGEGLKELSMDDRFTIANMAIEAGAKTGIFPVDEITIEYEKGRGK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 243 vngglrAEPKIHTSDPDAEYCQSITIDVEKLSPVIAYPFLPSNGKPVEQAVADRIKIDQVMIGSCTNGRLEDLRIAAEIV 322
Cdd:TIGR02083 242 ------REEKIYKADEDAKYVRVIEIDLSELEPQVAFPHLPENTKDISEAGKEEIKIDQVVIGSCTNGRLEDLRLAAEIL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 323 RGKRVARHTRMIVTPATQRIFMQAEKEGLIDTLIEAGAVVSNPTCGACLGGYMGILGDGEKCVSTTNRNFVGRMGARTSE 402
Cdd:TIGR02083 316 KGKTVAPDVRCIIIPGSQNVYLEAMKEGLLEIFIEAGAVVSTPTCGPCLGGHMGILAEGERAISTTNRNFVGRMGHPKSE 395
|
410 420
....*....|....*....|..
gi 503318543 403 IYLANSAVAAASAIEGYITDPR 424
Cdd:TIGR02083 396 VYLASPAVAAASAIKGYIASPE 417
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
30-420 |
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: 547.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 30 MVIGNDITTPISIRAFEESGAKELANPDGFAIVMDHYIPAKDIASANQAKISRDFALKHNLKyFFDEKDMGIEHALLPEK 109
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREKVWDPEKIVAVFDHNVPTPDIKAAEQVKTLRKFAKEFGIN-FFDVGRQGICHVILPEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 110 GLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISFAIITGGNWFKVPETIKVELVGKPGPHIYGKDIILEVIRILGVDG 189
Cdd:cd01583 80 GLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYIIGKIGVDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 190 ALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYLEERkkvnggLRAEPKIHTSDPDAEYCQSITID 269
Cdd:cd01583 160 ATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGR------GKAYWKELKSDEDAEYDKVVEID 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 270 VEKLSPVIAYPFLPSNGKPVEQAVAdrIKIDQVMIGSCTNGRLEDLRIAAEIVRGKRVARHTRMIVTPATQRIFMQAEKE 349
Cdd:cd01583 234 ASELEPQVAWPHSPDNVVPVSEVEG--IKIDQVFIGSCTNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKE 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503318543 350 GLIDTLIEAGAVVSNPTCGACLGGYMGILGDGEKCVSTTNRNFVGRMGARTSEIYLANSAVAAASAIEGYI 420
Cdd:cd01583 312 GLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTSNRNFKGRMGSPGARIYLASPATAAASAITGEI 382
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
4-424 |
0e+00 |
|
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: 545.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 4 TISEKIFSEHAGRPVKAGEIVRVDIDMVIGNDITTPISIRAFEESGAKELANPDGFAIVMDHYIPAKDIASANQAKISRD 83
Cdd:TIGR01343 1 TIAEKILSKKSGKEVYAGDLIEAEIDLAMVHDITAPLAIKTLEEYGIDKVWNPEKIVIVFDHQVPADTIKAAEMQKLARE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 84 FALKHNLKYFFDEKDmGIEHALLPEKGLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISFAIITGGNWFKVPETIKVE 163
Cdd:TIGR01343 81 FVKKQGIKYFYDVGE-GICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFKVPETIRVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 164 LVGKPGPHIYGKDIILEVIRILGVDGALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYLEERKKV 243
Cdd:TIGR01343 160 ITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYLKERRKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 244 ngglraEPKIHTSDPDAEYCQSITIDVEKLSPVIAYPFLPSNGKPVeqAVADRIKIDQVMIGSCTNGRLEDLRIAAEIVR 323
Cdd:TIGR01343 240 ------PFRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPV--SEVEGTEIDQVFIGSCTNGRLEDLRVAAKILK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 324 GKRVARHTRMIVTPATQRIFMQAEKEGLIDTLIEAGAVVSNPTCGACLGGYMGILGDGEKCVSTTNRNFVGRMGARTSEI 403
Cdd:TIGR01343 312 GRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMGHPNAEI 391
|
410 420
....*....|....*....|.
gi 503318543 404 YLANSAVAAASAIEGYITDPR 424
Cdd:TIGR01343 392 YLASPATAAASAVKGYIADPR 412
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
3-424 |
1.66e-177 |
|
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: 501.60 E-value: 1.66e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 3 QTISEKIFSEHAGRPVKAGEIVRVDIDMVIGNDITTPISIRAFEESGAKELANPDGFAIVMDHYIPAKDIASANQAKISR 82
Cdd:TIGR02086 1 MTLAEKILSEKVGRPVCAGEIVEVEVDLAMTHDGTGPLAIKALRELGVARVWDPEKIVIAFDHNVPPPTVEAAEMQKEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 83 DFALKHNLKYFfdEKDMGIEHALLPEKGLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISFAIITGGNWFKVPETIKV 162
Cdd:TIGR02086 81 EFAKRHGIKNF--DVGEGICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTWIKVPETIRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 163 ELVGKPGPHIYGKDIILEVIRILGVDGALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYLEERKk 242
Cdd:TIGR02086 159 VVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEETYEYLKKRR- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 243 vngglRAEPKIHTSDPDAEYCQSITIDVEKLSPVIAYPFLPSNGKPVEQavADRIKIDQVMIGSCTNGRLEDLRIAAEIV 322
Cdd:TIGR02086 238 -----GLEFRILVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVSD--VEGTEIDQVFIGSCTNGRLEDLRIAAEIL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 323 RGKRVARHTRMIVTPATQRIFMQAEKEGLIDTLIEAGAVVSNPTCGACLGGYMGILGDGEKCVSTTNRNFVGRMGARTSE 402
Cdd:TIGR02086 311 KGRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAGAMICPPGCGPCLGAHMGVLGDGEVCLSTTNRNFKGRMGSPNAE 390
|
410 420
....*....|....*....|..
gi 503318543 403 IYLANSAVAAASAIEGYITDPR 424
Cdd:TIGR02086 391 IYLASPATAAASAVEGYITDPE 412
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
4-423 |
3.60e-157 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 450.36 E-value: 3.60e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 4 TISEKIFSEHAGRPVKAGEIVRVDIDMVIGNDITTPISIRAFEESGAKeLANPDGFAIVMDHYIPAKDIASANQAKISRD 83
Cdd:NF040615 2 TLAEKILSKKLGKEVYAGDTVEVDVDLAMTHDGTTPLTYKAFKEISDK-VWDNEKIVIVFDHNVPANTVKAANMQKITRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 84 FALKHNLKYFFDEKDmGIEHALLPEKGLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISFAIITGGNWFKVPETIKVE 163
Cdd:NF040615 81 FVKEQGIKNFYLGGE-GICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 164 LVGKpGPHIYGKDIILEVIRILGVDGALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYLEErKKV 243
Cdd:NF040615 160 IVGK-NENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRK-EGV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 244 NGGLRAEPK---IHTSDPDAEYCQSITIDVEKLSPVIAYPFLPSNGKPVEQAVAdrIKIDQVMIGSCTNGRLEDLRIAAE 320
Cdd:NF040615 238 SEEEIAELKknrITVNEKEENYYKEIEIDITDMEEQVACPHHPDNVKPVSEVEG--TEIDQVFIGSCTNGRLSDLRIAAK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 321 IVRGKRVARHTRMIVTPATQRIFMQAEKEGLIDTLIEAGAVVSNPTCGACLGGYMGILGDGEKCVSTTNRNFVGRMGART 400
Cdd:NF040615 316 YLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGNIN 395
|
410 420
....*....|....*....|...
gi 503318543 401 SEIYLANSAVAAASAIEGYITDP 423
Cdd:NF040615 396 SYIYLSSPKIAAKSAVKGYITNE 418
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-400 |
5.43e-112 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 336.31 E-value: 5.43e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 7 EKIFSEHAGRPvKAGEIVRVdIDMVIGNDITTPISIRAFEESGAKeLANPDGFAIVMDHYIP-------AKDIASANQAK 79
Cdd:pfam00330 1 EKIWDAHLVEE-LDGSLLYI-PDRVLMHDVTSPQAFVDLRAAGRA-VRRPGGTPATIDHLVPtdlvidhAPDALDKNIED 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 80 -ISRD---------FALKHNLKYFfdEKDMGIEHALLPEKGLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISFAIIT 149
Cdd:pfam00330 78 eISRNkeqydflewNAKKFGIRFV--PPGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 150 GGNWFKVPETIKVELVGKPGPHIYGKDIILEVIRILGVDGALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAV 229
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 230 DDITLEYLE-----ERKKVNGGLRA-EPKIHTSDPDAEYCQSITIDVEKLSPVIAYPFLPSNGKPVEQAVADR------- 296
Cdd:pfam00330 236 DETTFEYLRatgrpEAPKGEAYDKAvAWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDPfadavkr 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 297 --------------------IKIDQVMIGSCTNGRLEDLRIAAEIVR-----GKRVARHTRMIVTPATQRIFMQAEKEGL 351
Cdd:pfam00330 316 kaaeraleymglgpgtplsdGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEAEGL 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 503318543 352 IDTLIEAGAVVSNPTCGACLGGYmGILGDGEKCVSTTNRNFVGRMGART 400
Cdd:pfam00330 396 DKILEEAGFEWRGPGCSMCIGNS-DRLPPGERCVSSSNRNFEGRQGPGG 443
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
1-425 |
4.12e-108 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 326.86 E-value: 4.12e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 1 MGQTISEKIFSEHAGRPVKAGEIVrVDIDMVIGNDITTPISIRAFEESGAKeLANPDGFAIVMDHYIP--------AKDI 72
Cdd:PRK12466 2 MPRTLYDKLWDSHTVARLDDGHVL-LYIDRHLLNEYTSPQAFSGLRARGRT-VRRPDLTLAVVDHVVPtrpgrdrgITDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 73 ASANQAKISRDFALKHNLKYF-FDEKDMGIEHALLPEKGLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISFAIITGG 151
Cdd:PRK12466 80 GGALQVDYLRENCADFGIRLFdVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 152 NWFKVPETIKVELVGKPGPHIYGKDIILEVIRILGVDGALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDD 231
Cdd:PRK12466 160 LVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 232 ITLEYLEERKKVNGGLRAEPKIH-----TSDPDAEYCQSITIDVEKLSPVI--------------AYPFLPSNGKPVEQA 292
Cdd:PRK12466 240 TTFDYLRGRPRAPKGALWDAALAywrtlRSDADAVFDREVEIDAADIAPQVtwgtspdqavpitgRVPDPAAEADPARRA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 293 VADR---------------IKIDQVMIGSCTNGRLEDLRIAAEIVRGKRVARHTRMIVTPATQRIFMQAEKEGLIDTLIE 357
Cdd:PRK12466 320 AMERaldymgltpgtplagIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503318543 358 AGAVVSNPTCGACLGgyMG--ILGDGEKCVSTTNRNFVGRMG--ARTseiYLANSAVAAASAIEGYITDPRA 425
Cdd:PRK12466 400 AGFEWREPGCSMCLA--MNddVLAPGERCASTTNRNFEGRQGpgART---HLMSPAMVAAAAVAGHITDVRS 466
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-424 |
2.36e-102 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 312.05 E-value: 2.36e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 1 MGQTISEKIFSEHAGRPVKAGE-IVRVDIDMVigNDITTPisiRAFE---ESGAKeLANPD-GFAiVMDHYIPAKDIASA 75
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPdLLYIDRHLV--HEVTSP---QAFEglrLAGRK-VRRPDlTFA-TMDHNVPTTDRDLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 76 NQAKISRDF--ALKHNLKYF------FDEKDMGIEHALLPEKGLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISFAI 147
Cdd:PRK05478 74 IADPVSRIQveTLEKNCKEFgitlfdLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 148 ITGGNWFKVPETIKVELVGKPGPHIYGKDIILEVIRILGVDGALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGII 227
Cdd:PRK05478 154 ATQTLLQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 228 AVDDITLEYLEERKKVNGGL---RAEPKIHT--SDPDAEYCQSITIDVEKLSPVIAY--------------PFLPSNGKP 288
Cdd:PRK05478 234 APDETTFEYLKGRPFAPKGEdwdKAVAYWKTlkSDEDAVFDKVVTLDAADIEPQVTWgtnpgqvisidgkvPDPEDFADP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 289 VEQAVADR---------------IKIDQVMIGSCTNGRLEDLRIAAEIVRGKRVARHTRMIVTPATQRIFMQAEKEGLID 353
Cdd:PRK05478 314 VKRASAERalaymglkpgtpitdIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDK 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503318543 354 TLIEAGAVVSNPTCGACLGgyMG--ILGDGEKCVSTTNRNFVGRMG--ARTseiYLANSAVAAASAIEGYITDPR 424
Cdd:PRK05478 394 IFIEAGFEWREPGCSMCLA--MNpdKLPPGERCASTSNRNFEGRQGkgGRT---HLVSPAMAAAAAITGHFVDVR 463
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
1-424 |
1.23e-95 |
|
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: 294.84 E-value: 1.23e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 1 MGQTISEKIFSEHAgrpVKAGE----IVRVDIDMVigNDITTPisiRAFE--ESGAKELANPDGFAIVMDHYIP--AKDI 72
Cdd:TIGR00170 1 MPRTLYEKLFDAHI---VYEAEgetpLLYIDRHLI--HEVTSP---QAFEglRQAGRKVRRPQKTFATMDHNIPtqNRDF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 73 -ASANQAKISRDfALKHNLKYF----FD--EKDMGIEHALLPEKGLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISF 145
Cdd:TIGR00170 73 nIKDEVAKIQVT-ELEKNCKEFgvrlFDlhSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 146 AIITGGNWFKVPETIKVELVGKPGPHIYGKDIILEVIRILGVDGALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNG 225
Cdd:TIGR00170 152 VLATQTLKQARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 226 IIAVDDITLEYLEERKKVNGGLR-----AEPKIHTSDPDAEYCQSITIDVEKLSPVIAY-----PFLPSNGK-------- 287
Cdd:TIGR00170 232 LIAPDETTFEYCKGRPHAPKGKEfdkavAYWKTLKTDEGAVFDTVITLEANDISPQVTWgtnpgQVLPVNSEvpdpesfa 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 288 -PVEQAVADR---------------IKIDQVMIGSCTNGRLEDLRIAAEIVRGKRVARHTRMIVTPATQRIFMQAEKEGL 351
Cdd:TIGR00170 312 dPVDKASAERalaymglepgtplkdIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGL 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503318543 352 IDTLIEAGAVVSNPTCGACLGGYMGILGDGEKCVSTTNRNFVGRMGaRTSEIYLANSAVAAASAIEGYITDPR 424
Cdd:TIGR00170 392 DKIFIEAGFEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQG-RGGRTHLVSPAMAAAAAIHGHFVDIR 463
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
31-405 |
2.48e-95 |
|
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: 291.32 E-value: 2.48e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 31 VIGNDITTPISIRAFEESGAKELANpDGFAIVMDHY--IPAKDIASANQAKISRDFAlkHNLKYFFDEKDMGIEHALLPE 108
Cdd:cd01351 2 VMLQDATGPMAMKAFEILAALGKVA-DPSQIACVHDhaVQLEKPVNNEGHKFLSFFA--ALQGIAFYRPGVGIIHQIMVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 109 KgLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISFAIITGGNWFKVPETIKVELVGKPGPHIYGKDIILEVIRILGVD 188
Cdd:cd01351 79 N-LALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLGGIVGVD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 189 GALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYLEERKKVNGGLRAE--PKIHTSDPDAEYCQSI 266
Cdd:cd01351 158 GVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWLafPEELLADEGAEYDQVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 267 TIDVEKLSPVIAYPFLPSNGKPVEQavADRIKIDQVMIGSCTNGRLEDLRIAAEIVRGKRVARHTRMIVTPATQRIFMQA 346
Cdd:cd01351 238 EIDLSELEPDISGPNRPDDAVSVSE--VEGTKIDQVLIGSCTNNRYSDMLAAAKLLKGAKVAPGVRLIVTPGSRMVYATL 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 503318543 347 EKEGLIDTLIEAGAVVSNPTCGACLGGYMGILGDGEKCVSTTNRNFVGRMGARTSEIYL 405
Cdd:cd01351 316 SREGYYEILVDSGARILPPGCGPCMGNGARLVADGEVGVSSGNRNFPGRLGTYERHVYL 374
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
1-424 |
5.75e-84 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 269.71 E-value: 5.75e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 1 MGQTISEKIFSEH--AGRPVkAGEIVRVDIDMVIGNDITTPISIRAFEESGAKELANPDGFAIVmDHYIPAKDIASANQA 78
Cdd:PRK07229 1 MGLTLTEKILYAHlvEGELE-PGEEIAIRIDQTLTQDATGTMAYLQFEAMGLDRVKTELSVQYV-DHNLLQADFENADDH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 79 KISRDFALKHNLkyFFDEKDMGIEHALLPEKgLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISFAIiTGGNWF-KVP 157
Cdd:PRK07229 79 RFLQSVAAKYGI--YFSKPGNGICHQVHLER-FAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAM-AGGPYYlKMP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 158 ETIKVELVGKPGPHIYGKDIILEVIRILGVDGALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYL 237
Cdd:PRK07229 155 KVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 238 E--ERKKVNGGLRAepkihtsDPDAEYCQSITIDVEKLSPVIAYPFLPSNGKPVEQaVADrIKIDQVMIGSCTNGRLEDL 315
Cdd:PRK07229 235 KaqGREDDWVELLA-------DPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSE-VAG-IKVDQVLIGSCTNSSYEDL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 316 RIAAEIVRGKRVARHTRMIVTPATQRIFMQAEKEGLIDTLIEAGAVVSNPTCGACLGgyMGILGdGEKCVS--TTNRNFV 393
Cdd:PRK07229 306 MRAASILKGKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIG--MGQAP-ATGNVSlrTFNRNFP 382
|
410 420 430
....*....|....*....|....*....|.
gi 503318543 394 GRMGARTSEIYLANSAVAAASAIEGYITDPR 424
Cdd:PRK07229 383 GRSGTKDAQVYLASPETAAASALTGVITDPR 413
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
29-420 |
6.08e-77 |
|
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: 243.90 E-value: 6.08e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 29 DMVIGNDITTPISIRAFEESGAKELANPDGFAIVmDHYIPAKDIASANQAKISRDFALKHNLkyFFDEKDMGIEHALLPE 108
Cdd:cd01585 1 DQTLTQDATGTMAYLQFEAMGVDRVRTELSVSYV-DHNTLQTDFENADDHRFLQTVAARYGI--YFSRPGNGICHQVHLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 109 KgLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISFAIITGGNWFKVPETIKVELVGKPGPHIYGKDIILEVIRILGVD 188
Cdd:cd01585 78 R-FAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 189 GALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYLEERKKVNGGLRAEPkihtsDPDAEYCQSITI 268
Cdd:cd01585 157 GGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGREDDWVELAA-----DADAEYDEEIEI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 269 DVEKLSPVIAYPFLPSNGKPVEQavADRIKIDQVMIGSCTNGRLEDLRIAAEIVRGKRVARHTRMIVTPATQRIFMQAEK 348
Cdd:cd01585 232 DLSELEPLIARPHSPDNVVPVRE--VAGIKVDQVAIGSCTNSSYEDLMTVAAILKGRRVHPHVSMVVAPGSKQVLEMLAR 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503318543 349 EGLIDTLIEAGAVVSNPTCGACLGgyMG-ILGDGEKCVSTTNRNFVGRMGARTSEIYLANSAVAAASAIEGYI 420
Cdd:cd01585 310 NGALADLLAAGARILESACGPCIG--MGqAPPTGGVSVRTFNRNFEGRSGTKDDLVYLASPEVAAAAALTGVI 380
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
31-420 |
1.09e-61 |
|
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: 203.61 E-value: 1.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 31 VIGNDITTPISIRaFEESGAKELANPDGFAIVMDHYIPAKDIASANQAKISRDFALKHNLKYFfdEKDMGIEHALLPEKG 110
Cdd:cd01582 2 CMTHDNSWPVALK-FMSIGATKIHNPDQIVMTLDHDVQNKSEKNLKKYKNIESFAKKHGIDFY--PAGRGIGHQIMIEEG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 111 LVVPGDVIIGADSHTCTHGALGAFSTGMGSTDISFAIITGGNWFKVPETIKVELVGKPGPHIYGKDIILEVIRILGVDGA 190
Cdd:cd01582 79 YAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCGLFNKDQV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 191 LYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDditleyleerkkvngglraepkihtsdpdaeyCQSITIDV 270
Cdd:cd01582 159 LNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTD--------------------------------AKHLILDL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 271 EKLSPVIAYPFLPSNGKPVEQAVADRIKIDQVMIGSCTNGRLEDLRIAAEIVRGKR-------VARHTRMIVTPATQRIF 343
Cdd:cd01582 207 STLSPYVSGPNSVKVSTPLKELEAQNIKINKAYLVSCTNSRASDIAAAADVVKGKKekngkipVAPGVEFYVAAASSEVQ 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503318543 344 MQAEKEGLIDTLIEAGAVVSNPTCGACLGGYMGILGDGEKCVSTTNRNFVGRMGARTSEIYLANSAVAAASAIEGYI 420
Cdd:cd01582 287 AAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQGLLEPGEVGISATNRNFKGRMGSTEALAYLASPAVVAASAISGKI 363
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
35-395 |
6.68e-40 |
|
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: 147.20 E-value: 6.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 35 DITTPISIRAFEESGAKELANPDgfAIVMDHYIPA-----KDIASAN-QAKISRDFALKHNLKYF--FDEKDMGIEHALL 106
Cdd:cd01584 6 DATAQMALLQFMSSGLPKVAVPS--TIHCDHLIEAqvggeKDLKRAKdINKEVYDFLASAGAKYGigFWKPGSGIIHQIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 107 PEKgLVVPGDVIIGADSHTCTHGALGAFSTGMGSTDiSFAIITGGNW-FKVPETIKVELVGKPGPHIYGKDIILEVIRIL 185
Cdd:cd01584 84 LEN-YAFPGLLMIGTDSHTPNAGGLGGIAIGVGGAD-AVDVMAGIPWeLKCPKVIGVKLTGKLSGWTSPKDVILKVAGIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 186 GVDGALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYLEE--RKKVNGGLRA-EPKIHTSDPDAEY 262
Cdd:cd01584 162 TVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKAtgRAEIADLADEfKDDLLVADEGAEY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 263 CQSITIDVEKLSPVIAYPFLPSNGKPVEQ--AVADR----IKIDQVMIGSCTNGRLEDLRIAAEIVR---GKRVARHTRM 333
Cdd:cd01584 242 DQLIEINLSELEPHINGPFTPDLATPVSKfkEVAEKngwpLDLRVGLIGSCTNSSYEDMGRAASIAKqalAHGLKCKSIF 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503318543 334 IVTPATQRIFMQAEKEGLIDTLIEAGAVVSNPTCGACLGGY--MGI-LGDGEKCVSTTNRNFVGR 395
Cdd:cd01584 322 TITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQWdrKDIkKGEKNTIVTSYNRNFTGR 386
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
115-399 |
2.15e-30 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 123.97 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 115 GDVIIGADSHTcTHGALGAFSTGMGSTDISFAIItGGNW-FKVPETIKVELVGKPGPHIYGKDIILEVIrilgvdGALY- 192
Cdd:PRK11413 142 GKMILGSDSHT-RYGALGTMAVGEGGGELVKQLL-NDTYdIDYPGVVAVYLTGKPAPGVGPQDVALAII------GAVFk 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 193 ------KALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYLEERKKVNGGLRAEPKihtsdPDAEYCQSI 266
Cdd:PRK11413 214 ngyvknKVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLALHGRGQDYCELNPQ-----PMAYYDGCI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 267 TIDVEKLSPVIAYPFLPSN--------------------------GKPVEQAVADRI-----KIDQVMIGSCTNGRLEDL 315
Cdd:PRK11413 289 SVDLSAIKPMIALPFHPSNvyeidelnqnltdilreveieservaHGKAKLSLLDKIengrlKVQQGIIAGCSGGNYENV 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 316 RIAAEIVRGKRV-ARHTRMIVTPATQRIFMQAEKEGLIDTLIEAGAVVSNPTCGACLGGymgilGD----GEKCVSTTNR 390
Cdd:PRK11413 369 IAAANALRGQSCgNDTFSLSVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFGA-----GDtpanNGLSIRHTTR 443
|
....*....
gi 503318543 391 NFVGRMGAR 399
Cdd:PRK11413 444 NFPNREGSK 452
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
83-405 |
1.75e-29 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 121.44 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 83 DFALKHNLKYFFDEKDmGIehALLPEKG--------LVVPGDVIIGADSHTcthgalgAFSTGM----GSTDISFAIITG 150
Cdd:PRK09238 442 DVKTHHTLPDFIMNRG-GV--SLRPGDGvihswlnrMLLPDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFAAATG 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 151 GNWFKVPETIKVELVGKPGPHIYGKDII------------LEVI----------RILGVDGalykaleftgdtLKYLSMD 208
Cdd:PRK09238 512 VMPLDMPESVLVRFKGEMQPGITLRDLVhaipyyaikqglLTVEkkgkknifsgRILEIEG------------LPDLKVE 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 209 DRFSICNMAIEAGAKNGIIAVDDITL-EYLE--------------------ER--KKVNGGLrAEPKIHTSDPDAEYCQS 265
Cdd:PRK09238 580 QAFELTDASAERSAAGCTIKLSKEPIiEYLRsnivllkwmiaegygdartlERriAAMEEWL-ANPELLEADADAEYAAV 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 266 ITIDVEKLS-PVIAYPFLPSNGKPVEQAVADriKIDQVMIGSC-TNgrLEDLRIAAEIVRGKRVARHTRMIVTPATQRIF 343
Cdd:PRK09238 659 IEIDLAEIKePILACPNDPDDVRLLSEVAGT--KIDEVFIGSCmTN--IGHFRAAGKLLEGKKGQLPTRLWVAPPTKMDA 734
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503318543 344 MQAEKEGLIDTLIEAGAVVSNPTCGACLGGYMGIlGDGEKCVSTTNRNFVGRMGARTsEIYL 405
Cdd:PRK09238 735 DQLTEEGYYSIFGKAGARIEMPGCSLCMGNQARV-ADGATVFSTSTRNFPNRLGKGA-NVYL 794
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
100-405 |
3.82e-29 |
|
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: 117.98 E-value: 3.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 100 GIEHALLPEkgLVVPGDVIIGADSHTctHGALGaFSTGMGSTDISFAIITGGNWFKVPETIKVELVGKPGPHIYGKDII- 178
Cdd:cd01581 94 GVIHSWLNR--MLLPDTVGTGGDSHT--RFPIG-ISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVn 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 179 -----------LEVIRILGVDGALYKALEFTGdtLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITL-EYLEERKKV--- 243
Cdd:cd01581 169 aipyyaiqqglLTVEKKGKKNVFNGRILEIEG--LPDLKVEQAFELTDASAERSAAACTVRLDKEPViEYLESNVVLmki 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 244 ---NG---------------GLRAEPKIHTSDPDAEYCQSITIDVEKLS-PVIAYPFLPSNGKPVEQAVADriKIDQVMI 304
Cdd:cd01581 247 miaNGyddartllrriiameEWLANPPLLEPDADAEYAAVIEIDLDDIKePILACPNDPDDVKLLSEVAGK--KIDEVFI 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 305 GSC-TNgrLEDLRIAAEIVRGKRVARhTRMIVTPATQRIFMQAEKEGLIDTLIEAGAVVSNPTCGACLGGYMGIlGDGEK 383
Cdd:cd01581 325 GSCmTN--IGHFRAAAKILRGKEFKP-TRLWVAPPTRMDWAILQEEGYYSIFGDAGARTEMPGCSLCMGNQARV-ADGAT 400
|
330 340
....*....|....*....|..
gi 503318543 384 CVSTTNRNFVGRMGaRTSEIYL 405
Cdd:cd01581 401 VFSTSTRNFDNRVG-KGAEVYL 421
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
110-395 |
5.52e-23 |
|
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: 101.72 E-value: 5.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 110 GLVVPGDVIIGADSHTCTHGALGAFSTGMGSTD---------ISfaiitggnwFKVPETIKVELVGKPGPHIYGKDIILE 180
Cdd:COG1048 198 ETVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEaeaamlgqpVS---------MLIPEVVGVKLTGKLPEGVTATDLVLT 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 181 VIRIL---GVDGalyKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYL------EERKKV------NG 245
Cdd:COG1048 269 VTEMLrkkGVVG---KFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLrltgrsEEQIELveayakAQ 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 246 GLRAEPkihtSDPDAEYCQSITIDVEKLSPVIAYPFLP-------------------SNGKPVEQAVADRIKIDQVM--- 303
Cdd:COG1048 346 GLWRDP----DAPEPYYSDVLELDLSTVEPSLAGPKRPqdriplsdlkeafraalaaPVGEELDKPVRVEVDGEEFElgh 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 304 -------IGSCTNGRLEDLRIAAEIV------RGKRVARHTRMIVTPATQRIFMQAEKEGLIDTLIEAGA-VVSNpTCGA 369
Cdd:COG1048 422 gavviaaITSCTNTSNPSVMIAAGLLakkaveKGLKVKPWVKTSLAPGSKVVTDYLERAGLLPYLEALGFnVVGY-GCTT 500
|
330 340 350
....*....|....*....|....*....|....*.
gi 503318543 370 CLG--G------YMGILGDGEKCVSTT--NRNFVGR 395
Cdd:COG1048 501 CIGnsGplppeiSEAIEENDLVVAAVLsgNRNFEGR 536
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
89-405 |
1.98e-21 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 97.00 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 89 NLKYffdekdmgIEHALLPEKGLVVPgDVIIGADSHTCTHGALGAFSTGMGSTD---------ISFAIitggnwfkvPET 159
Cdd:PTZ00092 191 NLEY--------LARVVFNKDGLLYP-DSVVGTDSHTTMINGLGVLGWGVGGIEaeavmlgqpISMVL---------PEV 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 160 IKVELVGKPGPHIYGKDIILEVIRILGVDGALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYL-- 237
Cdd:PTZ00092 253 VGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLkq 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 238 -----EERKKVNGGLRAEPKIHTSDPDAEYCQSITIDVEKLSPVIAYPFLPSNGKPV----------------------- 289
Cdd:PTZ00092 333 tgrseEKVELIEKYLKANGLFRTYAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLsdlkkdftaclsapvgfkgfgip 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 290 EQAVADRIKID-----------QVMIG---SCTNGRLEDLRIAAEIV------RGKRVARHTRMIVTPATQRIFMQAEKE 349
Cdd:PTZ00092 413 EEKHEKKVKFTykgkeytlthgSVVIAaitSCTNTSNPSVMLAAGLLakkaveKGLKVPPYIKTSLSPGSKVVTKYLEAS 492
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503318543 350 GLIDTLIEAGAVVSNPTCGACLGGYMGILGDGEKCVS----------TTNRNFVGRMGARTSEIYL 405
Cdd:PTZ00092 493 GLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITnndlvaaavlSGNRNFEGRVHPLTRANYL 558
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
100-423 |
2.19e-21 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 96.92 E-value: 2.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 100 GIEHALLPEkgLVVPGDVIIGADSHTcthgalgAFSTGM----GSTDISFAIITGGNWFKVPETIKVELVGKPGPHIYGK 175
Cdd:PLN00094 540 GVIHSWLNR--MLLPDTVGTGGDSHT-------RFPIGIsfpaGSGLVAFGAATGVIPLDMPESVLVRFTGTMQPGITLR 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 176 DIILEVIRILGVDGALYKALE-----FTG-----DTLKYLSMDDRFSICNMAIEAGAKNGIIAVDD-------------- 231
Cdd:PLN00094 611 DLVHAIPYTAIQDGLLTVEKKgkknvFSGrileiEGLPHLKCEQAFELSDASAERSAAGCTIKLDKepiieylnsnvvml 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 232 ---ITLEY-----LEERKKVNGGLRAEPKIHTSDPDAEYCQSITIDVEKLS-PVIAYPFLPSNGKPVEQAVADriKIDQV 302
Cdd:PLN00094 691 kwmIAEGYgdrrtLERRIARMQQWLADPELLEADPDAEYAAVIEIDMDEIKePILCAPNDPDDARLLSEVTGD--KIDEV 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 303 MIGSC-TNgrLEDLRIAAEIVRGKRVARHTRMIVTPATQRIFMQAEKEGLIDTLIEAGAVVSNPTCGACLGGYMGIlgdG 381
Cdd:PLN00094 769 FIGSCmTN--IGHFRAAGKLLNDNLSQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPGCSLCMGNQARV---A 843
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 503318543 382 EKC--VSTTNRNFVGRMGaRTSEIYLANSAVAAASAIEGYITDP 423
Cdd:PLN00094 844 EKStvVSTSTRNFPNRLG-KGANVYLASAELAAVAAILGRLPTV 886
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
108-405 |
3.26e-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: 3.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 108 EKGLVVPgDVIIGADSHTCTHGALGAFSTGMGSTDISFAIITGGNWFKVPETIKVELVGKPGPHIYGKDIIL---EVIRI 184
Cdd:cd01586 115 GDGVAYP-DSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTGKLRPGVTATDLVLtvtQMLRK 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 185 LGVDGalyKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDitleyleerkkvngglraepkihtsdpdaeycQ 264
Cdd:cd01586 194 VGVVG---KFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVDT--------------------------------Q 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 265 SITIDVEKLSPVIAYPFLPSngkpveqavaDRIKIDQVM----IGSCTNGRLEDLRIAAEIV------RGKRVARHTRMI 334
Cdd:cd01586 239 VVELDLSTVEPSVSGPKRPQ----------DRVPLHGSVviaaITSCTNTSNPSVMLAAGLLakkaveLGLKVKPYVKTS 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 335 VTPATQRIFMQAEKEGLIDTLIEAGAVVSNPTCGACLGGyMGILGDG-EKCVS----------TTNRNFVGRMGARTSEI 403
Cdd:cd01586 309 LAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGN-SGPLPEEvEEAIKendlvvaavlSGNRNFEGRIHPLVRAN 387
|
..
gi 503318543 404 YL 405
Cdd:cd01586 388 YL 389
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
116-395 |
1.57e-19 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 91.15 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 116 DVIIGADSHTCTHGALGAFSTGMGSTDISFAIITGGNWFKVPETIKVELVGKPGPHIYGKDIIL---EVIRILGVDGaly 192
Cdd:PRK12881 206 DTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIPDVVGVELTGKLREGVTATDLVLtvtEMLRKEGVVG--- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 193 KALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYL-------EERKKVNGGLRAEPKIHTSDPDAEYCQS 265
Cdd:PRK12881 283 KFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLrltgrteAQIALVEAYAKAQGLWGDPKAEPRYTRT 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 266 ITIDVEKLSPVIAYPFLPSN------------------------GKPVEQAVADRIKIDQVMIG---SCTNGRLEDLRIA 318
Cdd:PRK12881 363 LELDLSTVAPSLAGPKRPQDrialgnvksafsdlfskpvaengfAKKAQTSNGVDLPDGAVAIAaitSCTNTSNPSVLIA 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 319 AEIV------RGKRVARHTRMIVTPATQRIFMQAEKEGLIDTLIEAGAVVSNPTCGACLG--GYM------GILGDGEKC 384
Cdd:PRK12881 443 AGLLakkaveRGLTVKPWVKTSLAPGSKVVTEYLERAGLLPYLEKLGFGIVGYGCTTCIGnsGPLtpeieqAITKNDLVA 522
|
330
....*....|...
gi 503318543 385 VS--TTNRNFVGR 395
Cdd:PRK12881 523 AAvlSGNRNFEGR 535
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
116-283 |
1.07e-17 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 85.56 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 116 DVIIGADSHTcTH-GALGAFSTGMGstdisfaiitG--------GN--WFKVPETIKVELVGKPGPHIYGKDIILEVIRI 184
Cdd:PRK09277 206 DTLVGTDSHT-TMiNGLGVLGWGVG----------GieaeaamlGQpsSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEM 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 185 L---GVDGalyKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYLeerkKVNGglRAEPKI-------- 253
Cdd:PRK09277 275 LrkkGVVG---KFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYL----RLTG--RDEEQValveayak 345
|
170 180 190
....*....|....*....|....*....|....*
gi 503318543 254 -----HTSDPDAEYCQSITIDVEKLSPVIAYPFLP 283
Cdd:PRK09277 346 aqglwRDPLEEPVYTDVLELDLSTVEPSLAGPKRP 380
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
109-405 |
1.32e-15 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 79.08 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 109 KGLVVPgDVIIGADSHTCTHGALGAFSTGMGSTDISFAIITGGNWFKVPETIKVELVGKPGPHIYGKDIILEVIRILGVD 188
Cdd:PLN00070 235 DGILYP-DSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKH 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 189 GALYKALEFTGDTLKYLSMDDRFSICNMAIEAGAKNGIIAVDDITLEYL-------EERKKVNGGLRAEPK-IHTSDPDA 260
Cdd:PLN00070 314 GVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLkltgrsdETVAMIEAYLRANKMfVDYNEPQQ 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 261 E--YCQSITIDVEKLSPVIAYPFLPSNGKPVEQAVAD----------------------------------RIKIDQVMI 304
Cdd:PLN00070 394 ErvYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADwhscldnkvgfkgfavpkeaqskvakfsfhgqpaELRHGSVVI 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503318543 305 G---SCTNGRLEDLRIAAEIVRGK------RVARHTRMIVTPATQRIFMQAEKEGLIDTLIEAGAVVSNPTCGACLGGYm 375
Cdd:PLN00070 474 AaitSCTNTSNPSVMLGAGLVAKKacelglEVKPWIKTSLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIGNS- 552
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 503318543 376 gilGDGEKCVSTT--------------NRNFVGRMGARTSEIYL 405
Cdd:PLN00070 553 ---GELDESVASAitendivaaavlsgNRNFEGRVHPLTRANYL 593
|
|
| |
