|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-466 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 990.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 1 MAQTLYDKLWDSHVVDTASDGTTILYIDRHLVHEVTSPQAFDGLKLAGRQPWRLSANLAVADHNVPTTDRAQGIADPTSR 80
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLPIADPVSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 81 LQVETLDANAKTYGLTYFNMADKRQGIVHVIGPEQGATLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTLLT 160
Cdd:PRK05478 81 IQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 161 KKSRSMLVQIDGALPRGVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTTI 240
Cdd:PRK05478 161 KKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 241 DYVKGRPFSPVGPHWERAVSWWRTLHSDAGARFDLVVRLDASQVRPQVTWGTSPEMVVAIDDRVPDPDKEKDPTKRDSME 320
Cdd:PRK05478 241 EYLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVKRASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 321 KALAYMALKPNTAIADIRIDKVFIGSCTNSRIEDLRAAAAVVRGKFRASNVRlAMVVPGSGLVKEQAEREGLDKIFRDAG 400
Cdd:PRK05478 321 RALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVR-ALVVPGSGLVKAQAEAEGLDKIFIEAG 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327549395 401 FEWREPGCSMCLAMNADRLEPGERCASTSNRNFEGRQGAGGRTHLVSPAMAAAAGIAGHFVDVRTL 466
Cdd:PRK05478 400 FEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVREL 465
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
1-464 |
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: 737.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 1 MAQTLYDKLWDSHVVDTASDGTTILYIDRHLVHEVTSPQAFDGLKLAGRQPWRLSANLAVADHNVPTTDRAQGIADPTSR 80
Cdd:TIGR00170 1 MPRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFNIKDEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 81 LQVETLDANAKTYGLTYFNMADKRQGIVHVIGPEQGATLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTLLT 160
Cdd:TIGR00170 81 IQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 161 KKSRSMLVQIDGALPRGVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTTI 240
Cdd:TIGR00170 161 ARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 241 DYVKGRPFSPVGPHWERAVSWWRTLHSDAGARFDLVVRLDASQVRPQVTWGTSPEMVVAIDDRVPDPDKEKDPTKRDSME 320
Cdd:TIGR00170 241 EYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 321 KALAYMALKPNTAIADIRIDKVFIGSCTNSRIEDLRAAAAVVRGKFRASNVRlAMVVPGSGLVKEQAEREGLDKIFRDAG 400
Cdd:TIGR00170 321 RALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVK-ALVVPGSGLVKLQAEKEGLDKIFIEAG 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327549395 401 FEWREPGCSMCLAMNADRLEPGERCASTSNRNFEGRQGAGGRTHLVSPAMAAAAGIAGHFVDVR 464
Cdd:TIGR00170 400 FEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIR 463
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-448 |
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: 689.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 1 MAQTLYDKLWDSHVVDTASDGTTI-LYIDRHLVHEVTSPQAFDGLKLAG-RQPWRLSANLAVADHNVPTTDraqgiadPT 78
Cdd:COG0065 1 MGMTLAEKILARHAGREVEPGEIVlLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPTKD-------PK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 79 SRLQVETLDANAKTYGLTYFNMADKrqGIVHVIGPEQGATLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTL 158
Cdd:COG0065 74 SAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 159 LTKKSRSMLVQIDGALPRGVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDT 238
Cdd:COG0065 152 WFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 239 TIDYVKGRPFSPvgphweravswWRTLHSDAGARFDLVVRLDASQVRPQVTWGTSPEMVVAIDDrvpdpdkekdptkrds 318
Cdd:COG0065 232 TFEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE---------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 319 mekalaymalkpntaIADIRIDKVFIGSCTNSRIEDLRAAAAVVRGKFRASNVRlAMVVPGSGLVKEQAEREGLDKIFRD 398
Cdd:COG0065 285 ---------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVR-AIVVPGSQEVYRQAEAEGLDEIFIE 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 327549395 399 AGFEWREPGCSMCLAMNADRLEPGERCASTSNRNFEGRQG-AGGRTHLVSP 448
Cdd:COG0065 349 AGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASP 399
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-448 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 686.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 7 DKLWDSHVVDTASDgtTILYI-DRHLVHEVTSPQAFDGLKLAGRQPWRLSANLAVADHNVPTTDR--------AQGIADP 77
Cdd:pfam00330 1 EKIWDAHLVEELDG--SLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVidhapdalDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 78 TSR--LQVETLDANAKTYGLTYFNMAdkrQGIVHVIGPEQGATLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLAT 155
Cdd:pfam00330 79 ISRnkEQYDFLEWNAKKFGIRFVPPG---QGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 156 QTLLTKKSRSMLVQIDGALPRGVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAV 235
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 236 DDTTIDYVK--GRPFSPVGPHWERAVSWWrTLHSDAGARFDLVVRLDASQVRPQVTWGTSPEMVVAIDDRVPDPdkEKDP 313
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAVAWK-TLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDP--FADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 314 TKRDSMEKALAYMALKPNTAIADIRIDKVFIGSCTNSRIEDLRAAAAVVR-----GKFRASNVRlAMVVPGSGLVKEQAE 388
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVK-ASVVPGSEVVRAYAE 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 389 REGLDKIFRDAGFEWREPGCSMCLAmNADRLEPGERCASTSNRNFEGRQGAGGRTHLVSP 448
Cdd:pfam00330 392 AEGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASP 450
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
29-448 |
0e+00 |
|
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate; Aconatase-like catalytic domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes.
Pssm-ID: 153133 Cd Length: 382 Bit Score: 581.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 29 RHLVHEVTSPQAFDGLKLAGRQ-PWRLSANLAVADHNVPTtdraqgiADPTSRLQVETLDANAKTYGLTYFNMadKRQGI 107
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREkVWDPEKIVAVFDHNVPT-------PDIKAAEQVKTLRKFAKEFGINFFDV--GRQGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 108 VHVIGPEQGATLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTLLTKKSRSMLVQIDGALPRGVTAKDIVLAV 187
Cdd:cd01583 72 CHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 188 IGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTTIDYVKGRPFSPvgphweravswWRTLHS 267
Cdd:cd01583 152 IGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAY-----------WKELKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 268 DAGARFDLVVRLDASQVRPQVTWGTSPEMVVAIDDRVPdpdkekdptkrdsmekalaymalkpntaiadIRIDKVFIGSC 347
Cdd:cd01583 221 DEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQVFIGSC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 348 TNSRIEDLRAAAAVVRGKFRASNVRLaMVVPGSGLVKEQAEREGLDKIFRDAGFEWREPGCSMCLAMNADRLEPGERCAS 427
Cdd:cd01583 270 TNGRLEDLRAAAEILKGRKVADGVRL-IVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVS 348
|
410 420
....*....|....*....|..
gi 327549395 428 TSNRNFEGRQGAGG-RTHLVSP 448
Cdd:cd01583 349 TSNRNFKGRMGSPGaRIYLASP 370
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
4-448 |
1.28e-78 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 250.83 E-value: 1.28e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 4 TLYDKLWDSHVVDTASDGTTI-LYIDRHLVHEVTSPQAFDGLKLAGRQPWRLSANLAVADHNVP-TTDRAqgiadptSRL 81
Cdd:NF040615 2 TLAEKILSKKLGKEVYAGDTVeVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPaNTVKA-------ANM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 82 QVETLDAnAKTYGLTYFNMADkrQGIVHVIGPEQGATLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTLLTK 161
Cdd:NF040615 75 QKITREF-VKEQGIKNFYLGG--EGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 162 KSRSMLVQIDGALPRgVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTTID 241
Cdd:NF040615 152 VPKTIRVNIVGKNEN-ISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 242 YVKGRPFSpvgphwERAVSWW---RTLHSDAGARFDLVVRLDASQVRPQVTWGTSPEMVvaiddrvpdpdkekdptkrds 318
Cdd:NF040615 231 YLRKEGVS------EEEIAELkknRITVNEKEENYYKEIEIDITDMEEQVACPHHPDNV--------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 319 mekalaymalKPNTAIADIRIDKVFIGSCTNSRIEDLRAAAAVVRGKFRASNVRLaMVVPGSGLVKEQAEREGLDKIFRD 398
Cdd:NF040615 284 ----------KPVSEVEGTEIDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVRL-IVIPASKKVFKQALKEGLIEIFVK 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 327549395 399 AGFEWREPGCSMCLAMNADRLEPGERCASTSNRNFEGRQG-AGGRTHLVSP 448
Cdd:NF040615 353 AGAMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGnINSYIYLSSP 403
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-466 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 990.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 1 MAQTLYDKLWDSHVVDTASDGTTILYIDRHLVHEVTSPQAFDGLKLAGRQPWRLSANLAVADHNVPTTDRAQGIADPTSR 80
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLPIADPVSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 81 LQVETLDANAKTYGLTYFNMADKRQGIVHVIGPEQGATLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTLLT 160
Cdd:PRK05478 81 IQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 161 KKSRSMLVQIDGALPRGVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTTI 240
Cdd:PRK05478 161 KKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 241 DYVKGRPFSPVGPHWERAVSWWRTLHSDAGARFDLVVRLDASQVRPQVTWGTSPEMVVAIDDRVPDPDKEKDPTKRDSME 320
Cdd:PRK05478 241 EYLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVKRASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 321 KALAYMALKPNTAIADIRIDKVFIGSCTNSRIEDLRAAAAVVRGKFRASNVRlAMVVPGSGLVKEQAEREGLDKIFRDAG 400
Cdd:PRK05478 321 RALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVR-ALVVPGSGLVKAQAEAEGLDKIFIEAG 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327549395 401 FEWREPGCSMCLAMNADRLEPGERCASTSNRNFEGRQGAGGRTHLVSPAMAAAAGIAGHFVDVRTL 466
Cdd:PRK05478 400 FEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVREL 465
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
1-466 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 804.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 1 MAQTLYDKLWDSHVVDTASDGTTILYIDRHLVHEVTSPQAFDGLKLAGRQPWRLSANLAVADHNVPTTD-RAQGIADPTS 79
Cdd:PRK12466 2 MPRTLYDKLWDSHTVARLDDGHVLLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPTRPgRDRGITDPGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 80 RLQVETLDANAKTYGLTYFNMADKRQGIVHVIGPEQGATLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTLL 159
Cdd:PRK12466 82 ALQVDYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQTLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 160 TKKSRSMLVQIDGALPRGVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTT 239
Cdd:PRK12466 162 YRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 240 IDYVKGRPFSPVGPHWERAVSWWRTLHSDAGARFDLVVRLDASQVRPQVTWGTSPEMVVAIDDRVPDPDKEKDPTKRDSM 319
Cdd:PRK12466 242 FDYLRGRPRAPKGALWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAAEADPARRAAM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 320 EKALAYMALKPNTAIADIRIDKVFIGSCTNSRIEDLRAAAAVVRGKFRASNVRlAMVVPGSGLVKEQAEREGLDKIFRDA 399
Cdd:PRK12466 322 ERALDYMGLTPGTPLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVR-AMVVPGSGAVRRQAEAEGLARIFIAA 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 327549395 400 GFEWREPGCSMCLAMNADRLEPGERCASTSNRNFEGRQGAGGRTHLVSPAMAAAAGIAGHFVDVRTL 466
Cdd:PRK12466 401 GFEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHITDVRSL 467
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
1-464 |
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: 737.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 1 MAQTLYDKLWDSHVVDTASDGTTILYIDRHLVHEVTSPQAFDGLKLAGRQPWRLSANLAVADHNVPTTDRAQGIADPTSR 80
Cdd:TIGR00170 1 MPRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFNIKDEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 81 LQVETLDANAKTYGLTYFNMADKRQGIVHVIGPEQGATLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTLLT 160
Cdd:TIGR00170 81 IQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 161 KKSRSMLVQIDGALPRGVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTTI 240
Cdd:TIGR00170 161 ARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 241 DYVKGRPFSPVGPHWERAVSWWRTLHSDAGARFDLVVRLDASQVRPQVTWGTSPEMVVAIDDRVPDPDKEKDPTKRDSME 320
Cdd:TIGR00170 241 EYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 321 KALAYMALKPNTAIADIRIDKVFIGSCTNSRIEDLRAAAAVVRGKFRASNVRlAMVVPGSGLVKEQAEREGLDKIFRDAG 400
Cdd:TIGR00170 321 RALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVK-ALVVPGSGLVKLQAEKEGLDKIFIEAG 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327549395 401 FEWREPGCSMCLAMNADRLEPGERCASTSNRNFEGRQGAGGRTHLVSPAMAAAAGIAGHFVDVR 464
Cdd:TIGR00170 400 FEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIR 463
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-448 |
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: 689.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 1 MAQTLYDKLWDSHVVDTASDGTTI-LYIDRHLVHEVTSPQAFDGLKLAG-RQPWRLSANLAVADHNVPTTDraqgiadPT 78
Cdd:COG0065 1 MGMTLAEKILARHAGREVEPGEIVlLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPTKD-------PK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 79 SRLQVETLDANAKTYGLTYFNMADKrqGIVHVIGPEQGATLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTL 158
Cdd:COG0065 74 SAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 159 LTKKSRSMLVQIDGALPRGVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDT 238
Cdd:COG0065 152 WFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 239 TIDYVKGRPFSPvgphweravswWRTLHSDAGARFDLVVRLDASQVRPQVTWGTSPEMVVAIDDrvpdpdkekdptkrds 318
Cdd:COG0065 232 TFEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE---------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 319 mekalaymalkpntaIADIRIDKVFIGSCTNSRIEDLRAAAAVVRGKFRASNVRlAMVVPGSGLVKEQAEREGLDKIFRD 398
Cdd:COG0065 285 ---------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVR-AIVVPGSQEVYRQAEAEGLDEIFIE 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 327549395 399 AGFEWREPGCSMCLAMNADRLEPGERCASTSNRNFEGRQG-AGGRTHLVSP 448
Cdd:COG0065 349 AGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASP 399
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-448 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 686.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 7 DKLWDSHVVDTASDgtTILYI-DRHLVHEVTSPQAFDGLKLAGRQPWRLSANLAVADHNVPTTDR--------AQGIADP 77
Cdd:pfam00330 1 EKIWDAHLVEELDG--SLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVidhapdalDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 78 TSR--LQVETLDANAKTYGLTYFNMAdkrQGIVHVIGPEQGATLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLAT 155
Cdd:pfam00330 79 ISRnkEQYDFLEWNAKKFGIRFVPPG---QGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 156 QTLLTKKSRSMLVQIDGALPRGVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAV 235
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 236 DDTTIDYVK--GRPFSPVGPHWERAVSWWrTLHSDAGARFDLVVRLDASQVRPQVTWGTSPEMVVAIDDRVPDPdkEKDP 313
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAVAWK-TLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDP--FADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 314 TKRDSMEKALAYMALKPNTAIADIRIDKVFIGSCTNSRIEDLRAAAAVVR-----GKFRASNVRlAMVVPGSGLVKEQAE 388
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVK-ASVVPGSEVVRAYAE 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 389 REGLDKIFRDAGFEWREPGCSMCLAmNADRLEPGERCASTSNRNFEGRQGAGGRTHLVSP 448
Cdd:pfam00330 392 AEGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASP 450
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
29-448 |
0e+00 |
|
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate; Aconatase-like catalytic domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes.
Pssm-ID: 153133 Cd Length: 382 Bit Score: 581.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 29 RHLVHEVTSPQAFDGLKLAGRQ-PWRLSANLAVADHNVPTtdraqgiADPTSRLQVETLDANAKTYGLTYFNMadKRQGI 107
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREkVWDPEKIVAVFDHNVPT-------PDIKAAEQVKTLRKFAKEFGINFFDV--GRQGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 108 VHVIGPEQGATLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTLLTKKSRSMLVQIDGALPRGVTAKDIVLAV 187
Cdd:cd01583 72 CHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 188 IGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTTIDYVKGRPFSPvgphweravswWRTLHS 267
Cdd:cd01583 152 IGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAY-----------WKELKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 268 DAGARFDLVVRLDASQVRPQVTWGTSPEMVVAIDDRVPdpdkekdptkrdsmekalaymalkpntaiadIRIDKVFIGSC 347
Cdd:cd01583 221 DEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQVFIGSC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 348 TNSRIEDLRAAAAVVRGKFRASNVRLaMVVPGSGLVKEQAEREGLDKIFRDAGFEWREPGCSMCLAMNADRLEPGERCAS 427
Cdd:cd01583 270 TNGRLEDLRAAAEILKGRKVADGVRL-IVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVS 348
|
410 420
....*....|....*....|..
gi 327549395 428 TSNRNFEGRQGAGG-RTHLVSP 448
Cdd:cd01583 349 TSNRNFKGRMGSPGaRIYLASP 370
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
1-448 |
5.49e-127 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 374.90 E-value: 5.49e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 1 MAQTLYDKLWDSHVVDTASDGTTILY-IDRHLVHEVTSPQAFDGL-KLAGRQPWRLSANLAVADHNVPTtdraqgiADPT 78
Cdd:PRK00402 1 MGMTLAEKILARHSGRDVSPGDIVEAkVDLVMAHDITGPLAIKEFeKIGGDKVFDPSKIVIVFDHFVPA-------KDIK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 79 SRLQVETLDANAKTYGLTYFNmaDKRQGIVHVIGPEQGATLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTL 158
Cdd:PRK00402 74 SAEQQKILREFAKEQGIPNFF--DVGEGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 159 LTKKSRSMLVQIDGALPRGVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDT 238
Cdd:PRK00402 152 WFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 239 TIDYVKGRPfspvgphwERAVSWWRtlhSDAGARFDLVVRLDASQVRPQVTWGTSPEMVVAIDDrvpdpdkekdptkrds 318
Cdd:PRK00402 232 TLEYLKERA--------GRDYKPWK---SDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSE---------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 319 mekalaymalkpntaIADIRIDKVFIGSCTNSRIEDLRAAAAVVRGKFRASNVRLaMVVPGSGLVKEQAEREGLDKIFRD 398
Cdd:PRK00402 285 ---------------VEGTKVDQVFIGSCTNGRLEDLRIAAEILKGRKVAPGVRL-IVIPASQKIYLQALKEGLIEIFVD 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 327549395 399 AGFEWREPGCSMCLAMNADRLEPGERCASTSNRNFEGRQG-AGGRTHLVSP 448
Cdd:PRK00402 349 AGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGsPESEVYLASP 399
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
4-438 |
3.99e-106 |
|
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: 321.32 E-value: 3.99e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 4 TLYDKLWDSHVVDTASDGTTILY-IDRHLVHEVTSPQAFDGLK-LAGRQPWRLSANLAVADHNVPTTDRAqgiadpTSRL 81
Cdd:TIGR01343 1 TIAEKILSKKSGKEVYAGDLIEAeIDLAMVHDITAPLAIKTLEeYGIDKVWNPEKIVIVFDHQVPADTIK------AAEM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 82 QVETLDAnAKTYGLTYFNmaDKRQGIVHVIGPEQGATLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTLLTK 161
Cdd:TIGR01343 75 QKLAREF-VKKQGIKYFY--DVGEGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 162 KSRSMLVQIDGALPRGVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTTID 241
Cdd:TIGR01343 152 VPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 242 YVKgrpfspvgphwERAVSWWRTLHSDAGARFDLVVRLDASQVRPQVTWGTSPEMVvaiddrvpdpdkekdptkrdsmek 321
Cdd:TIGR01343 232 YLK-----------ERRKEPFRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNV------------------------ 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 322 alaymalKPNTAIADIRIDKVFIGSCTNSRIEDLRAAAAVVRGKFRASNVRLaMVVPGSGLVKEQAEREGLDKIFRDAGF 401
Cdd:TIGR01343 277 -------KPVSEVEGTEIDQVFIGSCTNGRLEDLRVAAKILKGRKVAPDVRL-IVIPASRAVYLQALKEGLIEIFVKAGA 348
|
410 420 430
....*....|....*....|....*....|....*..
gi 327549395 402 EWREPGCSMCLAMNADRLEPGERCASTSNRNFEGRQG 438
Cdd:TIGR01343 349 VVSTPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMG 385
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
3-448 |
8.66e-85 |
|
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: 266.63 E-value: 8.66e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 3 QTLYDKLWDSHVVDTASDGTTILY-IDRHLVHEVTSPQAFDGLKLAGR-QPWRLSANLAVADHNVPTTDRAqgiadpTSR 80
Cdd:TIGR02086 1 MTLAEKILSEKVGRPVCAGEIVEVeVDLAMTHDGTGPLAIKALRELGVaRVWDPEKIVIAFDHNVPPPTVE------AAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 81 LQVETLDAnAKTYGLTYFNMADkrqGIVHVIGPEQGATLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTLLT 160
Cdd:TIGR02086 75 MQKEIREF-AKRHGIKNFDVGE---GICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTWI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 161 KKSRSMLVQIDGALPRGVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTTI 240
Cdd:TIGR02086 151 KVPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEETY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 241 DYVKGRpfspvGPHWERAVSwwrtlhSDAGARFDLVVRLDASQVRPQVTWGTSPEMVVAIDDrvpdpdkekdptkrdsme 320
Cdd:TIGR02086 231 EYLKKR-----RGLEFRILV------PDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVSD------------------ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 321 kalaymalkpntaIADIRIDKVFIGSCTNSRIEDLRAAAAVVRGKFRASNVRLaMVVPGSGLVKEQAEREGLDKIFRDAG 400
Cdd:TIGR02086 282 -------------VEGTEIDQVFIGSCTNGRLEDLRIAAEILKGRRVHPDVRL-IVIPASRKVYLRALEEGIILTLVRAG 347
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 327549395 401 FEWREPGCSMCLAMNADRLEPGERCASTSNRNFEGRQGA-GGRTHLVSP 448
Cdd:TIGR02086 348 AMICPPGCGPCLGAHMGVLGDGEVCLSTTNRNFKGRMGSpNAEIYLASP 396
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
4-448 |
1.28e-78 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 250.83 E-value: 1.28e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 4 TLYDKLWDSHVVDTASDGTTI-LYIDRHLVHEVTSPQAFDGLKLAGRQPWRLSANLAVADHNVP-TTDRAqgiadptSRL 81
Cdd:NF040615 2 TLAEKILSKKLGKEVYAGDTVeVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPaNTVKA-------ANM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 82 QVETLDAnAKTYGLTYFNMADkrQGIVHVIGPEQGATLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTLLTK 161
Cdd:NF040615 75 QKITREF-VKEQGIKNFYLGG--EGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 162 KSRSMLVQIDGALPRgVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTTID 241
Cdd:NF040615 152 VPKTIRVNIVGKNEN-ISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 242 YVKGRPFSpvgphwERAVSWW---RTLHSDAGARFDLVVRLDASQVRPQVTWGTSPEMVvaiddrvpdpdkekdptkrds 318
Cdd:NF040615 231 YLRKEGVS------EEEIAELkknRITVNEKEENYYKEIEIDITDMEEQVACPHHPDNV--------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 319 mekalaymalKPNTAIADIRIDKVFIGSCTNSRIEDLRAAAAVVRGKFRASNVRLaMVVPGSGLVKEQAEREGLDKIFRD 398
Cdd:NF040615 284 ----------KPVSEVEGTEIDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVRL-IVIPASKKVFKQALKEGLIEIFVK 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 327549395 399 AGFEWREPGCSMCLAMNADRLEPGERCASTSNRNFEGRQG-AGGRTHLVSP 448
Cdd:NF040615 353 AGAMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGnINSYIYLSSP 403
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
31-448 |
7.81e-69 |
|
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: 224.30 E-value: 7.81e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 31 LVHEVTSPQAFDGLK--LAGRQPWRLSANLAVADHNVPttdraqgIADPTSRLQVETLDANAKTYGLTYFNMADkrqGIV 108
Cdd:cd01351 3 MLQDATGPMAMKAFEilAALGKVADPSQIACVHDHAVQ-------LEKPVNNEGHKFLSFFAALQGIAFYRPGV---GII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 109 HVIGPEQGAtLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTLLTKKSRSMLVQIDGALPRGVTAKDIVLAVI 188
Cdd:cd01351 73 HQIMVENLA-LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 189 GQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTTIDYVKGRPFSPVGPHWERAVSwwrTLHSD 268
Cdd:cd01351 152 GIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWLAFPE---ELLAD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 269 AGARFDLVVRLDASQVRPQVTWGTSPEMVVAIddrvpdpdkekdptkrdsmekalaymalkpnTAIADIRIDKVFIGSCT 348
Cdd:cd01351 229 EGAEYDQVIEIDLSELEPDISGPNRPDDAVSV-------------------------------SEVEGTKIDQVLIGSCT 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 349 NSRIEDLRAAAAVVRGKFRASNVRLaMVVPGSGLVKEQAEREGLDKIFRDAGFEWREPGCSMCLAMNADRLEPGERCAST 428
Cdd:cd01351 278 NNRYSDMLAAAKLLKGAKVAPGVRL-IVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLVADGEVGVSS 356
|
410 420
....*....|....*....|.
gi 327549395 429 SNRNFEGRQGAG-GRTHLVSP 448
Cdd:cd01351 357 GNRNFPGRLGTYeRHVYLASP 377
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
1-448 |
1.49e-48 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 176.11 E-value: 1.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 1 MAQTLYDKLWDSHVVD-TASDGTTI-LYIDRHLVHEVTSPQAFDGLKLAGRQpwRLSANLAVA--DHNVPTTDRAQgiAD 76
Cdd:PRK07229 1 MGLTLTEKILYAHLVEgELEPGEEIaIRIDQTLTQDATGTMAYLQFEAMGLD--RVKTELSVQyvDHNLLQADFEN--AD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 77 PTSRLQvetldANAKTYGLtYF----NmadkrqGIVHVIGPEQGATlPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHV 152
Cdd:PRK07229 77 DHRFLQ-----SVAAKYGI-YFskpgN------GICHQVHLERFAF-PGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 153 LATQTLLTKKSRSMLVQIDGALPRGVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGM 232
Cdd:PRK07229 144 MAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 233 IAVDDTTIDYVK--GRpfspvgphwERAvswWRTLHSDAGARFDLVVRLDASQVRPQVTWGTSPEMVVAIDDrvpdpdke 310
Cdd:PRK07229 224 FPSDERTREFLKaqGR---------EDD---WVELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSE-------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 311 kdptkrdsmekalaymalkpntaIADIRIDKVFIGSCTNSRIEDLRAAAAVVRGKFRASNVRLaMVVPGSGLVKEQAERE 390
Cdd:PRK07229 284 -----------------------VAGIKVDQVLIGSCTNSSYEDLMRAASILKGKKVHPKVSL-VINPGSRQVLEMLARD 339
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 327549395 391 GLDKIFRDAGFEWREPGCSMCLAMNADrlePGERCAS--TSNRNFEGRQG-AGGRTHLVSP 448
Cdd:PRK07229 340 GALADLIAAGARILENACGPCIGMGQA---PATGNVSlrTFNRNFPGRSGtKDAQVYLASP 397
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
53-448 |
1.42e-47 |
|
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: 168.01 E-value: 1.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 53 RLSANLAVA--DHNVPTTDRAQgiADPTSRLQvetldANAKTYGLTYfnmADKRQGIVHVIGPEQGAtLPGMTVVCGDSH 130
Cdd:cd01585 24 RVRTELSVSyvDHNTLQTDFEN--ADDHRFLQ-----TVAARYGIYF---SRPGNGICHQVHLERFA-VPGKTLLGSDSH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 131 TSTHGAFGCLAHGIGTSEVEHVLATQTLLTKKSRSMLVQIDGALPRGVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRS 210
Cdd:cd01585 93 TPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVKGGVGKIFEYTGPGVAT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 211 LSMEGRMTVCNMAIEAGARAGMIAVDDTTIDYVK--GRPfspvgphweravSWWRTLHSDAGARFDLVVRLDASQVRPQV 288
Cdd:cd01585 173 LSVPERATITNMGAELGATTSIFPSDERTREFLAaqGRE------------DDWVELAADADAEYDEEIEIDLSELEPLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 289 TWGTSPEMVVAIDDrvpdpdkekdptkrdsmekalaymalkpntaIADIRIDKVFIGSCTNSRIEDLRAAAAVVRGKFRA 368
Cdd:cd01585 241 ARPHSPDNVVPVRE-------------------------------VAGIKVDQVAIGSCTNSSYEDLMTVAAILKGRRVH 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 369 SNVRLaMVVPGSGLVKEQAEREGLDKIFRDAGFEWREPGCSMCLAMNAdrlEPGERCAS--TSNRNFEGRQG-AGGRTHL 445
Cdd:cd01585 290 PHVSM-VVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQ---APPTGGVSvrTFNRNFEGRSGtKDDLVYL 365
|
...
gi 327549395 446 VSP 448
Cdd:cd01585 366 ASP 368
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
90-448 |
2.80e-37 |
|
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: 140.06 E-value: 2.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 90 AKTYGLTYFNMAdkrQGIVHVIGPEQGATLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTLLTKKSRSMLVQ 169
Cdd:cd01582 55 AKKHGIDFYPAG---RGIGHQIMIEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 170 IDGALPRGVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTTIdyvkgrpfs 249
Cdd:cd01582 132 LKGQLPKGVTGKDVIVALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAKHL--------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 250 pvgphweravswwrtlhsdagarfdlvvRLDASQVRPQVTwgtspemvvaiddrvpDPDKEKDPTKRDSMEKalaymalk 329
Cdd:cd01582 203 ----------------------------ILDLSTLSPYVS----------------GPNSVKVSTPLKELEA-------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 330 pntaiADIRIDKVFIGSCTNSRIEDLRAAAAVVRGKfrASNVRLAMVVPG--------SGLVKEQAEREGLDKIFRDAGF 401
Cdd:cd01582 231 -----QNIKINKAYLVSCTNSRASDIAAAADVVKGK--KEKNGKIPVAPGvefyvaaaSSEVQAAAEKNGDWQTLLEAGA 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 327549395 402 EWREPGCSMCLAMNADRLEPGERCASTSNRNFEGRQGA-GGRTHLVSP 448
Cdd:cd01582 304 TPLPAGCGPCIGLGQGLLEPGEVGISATNRNFKGRMGStEALAYLASP 351
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
106-448 |
1.25e-32 |
|
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: 128.33 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 106 GIVHVIGPEQGAtLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTLLTKKSRSMLVQIDGALPRGVTAKDIVL 185
Cdd:cd01584 77 GIIHQIVLENYA-FPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVIL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 186 AVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTTIDYVKGRPFSPVGPHWERAVSwwRTL 265
Cdd:cd01584 156 KVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEIADLADEFKD--DLL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 266 HSDAGARFDLVVRLDASQVRPQVTWGTSPEMVVAIDDRVPDPDKEKDPTkrdsmekalaymalkpntaiaDIRIDkvFIG 345
Cdd:cd01584 234 VADEGAEYDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAEKNGWPL---------------------DLRVG--LIG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 346 SCTNSRIEDLRAAAAVVRGKFrASNVRLAM---VVPGSGLVKEQAEREGLDKIFRDAGFEWREPGCSMCLAMnADR--LE 420
Cdd:cd01584 291 SCTNSSYEDMGRAASIAKQAL-AHGLKCKSiftITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQ-WDRkdIK 368
|
330 340 350
....*....|....*....|....*....|..
gi 327549395 421 PGERCA--STSNRNFEGRQGAGGRTH--LVSP 448
Cdd:cd01584 369 KGEKNTivTSYNRNFTGRNDANPATHafVASP 400
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
106-436 |
5.94e-29 |
|
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle
Pssm-ID: 440669 [Multi-domain] Cd Length: 891 Bit Score: 120.59 E-value: 5.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 106 GIVH----------VIGPEQGATL---PGmTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTLltkksrSML----- 167
Cdd:COG1048 176 GIVHqvnleylafvVWTREEDGETvayPD-TLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPV------SMLipevv 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 168 -VQIDGALPRGVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTTIDYVK-- 244
Cdd:COG1048 249 gVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRlt 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 245 GRpfSPVGP----HWERAVSWWRTlHSDAGARFDLVVRLDASQV--------RPQvtwgtspemvvaidDRVPDPD-KEk 311
Cdd:COG1048 329 GR--SEEQIelveAYAKAQGLWRD-PDAPEPYYSDVLELDLSTVepslagpkRPQ--------------DRIPLSDlKE- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 312 dptkrdSMEKALAYMALKPNTAIADIRIDKVF------------IGSCTNSRIED-LRAAA-----AVVRGKFRASNVR- 372
Cdd:COG1048 391 ------AFRAALAAPVGEELDKPVRVEVDGEEfelghgavviaaITSCTNTSNPSvMIAAGllakkAVEKGLKVKPWVKt 464
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327549395 373 -LAmvvPGSGLVKEQAEREGLDKIFRDAGFEWREPGCSMCLAmNADRLEP---------GERCAS-TS-NRNFEGR 436
Cdd:COG1048 465 sLA---PGSKVVTDYLERAGLLPYLEALGFNVVGYGCTTCIG-NSGPLPPeiseaieenDLVVAAvLSgNRNFEGR 536
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
106-436 |
8.77e-27 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 113.87 E-value: 8.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 106 GIVHVIGPEQGATL-------------PGmTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTLltkksrSML----- 167
Cdd:PRK12881 178 GIMHQVNLEYLARVvhtkeddgdtvayPD-TLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPV------YMLipdvv 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 168 -VQIDGALPRGVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTTIDYVK-- 244
Cdd:PRK12881 251 gVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLRlt 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 245 GRPFSPVG--PHWERAVSWWRtlHSDAGARFDLVVRLDASQVRPQVTWGTSP-------EMVVAIDDRVPDPDKEKDPTK 315
Cdd:PRK12881 331 GRTEAQIAlvEAYAKAQGLWG--DPKAEPRYTRTLELDLSTVAPSLAGPKRPqdrialgNVKSAFSDLFSKPVAENGFAK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 316 RDSMEKAlaymALKPN--TAIADIRidkvfigSCTN-SRIEDLRAAA-----AVVRGKFRASNVR--LAmvvPGSGLVKE 385
Cdd:PRK12881 409 KAQTSNG----VDLPDgaVAIAAIT-------SCTNtSNPSVLIAAGllakkAVERGLTVKPWVKtsLA---PGSKVVTE 474
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 327549395 386 QAEREGLDKIFRDAGFEWREPGCSMCLAMNADRLEPGER--------CAS--TSNRNFEGR 436
Cdd:PRK12881 475 YLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQaitkndlvAAAvlSGNRNFEGR 535
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
106-436 |
1.18e-24 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 107.41 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 106 GIVHVIGPE--------QGATLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTLltkksrSMLV------QID 171
Cdd:PTZ00092 185 GIVHQVNLEylarvvfnKDGLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPI------SMVLpevvgfKLT 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 172 GALPRGVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTTIDYVK--GRPFS 249
Cdd:PTZ00092 259 GKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKqtGRSEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 250 PVG--PHWERAVSWWRTLHSDagARFDLVVRLDASQVRPQVTWGTSPEmvvaidDRVPDPDKEKD-------PT------ 314
Cdd:PTZ00092 339 KVEliEKYLKANGLFRTYAEQ--IEYSDVLELDLSTVVPSVAGPKRPH------DRVPLSDLKKDftaclsaPVgfkgfg 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 315 -KRDSMEKALAYMAlkpNTAIADIRIDKVFIG---SCTNSRIEDLRAAAAVVRGKFRASNVRLAMVV-----PGSGLVKE 385
Cdd:PTZ00092 411 iPEEKHEKKVKFTY---KGKEYTLTHGSVVIAaitSCTNTSNPSVMLAAGLLAKKAVEKGLKVPPYIktslsPGSKVVTK 487
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 327549395 386 QAEREGLDKIFRDAGFEWREPGCSMCLAMNADRLEPGERCAS----------TSNRNFEGR 436
Cdd:PTZ00092 488 YLEASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITnndlvaaavlSGNRNFEGR 548
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
123-436 |
1.50e-21 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 97.89 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 123 TVVCGDSHTsTH-GAFGCLAHGIGTSEVEHVLATQTLltkksrSML------VQIDGALPRGVTAKDIVLAVIGQIGTAG 195
Cdd:PRK09277 207 TLVGTDSHT-TMiNGLGVLGWGVGGIEAEAAMLGQPS------SMLipevvgVKLTGKLPEGVTATDLVLTVTEMLRKKG 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 196 GNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTTIDYVK--GRPFSPVG--PHWERAVSWWRTlhSDAGA 271
Cdd:PRK09277 280 VVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRltGRDEEQVAlvEAYAKAQGLWRD--PLEEP 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 272 RFDLVVRLDASQV--------RPQvtwgtspemvvaidDRVPDPD-KEkdpTKRDSMEKALAYMALKPNTAIADIRIDK- 341
Cdd:PRK09277 358 VYTDVLELDLSTVepslagpkRPQ--------------DRIPLSDvKE---AFAKSAELGVQGFGLDEAEEGEDYELPDg 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 342 -VFIG---SCTN-SRIEDLRAAA-----AVVRGKFRASNVR--LAmvvPGSGLVKEQAEREG----LDKI-FRDAGFewr 404
Cdd:PRK09277 421 aVVIAaitSCTNtSNPSVMIAAGllakkAVEKGLKVKPWVKtsLA---PGSKVVTDYLEKAGllpyLEALgFNLVGY--- 494
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 327549395 405 epGCSMCLAMNADRLEPGERC------ASTS----NRNFEGR 436
Cdd:PRK09277 495 --GCTTCIGNSGPLPPEIEKAindndlVVTAvlsgNRNFEGR 534
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
118-447 |
1.08e-19 |
|
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle; Aconitase B catalytic domain. Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle. Aconitase has an active (4FE-4S) and an inactive (3FE-4S) form. The active cluster is part of the catalytic site that interconverts citrate, cis-aconitase and isocitrate. The domain architecture of aconitase B is different from other aconitases in that the catalytic domain is normally found at C-terminus for other aconitases, but it is at N-terminus for B family. It also has a HEAT domain before domain 4 which plays a role in protein-protein interaction. This alignment is the core domain including domains 1,2 and 3.
Pssm-ID: 153131 Cd Length: 436 Bit Score: 91.02 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 118 TLPGMTVVCGDSHTSThgAFGClAHGIGTSEVEHVLATQTLLTKKSRSMLVQIDGALPRGVTAKDIVLAV----IGQ--- 190
Cdd:cd01581 104 LLPDTVGTGGDSHTRF--PIGI-SFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVNAIpyyaIQQgll 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 191 -IGTAGG----NGYAIEFAGstIRSLSMEGRMTVCNMAIEAGARAGMIAVDD-TTIDYVK----------GRPFSPVGPH 254
Cdd:cd01581 181 tVEKKGKknvfNGRILEIEG--LPDLKVEQAFELTDASAERSAAACTVRLDKePVIEYLEsnvvlmkimiANGYDDARTL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 255 WER--AVSWWRT----LHSDAGARFDLVVRLDASQVRpqvtwgtspEMVVAIDDrvpDPDKekdptkrdsmekalaymaL 328
Cdd:cd01581 259 LRRiiAMEEWLAnpplLEPDADAEYAAVIEIDLDDIK---------EPILACPN---DPDD------------------V 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 329 KPNTAIADIRIDKVFIGSC-TNsrIEDLRAAAAVVRGKfRASNVRLaMVVPGSGLVKEQAEREGLDKIFRDAGFEWREPG 407
Cdd:cd01581 309 KLLSEVAGKKIDEVFIGSCmTN--IGHFRAAAKILRGK-EFKPTRL-WVAPPTRMDWAILQEEGYYSIFGDAGARTEMPG 384
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 327549395 408 CSMCLAmNADRLEPGERCASTSNRNFEGRQGAGGRTHLVS 447
Cdd:cd01581 385 CSLCMG-NQARVADGATVFSTSTRNFDNRVGKGAEVYLGS 423
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
106-448 |
1.74e-19 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 91.79 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 106 GIVHVIGPE---------QGATLPGmTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTLltkksrSMLV------QI 170
Cdd:PLN00070 217 GIVHQVNLEylgrvvfntDGILYPD-SVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPM------SMVLpgvvgfKL 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 171 DGALPRGVTAKDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTTIDYVK--GRPF 248
Cdd:PLN00070 290 SGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKltGRSD 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 249 SPVG-----------------PHWERAVSWWrtlhsdagarfdlvVRLDASQVRPQVTWGTSPEmvvaidDRVPDPDKEK 311
Cdd:PLN00070 370 ETVAmieaylrankmfvdynePQQERVYSSY--------------LELDLEDVEPCISGPKRPH------DRVPLKEMKA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 312 D--------------PTKRDSMEKALAYmalKPNTAIADIRIDKVFIG---SCTNSRIEDLRAAAAVVRGKfrASNVRLA 374
Cdd:PLN00070 430 DwhscldnkvgfkgfAVPKEAQSKVAKF---SFHGQPAELRHGSVVIAaitSCTNTSNPSVMLGAGLVAKK--ACELGLE 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 375 M-------VVPGSGLVKEQAEREGLDKIFRDAGFEWREPGCSMCLAmNADRLEPGERCASTS-----------NRNFEGR 436
Cdd:PLN00070 505 VkpwiktsLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIG-NSGELDESVASAITEndivaaavlsgNRNFEGR 583
|
410
....*....|...
gi 327549395 437 QGAGGR-THLVSP 448
Cdd:PLN00070 584 VHPLTRaNYLASP 596
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
107-436 |
9.90e-18 |
|
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: 84.66 E-value: 9.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 107 IVHVIGPEQGATLPGMTVVCGDSHTSTHGAFGCLAHGIGTSEVEHVLATQTLltkksrSML------VQIDGALPRGVTA 180
Cdd:cd01586 107 VVFTSEEDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPI------SMLlpevvgVKLTGKLRPGVTA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 181 KDIVLAVIGQIGTAGGNGYAIEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTtidyvkgrpfspvgphweravs 260
Cdd:cd01586 181 TDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVDTQ---------------------- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 261 wwrtlhsdagarfdlVVRLDASQVRPQVTWGTSPEmvvaidDRVPdpdkekdptkrdsmekalaymaLKPNTAIADIRid 340
Cdd:cd01586 239 ---------------VVELDLSTVEPSVSGPKRPQ------DRVP----------------------LHGSVVIAAIT-- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 341 kvfigSCTNSRIEDLRAAAAVVRGKFRASNVRLAMVV-----PGSGLVKEQAEREGLDKIFRDAGFEWREPGCSMCLAMN 415
Cdd:cd01586 274 -----SCTNTSNPSVMLAAGLLAKKAVELGLKVKPYVktslaPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGNS 348
|
330 340 350
....*....|....*....|....*....|.
gi 327549395 416 ADRLEPGER---------CASTS-NRNFEGR 436
Cdd:cd01586 349 GPLPEEVEEaikendlvvAAVLSgNRNFEGR 379
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
329-447 |
7.83e-16 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 80.22 E-value: 7.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 329 KPNTAIADIRIDKVFIGSC-TNsrIEDLRAAAAVVRGKFRASNVRLaMVVPGSGLVKEQAEREGLDKIFRDAGFEWREPG 407
Cdd:PRK09238 681 RLLSEVAGTKIDEVFIGSCmTN--IGHFRAAGKLLEGKKGQLPTRL-WVAPPTKMDADQLTEEGYYSIFGKAGARIEMPG 757
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 327549395 408 CSMCLAmNADRLEPGERCASTSNRNFEGRQGAGGRTHLVS 447
Cdd:PRK09238 758 CSLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYLGS 796
|
|
| AcnB |
COG1049 |
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ... |
329-447 |
6.58e-14 |
|
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: 74.12 E-value: 6.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 329 KPNTAIADIRIDKVFIGSC-TNsrIEDLRAAAAVVRGKFrASNVRLaMVVPGSGLVKEQAEREGLDKIFRDAGFEWREPG 407
Cdd:COG1049 681 KLLSEVAGTKIDEVFIGSCmTN--IGHFRAAGKLLEGKG-NLPTRL-WIAPPTKMDEAQLTEEGYYSIFGAAGARTEMPG 756
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 327549395 408 CSMCLAmNADRLEPGERCASTSNRNFEGRQGAGGRTHLVS 447
Cdd:COG1049 757 CSLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYLGS 795
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
119-447 |
3.00e-13 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 72.26 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 119 LPGMTVVCGDSHTSthgafgcLAHGI----GTSEVEHVLATQTLLTKKSRSMLVQIDGALPRGVTAKDIVLAV---IGQI 191
Cdd:PLN00094 551 LPDTVGTGGDSHTR-------FPIGIsfpaGSGLVAFGAATGVIPLDMPESVLVRFTGTMQPGITLRDLVHAIpytAIQD 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 192 G--TAGGNGYAIEFAGstiRSLSMEGRMTV-CNMAIEAGARAGMIAVDDTTIDYVKgrpfSPVGPHWERAVSWWR-TLHS 267
Cdd:PLN00094 624 GllTVEKKGKKNVFSG---RILEIEGLPHLkCEQAFELSDASAERSAAGCTIKLDK----EPIIEYLNSNVVMLKwMIAE 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 268 DAGARFDLVVRLDASQvrpqvTWGTSPEMVVAiddrvpDPDKEKDPTKRDSMEKALAYMALKPN--------TAIADIRI 339
Cdd:PLN00094 697 GYGDRRTLERRIARMQ-----QWLADPELLEA------DPDAEYAAVIEIDMDEIKEPILCAPNdpddarllSEVTGDKI 765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 340 DKVFIGSC-TNsrIEDLRAAAAVVRGKFRASNVRLaMVVPGSGLVKEQAEREGLDKIFRDAGFEWREPGCSMCLAmNADR 418
Cdd:PLN00094 766 DEVFIGSCmTN--IGHFRAAGKLLNDNLSQLPTRL-WVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPGCSLCMG-NQAR 841
|
330 340
....*....|....*....|....*....
gi 327549395 419 LEPGERCASTSNRNFEGRQGAGGRTHLVS 447
Cdd:PLN00094 842 VAEKSTVVSTSTRNFPNRLGKGANVYLAS 870
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
122-380 |
1.24e-10 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 63.88 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 122 MTVVCG------DSHTStHGAFGCLAHGIGTSEVEHVLATQTLLTKKSRSMLVQIDGALPRGVTAKDIVLAVIGQIGtag 195
Cdd:PRK11413 137 MMAGGGkmilgsDSHTR-YGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVF--- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 196 GNGYA----IEFAGSTIRSLSMEGRMTVCNMAIEAGARAGMIAVDDTTIDYVK--GRPFSpvgphweravswWRTLHSDA 269
Cdd:PRK11413 213 KNGYVknkvMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLAlhGRGQD------------YCELNPQP 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327549395 270 GARFDLVVRLDASQVRPQVTWGTSPEMVVAIDDRVPDPDKEKDPTKRDSMEKALAYMALKPNTAIAD--IRIDKVFIGSC 347
Cdd:PRK11413 281 MAYYDGCISVDLSAIKPMIALPFHPSNVYEIDELNQNLTDILREVEIESERVAHGKAKLSLLDKIENgrLKVQQGIIAGC 360
|
250 260 270
....*....|....*....|....*....|...
gi 327549395 348 TNSRIEDLRAAAAVVRGKFRASNVRLAMVVPGS 380
Cdd:PRK11413 361 SGGNYENVIAAANALRGQSCGNDTFSLSVYPSS 393
|
|
| |
