|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
15-485 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 890.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 15 MTARTLYDKHIDSHTVCPLDDqGHVLLYIDRQVINEYTSPQAFSGLREAGRNVWRPGTALAVVDHVNPTTPKRIAAMPDA 94
Cdd:PRK12466 1 MMPRTLYDKLWDSHTVARLDD-GHVLLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPTRPGRDRGITDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 95 GGARQVSYLAENCRDFGIELLDILDKRQGIEHVIAPEQGFILPGMVIAAGDSHTTTYGALGAFGFGIGTSEIEHLLASQT 174
Cdd:PRK12466 80 GGALQVDYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 175 LVYKRLKTMCVSVDGDLAPGLTSKDVIMALIGKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDE 254
Cdd:PRK12466 160 LVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 255 KVFAYLKGKPRAPQGELWDQALAGWRLLHSDVGAVFDQEVQLDATTLEPMVTWGTSPDQAAPIGARVPDPQDVSDLILRQ 334
Cdd:PRK12466 240 TTFDYLRGRPRAPKGALWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAAEADPARRA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 335 DMRRALNYMGLEAGMRLSDIVISHAFIGSCTNARIEDLRDAASVVRGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAIFID 414
Cdd:PRK12466 320 AMERALDYMGLTPGTPLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 761531243 415 AGFEWRQSGCSMCLAMNDDVLAPGDRCASSTNRNFEGRQGAGARTHLMSPAMVAAAAITGRLTDIRHVGAR 485
Cdd:PRK12466 400 AGFEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHITDVRSLLQA 470
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
17-482 |
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: 663.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 17 ARTLYDKHIDSHTVCPLDDQGHVLLYIDRQVINEYTSPQAFSGLREAG-RNVWRPGTALAVVDHVNPTtpkriaamPDAG 95
Cdd:COG0065 2 GMTLAEKILARHAGREVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPT--------KDPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 96 GARQVSYLAENCRDFGIELLDILDKrqGIEHVIAPEQGFILPGMVIAAGDSHTTTYGALGAFGFGIGTSEIEHLLASQTL 175
Cdd:COG0065 74 SAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 176 VYKRLKTMCVSVDGDLAPGLTSKDVIMALIGKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEK 255
Cdd:COG0065 152 WFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 256 VFAYLKGKPRAPqgelwdqalagWRLLHSDVGAVFDQEVQLDATTLEPMVTWGTSPDQAAPIGArvpdpqdvsdlilrqd 335
Cdd:COG0065 232 TFEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE---------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 336 mrralnymgleagmrLSDIVISHAFIGSCTNARIEDLRDAASVVRGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAIFIDA 415
Cdd:COG0065 285 ---------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEA 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 761531243 416 GFEWRQSGCSMCLAMNDDVLAPGDRCASSTNRNFEGRQG-AGARTHLMSPAMVAAAAITGRLTDIRHV 482
Cdd:COG0065 350 GAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
17-482 |
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: 640.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 17 ARTLYDKHIDSHTVCPlDDQGHVLLYIDRQVINEYTSPQAFSGLREAGRNVWRPGTALAVVDHVNPTTPKRIAAMpDAGG 96
Cdd:TIGR00170 2 PRTLYEKLFDAHIVYE-AEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFNIK-DEVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 97 ARQVSYLAENCRDFGIELLDILDKRQGIEHVIAPEQGFILPGMVIAAGDSHTTTYGALGAFGFGIGTSEIEHLLASQTLV 176
Cdd:TIGR00170 80 KIQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 177 YKRLKTMCVSVDGDLAPGLTSKDVIMALIGKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEKV 256
Cdd:TIGR00170 160 QARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 257 FAYLKGKPRAPQGELWDQALAGWRLLHSDVGAVFDQEVQLDATTLEPMVTWGTSPDQAAPIGARVPDPQDVSDLILRQDM 336
Cdd:TIGR00170 240 FEYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKASA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 337 RRALNYMGLEAGMRLSDIVISHAFIGSCTNARIEDLRDAASVVRGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAIFIDAG 416
Cdd:TIGR00170 320 ERALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAG 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 761531243 417 FEWRQSGCSMCLAMNDDVLAPGDRCASSTNRNFEGRQGAGARTHLMSPAMVAAAAITGRLTDIRHV 482
Cdd:TIGR00170 400 FEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
22-474 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 623.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 22 DKHIDSHTVcplDDQGHVLLYI-DRQVINEYTSPQAFSGLREAGRNVWRPGTALAVVDHVNPTTP---------KRIAAM 91
Cdd:pfam00330 1 EKIWDAHLV---EELDGSLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLvidhapdalDKNIED 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 92 PDAGGARQVSYLAENCRDFGIELLDIldkRQGIEHVIAPEQGFILPGMVIAAGDSHTTTYGALGAFGFGIGTSEIEHLLA 171
Cdd:pfam00330 78 EISRNKEQYDFLEWNAKKFGIRFVPP---GQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 172 SQTLVYKRLKTMCVSVDGDLAPGLTSKDVIMALIGKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMA 251
Cdd:pfam00330 155 TQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 252 PDEKVFAYLK--GKPRAPQGELWDQAlAGWRLLHSDVGAVFDQEVQLDATTLEPMVTWGTSPDQAAPIGARVPDPqdVSD 329
Cdd:pfam00330 235 PDETTFEYLRatGRPEAPKGEAYDKA-VAWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDP--FAD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 330 LILRQDMRRALNYMGLEAGMRLSDIVISHAFIGSCTNARIEDLRDAASVVR-----GKHVAEHVRAMIVPGSTEVRDQAE 404
Cdd:pfam00330 312 AVKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAE 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 405 AEGLAAIFIDAGFEWRQSGCSMCLAmNDDVLAPGDRCASSTNRNFEGRQGAGARTHLMSPAMVAAAAITG 474
Cdd:pfam00330 392 AEGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASPALVAAAAIAG 460
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
45-476 |
0e+00 |
|
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate; Aconatase-like catalytic domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes.
Pssm-ID: 153133 Cd Length: 382 Bit Score: 547.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 45 RQVINEYTSPQAFSGLREAGR-NVWRPGTALAVVDHVNPTtpkriaamPDAGGARQVSYLAENCRDFGIELLDIldKRQG 123
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPT--------PDIKAAEQVKTLRKFAKEFGINFFDV--GRQG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 124 IEHVIAPEQGFILPGMVIAAGDSHTTTYGALGAFGFGIGTSEIEHLLASQTLVYKRLKTMCVSVDGDLAPGLTSKDVIMA 203
Cdd:cd01583 71 ICHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 204 LIGKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEKVFAYLKGKPRAPqgelwdqalagWRLLH 283
Cdd:cd01583 151 IIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAY-----------WKELK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 284 SDVGAVFDQEVQLDATTLEPMVTWGTSPDQAAPIGARVPdpqdvsdlilrqdmrralnymgleagmrlsdIVISHAFIGS 363
Cdd:cd01583 220 SDEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQVFIGS 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 364 CTNARIEDLRDAASVVRGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAIFIDAGFEWRQSGCSMCLAMNDDVLAPGDRCAS 443
Cdd:cd01583 269 CTNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVS 348
|
410 420 430
....*....|....*....|....*....|....
gi 761531243 444 STNRNFEGRQGA-GARTHLMSPAMVAAAAITGRL 476
Cdd:cd01583 349 TSNRNFKGRMGSpGARIYLASPATAAASAITGEI 382
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
15-485 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 890.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 15 MTARTLYDKHIDSHTVCPLDDqGHVLLYIDRQVINEYTSPQAFSGLREAGRNVWRPGTALAVVDHVNPTTPKRIAAMPDA 94
Cdd:PRK12466 1 MMPRTLYDKLWDSHTVARLDD-GHVLLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPTRPGRDRGITDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 95 GGARQVSYLAENCRDFGIELLDILDKRQGIEHVIAPEQGFILPGMVIAAGDSHTTTYGALGAFGFGIGTSEIEHLLASQT 174
Cdd:PRK12466 80 GGALQVDYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 175 LVYKRLKTMCVSVDGDLAPGLTSKDVIMALIGKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDE 254
Cdd:PRK12466 160 LVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 255 KVFAYLKGKPRAPQGELWDQALAGWRLLHSDVGAVFDQEVQLDATTLEPMVTWGTSPDQAAPIGARVPDPQDVSDLILRQ 334
Cdd:PRK12466 240 TTFDYLRGRPRAPKGALWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAAEADPARRA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 335 DMRRALNYMGLEAGMRLSDIVISHAFIGSCTNARIEDLRDAASVVRGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAIFID 414
Cdd:PRK12466 320 AMERALDYMGLTPGTPLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 761531243 415 AGFEWRQSGCSMCLAMNDDVLAPGDRCASSTNRNFEGRQGAGARTHLMSPAMVAAAAITGRLTDIRHVGAR 485
Cdd:PRK12466 400 AGFEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHITDVRSLLQA 470
|
|
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
16-480 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 806.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 16 TARTLYDKHIDSHTVCPLDDqGHVLLYIDRQVINEYTSPQAFSGLREAGRNVWRPGTALAVVDHVNPTTPKRIAAmPDAG 95
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEED-GPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLPI-ADPV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 96 GARQVSYLAENCRDFGIELLDILDKRQGIEHVIAPEQGFILPGMVIAAGDSHTTTYGALGAFGFGIGTSEIEHLLASQTL 175
Cdd:PRK05478 79 SRIQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 176 VYKRLKTMCVSVDGDLAPGLTSKDVIMALIGKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEK 255
Cdd:PRK05478 159 LQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDET 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 256 VFAYLKGKPRAPQGELWDQALAGWRLLHSDVGAVFDQEVQLDATTLEPMVTWGTSPDQAAPIGARVPDPQDVSDLILRQD 335
Cdd:PRK05478 239 TFEYLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVKRAS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 336 MRRALNYMGLEAGMRLSDIVISHAFIGSCTNARIEDLRDAASVVRGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAIFIDA 415
Cdd:PRK05478 319 AERALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 761531243 416 GFEWRQSGCSMCLAMNDDVLAPGDRCASSTNRNFEGRQGAGARTHLMSPAMVAAAAITGRLTDIR 480
Cdd:PRK05478 399 GFEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVR 463
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
17-482 |
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: 663.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 17 ARTLYDKHIDSHTVCPLDDQGHVLLYIDRQVINEYTSPQAFSGLREAG-RNVWRPGTALAVVDHVNPTtpkriaamPDAG 95
Cdd:COG0065 2 GMTLAEKILARHAGREVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPT--------KDPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 96 GARQVSYLAENCRDFGIELLDILDKrqGIEHVIAPEQGFILPGMVIAAGDSHTTTYGALGAFGFGIGTSEIEHLLASQTL 175
Cdd:COG0065 74 SAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 176 VYKRLKTMCVSVDGDLAPGLTSKDVIMALIGKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEK 255
Cdd:COG0065 152 WFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 256 VFAYLKGKPRAPqgelwdqalagWRLLHSDVGAVFDQEVQLDATTLEPMVTWGTSPDQAAPIGArvpdpqdvsdlilrqd 335
Cdd:COG0065 232 TFEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE---------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 336 mrralnymgleagmrLSDIVISHAFIGSCTNARIEDLRDAASVVRGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAIFIDA 415
Cdd:COG0065 285 ---------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEA 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 761531243 416 GFEWRQSGCSMCLAMNDDVLAPGDRCASSTNRNFEGRQG-AGARTHLMSPAMVAAAAITGRLTDIRHV 482
Cdd:COG0065 350 GAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
17-482 |
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: 640.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 17 ARTLYDKHIDSHTVCPlDDQGHVLLYIDRQVINEYTSPQAFSGLREAGRNVWRPGTALAVVDHVNPTTPKRIAAMpDAGG 96
Cdd:TIGR00170 2 PRTLYEKLFDAHIVYE-AEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFNIK-DEVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 97 ARQVSYLAENCRDFGIELLDILDKRQGIEHVIAPEQGFILPGMVIAAGDSHTTTYGALGAFGFGIGTSEIEHLLASQTLV 176
Cdd:TIGR00170 80 KIQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 177 YKRLKTMCVSVDGDLAPGLTSKDVIMALIGKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEKV 256
Cdd:TIGR00170 160 QARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 257 FAYLKGKPRAPQGELWDQALAGWRLLHSDVGAVFDQEVQLDATTLEPMVTWGTSPDQAAPIGARVPDPQDVSDLILRQDM 336
Cdd:TIGR00170 240 FEYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKASA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 337 RRALNYMGLEAGMRLSDIVISHAFIGSCTNARIEDLRDAASVVRGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAIFIDAG 416
Cdd:TIGR00170 320 ERALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAG 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 761531243 417 FEWRQSGCSMCLAMNDDVLAPGDRCASSTNRNFEGRQGAGARTHLMSPAMVAAAAITGRLTDIRHV 482
Cdd:TIGR00170 400 FEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
22-474 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 623.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 22 DKHIDSHTVcplDDQGHVLLYI-DRQVINEYTSPQAFSGLREAGRNVWRPGTALAVVDHVNPTTP---------KRIAAM 91
Cdd:pfam00330 1 EKIWDAHLV---EELDGSLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLvidhapdalDKNIED 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 92 PDAGGARQVSYLAENCRDFGIELLDIldkRQGIEHVIAPEQGFILPGMVIAAGDSHTTTYGALGAFGFGIGTSEIEHLLA 171
Cdd:pfam00330 78 EISRNKEQYDFLEWNAKKFGIRFVPP---GQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 172 SQTLVYKRLKTMCVSVDGDLAPGLTSKDVIMALIGKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMA 251
Cdd:pfam00330 155 TQPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 252 PDEKVFAYLK--GKPRAPQGELWDQAlAGWRLLHSDVGAVFDQEVQLDATTLEPMVTWGTSPDQAAPIGARVPDPqdVSD 329
Cdd:pfam00330 235 PDETTFEYLRatGRPEAPKGEAYDKA-VAWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDP--FAD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 330 LILRQDMRRALNYMGLEAGMRLSDIVISHAFIGSCTNARIEDLRDAASVVR-----GKHVAEHVRAMIVPGSTEVRDQAE 404
Cdd:pfam00330 312 AVKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAE 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 405 AEGLAAIFIDAGFEWRQSGCSMCLAmNDDVLAPGDRCASSTNRNFEGRQGAGARTHLMSPAMVAAAAITG 474
Cdd:pfam00330 392 AEGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASPALVAAAAIAG 460
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
45-476 |
0e+00 |
|
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate; Aconatase-like catalytic domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes.
Pssm-ID: 153133 Cd Length: 382 Bit Score: 547.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 45 RQVINEYTSPQAFSGLREAGR-NVWRPGTALAVVDHVNPTtpkriaamPDAGGARQVSYLAENCRDFGIELLDIldKRQG 123
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPT--------PDIKAAEQVKTLRKFAKEFGINFFDV--GRQG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 124 IEHVIAPEQGFILPGMVIAAGDSHTTTYGALGAFGFGIGTSEIEHLLASQTLVYKRLKTMCVSVDGDLAPGLTSKDVIMA 203
Cdd:cd01583 71 ICHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 204 LIGKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEKVFAYLKGKPRAPqgelwdqalagWRLLH 283
Cdd:cd01583 151 IIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAY-----------WKELK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 284 SDVGAVFDQEVQLDATTLEPMVTWGTSPDQAAPIGARVPdpqdvsdlilrqdmrralnymgleagmrlsdIVISHAFIGS 363
Cdd:cd01583 220 SDEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQVFIGS 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 364 CTNARIEDLRDAASVVRGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAIFIDAGFEWRQSGCSMCLAMNDDVLAPGDRCAS 443
Cdd:cd01583 269 CTNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVS 348
|
410 420 430
....*....|....*....|....*....|....
gi 761531243 444 STNRNFEGRQGA-GARTHLMSPAMVAAAAITGRL 476
Cdd:cd01583 349 TSNRNFKGRMGSpGARIYLASPATAAASAITGEI 382
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
43-482 |
3.00e-135 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 396.86 E-value: 3.00e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 43 IDRQVINEYTSPQAFSGLREAGRN-VWRPGTALAVVDHVNPttPKRIAAmpdaggARQVSYLAENCRDFGIEllDILDKR 121
Cdd:PRK00402 28 VDLVMAHDITGPLAIKEFEKIGGDkVFDPSKIVIVFDHFVP--AKDIKS------AEQQKILREFAKEQGIP--NFFDVG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 122 QGIEHVIAPEQGFILPGMVIAAGDSHTTTYGALGAFGFGIGTSEIEHLLASQTLVYKRLKTMCVSVDGDLAPGLTSKDVI 201
Cdd:PRK00402 98 EGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKTWFKVPETIKVVLEGKLPPGVTAKDVI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 202 MALIGKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEKVFAYLKGKPRAPqgelwdqalagWRL 281
Cdd:PRK00402 178 LHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLEYLKERAGRD-----------YKP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 282 LHSDVGAVFDQEVQLDATTLEPMVTWGTSPDQAAPIGarvpdpqdvsdlilrqdmrralnymgleagmRLSDIVISHAFI 361
Cdd:PRK00402 247 WKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVS-------------------------------EVEGTKVDQVFI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 362 GSCTNARIEDLRDAASVVRGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAIFIDAGFEWRQSGCSMCLAMNDDVLAPGDRC 441
Cdd:PRK00402 296 GSCTNGRLEDLRIAAEILKGRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVC 375
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 761531243 442 ASSTNRNFEGRQG-AGARTHLMSPAMVAAAAITGRLTDIRHV 482
Cdd:PRK00402 376 LSTTNRNFKGRMGsPESEVYLASPAVAAASAVTGKITDPREV 417
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
27-480 |
3.13e-113 |
|
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: 340.19 E-value: 3.13e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 27 SHTVCPLDdqgHVLLYIDRQVINEYTSPQAFSGLREAGRN-VWRPGTALAVVDHVNPttPKRIAAmpdaggARQVSYLAE 105
Cdd:TIGR01343 12 GKEVYAGD---LIEAEIDLAMVHDITAPLAIKTLEEYGIDkVWNPEKIVIVFDHQVP--ADTIKA------AEMQKLARE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 106 NCRDFGIELLdiLDKRQGIEHVIAPEQGFILPGMVIAAGDSHTTTYGALGAFGFGIGTSEIEHLLASQTLVYKRLKTMCV 185
Cdd:TIGR01343 81 FVKKQGIKYF--YDVGEGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFKVPETIRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 186 SVDGDLAPGLTSKDVIMALIGKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEKVFAYLKGKPR 265
Cdd:TIGR01343 159 NITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYLKERRK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 266 APqgelwdqalagWRLLHSDVGAVFDQEVQLDATTLEPMVTWGTSPDQAAPIGarvpdpqdvsdlilrqdmrralnymgl 345
Cdd:TIGR01343 239 EP-----------FRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVS--------------------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 346 eagmRLSDIVISHAFIGSCTNARIEDLRDAASVVRGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAIFIDAGFEWRQSGCS 425
Cdd:TIGR01343 281 ----EVEGTEIDQVFIGSCTNGRLEDLRVAAKILKGRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCG 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 761531243 426 MCLAMNDDVLAPGDRCASSTNRNFEGRQG-AGARTHLMSPAMVAAAAITGRLTDIR 480
Cdd:TIGR01343 357 PCLGSHQGVLAPGEVCISTSNRNFKGRMGhPNAEIYLASPATAAASAVKGYIADPR 412
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
39-478 |
6.02e-96 |
|
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: 295.90 E-value: 6.02e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 39 VLLYIDRQVINEYTSPQAFSGLREAGR-NVWRPGTALAVVDHVNPTtpkriaamPDAGGARQVSYLAENCRDFGIELLDI 117
Cdd:TIGR02086 22 VEVEVDLAMTHDGTGPLAIKALRELGVaRVWDPEKIVIAFDHNVPP--------PTVEAAEMQKEIREFAKRHGIKNFDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 118 LDkrqGIEHVIAPEQGFILPGMVIAAGDSHTTTYGALGAFGFGIGTSEIEHLLASQTLVYKRLKTMCVSVDGDLAPGLTS 197
Cdd:TIGR02086 94 GE---GICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTWIKVPETIRVVVEGKPEEGVTA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 198 KDVIMALIGKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEKVFAYLKGKPRAPQgelwdqala 277
Cdd:TIGR02086 171 KDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEETYEYLKKRRGLEF--------- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 278 gwRLLHSDVGAVFDQEVQLDATTLEPMVTWGTSPDQAAPIGarvpdpqDVSdlilrqdmrralnymGLEagmrlsdivIS 357
Cdd:TIGR02086 242 --RILVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVS-------DVE---------------GTE---------ID 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 358 HAFIGSCTNARIEDLRDAASVVRGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAIFIDAGFEWRQSGCSMCLAMNDDVLAP 437
Cdd:TIGR02086 289 QVFIGSCTNGRLEDLRIAAEILKGRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAGAMICPPGCGPCLGAHMGVLGD 368
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 761531243 438 GDRCASSTNRNFEGRQGA-GARTHLMSPAMVAAAAITGRLTD 478
Cdd:TIGR02086 369 GEVCLSTTNRNFKGRMGSpNAEIYLASPATAAASAVEGYITD 410
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
123-476 |
4.36e-68 |
|
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: 223.14 E-value: 4.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 123 GIEHVIAPEQgFILPGMVIAAGDSHTTTYGALGAFGFGIGTSEIEHLLASQTLVYKRLKTMCVSVDGDLAPGLTSKDVIM 202
Cdd:cd01351 70 GIIHQIMVEN-LALPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 203 ALIGKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEKVFAYLKGKPRAPQGELWDqalAGWRLL 282
Cdd:cd01351 149 KLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWL---AFPEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 283 HSDVGAVFDQEVQLDATTLEPMVTWGTSPDQAAPIGArvpdpqdvsdlilrqdmrralnymgleagmrLSDIVISHAFIG 362
Cdd:cd01351 226 LADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSE-------------------------------VEGTKIDQVLIG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 363 SCTNARIEDLRDAASVVRGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAIFIDAGFEWRQSGCSMCLAMNDDVLAPGDRCA 442
Cdd:cd01351 275 SCTNNRYSDMLAAAKLLKGAKVAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLVADGEVGV 354
|
330 340 350
....*....|....*....|....*....|....*
gi 761531243 443 SSTNRNFEGRQGAG-ARTHLMSPAMVAAAAITGRL 476
Cdd:cd01351 355 SSGNRNFPGRLGTYeRHVYLASPELAAATAIAGKI 389
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
123-480 |
1.84e-57 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 201.14 E-value: 1.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 123 GIEHVIAPEQgFILPGMVIAAGDSHTTTYGALGAFGFGIGTSEIEHLLASQTLVYKRLKTMCVSVDGDLAPGLTSKDVIM 202
Cdd:PRK07229 98 GICHQVHLER-FAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVIL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 203 ALIGKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEKVFAYLKGKPRapqGELWDQalagwrlL 282
Cdd:PRK07229 177 ELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLKAQGR---EDDWVE-------L 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 283 HSDVGAVFDQEVQLDATTLEPMVTWGTSPDQAAPigarvpdpqdVSDLilrqdmrralnymgleagmrlSDIVISHAFIG 362
Cdd:PRK07229 247 LADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVP----------VSEV---------------------AGIKVDQVLIG 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 363 SCTNARIEDLRDAASVVRGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAIFIDAGFEWRQSGCSMCLAMNDdvlAPGDRCA 442
Cdd:PRK07229 296 SCTNSSYEDLMRAASILKGKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMGQ---APATGNV 372
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 761531243 443 S--STNRNFEGRQG-AGARTHLMSPAMVAAAAITGRLTDIR 480
Cdd:PRK07229 373 SlrTFNRNFPGRSGtKDAQVYLASPETAAASALTGVITDPR 413
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
123-476 |
1.49e-52 |
|
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: 181.88 E-value: 1.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 123 GIEHVIAPEQgFILPGMVIAAGDSHTTTYGALGAFGFGIGTSEIEHLLASQTLVYKRLKTMCVSVDGDLAPGLTSKDVIM 202
Cdd:cd01585 69 GICHQVHLER-FAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVIL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 203 ALIGKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEKVFAYLKGKPRApqgelwdqalAGWRLL 282
Cdd:cd01585 148 ELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAAQGRE----------DDWVEL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 283 HSDVGAVFDQEVQLDATTLEPMVTWGTSPDQAAPigarvpdpqdVSDLilrqdmrralnymgleAGMRLSDIVishafIG 362
Cdd:cd01585 218 AADADAEYDEEIEIDLSELEPLIARPHSPDNVVP----------VREV----------------AGIKVDQVA-----IG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 363 SCTNARIEDLRDAASVVRGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAIFIDAGFEWRQSGCSMCLAMNDdvlAPGDRCA 442
Cdd:cd01585 267 SCTNSSYEDLMTVAAILKGRRVHPHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQ---APPTGGV 343
|
330 340 350
....*....|....*....|....*....|....*..
gi 761531243 443 S--STNRNFEGRQG-AGARTHLMSPAMVAAAAITGRL 476
Cdd:cd01585 344 SvrTFNRNFEGRSGtKDDLVYLASPEVAAAAALTGVI 380
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
122-476 |
5.06e-46 |
|
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: 163.94 E-value: 5.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 122 QGIEHVIAPEQGFILPGMVIAAGDSHTTTYGALGAFGFGIGTSEIEHLLASQTLVYKRLKTMCVSVDGDLAPGLTSKDVI 201
Cdd:cd01582 67 RGIGHQIMIEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 202 MALIGKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEKvfaylkgkprapqgelwdqalagwrl 281
Cdd:cd01582 147 VALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAK-------------------------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 282 lhsdvgavfdqEVQLDATTLEPMVTwgtspdqaAPIGARVPDPQDVsdlilrqdmrralnymgLEAgmrlSDIVISHAFI 361
Cdd:cd01582 201 -----------HLILDLSTLSPYVS--------GPNSVKVSTPLKE-----------------LEA----QNIKINKAYL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 362 GSCTNARIEDLRDAASVVRGK-------HVAEHVRAMIVPGSTEVRDQAEAEGLAAIFIDAGFEWRQSGCSMCLAMNDDV 434
Cdd:cd01582 241 VSCTNSRASDIAAAADVVKGKkekngkiPVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQGL 320
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 761531243 435 LAPGDRCASSTNRNFEGRQGA-GARTHLMSPAMVAAAAITGRL 476
Cdd:cd01582 321 LEPGEVGISATNRNFKGRMGStEALAYLASPAVVAASAISGKI 363
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
123-476 |
7.47e-41 |
|
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: 151.44 E-value: 7.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 123 GIEHVIAPEQgFILPGMVIAAGDSHTTTYGALGAFGFGIGTSEIEHLLASQTLVYKRLKTMCVSVDGDLAPGLTSKDVIM 202
Cdd:cd01584 77 GIIHQIVLEN-YAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVIL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 203 ALIGKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEKVFAYLKGKPRAPQGELWDQALAgwRLL 282
Cdd:cd01584 156 KVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEIADLADEFKD--DLL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 283 HSDVGAVFDQEVQLDATTLEPMVTWGTSPDQAAPIgarvpdpqdvsdlilrQDMRRALNYMGLEAGMRLSdivishaFIG 362
Cdd:cd01584 234 VADEGAEYDQLIEINLSELEPHINGPFTPDLATPV----------------SKFKEVAEKNGWPLDLRVG-------LIG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 363 SCTNARIEDLRDAASVVrgKHVAEH-----VRAMIVPGSTEVRDQAEAEGLAAIFIDAGFEWRQSGCSMCLAMNDDV-LA 436
Cdd:cd01584 291 SCTNSSYEDMGRAASIA--KQALAHglkckSIFTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQWDRKdIK 368
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 761531243 437 PGDRCA--SSTNRNFEGRQGAGARTH--LMSPAMVAAAAITGRL 476
Cdd:cd01584 369 KGEKNTivTSYNRNFTGRNDANPATHafVASPEIVTAMAIAGTL 412
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
137-481 |
5.34e-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: 124.06 E-value: 5.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 137 PGMVIaaG-DSHTTTYGALGAFGFGIGTSEIEHLLASQ---TLVYK----RLKtmcvsvdGDLAPGLTSKDVIMALIGKI 208
Cdd:COG1048 203 PDTLV--GtDSHTTMINGLGVLGWGVGGIEAEAAMLGQpvsMLIPEvvgvKLT-------GKLPEGVTATDLVLTVTEML 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 209 GASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEKVFAYLKGKPRAP------------QGeLWDQAL 276
Cdd:COG1048 274 RKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRLTGRSEeqielveayakaQG-LWRDPD 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 277 AGWrllhsdvgAVFDQEVQLDATTLEPMVTWGTSPDQAAPIGARVPDPQDVSDLILRQDMRRALNYMGLEAGMRLSD--I 354
Cdd:COG1048 353 APE--------PYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAAPVGEELDKPVRVEVDGEEFELGHgaV 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 355 VIshAFIGSCTNARIEDLRDAASVV------RGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAIFIDAGFEWRQSGCSMCL 428
Cdd:COG1048 425 VI--AAITSCTNTSNPSVMIAAGLLakkaveKGLKVKPWVKTSLAPGSKVVTDYLERAGLLPYLEALGFNVVGYGCTTCI 502
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 761531243 429 AMNDDVLAP-------GD-RCAS--STNRNFEGRQGAGART-HLMSPAMVAAAAITGRLT-DIRH 481
Cdd:COG1048 503 GNSGPLPPEiseaieeNDlVVAAvlSGNRNFEGRIHPDVKAnFLASPPLVVAYALAGTVDiDLTT 567
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
123-481 |
2.77e-27 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 115.80 E-value: 2.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 123 GIEHVIAPEQ-------------GFILPGMVIAAgDSHTTTYGALGAFGFGIGTSEIEHLLASQTlVYKRL-KTMCVSVD 188
Cdd:PRK12881 178 GIMHQVNLEYlarvvhtkeddgdTVAYPDTLVGT-DSHTTMINGIGVLGWGVGGIEAEAVMLGQP-VYMLIpDVVGVELT 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 189 GDLAPGLTSKDVIMALIGKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEKVFAYLKGKPRAPQ 268
Cdd:PRK12881 256 GKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLRLTGRTEA 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 269 G----ELWDQALAGWRllHSDVGAVFDQEVQLDATTLEPMVTWGTSPDQAAPIGARvpdPQDVSDLILRQDMRRALNYMG 344
Cdd:PRK12881 336 QialvEAYAKAQGLWG--DPKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNV---KSAFSDLFSKPVAENGFAKKA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 345 ---LEAGMRLSDIVIshAFIGSCTNARIEDLRDAASVV------RGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAIFIDA 415
Cdd:PRK12881 411 qtsNGVDLPDGAVAI--AAITSCTNTSNPSVLIAAGLLakkaveRGLTVKPWVKTSLAPGSKVVTEYLERAGLLPYLEKL 488
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 761531243 416 GFEWRQSGCSMCLAMNDDVLAP-------GD-RCAS--STNRNFEGRQGAGARTH-LMSPAMVAAAAITGRLT-DIRH 481
Cdd:PRK12881 489 GFGIVGYGCTTCIGNSGPLTPEieqaitkNDlVAAAvlSGNRNFEGRIHPNIKANfLASPPLVVAYALAGTVRrDLMT 566
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
126-477 |
8.47e-26 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 111.26 E-value: 8.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 126 HVIAPEQGFILPGMVIAAgDSHTTTYGALGAFGFGIGTSEIEHLLASQTLVYKRLKTMCVSVDGDLAPGLTSKDVIMALI 205
Cdd:PTZ00092 197 RVVFNKDGLLYPDSVVGT-DSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTGKLSEHVTATDLVLTVT 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 206 GKIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEKVFAYLK--GKPrAPQGELWDQALAGwRLLH 283
Cdd:PTZ00092 276 SMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKqtGRS-EEKVELIEKYLKA-NGLF 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 284 SDVGA--VFDQEVQLDATTLEPMVtwgtspdqAAPigARvpdPQD---VSDliLRQDMRRAL------------------ 340
Cdd:PTZ00092 354 RTYAEqiEYSDVLELDLSTVVPSV--------AGP--KR---PHDrvpLSD--LKKDFTACLsapvgfkgfgipeekhek 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 341 ----NYMGLEAGMRLSDIVIshAFIGSCTNARIEDLRDAA------SVVRGKHVAEHVRAMIVPGSTEVRDQAEAEGLAA 410
Cdd:PTZ00092 419 kvkfTYKGKEYTLTHGSVVI--AAITSCTNTSNPSVMLAAgllakkAVEKGLKVPPYIKTSLSPGSKVVTKYLEASGLLK 496
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 761531243 411 IFIDAGFEWRQSGCSMCLAMNDDVLAPGDRCAS----------STNRNFEGRQGAGAR-THLMSPAMVAAAAITGRLT 477
Cdd:PTZ00092 497 YLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITnndlvaaavlSGNRNFEGRVHPLTRaNYLASPPLVVAYALAGRVN 574
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
131-475 |
1.57e-22 |
|
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: 99.30 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 131 EQGFILPGMVIAaGDSHTTTYGALGAFGFGIGTSEIEHLLASQTLVYKRLKTMCVSVDGDLAPGLTSKDVIMALIGKIGA 210
Cdd:cd01586 115 GDGVAYPDSVVG-TDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTGKLRPGVTATDLVLTVTQMLRK 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 211 SGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEKVfaylkgkprapqgelwdqalagwrllhsdvgavf 290
Cdd:cd01586 194 VGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVDTQV---------------------------------- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 291 dqeVQLDATTLEPMVtwgtspdqAAPigarvPDPQDvsdlilrqdmRRALNymgleagmrlSDIVIshAFIGSCTNARIE 370
Cdd:cd01586 240 ---VELDLSTVEPSV--------SGP-----KRPQD----------RVPLH----------GSVVI--AAITSCTNTSNP 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 371 DLRDAASVV------RGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAIFIDAGFEWRQSGCSMCLA----MNDDV---LAP 437
Cdd:cd01586 282 SVMLAAGLLakkaveLGLKVKPYVKTSLAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGnsgpLPEEVeeaIKE 361
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 761531243 438 GDRCAS---STNRNFEGRQGAGAR-THLMSPAMVAAAAITGR 475
Cdd:cd01586 362 NDLVVAavlSGNRNFEGRIHPLVRaNYLASPPLVVAYALAGT 403
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
127-474 |
1.61e-22 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 101.42 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 127 VIAPEQGFILPGMVIAAgDSHTTTYGALGAFGFGIGTSEIEHLLASQTLVYKRLKTMCVSVDGDLAPGLTSKDVIMALIG 206
Cdd:PLN00070 230 VVFNTDGILYPDSVVGT-DSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 207 KIGASGATGYAIEFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEKVFAYLKGKPRAPQG-ELWDQALAGWRLL--H 283
Cdd:PLN00070 309 MLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKLTGRSDETvAMIEAYLRANKMFvdY 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 284 SD--VGAVFDQEVQLDATTLEPMVTWGTSPDQAAPIGARVPDPQDVSDLIL----------RQDMRRALNYMGLEAGMRL 351
Cdd:PLN00070 389 NEpqQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHSCLDNKVgfkgfavpkeAQSKVAKFSFHGQPAELRH 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 352 SDIVIshAFIGSCTNARIEDLRDAASVVRGK------HVAEHVRAMIVPGSTEVRDQAEAEGLAAIFIDAGFEWRQSGCS 425
Cdd:PLN00070 469 GSVVI--AAITSCTNTSNPSVMLGAGLVAKKacelglEVKPWIKTSLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCT 546
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 426 MCLAMNDDV-------LAPGDRCAS---STNRNFEGRQGAGAR-THLMSPAMVAAAAITG 474
Cdd:PLN00070 547 TCIGNSGELdesvasaITENDIVAAavlSGNRNFEGRVHPLTRaNYLASPPLVVAYALAG 606
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
138-477 |
7.21e-19 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 89.68 E-value: 7.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 138 GMVIAAGDSHTTtYGALGAFGFGIGTSEIEHLLASQTLVYKRLKTMCVSVDGDLAPGLTSKDVIMALIGKIGASGATGYA 217
Cdd:PRK11413 142 GKMILGSDSHTR-YGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVKNK 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 218 I-EFRGSTLDALSVEARMTICNMAVEAGARGAFMAPDEKVFAYLK--GKPRAPQgelwdqalagwRLLHSDVgAVFDQEV 294
Cdd:PRK11413 221 VmEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLAlhGRGQDYC-----------ELNPQPM-AYYDGCI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 295 QLDATTLEPMVTWGTSPDQAAPIGARVPDPQDvsdlILRQDMRRALNYMGLEAGMRLSD------IVISHAFIGSCTNAR 368
Cdd:PRK11413 289 SVDLSAIKPMIALPFHPSNVYEIDELNQNLTD----ILREVEIESERVAHGKAKLSLLDkiengrLKVQQGIIAGCSGGN 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 369 IEDLRDAASVVRGKHVAEHVRAMIV-PGSTEVRDQAEAEGLAAIFIDAGFEWRQSGCSMCLAMNDdvlAPGDRCAS--ST 445
Cdd:PRK11413 365 YENVIAAANALRGQSCGNDTFSLSVyPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFGAGD---TPANNGLSirHT 441
|
330 340 350
....*....|....*....|....*....|....*....
gi 761531243 446 NRNFEGRQGAG------ARTHLMSPAMVAAAAIT-GRLT 477
Cdd:PRK11413 442 TRNFPNREGSKpangqmSAVALMDARSIAATAANgGYLT 480
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
135-476 |
4.71e-17 |
|
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: 83.32 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 135 ILPGMVIAAGDSHTTTygALG-AFGFGIGTseIEHLLASQTLVYKRLKTMCVSVDGDLAPGLTSKDVIMAL--------- 204
Cdd:cd01581 104 LLPDTVGTGGDSHTRF--PIGiSFPAGSGL--VAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVNAIpyyaiqqgl 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 205 --IGKIGASGA-TGYAIEFRGstLDALSVEARMTICNMAVEAGARGAFMAPDEK-VFAYL------------KGKPRAPQ 268
Cdd:cd01581 180 ltVEKKGKKNVfNGRILEIEG--LPDLKVEQAFELTDASAERSAAACTVRLDKEpVIEYLesnvvlmkimiaNGYDDART 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 269 GELWDQALAGWR----LLHSDVGAVFDQEVQLD-ATTLEPMVtwgtspdqAAPigarvPDPQDVsdlilrqdmrRALNYM 343
Cdd:cd01581 258 LLRRIIAMEEWLanppLLEPDADAEYAAVIEIDlDDIKEPIL--------ACP-----NDPDDV----------KLLSEV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 344 gleagmrlSDIVISHAFIGSC-TNarIEDLRDAASVVRGKHVAEhVRAMIVPGSTEVRDQAEAEGLAAIFIDAGFEWRQS 422
Cdd:cd01581 315 --------AGKKIDEVFIGSCmTN--IGHFRAAAKILRGKEFKP-TRLWVAPPTRMDWAILQEEGYYSIFGDAGARTEMP 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 761531243 423 GCSMCLAmNDDVLAPGDRCASSTNRNFEGRQGAGARTHLMSPAMVAAAAITGRL 476
Cdd:cd01581 384 GCSLCMG-NQARVADGATVFSTSTRNFDNRVGKGAEVYLGSAELAAVCALLGRI 436
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
145-479 |
8.95e-16 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 80.17 E-value: 8.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 145 DSHTTTYGALGAFGFGIGTSEIEHLLASQTlVYKRL-KTMCVSVDGDLAPGLTSKDVIMALIGKIGASGATGYAIEFRGS 223
Cdd:PRK09277 212 DSHTTMINGLGVLGWGVGGIEAEAAMLGQP-SSMLIpEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 224 TLDALSVEARMTICNMAVEAGARGAFMAPDEKVFAYLKGKPRAP------------QGeLWdqalagwrlLHSDVGAVFD 291
Cdd:PRK09277 291 GLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRLTGRDEeqvalveayakaQG-LW---------RDPLEEPVYT 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 292 QEVQLDATTLEPMVtwgtspdqAAPigARvpdPQD---VSDL--ILRQDMRRALNYMGLEAGMRLSDIVISH-----AFI 361
Cdd:PRK09277 361 DVLELDLSTVEPSL--------AGP--KR---PQDripLSDVkeAFAKSAELGVQGFGLDEAEEGEDYELPDgavviAAI 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 362 GSCTN-------------ARiedlrdaASVVRGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAiFIDA-GFEWRQSGCSMC 427
Cdd:PRK09277 428 TSCTNtsnpsvmiaagllAK-------KAVEKGLKVKPWVKTSLAPGSKVVTDYLEKAGLLP-YLEAlGFNLVGYGCTTC 499
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 761531243 428 L------------AMNDDVLApgdrCAS--STNRNFEGRQGAGART-HLMSPAMVAAAAITGRLT-DI 479
Cdd:PRK09277 500 IgnsgplppeiekAINDNDLV----VTAvlSGNRNFEGRIHPLVKAnYLASPPLVVAYALAGTVDiDL 563
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
351-476 |
1.27e-13 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 73.29 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 351 LSDIV---ISHAFIGSC-TNarIEDLRDAASVVRGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAIFIDAGFEWRQSGCSM 426
Cdd:PRK09238 683 LSEVAgtkIDEVFIGSCmTN--IGHFRAAGKLLEGKKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSL 760
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 761531243 427 CLAmNDDVLAPGDRCASSTNRNFEGRQGAGARTHLMSPAMVAAAAITGRL 476
Cdd:PRK09238 761 CMG-NQARVADGATVFSTSTRNFPNRLGKGANVYLGSAELAAVCALLGRI 809
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
135-476 |
1.25e-12 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 70.34 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 135 ILPGMVIAAGDSHTTtygalgaFGFGI----GTSEIEHLLASQTLVYKRLKTMCVSVDGDLAPGLTSKDVIMAL------ 204
Cdd:PLN00094 550 LLPDTVGTGGDSHTR-------FPIGIsfpaGSGLVAFGAATGVIPLDMPESVLVRFTGTMQPGITLRDLVHAIpytaiq 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 205 -----IGKIGASGA-TGYAIEFRGstLDALSVEARMTICNMAVEAGARGAFMAPDEK-VFAYLK--------------GK 263
Cdd:PLN00094 623 dglltVEKKGKKNVfSGRILEIEG--LPHLKCEQAFELSDASAERSAAGCTIKLDKEpIIEYLNsnvvmlkwmiaegyGD 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 264 PRAPQGEL--WDQALAGWRLLHSDVGAVFDQEVQLDATTL-EPMVTWGTSPDQAAPIGARVPDPqdvsdlilrqdmrral 340
Cdd:PLN00094 701 RRTLERRIarMQQWLADPELLEADPDAEYAAVIEIDMDEIkEPILCAPNDPDDARLLSEVTGDK---------------- 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 761531243 341 nymgleagmrlsdivISHAFIGSC-TNarIEDLRDAASVVRGKHVAEHVRAMIVPGSTEVRDQAEAEGLAAIFIDAGFEW 419
Cdd:PLN00094 765 ---------------IDEVFIGSCmTN--IGHFRAAGKLLNDNLSQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGART 827
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 761531243 420 RQSGCSMCLAmNDDVLAPGDRCASSTNRNFEGRQGAGARTHLMSPAMVAAAAITGRL 476
Cdd:PLN00094 828 EMPGCSLCMG-NQARVAEKSTVVSTSTRNFPNRLGKGANVYLASAELAAVAAILGRL 883
|
|
| |
