|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-456 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 849.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 1 MQRTLYQKLWDAHVVVESDD-RALLYIDRHLLHEVSTPQSFEALREDGLTVRRPETQLAVADHSVPTHDRAEGIKDSQAA 79
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDgPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLPIADPVSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 80 AQVALLESNCAEFGIEYLRLDGEDQGIVHVIGPEQGFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQALWQ 159
Cdd:PRK05478 81 IQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 160 AKAKTMRVTFTGKLQAGVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTF 239
Cdd:PRK05478 161 KKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 240 AYVKGRPRAPHGADWDAAIAYWRTLTSDADALFDSEITIESETIAPQVTFGTSPDQVVSVRSLLPDDDRFAKP------- 312
Cdd:PRK05478 241 EYLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPvkrasae 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 313 --MRYMGVHAGEAMNGLTIDHAFIGSCTNGRIEDLRSAASIIRGGHVAPGVRALVVPGSMRVKAQAESEGLDKLFLDAGF 390
Cdd:PRK05478 321 raLAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1891802018 391 EWREPGCSLCVAMNTDRLPAGARCASTSNRNFEGRQGAGARTHLMSPVMVAAAAISGRIVDVREML 456
Cdd:PRK05478 401 EWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| 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: 684.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 1 MQRTLYQKLWDAHVVVESDDRA-LLYIDRHLLHEVSTPQSFEALREDGLTVRRPETQLAVADHSVPTHDRAEGIKDSQAA 79
Cdd:TIGR00170 1 MPRTLYEKLFDAHIVYEAEGETpLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFNIKDEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 80 AQVALLESNCAEFGIEYLRLDGEDQGIVHVIGPEQGFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQALWQ 159
Cdd:TIGR00170 81 IQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 160 AKAKTMRVTFTGKLQAGVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTF 239
Cdd:TIGR00170 161 ARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 240 AYVKGRPRAPHGADWDAAIAYWRTLTSDADALFDSEITIESETIAPQVTFGTSPDQVVSVRSLLPDDDRFAKPMR----- 314
Cdd:TIGR00170 241 EYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDkasae 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 315 ----YMGVHAGEAMNGLTIDHAFIGSCTNGRIEDLRSAASIIRGGHVAPGVRALVVPGSMRVKAQAESEGLDKLFLDAGF 390
Cdd:TIGR00170 321 ralaYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1891802018 391 EWREPGCSLCVAMNTDRLPAGARCASTSNRNFEGRQGAGARTHLMSPVMVAAAAISGRIVDVRE 454
Cdd:TIGR00170 401 EWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRK 464
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-455 |
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: 677.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 1 MQRTLYQKLWDAHVV--VESDDRALLYIDRHLLHEVSTPQSFEALREDG-LTVRRPETQLAVADHSVPThdraegiKDSQ 77
Cdd:COG0065 1 MGMTLAEKILARHAGreVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPT-------KDPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 78 AAAQVALLESNCAEFGIEYLrlDGEDQGIVHVIGPEQGFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQAL 157
Cdd:COG0065 74 SAEQVKTLREFAKEFGITFF--DVGDPGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 158 WQAKAKTMRVTFTGKLQAGVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVK 237
Cdd:COG0065 152 WFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 238 TFAYVKGRPRAPhgadwdaaiayWRTLTSDADALFDSEITIESETIAPQVTFGTSPDQVVSVRsllpdddrfakpmrymg 317
Cdd:COG0065 232 TFEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVS----------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 318 vhageAMNGLTIDHAFIGSCTNGRIEDLRSAASIIRGGHVAPGVRALVVPGSMRVKAQAESEGLDKLFLDAGFEWREPGC 397
Cdd:COG0065 284 -----ELEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGC 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1891802018 398 SLCVAMNTDRLPAGARCASTSNRNFEGRQG-AGARTHLMSPVMVAAAAISGRIVDVREM 455
Cdd:COG0065 359 GMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-447 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 615.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 7 QKLWDAHVVVESDDrALLYI-DRHLLHEVSTPQSFEALREDGLTVRRPETQLAVADHSVPTHDR--------AEGIKD-- 75
Cdd:pfam00330 1 EKIWDAHLVEELDG-SLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVidhapdalDKNIEDei 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 76 SQAAAQVALLESNCAEFGIeylRLDGEDQGIVHVIGPEQGFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQ 155
Cdd:pfam00330 80 SRNKEQYDFLEWNAKKFGI---RFVPPGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLATQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 156 ALWQAKAKTMRVTFTGKLQAGVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPD 235
Cdd:pfam00330 157 PLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 236 VKTFAYVK--GRPRAPHGADWDAAIAyWRTLTSDADALFDSEITIESETIAPQVTFGTSPDQVVSVRSLLPD-------D 306
Cdd:pfam00330 237 ETTFEYLRatGRPEAPKGEAYDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDpfadavkR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 307 DRFAKPMRYMGVHAGEAMNGLTIDHAFIGSCTNGRIEDLRSAASIIR-----GGHVAPGVRALVVPGSMRVKAQAESEGL 381
Cdd:pfam00330 316 KAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEAEGL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1891802018 382 DKLFLDAGFEWREPGCSLCVAmNTDRLPAGARCASTSNRNFEGRQGAGARTHLMSPVMVAAAAISG 447
Cdd:pfam00330 396 DKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASPALVAAAAIAG 460
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
28-449 |
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: 561.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 28 RHLLHEVSTPQSFEALREDGL-TVRRPETQLAVADHSVPTHDRAegikdsqAAAQVALLESNCAEFGIEYLrlDGEDQGI 106
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPTPDIK-------AAEQVKTLRKFAKEFGINFF--DVGRQGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 107 VHVIGPEQGFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQALWQAKAKTMRVTFTGKLQAGVSAKDMALAF 186
Cdd:cd01583 72 CHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 187 IGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTFAYVKGRPRaphgadwdaaiAYWRTLTS 266
Cdd:cd01583 152 IGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGK-----------AYWKELKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 267 DADALFDSEITIESETIAPQVTFGTSPDQVVSVRSLLPdddrfakpmrymgvhageamngLTIDHAFIGSCTNGRIEDLR 346
Cdd:cd01583 221 DEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG----------------------IKIDQVFIGSCTNGRLEDLR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 347 SAASIIRGGHVAPGVRALVVPGSMRVKAQAESEGLDKLFLDAGFEWREPGCSLCVAMNTDRLPAGARCASTSNRNFEGRQ 426
Cdd:cd01583 279 AAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTSNRNFKGRM 358
|
410 420
....*....|....*....|....
gi 1891802018 427 GA-GARTHLMSPVMVAAAAISGRI 449
Cdd:cd01583 359 GSpGARIYLASPATAAASAITGEI 382
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
16-449 |
1.73e-94 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 291.28 E-value: 1.73e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 16 VESDDRALLYIDRHLLHEVSTPQSFEALREDGLTVRRPETQLAVADHSVPTHDraegikdSQAAAQVALLESNCAEFGIE 95
Cdd:NF040615 16 VYAGDTVEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPANT-------VKAANMQKITREFVKEQGIK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 96 YLRLDGEdqGIVHVIGPEQGFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQALWQAKAKTMRVTFTGKlQA 175
Cdd:NF040615 89 NFYLGGE--GICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVNIVGK-NE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 176 GVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTFAYVKGRPRAphgadwD 255
Cdd:NF040615 166 NISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEGVS------E 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 256 AAIAYW---RTLTSDADALFDSEITIESETIAPQVTFGTSPDQVvsvrsllpdddrfaKPMrymgvhagEAMNGLTIDHA 332
Cdd:NF040615 240 EEIAELkknRITVNEKEENYYKEIEIDITDMEEQVACPHHPDNV--------------KPV--------SEVEGTEIDQV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 333 FIGSCTNGRIEDLRSAASIIRGGHVAPGVRALVVPGSMRVKAQAESEGLDKLFLDAGFEWREPGCSLCVAMNTDRLPAGA 412
Cdd:NF040615 298 FIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGE 377
|
410 420 430
....*....|....*....|....*....|....*...
gi 1891802018 413 RCASTSNRNFEGRQG-AGARTHLMSPVMVAAAAISGRI 449
Cdd:NF040615 378 VCLSTTNRNFKGRMGnINSYIYLSSPKIAAKSAVKGYI 415
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-456 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 849.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 1 MQRTLYQKLWDAHVVVESDD-RALLYIDRHLLHEVSTPQSFEALREDGLTVRRPETQLAVADHSVPTHDRAEGIKDSQAA 79
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDgPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLPIADPVSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 80 AQVALLESNCAEFGIEYLRLDGEDQGIVHVIGPEQGFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQALWQ 159
Cdd:PRK05478 81 IQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 160 AKAKTMRVTFTGKLQAGVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTF 239
Cdd:PRK05478 161 KKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 240 AYVKGRPRAPHGADWDAAIAYWRTLTSDADALFDSEITIESETIAPQVTFGTSPDQVVSVRSLLPDDDRFAKP------- 312
Cdd:PRK05478 241 EYLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPvkrasae 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 313 --MRYMGVHAGEAMNGLTIDHAFIGSCTNGRIEDLRSAASIIRGGHVAPGVRALVVPGSMRVKAQAESEGLDKLFLDAGF 390
Cdd:PRK05478 321 raLAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1891802018 391 EWREPGCSLCVAMNTDRLPAGARCASTSNRNFEGRQGAGARTHLMSPVMVAAAAISGRIVDVREML 456
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: 763.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 1 MQRTLYQKLWDAHVVVESDD-RALLYIDRHLLHEVSTPQSFEALREDGLTVRRPETQLAVADHSVPTHD-RAEGIKDSQA 78
Cdd:PRK12466 2 MPRTLYDKLWDSHTVARLDDgHVLLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPTRPgRDRGITDPGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 79 AAQVALLESNCAEFGIEYLRLDGEDQGIVHVIGPEQGFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQALW 158
Cdd:PRK12466 82 ALQVDYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQTLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 159 QAKAKTMRVTFTGKLQAGVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKT 238
Cdd:PRK12466 162 YRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 239 FAYVKGRPRAPHGADWDAAIAYWRTLTSDADALFDSEITIESETIAPQVTFGTSPDQVVSVRSLLPDDDRFAKPMR---- 314
Cdd:PRK12466 242 FDYLRGRPRAPKGALWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAAEADPARraam 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 315 -----YMGVHAGEAMNGLTIDHAFIGSCTNGRIEDLRSAASIIRGGHVAPGVRALVVPGSMRVKAQAESEGLDKLFLDAG 389
Cdd:PRK12466 322 eraldYMGLTPGTPLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAG 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1891802018 390 FEWREPGCSLCVAMNTDRLPAGARCASTSNRNFEGRQGAGARTHLMSPVMVAAAAISGRIVDVREML 456
Cdd:PRK12466 402 FEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHITDVRSLL 468
|
|
| 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: 684.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 1 MQRTLYQKLWDAHVVVESDDRA-LLYIDRHLLHEVSTPQSFEALREDGLTVRRPETQLAVADHSVPTHDRAEGIKDSQAA 79
Cdd:TIGR00170 1 MPRTLYEKLFDAHIVYEAEGETpLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFNIKDEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 80 AQVALLESNCAEFGIEYLRLDGEDQGIVHVIGPEQGFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQALWQ 159
Cdd:TIGR00170 81 IQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 160 AKAKTMRVTFTGKLQAGVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTF 239
Cdd:TIGR00170 161 ARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 240 AYVKGRPRAPHGADWDAAIAYWRTLTSDADALFDSEITIESETIAPQVTFGTSPDQVVSVRSLLPDDDRFAKPMR----- 314
Cdd:TIGR00170 241 EYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDkasae 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 315 ----YMGVHAGEAMNGLTIDHAFIGSCTNGRIEDLRSAASIIRGGHVAPGVRALVVPGSMRVKAQAESEGLDKLFLDAGF 390
Cdd:TIGR00170 321 ralaYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1891802018 391 EWREPGCSLCVAMNTDRLPAGARCASTSNRNFEGRQGAGARTHLMSPVMVAAAAISGRIVDVRE 454
Cdd:TIGR00170 401 EWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRK 464
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-455 |
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: 677.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 1 MQRTLYQKLWDAHVV--VESDDRALLYIDRHLLHEVSTPQSFEALREDG-LTVRRPETQLAVADHSVPThdraegiKDSQ 77
Cdd:COG0065 1 MGMTLAEKILARHAGreVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPT-------KDPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 78 AAAQVALLESNCAEFGIEYLrlDGEDQGIVHVIGPEQGFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQAL 157
Cdd:COG0065 74 SAEQVKTLREFAKEFGITFF--DVGDPGICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 158 WQAKAKTMRVTFTGKLQAGVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVK 237
Cdd:COG0065 152 WFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 238 TFAYVKGRPRAPhgadwdaaiayWRTLTSDADALFDSEITIESETIAPQVTFGTSPDQVVSVRsllpdddrfakpmrymg 317
Cdd:COG0065 232 TFEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVS----------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 318 vhageAMNGLTIDHAFIGSCTNGRIEDLRSAASIIRGGHVAPGVRALVVPGSMRVKAQAESEGLDKLFLDAGFEWREPGC 397
Cdd:COG0065 284 -----ELEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGC 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1891802018 398 SLCVAMNTDRLPAGARCASTSNRNFEGRQG-AGARTHLMSPVMVAAAAISGRIVDVREM 455
Cdd:COG0065 359 GMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-447 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 615.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 7 QKLWDAHVVVESDDrALLYI-DRHLLHEVSTPQSFEALREDGLTVRRPETQLAVADHSVPTHDR--------AEGIKD-- 75
Cdd:pfam00330 1 EKIWDAHLVEELDG-SLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVidhapdalDKNIEDei 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 76 SQAAAQVALLESNCAEFGIeylRLDGEDQGIVHVIGPEQGFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQ 155
Cdd:pfam00330 80 SRNKEQYDFLEWNAKKFGI---RFVPPGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLATQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 156 ALWQAKAKTMRVTFTGKLQAGVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPD 235
Cdd:pfam00330 157 PLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 236 VKTFAYVK--GRPRAPHGADWDAAIAyWRTLTSDADALFDSEITIESETIAPQVTFGTSPDQVVSVRSLLPD-------D 306
Cdd:pfam00330 237 ETTFEYLRatGRPEAPKGEAYDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDpfadavkR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 307 DRFAKPMRYMGVHAGEAMNGLTIDHAFIGSCTNGRIEDLRSAASIIR-----GGHVAPGVRALVVPGSMRVKAQAESEGL 381
Cdd:pfam00330 316 KAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEAEGL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1891802018 382 DKLFLDAGFEWREPGCSLCVAmNTDRLPAGARCASTSNRNFEGRQGAGARTHLMSPVMVAAAAISG 447
Cdd:pfam00330 396 DKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASPALVAAAAIAG 460
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
28-449 |
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: 561.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 28 RHLLHEVSTPQSFEALREDGL-TVRRPETQLAVADHSVPTHDRAegikdsqAAAQVALLESNCAEFGIEYLrlDGEDQGI 106
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPTPDIK-------AAEQVKTLRKFAKEFGINFF--DVGRQGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 107 VHVIGPEQGFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQALWQAKAKTMRVTFTGKLQAGVSAKDMALAF 186
Cdd:cd01583 72 CHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 187 IGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTFAYVKGRPRaphgadwdaaiAYWRTLTS 266
Cdd:cd01583 152 IGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGK-----------AYWKELKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 267 DADALFDSEITIESETIAPQVTFGTSPDQVVSVRSLLPdddrfakpmrymgvhageamngLTIDHAFIGSCTNGRIEDLR 346
Cdd:cd01583 221 DEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG----------------------IKIDQVFIGSCTNGRLEDLR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 347 SAASIIRGGHVAPGVRALVVPGSMRVKAQAESEGLDKLFLDAGFEWREPGCSLCVAMNTDRLPAGARCASTSNRNFEGRQ 426
Cdd:cd01583 279 AAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTSNRNFKGRM 358
|
410 420
....*....|....*....|....
gi 1891802018 427 GA-GARTHLMSPVMVAAAAISGRI 449
Cdd:cd01583 359 GSpGARIYLASPATAAASAITGEI 382
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
1-456 |
1.09e-142 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 414.57 E-value: 1.09e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 1 MQRTLYQKLWDAHVV--VESDDRALLYIDRHLLHEVSTPQSFEALREDGLT-VRRPETQLAVADHSVPThdraegiKDSQ 77
Cdd:PRK00402 1 MGMTLAEKILARHSGrdVSPGDIVEAKVDLVMAHDITGPLAIKEFEKIGGDkVFDPSKIVIVFDHFVPA-------KDIK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 78 AAAQVALLESNCAEFGIEYLrLDGEDqGIVHVIGPEQGFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQAL 157
Cdd:PRK00402 74 SAEQQKILREFAKEQGIPNF-FDVGE-GICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 158 WQAKAKTMRVTFTGKLQAGVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVK 237
Cdd:PRK00402 152 WFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 238 TFAYVKGRPRAPhgadwdaaiayWRTLTSDADALFDSEITIESETIAPQVTFGTSPDQVVSVRSllpdddrfakpmrymg 317
Cdd:PRK00402 232 TLEYLKERAGRD-----------YKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSE---------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 318 vhageaMNGLTIDHAFIGSCTNGRIEDLRSAASIIRGGHVAPGVRALVVPGSMRVKAQAESEGLDKLFLDAGFEWREPGC 397
Cdd:PRK00402 285 ------VEGTKVDQVFIGSCTNGRLEDLRIAAEILKGRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTC 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 398 SLCVAMNTDRLPAGARCASTSNRNFEGRQG-AGARTHLMSPVMVAAAAISGRIVDVREML 456
Cdd:PRK00402 359 GPCLGGHMGVLAPGEVCLSTTNRNFKGRMGsPESEVYLASPAVAAASAVTGKITDPREVL 418
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
4-453 |
3.51e-120 |
|
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: 357.14 E-value: 3.51e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 4 TLYQKLWDAHV--VVESDDRALLYIDRHLLHEVSTPQSFEALREDGLT-VRRPETQLAVADHSVPTHDRaegikdsQAAA 80
Cdd:TIGR01343 1 TIAEKILSKKSgkEVYAGDLIEAEIDLAMVHDITAPLAIKTLEEYGIDkVWNPEKIVIVFDHQVPADTI-------KAAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 81 QVALLESNCAEFGIEYLRLDGEdqGIVHVIGPEQGFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQALWQA 160
Cdd:TIGR01343 74 MQKLAREFVKKQGIKYFYDVGE--GICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 161 KAKTMRVTFTGKLQAGVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTFA 240
Cdd:TIGR01343 152 VPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 241 YVKGRPRAPhgadwdaaiayWRTLTSDADALFDSEITIESETIAPQVTFGTSPDQVVSVRSLlpdddrfakpmrymgvha 320
Cdd:TIGR01343 232 YLKERRKEP-----------FRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEV------------------ 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 321 geamNGLTIDHAFIGSCTNGRIEDLRSAASIIRGGHVAPGVRALVVPGSMRVKAQAESEGLDKLFLDAGFEWREPGCSLC 400
Cdd:TIGR01343 283 ----EGTEIDQVFIGSCTNGRLEDLRVAAKILKGRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPC 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1891802018 401 VAMNTDRLPAGARCASTSNRNFEGRQG-AGARTHLMSPVMVAAAAISGRIVDVR 453
Cdd:TIGR01343 359 LGSHQGVLAPGEVCISTSNRNFKGRMGhPNAEIYLASPATAAASAVKGYIADPR 412
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
4-454 |
2.44e-98 |
|
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA family (Homoaconitate hydratase family, TIGR01343) and is most closely related to the 3-isopropylmalate dehydratase, large subunits which form TIGR00170. This subfamily includes the members of TIGR01343 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities.
Pssm-ID: 273960 Cd Length: 413 Bit Score: 301.30 E-value: 2.44e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 4 TLYQKLWDAHV--VVESDDRALLYIDRHLLHEVSTPQSFEALREDG-LTVRRPETQLAVADHSVPTHDRaegikdSQAAA 80
Cdd:TIGR02086 2 TLAEKILSEKVgrPVCAGEIVEVEVDLAMTHDGTGPLAIKALRELGvARVWDPEKIVIAFDHNVPPPTV------EAAEM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 81 QVALLESnCAEFGIEYLRLDgedQGIVHVIGPEQGFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQALWQA 160
Cdd:TIGR02086 76 QKEIREF-AKRHGIKNFDVG---EGICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTWIK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 161 KAKTMRVTFTGKLQAGVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTFA 240
Cdd:TIGR02086 152 VPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEETYE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 241 YVKGRPRAPhgadwdaaiayWRTLTSDADALFDSEITIESETIAPQVTFGTSPDQVVSVrsllpdddrfakpmrymgvha 320
Cdd:TIGR02086 232 YLKKRRGLE-----------FRILVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPV--------------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 321 gEAMNGLTIDHAFIGSCTNGRIEDLRSAASIIRGGHVAPGVRALVVPGSMRVKAQAESEGLDKLFLDAGFEWREPGCSLC 400
Cdd:TIGR02086 280 -SDVEGTEIDQVFIGSCTNGRLEDLRIAAEILKGRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAGAMICPPGCGPC 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1891802018 401 VAMNTDRLPAGARCASTSNRNFEGRQGA-GARTHLMSPVMVAAAAISGRIVDVRE 454
Cdd:TIGR02086 359 LGAHMGVLGDGEVCLSTTNRNFKGRMGSpNAEIYLASPATAAASAVEGYITDPED 413
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
16-449 |
1.73e-94 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 291.28 E-value: 1.73e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 16 VESDDRALLYIDRHLLHEVSTPQSFEALREDGLTVRRPETQLAVADHSVPTHDraegikdSQAAAQVALLESNCAEFGIE 95
Cdd:NF040615 16 VYAGDTVEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPANT-------VKAANMQKITREFVKEQGIK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 96 YLRLDGEdqGIVHVIGPEQGFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQALWQAKAKTMRVTFTGKlQA 175
Cdd:NF040615 89 NFYLGGE--GICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVNIVGK-NE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 176 GVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTFAYVKGRPRAphgadwD 255
Cdd:NF040615 166 NISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEGVS------E 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 256 AAIAYW---RTLTSDADALFDSEITIESETIAPQVTFGTSPDQVvsvrsllpdddrfaKPMrymgvhagEAMNGLTIDHA 332
Cdd:NF040615 240 EEIAELkknRITVNEKEENYYKEIEIDITDMEEQVACPHHPDNV--------------KPV--------SEVEGTEIDQV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 333 FIGSCTNGRIEDLRSAASIIRGGHVAPGVRALVVPGSMRVKAQAESEGLDKLFLDAGFEWREPGCSLCVAMNTDRLPAGA 412
Cdd:NF040615 298 FIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGE 377
|
410 420 430
....*....|....*....|....*....|....*...
gi 1891802018 413 RCASTSNRNFEGRQG-AGARTHLMSPVMVAAAAISGRI 449
Cdd:NF040615 378 VCLSTTNRNFKGRMGnINSYIYLSSPKIAAKSAVKGYI 415
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
30-449 |
3.72e-80 |
|
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: 253.57 E-value: 3.72e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 30 LLHEVSTP---QSFEALREDGLtVRRPETQLAVADHSVPthdraegIKDSQAAAQVALLESNCAEFGIEYLRLDGedqGI 106
Cdd:cd01351 3 MLQDATGPmamKAFEILAALGK-VADPSQIACVHDHAVQ-------LEKPVNNEGHKFLSFFAALQGIAFYRPGV---GI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 107 VHVIGPEQgFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQALWQAKAKTMRVTFTGKLQAGVSAKDMALAF 186
Cdd:cd01351 72 IHQIMVEN-LALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 187 IGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTFAYVKGRPRAPHGADWDaaiAYWRTLTS 266
Cdd:cd01351 151 GGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWL---AFPEELLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 267 DADALFDSEITIESETIAPQVTFGTSPDQVVSVrsllpdddrfakpmrymgvhagEAMNGLTIDHAFIGSCTNGRIEDLR 346
Cdd:cd01351 228 DEGAEYDQVIEIDLSELEPDISGPNRPDDAVSV----------------------SEVEGTKIDQVLIGSCTNNRYSDML 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 347 SAASIIRGGHVAPGVRALVVPGSMRVKAQAESEGLDKLFLDAGFEWREPGCSLCVAMNTDRLPAGARCASTSNRNFEGRQ 426
Cdd:cd01351 286 AAAKLLKGAKVAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLVADGEVGVSSGNRNFPGRL 365
|
410 420
....*....|....*....|....
gi 1891802018 427 GAG-ARTHLMSPVMVAAAAISGRI 449
Cdd:cd01351 366 GTYeRHVYLASPELAAATAIAGKI 389
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
1-455 |
1.87e-64 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 219.25 E-value: 1.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 1 MQRTLYQKLWDAHVV---VESDDRALLYIDRHLLHEvSTPQ----SFEALREDgltvrRPETQLAVA--DHSVPThdrae 71
Cdd:PRK07229 1 MGLTLTEKILYAHLVegeLEPGEEIAIRIDQTLTQD-ATGTmaylQFEAMGLD-----RVKTELSVQyvDHNLLQ----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 72 giKDSQAAAQVALLESNCAEFGIEYLRLDGedqGIVHVIGPEQgFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTV 151
Cdd:PRK07229 70 --ADFENADDHRFLQSVAAKYGIYFSKPGN---GICHQVHLER-FAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 152 MATQALWQAKAKTMRVTFTGKLQAGVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGL 231
Cdd:PRK07229 144 MAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 232 VAPDVKTFAYVK--GRpraphGADWDAaiaywrtLTSDADALFDSEITIESETIAPQVTFGTSPDQVVSVRSLlpdddrf 309
Cdd:PRK07229 224 FPSDERTREFLKaqGR-----EDDWVE-------LLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSEV------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 310 akpmrymgvhAGEAmngltIDHAFIGSCTNGRIEDLRSAASIIRGGHVAPGVRALVVPGSMRVKAQAESEGLDKLFLDAG 389
Cdd:PRK07229 285 ----------AGIK-----VDQVLIGSCTNSSYEDLMRAASILKGKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAG 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1891802018 390 FEWREPGCSLCVAMNTDrlPA-GARCASTSNRNFEGRQG-AGARTHLMSPVMVAAAAISGRIVDVREM 455
Cdd:PRK07229 350 ARILENACGPCIGMGQA--PAtGNVSLRTFNRNFPGRSGtKDAQVYLASPETAAASALTGVITDPRTL 415
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
85-449 |
1.86e-59 |
|
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: 199.21 E-value: 1.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 85 LESNCAEFGIEYLRldgEDQGIVHVIGPEQgFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQALWQAKAKT 164
Cdd:cd01585 52 LQTVAARYGIYFSR---PGNGICHQVHLER-FAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 165 MRVTFTGKLQAGVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTFAYVKG 244
Cdd:cd01585 128 VGVRLTGELPPWVTAKDVILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 245 RPRAphgadwdaaiAYWRTLTSDADALFDSEITIESETIAPQVTFGTSPDQVVSVRSLlpdddrfakpmrymgvhageam 324
Cdd:cd01585 208 QGRE----------DDWVELAADADAEYDEEIEIDLSELEPLIARPHSPDNVVPVREV---------------------- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 325 NGLTIDHAFIGSCTNGRIEDLRSAASIIRGGHVAPGVRALVVPGSMRVKAQAESEGLDKLFLDAGFEWREPGCSLCVAMN 404
Cdd:cd01585 256 AGIKVDQVAIGSCTNSSYEDLMTVAAILKGRRVHPHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMG 335
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1891802018 405 TDRlPAGARCASTSNRNFEGRQG-AGARTHLMSPVMVAAAAISGRI 449
Cdd:cd01585 336 QAP-PTGGVSVRTFNRNFEGRSGtKDDLVYLASPEVAAAAALTGVI 380
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
85-449 |
3.47e-43 |
|
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: 156.83 E-value: 3.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 85 LESNCAEFGIEYLRldgEDQGIVHVIGPEQgFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQAlWQAKA-K 163
Cdd:cd01584 60 LASAGAKYGIGFWK---PGSGIIHQIVLEN-YAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIP-WELKCpK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 164 TMRVTFTGKLQAGVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTFAYVK 243
Cdd:cd01584 135 VIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 244 GRPRAphGADWDAAIAYWRTLTSDADALFDSEITIESETIAPQVTFGTSPDqvvsvrsllpdddrFAKPMRYMGVHAGEA 323
Cdd:cd01584 215 ATGRA--EIADLADEFKDDLLVADEGAEYDQLIEINLSELEPHINGPFTPD--------------LATPVSKFKEVAEKN 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 324 MNGLTIDHAFIGSCTNGRIEDLRSAASIIRGGhVAPGVRA----LVVPGSMRVKAQAESEGLDKLFLDAGFEWREPGCSL 399
Cdd:cd01584 279 GWPLDLRVGLIGSCTNSSYEDMGRAASIAKQA-LAHGLKCksifTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGP 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1891802018 400 CVAMnTDR--LPAGARCA--STSNRNFEGRQGAGARTH--LMSPVMVAAAAISGRI 449
Cdd:cd01584 358 CIGQ-WDRkdIKKGEKNTivTSYNRNFTGRNDANPATHafVASPEIVTAMAIAGTL 412
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
104-449 |
1.41e-41 |
|
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: 151.61 E-value: 1.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 104 QGIVHVIGPEQGFTLPGMTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQALWQAKAKTMRVTFTGKLQAGVSAKDMA 183
Cdd:cd01582 67 RGIGHQIMIEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 184 LAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKtfayvkgrpraphgadwdaaiaywrt 263
Cdd:cd01582 147 VALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAK-------------------------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 264 ltsdadalfdsEITIESETIAPQVTfgtSPDqvvSVRSLLPDDDRFAKPMRymgvhageamngltIDHAFIGSCTNGRIE 343
Cdd:cd01582 201 -----------HLILDLSTLSPYVS---GPN---SVKVSTPLKELEAQNIK--------------INKAYLVSCTNSRAS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 344 DLRSAASIIRG-------GHVAPGVRALVVPGSMRVKAQAESEGLDKLFLDAGFEWREPGCSLCVAMNTDRLPAGARCAS 416
Cdd:cd01582 250 DIAAAADVVKGkkekngkIPVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQGLLEPGEVGIS 329
|
330 340 350
....*....|....*....|....*....|....
gi 1891802018 417 TSNRNFEGRQGA-GARTHLMSPVMVAAAAISGRI 449
Cdd:cd01582 330 ATNRNFKGRMGStEALAYLASPAVVAASAISGKI 363
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
105-449 |
2.03e-30 |
|
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: 124.83 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 105 GIVH----------VIGPEQGFTL---PGmTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQALwqakakTMR----- 166
Cdd:COG1048 176 GIVHqvnleylafvVWTREEDGETvayPD-TLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPV------SMLipevv 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 167 -VTFTGKLQAGVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTFAYVK-- 243
Cdd:COG1048 249 gVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRlt 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 244 GRPraphgadwDAAI----AY------WRTlTSDADALFDSEITIESETIAPQVTFGTSPDQVV-------SVRSLLPDD 306
Cdd:COG1048 329 GRS--------EEQIelveAYakaqglWRD-PDAPEPYYSDVLELDLSTVEPSLAGPKRPQDRIplsdlkeAFRAALAAP 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 307 DRFAKPMRYMGVHAGEamnGLTIDH-----AFIGSCTNGRIEDLRSAASII------RGGHVAPGVRALVVPGSMRVKAQ 375
Cdd:COG1048 400 VGEELDKPVRVEVDGE---EFELGHgavviAAITSCTNTSNPSVMIAAGLLakkaveKGLKVKPWVKTSLAPGSKVVTDY 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 376 AESEGLDKlFLDA------GFewrepGCSLCVAmNTDRLPA---------GARCAS-TS-NRNFEGRQGAGART-HLMSP 437
Cdd:COG1048 477 LERAGLLP-YLEAlgfnvvGY-----GCTTCIG-NSGPLPPeiseaieenDLVVAAvLSgNRNFEGRIHPDVKAnFLASP 549
|
410
....*....|..
gi 1891802018 438 VMVAAAAISGRI 449
Cdd:COG1048 550 PLVVAYALAGTV 561
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
105-449 |
8.37e-29 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 120.04 E-value: 8.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 105 GIVHVIGPEQ-------------GFTLPGmTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQALWQAKAKTMRVTFTG 171
Cdd:PRK12881 178 GIMHQVNLEYlarvvhtkeddgdTVAYPD-TLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIPDVVGVELTG 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 172 KLQAGVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTFAYVK--GRPrap 249
Cdd:PRK12881 257 KLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLRltGRT--- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 250 hgadwDAAIAYWRTLT--------SDADALFDSEITIESETIAPQVTFGTSPDQVVSVRSLLPD-DDRFAKPMRYMGV-H 319
Cdd:PRK12881 334 -----EAQIALVEAYAkaqglwgdPKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAfSDLFSKPVAENGFaK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 320 AGEAMNGLTIDH-----AFIGSCTNGRIEDLRSAASII------RGGHVAPGVRALVVPGSMRVKAQAESEGLDKlFLDA 388
Cdd:PRK12881 409 KAQTSNGVDLPDgavaiAAITSCTNTSNPSVLIAAGLLakkaveRGLTVKPWVKTSLAPGSKVVTEYLERAGLLP-YLEK 487
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1891802018 389 -GFEWREPGCSLCVAMNTDRLPA--------GARCAS--TSNRNFEGRQGAGARTH-LMSPVMVAAAAISGRI 449
Cdd:PRK12881 488 lGFGIVGYGCTTCIGNSGPLTPEieqaitknDLVAAAvlSGNRNFEGRIHPNIKANfLASPPLVVAYALAGTV 560
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
105-449 |
5.67e-26 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 111.26 E-value: 5.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 105 GIVH---------VIGPEQGFTLPGmTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQALWQAKAKTMRVTFTGKLQA 175
Cdd:PTZ00092 185 GIVHqvnleylarVVFNKDGLLYPD-SVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTGKLSE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 176 GVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTFAYVK--GRPRaphgAD 253
Cdd:PTZ00092 264 HVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKqtGRSE----EK 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 254 WDAAIAYWR----TLTSDADALFDSEITIESETIAPQVTFGTSPDQVVSVRSL------------------LPDDDRfAK 311
Cdd:PTZ00092 340 VELIEKYLKanglFRTYAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLkkdftaclsapvgfkgfgIPEEKH-EK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 312 PMRYMgVHAGEAmnglTIDH-----AFIGSCTNGRIEDLRSAASII------RGGHVAPGVRALVVPGSMRVKAQAESEG 380
Cdd:PTZ00092 419 KVKFT-YKGKEY----TLTHgsvviAAITSCTNTSNPSVMLAAGLLakkaveKGLKVPPYIKTSLSPGSKVVTKYLEASG 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 381 LDKlFLDA-GFEWREPGCSLCVAMNTDRLPAGARCAS----------TSNRNFEGRQGAGAR-THLMSPVMVAAAAISGR 448
Cdd:PTZ00092 494 LLK-YLEKlGFYTAGYGCMTCIGNSGDLDPEVSEAITnndlvaaavlSGNRNFEGRVHPLTRaNYLASPPLVVAYALAGR 572
|
.
gi 1891802018 449 I 449
Cdd:PTZ00092 573 V 573
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
117-449 |
1.97e-21 |
|
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle; Aconitase B catalytic domain. Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle. Aconitase has an active (4FE-4S) and an inactive (3FE-4S) form. The active cluster is part of the catalytic site that interconverts citrate, cis-aconitase and isocitrate. The domain architecture of aconitase B is different from other aconitases in that the catalytic domain is normally found at C-terminus for other aconitases, but it is at N-terminus for B family. It also has a HEAT domain before domain 4 which plays a role in protein-protein interaction. This alignment is the core domain including domains 1,2 and 3.
Pssm-ID: 153131 Cd Length: 436 Bit Score: 96.03 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 117 TLPGMTLVCGDSHTSthgaFG-ALAFGVGASECGTVMATQALWQAKAKTMRVTFTGKLQAGVSAKDMALAF--------I 187
Cdd:cd01581 104 LLPDTVGTGGDSHTR----FPiGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVNAIpyyaiqqgL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 188 GTVGASGGSGYateFAG-----EAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTFA-YV------------KGRPRAP 249
Cdd:cd01581 180 LTVEKKGKKNV---FNGrileiEGLPDLKVEQAFELTDASAERSAAACTVRLDKEPVIeYLesnvvlmkimiaNGYDDAR 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 250 HGADWDAAIAYWRT----LTSDADALFDSEITIESETIAPQVTfgTSPDQvvsvrsllPDDDrfaKPMRYmgVHageamn 325
Cdd:cd01581 257 TLLRRIIAMEEWLAnpplLEPDADAEYAAVIEIDLDDIKEPIL--ACPND--------PDDV---KLLSE--VA------ 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 326 GLTIDHAFIGSC-TNgrIEDLRSAASIIRGGHVAPgVRALVVPGSMRVKAQAESEGLDKLFLDAGFEWREPGCSLCVAmN 404
Cdd:cd01581 316 GKKIDEVFIGSCmTN--IGHFRAAAKILRGKEFKP-TRLWVAPPTRMDWAILQEEGYYSIFGDAGARTEMPGCSLCMG-N 391
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1891802018 405 TDRLPAGARCASTSNRNFEGRQGAGARTHLMSPVMVAAAAISGRI 449
Cdd:cd01581 392 QARVADGATVFSTSTRNFDNRVGKGAEVYLGSAELAAVCALLGRI 436
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
105-452 |
7.33e-20 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 92.56 E-value: 7.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 105 GIVHVIGPE---------QGFTLPGmTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQALWQAKAKTMRVTFTGKLQA 175
Cdd:PLN00070 217 GIVHQVNLEylgrvvfntDGILYPD-SVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRD 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 176 GVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTFAYVK--GRpraphgAD 253
Cdd:PLN00070 296 GVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKltGR------SD 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 254 WDAAI--AYWRT-------LTSDADALFDSEITIESETIAPQVTFGTSPDQVVSVRSLLPD-----DDR-----FAKPMR 314
Cdd:PLN00070 370 ETVAMieAYLRAnkmfvdyNEPQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADwhsclDNKvgfkgFAVPKE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 315 YMGVHAGEAMNGLT--IDH-----AFIGSCTNGRIEDLRSAASIIR------GGHVAPGVRALVVPGSMRVKAQAESEGL 381
Cdd:PLN00070 450 AQSKVAKFSFHGQPaeLRHgsvviAAITSCTNTSNPSVMLGAGLVAkkacelGLEVKPWIKTSLAPGSGVVTKYLLKSGL 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 382 DKLFLDAGFEWREPGCSLCVAMNTDRLPAGARCAS----------TSNRNFEGRQGAGAR-THLMSPVMVAAAAISGrIV 450
Cdd:PLN00070 530 QKYLNQQGFHIVGYGCTTCIGNSGELDESVASAITendivaaavlSGNRNFEGRVHPLTRaNYLASPPLVVAYALAG-TV 608
|
..
gi 1891802018 451 DV 452
Cdd:PLN00070 609 DI 610
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
105-449 |
5.18e-19 |
|
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: 88.52 E-value: 5.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 105 GIVHVIGPE-------------QGFTLPGmTLVCGDSHTSTHGAFGALAFGVGASECGTVMATQALWQAKAKTMRVTFTG 171
Cdd:cd01586 94 GIIHQVNLEylarvvftseedgDGVAYPD-SVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 172 KLQAGVSAKDMALAFIGTVGASGGSGYATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTfayvkgrpraphg 251
Cdd:cd01586 173 KLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVDTQV------------- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 252 adwdaaiaywrtltsdadalfdseITIESETIAPQVTFGTSPDQVVSvrsllpdddrfakpmrymgVHAgeamnglTIDH 331
Cdd:cd01586 240 ------------------------VELDLSTVEPSVSGPKRPQDRVP-------------------LHG-------SVVI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 332 AFIGSCTNGRIEDLRSAASII------RGGHVAPGVRALVVPGSMRVKAQAESEGLDKlFLDA-GFEWREPGCSLCVAmN 404
Cdd:cd01586 270 AAITSCTNTSNPSVMLAAGLLakkaveLGLKVKPYVKTSLAPGSRVVTKYLEASGLLP-YLEKlGFHVVGYGCTTCIG-N 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1891802018 405 TDRLPA---------GARCAS--TSNRNFEGRQGAGAR-THLMSPVMVAAAAISGRI 449
Cdd:cd01586 348 SGPLPEeveeaikenDLVVAAvlSGNRNFEGRIHPLVRaNYLASPPLVVAYALAGTV 404
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
122-449 |
3.23e-18 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 87.49 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 122 TLVCGDSHTsTH-GAFGALAFGVGASECGTVMATQALWqakaktMR------VTFTGKLQAGVSAKDMALAF------IG 188
Cdd:PRK09277 207 TLVGTDSHT-TMiNGLGVLGWGVGGIEAEAAMLGQPSS------MLipevvgVKLTGKLPEGVTATDLVLTVtemlrkKG 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 189 TVGAsggsgyATEFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTFAYVK--GRPraphgadwDAAI----AY-- 260
Cdd:PRK09277 280 VVGK------FVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRltGRD--------EEQValveAYak 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 261 ----WRtlTSDADALFDSEITIESETIAPQVTFGTSPDQVVSVRSLlpdDDRFAK----PMRYMGVHAGEAMNGLTIDH- 331
Cdd:PRK09277 346 aqglWR--DPLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDV---KEAFAKsaelGVQGFGLDEAEEGEDYELPDg 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 332 ----AFIGSCTNgriedlRS------AASII------RGGHVAPGVRALVVPGSMRVKAQAESEGLDKlFLDA------G 389
Cdd:PRK09277 421 avviAAITSCTN------TSnpsvmiAAGLLakkaveKGLKVKPWVKTSLAPGSKVVTDYLEKAGLLP-YLEAlgfnlvG 493
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1891802018 390 FewrepGCSLCVAMNTDRLPAGARC------ASTS----NRNFEGRQGAGART-HLMSPVMVAAAAISGRI 449
Cdd:PRK09277 494 Y-----GCTTCIGNSGPLPPEIEKAindndlVVTAvlsgNRNFEGRIHPLVKAnYLASPPLVVAYALAGTV 559
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
304-457 |
7.81e-18 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 86.39 E-value: 7.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 304 PDDdrfAKPMRYMGvhageamnGLTIDHAFIGSC-TNgrIEDLRSAASIIRGGHVAPGVRALVVPGSMRVKAQAESEGLD 382
Cdd:PRK09238 677 PDD---VRLLSEVA--------GTKIDEVFIGSCmTN--IGHFRAAGKLLEGKKGQLPTRLWVAPPTKMDADQLTEEGYY 743
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1891802018 383 KLFLDAGFEWREPGCSLCvaM-NTDRLPAGARCASTSNRNFEGRQGAGARTHLMSPVMVAAAAISGRIVDVREMLA 457
Cdd:PRK09238 744 SIFGKAGARIEMPGCSLC--MgNQARVADGATVFSTSTRNFPNRLGKGANVYLGSAELAAVCALLGRIPTVEEYQE 817
|
|
| AcnB |
COG1049 |
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ... |
326-457 |
2.13e-16 |
|
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440670 [Multi-domain] Cd Length: 852 Bit Score: 81.82 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 326 GLTIDHAFIGSC-TNgrIEDLRSAASIIRGGHVAPgVRALVVPGSMRVKAQAESEGLDKLFLDAGFEWREPGCSLCvaM- 403
Cdd:COG1049 688 GTKIDEVFIGSCmTN--IGHFRAAGKLLEGKGNLP-TRLWIAPPTKMDEAQLTEEGYYSIFGAAGARTEMPGCSLC--Mg 762
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1891802018 404 NTDRLPAGARCASTSNRNFEGRQGAGARTHLMSPVMVAAAAISGRIVDVREMLA 457
Cdd:COG1049 763 NQARVADGATVFSTSTRNFPNRLGKGANVYLGSAELAAVCALLGRLPTVEEYME 816
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
326-457 |
1.73e-14 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 76.11 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 326 GLTIDHAFIGSC-TNgrIEDLRSAASIIRGGHVAPGVRALVVPGSMRVKAQAESEGLDKLFLDAGFEWREPGCSLCVAmN 404
Cdd:PLN00094 762 GDKIDEVFIGSCmTN--IGHFRAAGKLLNDNLSQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPGCSLCMG-N 838
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1891802018 405 TDRLPAGARCASTSNRNFEGRQGAGARTHLMSPVMVAAAAISGRIVDVREMLA 457
Cdd:PLN00094 839 QARVAEKSTVVSTSTRNFPNRLGKGANVYLASAELAAVAAILGRLPTVEEYLS 891
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
127-447 |
4.80e-12 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 68.11 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 127 DSHTStHGAFGALAFGVGASEcgtvMATQALWQ----AKAKTMRVTFTGKLQAGVSAKDMALAFIGTVgasGGSGYAT-- 200
Cdd:PRK11413 149 DSHTR-YGALGTMAVGEGGGE----LVKQLLNDtydiDYPGVVAVYLTGKPAPGVGPQDVALAIIGAV---FKNGYVKnk 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 201 --EFAGEAVQALSMEGRMTLCNMAIEAGSRTGLVAPDVKTFAYVK--GRPRAphgadwdaaiayWRTLTSDADALFDSEI 276
Cdd:PRK11413 221 vmEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLAlhGRGQD------------YCELNPQPMAYYDGCI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 277 TIESETIAPQVTFGTSPDQVVSVRSL-------LPDDDRFAKPMRYMGVH---AGEAMNG-LTIDHAFIGSCTNGRIEDL 345
Cdd:PRK11413 289 SVDLSAIKPMIALPFHPSNVYEIDELnqnltdiLREVEIESERVAHGKAKlslLDKIENGrLKVQQGIIAGCSGGNYENV 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891802018 346 RSAASIIRGGHVAPGVRAL-VVPGSMRVKAQAESEGLDKLFLDAGFEWREPGCSLCV-AMNTdrlPA-GARCASTSNRNF 422
Cdd:PRK11413 369 IAAANALRGQSCGNDTFSLsVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFgAGDT---PAnNGLSIRHTTRNF 445
|
330 340 350
....*....|....*....|....*....|.
gi 1891802018 423 EGRQGAG------ARTHLMSPVMVAAAAISG 447
Cdd:PRK11413 446 PNREGSKpangqmSAVALMDARSIAATAANG 476
|
|
| |
