|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-455 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 919.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 1 MGQTLFDKVWNRHVLYGKLGEPQLLYIDLHLIHEVTSPQAFEGLRLQNRKLRRPDLTFATLDHNVPTIDI-FNIKDEIAN 79
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRdLPIADPVSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 80 KQITTLQKNAIDFGVHIFDMGSDEQGIVHMVGPETGLTQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTLWQ 159
Cdd:PRK05478 81 IQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 160 TKPKNLKIDINGTLPTGVYAKDIILHLIKTYGVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDITF 239
Cdd:PRK05478 161 KKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 240 EYVKGRPFA---DNFAKSVDKWRELYSDDDAIFDRVIELDVSTLEPQVTWGTNPEMGVNFSEPFPEINDIND-------Q 309
Cdd:PRK05478 241 EYLKGRPFApkgEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADpvkrasaE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 310 RAYDYMGLEPGQKAEDIDLGYVFLGSCTNARLSDLIEASHIVKGNKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAGF 389
Cdd:PRK05478 321 RALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 584659931 390 EWREPGCSMCLGMNPDQVPEGVHCASTSNRNFEGRQGKGARTHLVSPAMAAAAAIHGKFVDVRKVV 455
Cdd:PRK05478 401 EWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-454 |
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: 696.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 1 MGQTLFDKVWNRHVLYGKL-GEPQLLYIDLHLIHEVTSPQAFEGLRLQN-RKLRRPDLTFATLDHNVPTidifniKDEIA 78
Cdd:COG0065 1 MGMTLAEKILARHAGREVEpGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPT------KDPKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 79 NKQITTLQKNAIDFGVHIFDMGsdEQGIVHMVGPETGLTQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTLW 158
Cdd:COG0065 75 AEQVKTLREFAKEFGITFFDVG--DPGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 159 QTKPKNLKIDINGTLPTGVYAKDIILHLIKTYGVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDIT 238
Cdd:COG0065 153 FKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 239 FEYVKGRPFADnfaksvdkWRELYSDDDAIFDRVIELDVSTLEPQVTWGTNPEMGVNFSEpfpeindindqraydymgle 318
Cdd:COG0065 233 FEYLKGRPFAP--------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE-------------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 319 pgqkAEDIDLGYVFLGSCTNARLSDLIEASHIVKGNKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAGFEWREPGCSM 398
Cdd:COG0065 285 ----LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGM 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 584659931 399 CLGMNPDQVPEGVHCASTSNRNFEGRQG-KGARTHLVSPAMAAAAAIHGKFVDVRKV 454
Cdd:COG0065 361 CLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
1-454 |
0e+00 |
|
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate dehydratase, large subunit, or the large subunit domain of single-chain forms. Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. These homologs are now described by a separate model of subfamily (rather than equivalog) homology type, and the priors and cutoffs for this model have been changed to focus this equivalog family more narrowly. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 272940 Cd Length: 465 Bit Score: 680.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 1 MGQTLFDKVWNRHVLYGKLGEPQLLYIDLHLIHEVTSPQAFEGLRLQNRKLRRPDLTFATLDHNVPTID-IFNIKDEIAN 79
Cdd:TIGR00170 1 MPRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNrDFNIKDEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 80 KQITTLQKNAIDFGVHIFDMGSDEQGIVHMVGPETGLTQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTLWQ 159
Cdd:TIGR00170 81 IQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 160 TKPKNLKIDINGTLPTGVYAKDIILHLIKTYGVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDITF 239
Cdd:TIGR00170 161 ARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 240 EYVKGRPFA---DNFAKSVDKWRELYSDDDAIFDRVIELDVSTLEPQVTWGTNPEMGVNFSEPFPEINDIND-------Q 309
Cdd:TIGR00170 241 EYCKGRPHApkgKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADpvdkasaE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 310 RAYDYMGLEPGQKAEDIDLGYVFLGSCTNARLSDLIEASHIVKGNKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAGF 389
Cdd:TIGR00170 321 RALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 584659931 390 EWREPGCSMCLGMNPDQVPEGVHCASTSNRNFEGRQGKGARTHLVSPAMAAAAAIHGKFVDVRKV 454
Cdd:TIGR00170 401 EWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-436 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 637.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 7 DKVWNRHVLYGklGEPQLLYI-DLHLIHEVTSPQAFEGLRLQNRKLRRPDLTFATLDHNVPTIDI---------FNIKDE 76
Cdd:pfam00330 1 EKIWDAHLVEE--LDGSLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVidhapdaldKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 77 IA--NKQITTLQKNAIDFGVHIFDMGsdeQGIVHMVGPETGLTQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFAT 154
Cdd:pfam00330 79 ISrnKEQYDFLEWNAKKFGIRFVPPG---QGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 155 QTLWQTKPKNLKIDINGTLPTGVYAKDIILHLIKTYGVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQP 234
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 235 DDITFEYVK--GRPFA---DNFAKSVdKWRELYSDDDAIFDRVIELDVSTLEPQVTWGTNPEMGVNFSEPFP-----EIN 304
Cdd:pfam00330 236 DETTFEYLRatGRPEApkgEAYDKAV-AWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPdpfadAVK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 305 DINDQRAYDYMGLEPGQKAEDIDLGYVFLGSCTNARLSDLIEASHIVK-----GNKVHPNITAIVVPGSRTVKKEAEKLG 379
Cdd:pfam00330 315 RKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEAEG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 584659931 380 LDTIFKNAGFEWREPGCSMCLGmNPDQVPEGVHCASTSNRNFEGRQGKGARTHLVSP 436
Cdd:pfam00330 395 LDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASP 450
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
29-448 |
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: 586.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 29 LHLIHEVTSPQAFEGLRLQNR-KLRRPDLTFATLDHNVPTidifniKDEIANKQITTLQKNAIDFGVHIFDMGsdEQGIV 107
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPT------PDIKAAEQVKTLRKFAKEFGINFFDVG--RQGIC 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 108 HMVGPETGLTQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTLWQTKPKNLKIDINGTLPTGVYAKDIILHLI 187
Cdd:cd01583 73 HVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYII 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 188 KTYGVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDITFEYVKGRPFADnfaksvdkWRELYSDDDA 267
Cdd:cd01583 153 GKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAY--------WKELKSDEDA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 268 IFDRVIELDVSTLEPQVTWGTNPEMGVNFSEpfpeindindqraydymglepgqkAEDIDLGYVFLGSCTNARLSDLIEA 347
Cdd:cd01583 225 EYDKVVEIDASELEPQVAWPHSPDNVVPVSE------------------------VEGIKIDQVFIGSCTNGRLEDLRAA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 348 SHIVKGNKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAGFEWREPGCSMCLGMNPDQVPEGVHCASTSNRNFEGRQG- 426
Cdd:cd01583 281 AEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTSNRNFKGRMGs 360
|
410 420
....*....|....*....|..
gi 584659931 427 KGARTHLVSPAMAAAAAIHGKF 448
Cdd:cd01583 361 PGARIYLASPATAAASAITGEI 382
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
27-446 |
1.71e-90 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 281.26 E-value: 1.71e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 27 IDLHLIHEVTSPQAFEGLRLQNRKLRRPDLTFATLDHNVPTIDIfnikdEIANKQITTLQkNAIDFGVHIFDMGSdeQGI 106
Cdd:NF040615 26 VDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPANTV-----KAANMQKITRE-FVKEQGIKNFYLGG--EGI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 107 VHMVGPETGLTQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTLWQTKPKNLKIDINGTLPTgVYAKDIILHL 186
Cdd:NF040615 98 CHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVNIVGKNEN-ISGKDIILKV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 187 IKTYGVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDITFEYVKGRPFADNFAKSVDKWRELYSDDD 266
Cdd:NF040615 177 CKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEGVSEEEIAELKKNRITVNEKE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 267 AIFDRVIELDVSTLEPQVTWGTNPEmgvnfsepfpeindiNDQRAYDYMGLEPGQkaedidlgyVFLGSCTNARLSDLIE 346
Cdd:NF040615 257 ENYYKEIEIDITDMEEQVACPHHPD---------------NVKPVSEVEGTEIDQ---------VFIGSCTNGRLSDLRI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 347 ASHIVKGNKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAGFEWREPGCSMCLGMNPDQVPEGVHCASTSNRNFEGRQG 426
Cdd:NF040615 313 AAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMG 392
|
410 420
....*....|....*....|.
gi 584659931 427 -KGARTHLVSPAMAAAAAIHG 446
Cdd:NF040615 393 nINSYIYLSSPKIAAKSAVKG 413
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-455 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 919.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 1 MGQTLFDKVWNRHVLYGKLGEPQLLYIDLHLIHEVTSPQAFEGLRLQNRKLRRPDLTFATLDHNVPTIDI-FNIKDEIAN 79
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRdLPIADPVSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 80 KQITTLQKNAIDFGVHIFDMGSDEQGIVHMVGPETGLTQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTLWQ 159
Cdd:PRK05478 81 IQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 160 TKPKNLKIDINGTLPTGVYAKDIILHLIKTYGVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDITF 239
Cdd:PRK05478 161 KKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 240 EYVKGRPFA---DNFAKSVDKWRELYSDDDAIFDRVIELDVSTLEPQVTWGTNPEMGVNFSEPFPEINDIND-------Q 309
Cdd:PRK05478 241 EYLKGRPFApkgEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADpvkrasaE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 310 RAYDYMGLEPGQKAEDIDLGYVFLGSCTNARLSDLIEASHIVKGNKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAGF 389
Cdd:PRK05478 321 RALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 584659931 390 EWREPGCSMCLGMNPDQVPEGVHCASTSNRNFEGRQGKGARTHLVSPAMAAAAAIHGKFVDVRKVV 455
Cdd:PRK05478 401 EWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
1-456 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 710.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 1 MGQTLFDKVWNRHVLYGKLGEPQLLYIDLHLIHEVTSPQAFEGLRLQNRKLRRPDLTFATLDHNVPTID--IFNIKDEIA 78
Cdd:PRK12466 2 MPRTLYDKLWDSHTVARLDDGHVLLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPTRPgrDRGITDPGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 79 NKQITTLQKNAIDFGVHIFDMGSDEQGIVHMVGPETGLTQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTLW 158
Cdd:PRK12466 82 ALQVDYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQTLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 159 QTKPKNLKIDINGTLPTGVYAKDIILHLIKTYGVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDIT 238
Cdd:PRK12466 162 YRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 239 FEYVKGRPFA---DNFAKSVDKWRELYSDDDAIFDRVIELDVSTLEPQVTWGTNPEMGVNFSEPFPEINDIND------- 308
Cdd:PRK12466 242 FDYLRGRPRApkgALWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAAEADparraam 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 309 QRAYDYMGLEPGQKAEDIDLGYVFLGSCTNARLSDLIEASHIVKGNKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAG 388
Cdd:PRK12466 322 ERALDYMGLTPGTPLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAG 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 584659931 389 FEWREPGCSMCLGMNPDQVPEGVHCASTSNRNFEGRQGKGARTHLVSPAMAAAAAIHGKFVDVRKVVV 456
Cdd:PRK12466 402 FEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHITDVRSLLQ 469
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-454 |
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: 696.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 1 MGQTLFDKVWNRHVLYGKL-GEPQLLYIDLHLIHEVTSPQAFEGLRLQN-RKLRRPDLTFATLDHNVPTidifniKDEIA 78
Cdd:COG0065 1 MGMTLAEKILARHAGREVEpGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPT------KDPKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 79 NKQITTLQKNAIDFGVHIFDMGsdEQGIVHMVGPETGLTQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTLW 158
Cdd:COG0065 75 AEQVKTLREFAKEFGITFFDVG--DPGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 159 QTKPKNLKIDINGTLPTGVYAKDIILHLIKTYGVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDIT 238
Cdd:COG0065 153 FKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 239 FEYVKGRPFADnfaksvdkWRELYSDDDAIFDRVIELDVSTLEPQVTWGTNPEMGVNFSEpfpeindindqraydymgle 318
Cdd:COG0065 233 FEYLKGRPFAP--------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE-------------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 319 pgqkAEDIDLGYVFLGSCTNARLSDLIEASHIVKGNKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAGFEWREPGCSM 398
Cdd:COG0065 285 ----LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGM 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 584659931 399 CLGMNPDQVPEGVHCASTSNRNFEGRQG-KGARTHLVSPAMAAAAAIHGKFVDVRKV 454
Cdd:COG0065 361 CLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
1-454 |
0e+00 |
|
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate dehydratase, large subunit, or the large subunit domain of single-chain forms. Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases (EC 4.2.1.-) and bind a Fe-4S iron-sulfur cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. These homologs are now described by a separate model of subfamily (rather than equivalog) homology type, and the priors and cutoffs for this model have been changed to focus this equivalog family more narrowly. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 272940 Cd Length: 465 Bit Score: 680.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 1 MGQTLFDKVWNRHVLYGKLGEPQLLYIDLHLIHEVTSPQAFEGLRLQNRKLRRPDLTFATLDHNVPTID-IFNIKDEIAN 79
Cdd:TIGR00170 1 MPRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNrDFNIKDEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 80 KQITTLQKNAIDFGVHIFDMGSDEQGIVHMVGPETGLTQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTLWQ 159
Cdd:TIGR00170 81 IQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 160 TKPKNLKIDINGTLPTGVYAKDIILHLIKTYGVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDITF 239
Cdd:TIGR00170 161 ARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 240 EYVKGRPFA---DNFAKSVDKWRELYSDDDAIFDRVIELDVSTLEPQVTWGTNPEMGVNFSEPFPEINDIND-------Q 309
Cdd:TIGR00170 241 EYCKGRPHApkgKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADpvdkasaE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 310 RAYDYMGLEPGQKAEDIDLGYVFLGSCTNARLSDLIEASHIVKGNKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAGF 389
Cdd:TIGR00170 321 RALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 584659931 390 EWREPGCSMCLGMNPDQVPEGVHCASTSNRNFEGRQGKGARTHLVSPAMAAAAAIHGKFVDVRKV 454
Cdd:TIGR00170 401 EWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-436 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 637.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 7 DKVWNRHVLYGklGEPQLLYI-DLHLIHEVTSPQAFEGLRLQNRKLRRPDLTFATLDHNVPTIDI---------FNIKDE 76
Cdd:pfam00330 1 EKIWDAHLVEE--LDGSLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVidhapdaldKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 77 IA--NKQITTLQKNAIDFGVHIFDMGsdeQGIVHMVGPETGLTQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFAT 154
Cdd:pfam00330 79 ISrnKEQYDFLEWNAKKFGIRFVPPG---QGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 155 QTLWQTKPKNLKIDINGTLPTGVYAKDIILHLIKTYGVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQP 234
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 235 DDITFEYVK--GRPFA---DNFAKSVdKWRELYSDDDAIFDRVIELDVSTLEPQVTWGTNPEMGVNFSEPFP-----EIN 304
Cdd:pfam00330 236 DETTFEYLRatGRPEApkgEAYDKAV-AWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPdpfadAVK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 305 DINDQRAYDYMGLEPGQKAEDIDLGYVFLGSCTNARLSDLIEASHIVK-----GNKVHPNITAIVVPGSRTVKKEAEKLG 379
Cdd:pfam00330 315 RKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEAEG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 584659931 380 LDTIFKNAGFEWREPGCSMCLGmNPDQVPEGVHCASTSNRNFEGRQGKGARTHLVSP 436
Cdd:pfam00330 395 LDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASP 450
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
29-448 |
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: 586.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 29 LHLIHEVTSPQAFEGLRLQNR-KLRRPDLTFATLDHNVPTidifniKDEIANKQITTLQKNAIDFGVHIFDMGsdEQGIV 107
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPT------PDIKAAEQVKTLRKFAKEFGINFFDVG--RQGIC 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 108 HMVGPETGLTQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTLWQTKPKNLKIDINGTLPTGVYAKDIILHLI 187
Cdd:cd01583 73 HVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYII 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 188 KTYGVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDITFEYVKGRPFADnfaksvdkWRELYSDDDA 267
Cdd:cd01583 153 GKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAY--------WKELKSDEDA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 268 IFDRVIELDVSTLEPQVTWGTNPEMGVNFSEpfpeindindqraydymglepgqkAEDIDLGYVFLGSCTNARLSDLIEA 347
Cdd:cd01583 225 EYDKVVEIDASELEPQVAWPHSPDNVVPVSE------------------------VEGIKIDQVFIGSCTNGRLEDLRAA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 348 SHIVKGNKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAGFEWREPGCSMCLGMNPDQVPEGVHCASTSNRNFEGRQG- 426
Cdd:cd01583 281 AEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTSNRNFKGRMGs 360
|
410 420
....*....|....*....|..
gi 584659931 427 KGARTHLVSPAMAAAAAIHGKF 448
Cdd:cd01583 361 PGARIYLASPATAAASAITGEI 382
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
1-455 |
1.49e-135 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 396.47 E-value: 1.49e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 1 MGQTLFDKVWNRHVlyGKLGEP-QLLY--IDLHLIHEVTSPQAFEGLR-LQNRKLRRPDLTFATLDHNVPTIDIfnikdE 76
Cdd:PRK00402 1 MGMTLAEKILARHS--GRDVSPgDIVEakVDLVMAHDITGPLAIKEFEkIGGDKVFDPSKIVIVFDHFVPAKDI-----K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 77 IANkqittLQKNAIDFG-----VHIFDMGsdeQGIVHMVGPETGLTQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEHV 151
Cdd:PRK00402 74 SAE-----QQKILREFAkeqgiPNFFDVG---EGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 152 FATQTLWQTKPKNLKIDINGTLPTGVYAKDIILHLIKTYGVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGI 231
Cdd:PRK00402 146 MATGKTWFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 232 IQPDDITFEYVKGRPFADnfaksvdkWRELYSDDDAIFDRVIELDVSTLEPQVTWGTNPEMGVNFSEpfpeindindqra 311
Cdd:PRK00402 226 FAPDEKTLEYLKERAGRD--------YKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSE------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 312 ydymglepgqkAEDIDLGYVFLGSCTNARLSDLIEASHIVKGNKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAGFEW 391
Cdd:PRK00402 285 -----------VEGTKVDQVFIGSCTNGRLEDLRIAAEILKGRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVV 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 584659931 392 REPGCSMCLGMNPDQVPEGVHCASTSNRNFEGRQGK-GARTHLVSPAMAAAAAIHGKFVDVRKVV 455
Cdd:PRK00402 354 STPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGSpESEVYLASPAVAAASAVTGKITDPREVL 418
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
27-452 |
1.43e-114 |
|
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: 342.50 E-value: 1.43e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 27 IDLHLIHEVTSPQAFEGL-RLQNRKLRRPDLTFATLDHNVPTIDIfnikdEIANKQITtLQKNAIDFGV-HIFDMGsdeQ 104
Cdd:TIGR01343 25 IDLAMVHDITAPLAIKTLeEYGIDKVWNPEKIVIVFDHQVPADTI-----KAAEMQKL-AREFVKKQGIkYFYDVG---E 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 105 GIVHMVGPETGLTQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTLWQTKPKNLKIDINGTLPTGVYAKDIIL 184
Cdd:TIGR01343 96 GICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFKVPETIRVNITGKLNPGVTAKDVIL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 185 HLIKTYGVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDITFEYVKGRpfadnfakSVDKWRELYSD 264
Cdd:TIGR01343 176 EVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYLKER--------RKEPFRVYKSD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 265 DDAIFDRVIELDVSTLEPQVTWGTNPEMGVNFSEpfpeindindqraydymglepgqkAEDIDLGYVFLGSCTNARLSDL 344
Cdd:TIGR01343 248 EDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSE------------------------VEGTEIDQVFIGSCTNGRLEDL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 345 IEASHIVKGNKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAGFEWREPGCSMCLGMNPDQVPEGVHCASTSNRNFEGR 424
Cdd:TIGR01343 304 RVAAKILKGRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLGSHQGVLAPGEVCISTSNRNFKGR 383
|
410 420
....*....|....*....|....*....
gi 584659931 425 QG-KGARTHLVSPAMAAAAAIHGKFVDVR 452
Cdd:TIGR01343 384 MGhPNAEIYLASPATAAASAVKGYIADPR 412
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
3-452 |
2.49e-106 |
|
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: 321.71 E-value: 2.49e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 3 QTLFDKVWNRHVLYG-KLGEPQLLYIDLHLIHEVTSPQAFEGLR-LQNRKLRRPDLTFATLDHNVPTIDIfnikdEIANK 80
Cdd:TIGR02086 1 MTLAEKILSEKVGRPvCAGEIVEVEVDLAMTHDGTGPLAIKALReLGVARVWDPEKIVIAFDHNVPPPTV-----EAAEM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 81 QiTTLQKNAIDFGVHIFDMGsdeQGIVHMVGPETGLTQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTLWQT 160
Cdd:TIGR02086 76 Q-KEIREFAKRHGIKNFDVG---EGICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTWIK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 161 KPKNLKIDINGTLPTGVYAKDIILHLIKTYGVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDITFE 240
Cdd:TIGR02086 152 VPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEETYE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 241 YVKGRpfadnfakSVDKWRELYSDDDAIFDRVIELDVSTLEPQVtwgtnpemgvnfSEPFpeinDINDQRaydymglePG 320
Cdd:TIGR02086 232 YLKKR--------RGLEFRILVPDPGANYYKEIEIDLSDLEPQV------------AVPH----SVDNVK--------PV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 321 QKAEDIDLGYVFLGSCTNARLSDLIEASHIVKGNKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAGFEWREPGCSMCL 400
Cdd:TIGR02086 280 SDVEGTEIDQVFIGSCTNGRLEDLRIAAEILKGRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAGAMICPPGCGPCL 359
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 584659931 401 GMNPDQVPEGVHCASTSNRNFEGRQG-KGARTHLVSPAMAAAAAIHGKFVDVR 452
Cdd:TIGR02086 360 GAHMGVLGDGEVCLSTTNRNFKGRMGsPNAEIYLASPATAAASAVEGYITDPE 412
|
|
| LEU2 |
TIGR02083 |
3-isopropylmalate dehydratase, large subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
20-454 |
4.51e-91 |
|
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: 282.47 E-value: 4.51e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 20 GEPQLLYIDLHLIHEVTSPQAFEGLR-LQNRKLRRPDLTFATLDHNVPTIDIfnikdeIANKQITTLQKNAIDFGV-HIF 97
Cdd:TIGR02083 20 GELILAKLDIVLGNDITTPLAIKAFKeYGGKKVFDPDRVALVPDHFTPNKDI------KSAEQCKMMREFAREQGIeKFF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 98 DMGsdEQGIVHMVGPETGLTQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTLWQTKPKNLKIDINGTLPTGV 177
Cdd:TIGR02083 94 EIG--NMGIEHALLPEEGIVKPGDLIIGADSHTCTYGALGAFATGVGSTDMAVGMATGKAWFRVPEAIKFVLKGKLKPWV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 178 YAKDIILHLIKTYGVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDITFEYVKGRpfadnfakSVDK 257
Cdd:TIGR02083 172 TGKDLILHIIGIIGVDGALYKSMEFSGEGLKELSMDDRFTIANMAIEAGAKTGIFPVDEITIEYEKGR--------GKRE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 258 WRELYSDDDAIFDRVIELDVSTLEPQVTWGTNPEMGVNFSEpfpeindindqraydymglepgQKAEDIDLGYVFLGSCT 337
Cdd:TIGR02083 244 EKIYKADEDAKYVRVIEIDLSELEPQVAFPHLPENTKDISE----------------------AGKEEIKIDQVVIGSCT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 338 NARLSDLIEASHIVKGNKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAGFEWREPGCSMCLGMNPDQVPEGVHCASTS 417
Cdd:TIGR02083 302 NGRLEDLRLAAEILKGKTVAPDVRCIIIPGSQNVYLEAMKEGLLEIFIEAGAVVSTPTCGPCLGGHMGILAEGERAISTT 381
|
410 420 430
....*....|....*....|....*....|....*...
gi 584659931 418 NRNFEGRQGK-GARTHLVSPAMAAAAAIHGKFVDVRKV 454
Cdd:TIGR02083 382 NRNFVGRMGHpKSEVYLASPAVAAASAIKGYIASPEEV 419
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
27-446 |
1.71e-90 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 281.26 E-value: 1.71e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 27 IDLHLIHEVTSPQAFEGLRLQNRKLRRPDLTFATLDHNVPTIDIfnikdEIANKQITTLQkNAIDFGVHIFDMGSdeQGI 106
Cdd:NF040615 26 VDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPANTV-----KAANMQKITRE-FVKEQGIKNFYLGG--EGI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 107 VHMVGPETGLTQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTLWQTKPKNLKIDINGTLPTgVYAKDIILHL 186
Cdd:NF040615 98 CHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVNIVGKNEN-ISGKDIILKV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 187 IKTYGVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDITFEYVKGRPFADNFAKSVDKWRELYSDDD 266
Cdd:NF040615 177 CKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEGVSEEEIAELKKNRITVNEKE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 267 AIFDRVIELDVSTLEPQVTWGTNPEmgvnfsepfpeindiNDQRAYDYMGLEPGQkaedidlgyVFLGSCTNARLSDLIE 346
Cdd:NF040615 257 ENYYKEIEIDITDMEEQVACPHHPD---------------NVKPVSEVEGTEIDQ---------VFIGSCTNGRLSDLRI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 347 ASHIVKGNKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAGFEWREPGCSMCLGMNPDQVPEGVHCASTSNRNFEGRQG 426
Cdd:NF040615 313 AAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMG 392
|
410 420
....*....|....*....|.
gi 584659931 427 -KGARTHLVSPAMAAAAAIHG 446
Cdd:NF040615 393 nINSYIYLSSPKIAAKSAVKG 413
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
31-447 |
1.56e-73 |
|
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: 236.24 E-value: 1.56e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 31 LIHEVTSPQA---FEGLRLQNrKLRRPDLTFATLDHNVPtidifnIKDEIANKQITTLQKNAIDFGVHIFDMGSdeqGIV 107
Cdd:cd01351 3 MLQDATGPMAmkaFEILAALG-KVADPSQIACVHDHAVQ------LEKPVNNEGHKFLSFFAALQGIAFYRPGV---GII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 108 HMVGPETGLtQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTLWQTKPKNLKIDINGTLPTGVYAKDIILHLI 187
Cdd:cd01351 73 HQIMVENLA-LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 188 KTYGVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDITFEYVKGRPFADNFAKSVDKWRELYSDDDA 267
Cdd:cd01351 152 GIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWLAFPEELLADEGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 268 IFDRVIELDVSTLEPQVtwgtnpemgvnfSEPfpeiNDINDQRAYDYMglepgqkaEDIDLGYVFLGSCTNARLSDLIEA 347
Cdd:cd01351 232 EYDQVIEIDLSELEPDI------------SGP----NRPDDAVSVSEV--------EGTKIDQVLIGSCTNNRYSDMLAA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 348 SHIVKGNKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAGFEWREPGCSMCLGMNPDQVPEGVHCASTSNRNFEGRQGK 427
Cdd:cd01351 288 AKLLKGAKVAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLVADGEVGVSSGNRNFPGRLGT 367
|
410 420
....*....|....*....|.
gi 584659931 428 G-ARTHLVSPAMAAAAAIHGK 447
Cdd:cd01351 368 YeRHVYLASPELAAATAIAGK 388
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
1-453 |
1.99e-64 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 218.86 E-value: 1.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 1 MGQTLFDKVWNRHVLYGKL--GEPQLLYIDLHLIHEVTSPQA---FEGLRLQNRKLrrpDLTFATLDHNVPTIDIFNIKD 75
Cdd:PRK07229 1 MGLTLTEKILYAHLVEGELepGEEIAIRIDQTLTQDATGTMAylqFEAMGLDRVKT---ELSVQYVDHNLLQADFENADD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 76 -----EIANKqittlqknaidFGVHIFDMGSdeqGIVHMVGPEtGLTQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEH 150
Cdd:PRK07229 78 hrflqSVAAK-----------YGIYFSKPGN---GICHQVHLE-RFAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVAL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 151 VFATQTLWQTKPKNLKIDINGTLPTGVYAKDIILHLIKTYGVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYG 230
Cdd:PRK07229 143 AMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 231 IIQPDDITFEYVK--GRPfadnfaksvDKWRELYSDDDAIFDRVIELDVSTLEPQVTWGTNPEMGVNFSEpfpeindind 308
Cdd:PRK07229 223 IFPSDERTREFLKaqGRE---------DDWVELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSE---------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 309 qraydymglepgqkAEDIDLGYVFLGSCTNARLSDLIEASHIVKGNKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAG 388
Cdd:PRK07229 284 --------------VAGIKVDQVLIGSCTNSSYEDLMRAASILKGKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAG 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 584659931 389 FEWREPGCSMCLGMnpDQVP-EGVHCASTSNRNFEGRQG-KGARTHLVSPAMAAAAAIHGKFVDVRK 453
Cdd:PRK07229 350 ARILENACGPCIGM--GQAPaTGNVSLRTFNRNFPGRSGtKDAQVYLASPETAAASALTGVITDPRT 414
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
53-448 |
1.10e-63 |
|
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: 210.38 E-value: 1.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 53 RPDLTFATLDHNVPTIDIFNIKDEIankqitTLQKNAIDFGVHIFDMGSdeqGIVHMVGPETgLTQPGKTIVCGDSHTAT 132
Cdd:cd01585 26 RTELSVSYVDHNTLQTDFENADDHR------FLQTVAARYGIYFSRPGN---GICHQVHLER-FAVPGKTLLGSDSHTPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 133 HGAFGAIAFGIGTSEVEHVFATQTLWQTKPKNLKIDINGTLPTGVYAKDIILHLIKTYGVDFGTGYALEFTGETIKNLSM 212
Cdd:cd01585 96 AGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVKGGVGKIFEYTGPGVATLSV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 213 DGRMTICNMAIEGGAKYGIIQPDDITFEYVK--GRPfadnfaksvDKWRELYSDDDAIFDRVIELDVSTLEPQVTWGTNP 290
Cdd:cd01585 176 PERATITNMGAELGATTSIFPSDERTREFLAaqGRE---------DDWVELAADADAEYDEEIEIDLSELEPLIARPHSP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 291 EmgvnfsepfpeindiNDQRAYDYMGLEPGQkaedidlgyVFLGSCTNARLSDLIEASHIVKGNKVHPNITAIVVPGSRT 370
Cdd:cd01585 247 D---------------NVVPVREVAGIKVDQ---------VAIGSCTNSSYEDLMTVAAILKGRRVHPHVSMVVAPGSKQ 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 584659931 371 VKKEAEKLGLDTIFKNAGFEWREPGCSMCLGMNPDQVPEGVhCASTSNRNFEGRQG-KGARTHLVSPAMAAAAAIHGKF 448
Cdd:cd01585 303 VLEMLARNGALADLLAAGARILESACGPCIGMGQAPPTGGV-SVRTFNRNFEGRSGtKDDLVYLASPEVAAAAALTGVI 380
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
33-447 |
2.77e-42 |
|
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: 153.54 E-value: 2.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 33 HEVTSPQAFEGLRLQNRKLRRPDLTFATLDHNVPTIDIFNIKDEianKQITTL-QKNAIDFgvhiFDMGsdeQGIVHMVG 111
Cdd:cd01582 5 HDNSWPVALKFMSIGATKIHNPDQIVMTLDHDVQNKSEKNLKKY---KNIESFaKKHGIDF----YPAG---RGIGHQIM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 112 PETGLTQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFAT-QTLWQTkPKNLKIDINGTLPTGVYAKDIILHLIKTY 190
Cdd:cd01582 75 IEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATgQTWWQI-PPVAKVELKGQLPKGVTGKDVIVALCGLF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 191 GVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDitfeyvkgrpfadnfaksvdkwRELYsdddaifd 270
Cdd:cd01582 154 NKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDA----------------------KHLI-------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 271 rvieLDVSTLEPQVTwGTNpemGVNFSEPFPEIndindqraydymglepgqKAEDIDLGYVFLGSCTNARLSDLIEASHI 350
Cdd:cd01582 204 ----LDLSTLSPYVS-GPN---SVKVSTPLKEL------------------EAQNIKINKAYLVSCTNSRASDIAAAADV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 351 VKG-------NKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAGFEWREPGCSMCLGMNPDQVPEGVHCASTSNRNFEG 423
Cdd:cd01582 258 VKGkkekngkIPVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQGLLEPGEVGISATNRNFKG 337
|
410 420
....*....|....*....|....*
gi 584659931 424 RQG-KGARTHLVSPAMAAAAAIHGK 447
Cdd:cd01582 338 RMGsTEALAYLASPAVVAASAISGK 362
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
92-447 |
2.73e-36 |
|
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: 138.34 E-value: 2.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 92 FGVHIFDMGSdeqGIVHMVGPETgLTQPGKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTlWQTK-PKNLKIDIN 170
Cdd:cd01584 67 YGIGFWKPGS---GIIHQIVLEN-YAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIP-WELKcPKVIGVKLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 171 GTLPTGVYAKDIILHLIKTYGVDFGTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDITFEYVK--GRPFA 248
Cdd:cd01584 142 GKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKatGRAEI 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 249 DNFAKSVdKWRELYSDDDAIFDRVIELDVSTLEPQVTWGTNPEMGVNFSEpfpeindindqraydyMGLEPGQKAEDIDL 328
Cdd:cd01584 222 ADLADEF-KDDLLVADEGAEYDQLIEINLSELEPHINGPFTPDLATPVSK----------------FKEVAEKNGWPLDL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 329 GYVFLGSCTNARLSDLIEASHIVK-----GNKVHPNITaiVVPGSRTVKKEAEKLGLDTIFKNAGFEWREPGCSMCLGM- 402
Cdd:cd01584 285 RVGLIGSCTNSSYEDMGRAASIAKqalahGLKCKSIFT--ITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQw 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 584659931 403 NPDQVPEGVHCA--STSNRNFEGRQGKGARTH--LVSPAMAAAAAIHGK 447
Cdd:cd01584 363 DRKDIKKGEKNTivTSYNRNFTGRNDANPATHafVASPEIVTAMAIAGT 411
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
61-424 |
8.14e-31 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 125.89 E-value: 8.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 61 LDHNVpTIDIFNIKDEIANKQITTLQKNAIDF-----GVHIFDM------GSdeqGIVHMVGPE---------TGLTQPg 120
Cdd:PTZ00092 134 IDHSV-QVDFSRSPDALELNQEIEFERNLERFeflkwGSKAFKNllivppGS---GIVHQVNLEylarvvfnkDGLLYP- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 121 KTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTLWQTKPKNLKIDINGTLPTGVYAKDIIL---HLIKTYGVdfgTG 197
Cdd:PTZ00092 209 DSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTGKLSEHVTATDLVLtvtSMLRKRGV---VG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 198 YALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDITFEYVK--GRP-----FADNFAKSVDKWRElySDDDAIFD 270
Cdd:PTZ00092 286 KFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKqtGRSeekveLIEKYLKANGLFRT--YAEQIEYS 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 271 RVIELDVSTLEPQVTWGTNPEMGV---NFSEPFPEI--------------NDINDQRAYDYMGlepgqKAEDIDLGYVFL 333
Cdd:PTZ00092 364 DVLELDLSTVVPSVAGPKRPHDRVplsDLKKDFTAClsapvgfkgfgipeEKHEKKVKFTYKG-----KEYTLTHGSVVI 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 334 G---SCTNARLSDLIEASHIV------KGNKVHPNITAIVVPGSRTVKKEAEKLGLDTI-----FKNAGFewrepGCSMC 399
Cdd:PTZ00092 439 AaitSCTNTSNPSVMLAAGLLakkaveKGLKVPPYIKTSLSPGSKVVTKYLEASGLLKYleklgFYTAGY-----GCMTC 513
|
410 420 430
....*....|....*....|....*....|....*.
gi 584659931 400 LGmNPDQVPEGVH---------CAS--TSNRNFEGR 424
Cdd:PTZ00092 514 IG-NSGDLDPEVSeaitnndlvAAAvlSGNRNFEGR 548
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
105-424 |
1.80e-28 |
|
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: 119.05 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 105 GIVH-----------MVGPETGLTQ--PGkTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTLWQTKPK----NLKi 167
Cdd:COG1048 176 GIVHqvnleylafvvWTREEDGETVayPD-TLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEvvgvKLT- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 168 dinGTLPTGVYAKDIILHL---IKTYGVdfgTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDITFEYVK- 243
Cdd:COG1048 254 ---GKLPEGVTATDLVLTVtemLRKKGV---VGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRl 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 244 -GRP-----FADNFAKSVDKWRElYSDDDAIFDRVIELDVSTLEPQVTWGTNP-------EMGVNFSEPFPEINDINDQR 310
Cdd:COG1048 328 tGRSeeqieLVEAYAKAQGLWRD-PDAPEPYYSDVLELDLSTVEPSLAGPKRPqdriplsDLKEAFRAALAAPVGEELDK 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 311 AYDYmglEPGQKAEDIDLGYVFL---GSCTNARLSDLIEASHIV------KGNKVHPNITAIVVPGSRTVKKEAEKLGL- 380
Cdd:COG1048 407 PVRV---EVDGEEFELGHGAVVIaaiTSCTNTSNPSVMIAAGLLakkaveKGLKVKPWVKTSLAPGSKVVTDYLERAGLl 483
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 584659931 381 ---DTI-FKNAGFewrepGCSMCLGMN---PDQVPEGVH------CASTS-NRNFEGR 424
Cdd:COG1048 484 pylEALgFNVVGY-----GCTTCIGNSgplPPEISEAIEendlvvAAVLSgNRNFEGR 536
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
105-424 |
4.81e-28 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 117.73 E-value: 4.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 105 GIVHMVGPE------TGLTQPGK------TIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTLWQTKPKNLKIDINGT 172
Cdd:PRK12881 178 GIMHQVNLEylarvvHTKEDDGDtvaypdTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIPDVVGVELTGK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 173 LPTGVYAKDIIL---HLIKTYGVdfgTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDITFEYVK--GRP- 246
Cdd:PRK12881 258 LREGVTATDLVLtvtEMLRKEGV---VGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLRltGRTe 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 247 ----FADNFAKSVDKWRElySDDDAIFDRVIELDVSTLEPQVTWGTNPEMGVNFSEPFPEINDINDQRAYDYMGLEPGQK 322
Cdd:PRK12881 335 aqiaLVEAYAKAQGLWGD--PKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFSKPVAENGFAKKAQT 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 323 AEDIDL--GYVFLG---SCTNArlSD---LIEASHIVK-----GNKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAGF 389
Cdd:PRK12881 413 SNGVDLpdGAVAIAaitSCTNT--SNpsvLIAAGLLAKkaverGLTVKPWVKTSLAPGSKVVTEYLERAGLLPYLEKLGF 490
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 584659931 390 EWREPGCSMCLGMNPDQVPE--------GVHCAS--TSNRNFEGR 424
Cdd:PRK12881 491 GIVGYGCTTCIGNSGPLTPEieqaitknDLVAAAvlSGNRNFEGR 535
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
105-436 |
2.98e-23 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 103.35 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 105 GIVHMVGPE---------TGLTQPgKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTLWQTKPKNLKIDINGTLPT 175
Cdd:PLN00070 217 GIVHQVNLEylgrvvfntDGILYP-DSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRD 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 176 GVYAKDIIL---HLIKTYGVdfgTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDITFEYVK--GRpfADN 250
Cdd:PLN00070 296 GVTATDLVLtvtQMLRKHGV---VGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKltGR--SDE 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 251 FAKSVDKW---RELYSD-----DDAIFDRVIELDVSTLEPQVTWGTNPEMGVNFSEPFPEINDINDQRAyDYMGLEPGQK 322
Cdd:PLN00070 371 TVAMIEAYlraNKMFVDynepqQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHSCLDNKV-GFKGFAVPKE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 323 AEDIDLGYVFLG----------------SCTN-ARLSDLIEASHIVK-----GNKVHPNITAIVVPGSRTVKKEAEKLGL 380
Cdd:PLN00070 450 AQSKVAKFSFHGqpaelrhgsvviaaitSCTNtSNPSVMLGAGLVAKkacelGLEVKPWIKTSLAPGSGVVTKYLLKSGL 529
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 584659931 381 DTIFKNAGFEWREPGCSMCLGmNPDQVPEGVHCASTS-----------NRNFEGRQGKGAR-THLVSP 436
Cdd:PLN00070 530 QKYLNQQGFHIVGYGCTTCIG-NSGELDESVASAITEndivaaavlsgNRNFEGRVHPLTRaNYLASP 596
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
105-436 |
1.44e-21 |
|
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: 96.22 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 105 GIVHMVGPE-------------TGLTQPgKTIVCGDSHTATHGAFGAIAFGIGTSEVEHVFATQTLWQTKPKNLKIDING 171
Cdd:cd01586 94 GIIHQVNLEylarvvftseedgDGVAYP-DSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 172 TLPTGVYAKDIIL----HLIKtYGVdfgTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDditfeyvkgrpf 247
Cdd:cd01586 173 KLRPGVTATDLVLtvtqMLRK-VGV---VGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD------------ 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 248 adnfaksvdkwrelysdddaifDRVIELDVSTLEPQVTWGTNPEMGVnfsepfpeindindqraydymglepgqkAEDID 327
Cdd:cd01586 237 ----------------------TQVVELDLSTVEPSVSGPKRPQDRV----------------------------PLHGS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 328 LGYVFLGSCTN-ARLSDLIEASHIVK-----GNKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAGFEWREPGCSMCLG 401
Cdd:cd01586 267 VVIAAITSCTNtSNPSVMLAAGLLAKkavelGLKVKPYVKTSLAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIG 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 584659931 402 MN---PDQVPEGVH------CASTS-NRNFEGRQGKGAR-THLVSP 436
Cdd:cd01586 347 NSgplPEEVEEAIKendlvvAAVLSgNRNFEGRIHPLVRaNYLASP 392
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
105-424 |
8.69e-21 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 95.58 E-value: 8.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 105 GIVHMV-----GPETGLTQPGK------TIVCGDSHTaTH-GAFGAIAFGIGTSEVEHVFATQTLWQTKPKNLKIDINGT 172
Cdd:PRK09277 179 GICHQVnleylAPVVWTREDGElvaypdTLVGTDSHT-TMiNGLGVLGWGVGGIEAEAAMLGQPSSMLIPEVVGVKLTGK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 173 LPTGVYAKDIILHL---IKTYGVdfgTGYALEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDITFEYVK--GRPF 247
Cdd:PRK09277 258 LPEGVTATDLVLTVtemLRKKGV---VGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRltGRDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 248 A-----DNFAKSVDKWRElySDDDAIFDRVIELDVSTLEPQVTWGTNP-------EMGVNFSEPFPEindindqrAYDYM 315
Cdd:PRK09277 335 EqvalvEAYAKAQGLWRD--PLEEPVYTDVLELDLSTVEPSLAGPKRPqdriplsDVKEAFAKSAEL--------GVQGF 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 316 GLEPGQKAEDIDL--GYVFLG---SCTNArlSD---LIEASHIVK-----GNKVHPNITAIVVPGSRTVK---KEA---- 375
Cdd:PRK09277 405 GLDEAEEGEDYELpdGAVVIAaitSCTNT--SNpsvMIAAGLLAKkavekGLKVKPWVKTSLAPGSKVVTdylEKAgllp 482
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 584659931 376 --EKLGldtiFKNAGFewrepGCSMCLGMN---PDQVPE-----GVHCAS--TSNRNFEGR 424
Cdd:PRK09277 483 ylEALG----FNLVGY-----GCTTCIGNSgplPPEIEKaindnDLVVTAvlSGNRNFEGR 534
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
105-435 |
7.30e-19 |
|
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: 88.32 E-value: 7.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 105 GIVHMVgpETGLTQPGKTIVCGDSHTAthgaFG-AIAFGIGTSEVEHVFATQTLWQTKPKNLKIDINGTLPTGVYAKDII 183
Cdd:cd01581 94 GVIHSW--LNRMLLPDTVGTGGDSHTR----FPiGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 184 ------------LHLIKTYGVDFGTGYALEFTGetIKNLSMDGRMTICNMAIEGGAKYGIIQPDDITF-EYVK------- 243
Cdd:cd01581 168 naipyyaiqqglLTVEKKGKKNVFNGRILEIEG--LPDLKVEQAFELTDASAERSAAACTVRLDKEPViEYLEsnvvlmk 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 244 ---GRPFADNFA-----KSVDKWRE----LYSDDDAIFDRVIELDVSTL-EPQVtwgtnpemgvnfSEPfpeiNDINDQR 310
Cdd:cd01581 246 imiANGYDDARTllrriIAMEEWLAnpplLEPDADAEYAAVIEIDLDDIkEPIL------------ACP----NDPDDVK 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 311 AYDYMglepgqKAEDIDLgyVFLGSC-TNarLSDLIEASHIVKGNKVHPNITaIVVPGSRTVKKEAEKLGLDTIFKNAGF 389
Cdd:cd01581 310 LLSEV------AGKKIDE--VFIGSCmTN--IGHFRAAAKILRGKEFKPTRL-WVAPPTRMDWAILQEEGYYSIFGDAGA 378
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 584659931 390 EWREPGCSMCLGmNPDQVPEGVHCASTSNRNFEGRQGKGARTHLVS 435
Cdd:cd01581 379 RTEMPGCSLCMG-NQARVADGATVFSTSTRNFDNRVGKGAEVYLGS 423
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
116-426 |
1.68e-15 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 78.90 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 116 LTQPGKTIVCGDSHTaTHGAFGAIAFGIGTSEVehvfATQTLWQT----KPKNLKIDINGTLPTGVYAKDIILHLIktyG 191
Cdd:PRK11413 138 MAGGGKMILGSDSHT-RYGALGTMAVGEGGGEL----VKQLLNDTydidYPGVVAVYLTGKPAPGVGPQDVALAII---G 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 192 VDFGTGYA----LEFTGETIKNLSMDGRMTICNMAIEGGAKYGIIQPDDITFEYVK--GRPfadnfaksvDKWRELYSDD 265
Cdd:PRK11413 210 AVFKNGYVknkvMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLAlhGRG---------QDYCELNPQP 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 266 DAIFDRVIELDVSTLEPQVTWGTNP-------EMGVNFSEPFPEINDINDQRAYDYMGLEPGQKAEDIDLgYV---FLGS 335
Cdd:PRK11413 281 MAYYDGCISVDLSAIKPMIALPFHPsnvyeidELNQNLTDILREVEIESERVAHGKAKLSLLDKIENGRL-KVqqgIIAG 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 336 CTNARLSDLIEASHIVKGNKVHPNITAI-VVPGSRTVKKEAEKLGLDTIFKNAGFEWREPGCSMCLGMNPDQVPEGVHCA 414
Cdd:PRK11413 360 CSGGNYENVIAAANALRGQSCGNDTFSLsVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFGAGDTPANNGLSIR 439
|
330
....*....|..
gi 584659931 415 STSnRNFEGRQG 426
Cdd:PRK11413 440 HTT-RNFPNREG 450
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
323-435 |
7.45e-12 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 67.51 E-value: 7.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 323 AEDIDLgyVFLGSC-TNarLSDLIEASHIVKGNKVHPNITAIVVPGSRTVKKEAEKLGLDTIFKNAGFEWREPGCSMCLG 401
Cdd:PRK09238 688 GTKIDE--VFIGSCmTN--IGHFRAAGKLLEGKKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMG 763
|
90 100 110
....*....|....*....|....*....|....
gi 584659931 402 mNPDQVPEGVHCASTSNRNFEGRQGKGARTHLVS 435
Cdd:PRK09238 764 -NQARVADGATVFSTSTRNFPNRLGKGANVYLGS 796
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
105-447 |
9.84e-11 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 64.17 E-value: 9.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 105 GIVH-----MVGPETGLTQpgktivcGDSHTAthgaFG-AIAFGIGTSEVEHVFATQTLWQTKPKNLKIDINGTLPTGVY 178
Cdd:PLN00094 540 GVIHswlnrMLLPDTVGTG-------GDSHTR----FPiGISFPAGSGLVAFGAATGVIPLDMPESVLVRFTGTMQPGIT 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 179 AKDIIlHLIKTYGVDFG-------------TGYALEFTGetIKNLSMDGRMTICNMAIEGGAKYGIIQPDD--------- 236
Cdd:PLN00094 609 LRDLV-HAIPYTAIQDGlltvekkgkknvfSGRILEIEG--LPHLKCEQAFELSDASAERSAAGCTIKLDKepiieylns 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 237 --------ITFEYVKGRPFADNFAKsVDKWRE----LYSDDDAIFDRVIELDVSTL-EPQVTWGTNPEMGVNFSEPfpei 303
Cdd:PLN00094 686 nvvmlkwmIAEGYGDRRTLERRIAR-MQQWLAdpelLEADPDAEYAAVIEIDMDEIkEPILCAPNDPDDARLLSEV---- 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584659931 304 ndindqraydymglePGQKAEDidlgyVFLGSC-TNarLSDLIEASHIVKGNKVHPNITAIVVPGSRTVKKEAEKLGLDT 382
Cdd:PLN00094 761 ---------------TGDKIDE-----VFIGSCmTN--IGHFRAAGKLLNDNLSQLPTRLWVAPPTKMDEAQLKAEGYYS 818
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 584659931 383 IFKNAGFEWREPGCSMCLGmNPDQVPEGVHCASTSNRNFEGRQGKGARTHLVSPAMAAAAAIHGK 447
Cdd:PLN00094 819 TFGTVGARTEMPGCSLCMG-NQARVAEKSTVVSTSTRNFPNRLGKGANVYLASAELAAVAAILGR 882
|
|
| |
