|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-467 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 1019.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 1 MAKTLYDKLWDAHLVHQDDDGTALLYIDRQLLHEVTSPQAFEGLRLAGRKPRRIDANLAVPDHNVPTDDRSSEIADPVSR 80
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLPIADPVSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 81 LQVETLEKNCKEFGITMFAMNDPRQGIVHVIGPEQGATLPGMTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCLIQ 160
Cdd:PRK05478 81 IQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 161 KKSKTMLIEVNGELPSGLTAKDIVLAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTI 240
Cdd:PRK05478 161 KKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 241 DYVEGRPFAPQGADWELAVASWRQLKSDPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIADRVPSPAEEADPVKQEGMQ 320
Cdd:PRK05478 241 EYLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVKRASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 321 AALKYMGLEPGTPINQIKPDIVFIGSCTNGRIEDLRAVAAVAKGRKVADNIkQALIVPGSGLVKQQAEKEGLDKIFIDAG 400
Cdd:PRK05478 321 RALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGV-RALVVPGSGLVKAQAEAEGLDKIFIEAG 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1120034798 401 FEWREPGCSMCLAMNNDRLKPGERCASTSNRNFEGRQGQGGRTHLVSPAMAAAAAVTGHFVDVRSLE 467
Cdd:PRK05478 400 FEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| 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: 791.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 1 MAKTLYDKLWDAHLVHQDDDGTALLYIDRQLLHEVTSPQAFEGLRLAGRKPRRIDANLAVPDHNVPTDDRSSEIADPVSR 80
Cdd:TIGR00170 1 MPRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFNIKDEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 81 LQVETLEKNCKEFGITMFAMNDPRQGIVHVIGPEQGATLPGMTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCLIQ 160
Cdd:TIGR00170 81 IQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 161 KKSKTMLIEVNGELPSGLTAKDIVLAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTI 240
Cdd:TIGR00170 161 ARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 241 DYVEGRPFAPQGADWELAVASWRQLKSDPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIADRVPSPAEEADPVKQEGMQ 320
Cdd:TIGR00170 241 EYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 321 AALKYMGLEPGTPINQIKPDIVFIGSCTNGRIEDLRAVAAVAKGRKVADNIKqALIVPGSGLVKQQAEKEGLDKIFIDAG 400
Cdd:TIGR00170 321 RALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVK-ALVVPGSGLVKLQAEKEGLDKIFIEAG 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1120034798 401 FEWREPGCSMCLAMNNDRLKPGERCASTSNRNFEGRQGQGGRTHLVSPAMAAAAAVTGHFVDVR 464
Cdd:TIGR00170 400 FEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIR 463
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-466 |
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: 723.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 1 MAKTLYDKLWDAHLVHQD-DDGTALLYIDRQLLHEVTSPQAFEGLRLAG-RKPRRIDANLAVPDHNVPTDDrsseiadPV 78
Cdd:COG0065 1 MGMTLAEKILARHAGREVePGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPTKD-------PK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 79 SRLQVETLEKNCKEFGITMFAMNDPrqGIVHVIGPEQGATLPGMTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCL 158
Cdd:COG0065 74 SAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 159 IQKKSKTMLIEVNGELPSGLTAKDIVLAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQK 238
Cdd:COG0065 152 WFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 239 TIDYVEGRPFAPqgadwelavasWRQLKSDPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIADrvpspaeeadpvkqeg 318
Cdd:COG0065 232 TFEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE---------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 319 mqaalkymgLEpGTPInqikpDIVFIGSCTNGRIEDLRAVAAVAKGRKVADNIKqALIVPGSGLVKQQAEKEGLDKIFID 398
Cdd:COG0065 285 ---------LE-GIKI-----DQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVR-AIVVPGSQEVYRQAEAEGLDEIFIE 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1120034798 399 AGFEWREPGCSMCLAMNNDRLKPGERCASTSNRNFEGRQG-QGGRTHLVSPAMAAAAAVTGHFVDVRSL 466
Cdd:COG0065 349 AGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-448 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 707.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 7 DKLWDAHLVHQDDDgtALLYI-DRQLLHEVTSPQAFEGLRLAGRKPRRIDANLAVPDHNVPTD---DRSSE-----IADP 77
Cdd:pfam00330 1 EKIWDAHLVEELDG--SLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDlviDHAPDaldknIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 78 VSR--LQVETLEKNCKEFGITMFamnDPRQGIVHVIGPEQGATLPGMTVVCGDSHTATHGAFGALAFGIGTSEVEHVLAT 155
Cdd:pfam00330 79 ISRnkEQYDFLEWNAKKFGIRFV---PPGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 156 QCLIQKKSKTMLIEVNGELPSGLTAKDIVLAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAV 235
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 236 DQKTIDYVE--GRPFAPQGADWELAVAsWRQLKSDPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIADRVPSPaeEADP 313
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDP--FADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 314 VKQEGMQAALKYMGLEPGTPINQIKPDIVFIGSCTNGRIEDLRAVA-----AVAKGRKVADNIKqALIVPGSGLVKQQAE 388
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAgllkkAVEKGLKVAPGVK-ASVVPGSEVVRAYAE 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 389 KEGLDKIFIDAGFEWREPGCSMCLAmNNDRLKPGERCASTSNRNFEGRQGQGGRTHLVSP 448
Cdd:pfam00330 392 AEGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASP 450
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
29-460 |
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: 596.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 29 RQLLHEVTSPQAFEGLRLAGR-KPRRIDANLAVPDHNVPTDDrsseiadPVSRLQVETLEKNCKEFGITMFAMNdpRQGI 107
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPTPD-------IKAAEQVKTLRKFAKEFGINFFDVG--RQGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 108 VHVIGPEQGATLPGMTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCLIQKKSKTMLIEVNGELPSGLTAKDIVLAI 187
Cdd:cd01583 72 CHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 188 IGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTIDYVEGRPFAPqgadwelavasWRQLKS 267
Cdd:cd01583 152 IGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAY-----------WKELKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 268 DPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIADRVPspaeeadpvkqegmqaalkymglepgtpinqIKPDIVFIGSC 347
Cdd:cd01583 221 DEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQVFIGSC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 348 TNGRIEDLRAVAAVAKGRKVADNIKqALIVPGSGLVKQQAEKEGLDKIFIDAGFEWREPGCSMCLAMNNDRLKPGERCAS 427
Cdd:cd01583 270 TNGRLEDLRAAAEILKGRKVADGVR-LIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVS 348
|
410 420 430
....*....|....*....|....*....|....
gi 1120034798 428 TSNRNFEGRQG-QGGRTHLVSPAMAAAAAVTGHF 460
Cdd:cd01583 349 TSNRNFKGRMGsPGARIYLASPATAAASAITGEI 382
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
27-459 |
9.12e-89 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 277.02 E-value: 9.12e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 27 IDRQLLHEVTSPQAFEGLRLAGRK---PRRIdanLAVPDHNVPTDDRSSeiadpvSRLQVETLEkNCKEFGITMFAMNDp 103
Cdd:NF040615 26 VDLAMTHDGTTPLTYKAFKEISDKvwdNEKI---VIVFDHNVPANTVKA------ANMQKITRE-FVKEQGIKNFYLGG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 104 rQGIVHVIGPEQGATLPGMTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCLIQKKSKTMLIEVNGELPSgLTAKDI 183
Cdd:NF040615 95 -EGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVNIVGKNEN-ISGKDI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 184 VLAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTIDYVEGRPFAPQGAdweLAVASWR 263
Cdd:NF040615 173 ILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEGVSEEEI---AELKKNR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 264 QLKSDPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIADRVpspaeeadpvkqegmqaalkymglepGTPINQikpdiVF 343
Cdd:NF040615 250 ITVNEKEENYYKEIEIDITDMEEQVACPHHPDNVKPVSEVE--------------------------GTEIDQ-----VF 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 344 IGSCTNGRIEDLRAVAAVAKGRKVADNIKqALIVPGSGLVKQQAEKEGLDKIFIDAGFEWREPGCSMCLAMNNDRLKPGE 423
Cdd:NF040615 299 IGSCTNGRLSDLRIAAKYLKGKKVHKDVR-LIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGE 377
|
410 420 430
....*....|....*....|....*....|....*..
gi 1120034798 424 RCASTSNRNFEGRQGQ-GGRTHLVSPAMAAAAAVTGH 459
Cdd:NF040615 378 VCLSTTNRNFKGRMGNiNSYIYLSSPKIAAKSAVKGY 414
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-467 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 1019.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 1 MAKTLYDKLWDAHLVHQDDDGTALLYIDRQLLHEVTSPQAFEGLRLAGRKPRRIDANLAVPDHNVPTDDRSSEIADPVSR 80
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLPIADPVSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 81 LQVETLEKNCKEFGITMFAMNDPRQGIVHVIGPEQGATLPGMTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCLIQ 160
Cdd:PRK05478 81 IQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 161 KKSKTMLIEVNGELPSGLTAKDIVLAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTI 240
Cdd:PRK05478 161 KKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 241 DYVEGRPFAPQGADWELAVASWRQLKSDPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIADRVPSPAEEADPVKQEGMQ 320
Cdd:PRK05478 241 EYLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVKRASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 321 AALKYMGLEPGTPINQIKPDIVFIGSCTNGRIEDLRAVAAVAKGRKVADNIkQALIVPGSGLVKQQAEKEGLDKIFIDAG 400
Cdd:PRK05478 321 RALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGV-RALVVPGSGLVKAQAEAEGLDKIFIEAG 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1120034798 401 FEWREPGCSMCLAMNNDRLKPGERCASTSNRNFEGRQGQGGRTHLVSPAMAAAAAVTGHFVDVRSLE 467
Cdd:PRK05478 400 FEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
1-469 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 852.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 1 MAKTLYDKLWDAHLVHQDDDGTALLYIDRQLLHEVTSPQAFEGLRLAGRKPRRIDANLAVPDHNVPT-DDRSSEIADPVS 79
Cdd:PRK12466 2 MPRTLYDKLWDSHTVARLDDGHVLLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPTrPGRDRGITDPGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 80 RLQVETLEKNCKEFGITMFAMNDPRQGIVHVIGPEQGATLPGMTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCLI 159
Cdd:PRK12466 82 ALQVDYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQTLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 160 QKKSKTMLIEVNGELPSGLTAKDIVLAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKT 239
Cdd:PRK12466 162 YRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 240 IDYVEGRPFAPQGADWELAVASWRQLKSDPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIADRVPSPAEEADPVKQEGM 319
Cdd:PRK12466 242 FDYLRGRPRAPKGALWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAAEADPARRAAM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 320 QAALKYMGLEPGTPINQIKPDIVFIGSCTNGRIEDLRAVAAVAKGRKVADNIkQALIVPGSGLVKQQAEKEGLDKIFIDA 399
Cdd:PRK12466 322 ERALDYMGLTPGTPLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGV-RAMVVPGSGAVRRQAEAEGLARIFIAA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 400 GFEWREPGCSMCLAMNNDRLKPGERCASTSNRNFEGRQGQGGRTHLVSPAMAAAAAVTGHFVDVRSLEVK 469
Cdd:PRK12466 401 GFEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHITDVRSLLQA 470
|
|
| 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: 791.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 1 MAKTLYDKLWDAHLVHQDDDGTALLYIDRQLLHEVTSPQAFEGLRLAGRKPRRIDANLAVPDHNVPTDDRSSEIADPVSR 80
Cdd:TIGR00170 1 MPRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFNIKDEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 81 LQVETLEKNCKEFGITMFAMNDPRQGIVHVIGPEQGATLPGMTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCLIQ 160
Cdd:TIGR00170 81 IQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 161 KKSKTMLIEVNGELPSGLTAKDIVLAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTI 240
Cdd:TIGR00170 161 ARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 241 DYVEGRPFAPQGADWELAVASWRQLKSDPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIADRVPSPAEEADPVKQEGMQ 320
Cdd:TIGR00170 241 EYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 321 AALKYMGLEPGTPINQIKPDIVFIGSCTNGRIEDLRAVAAVAKGRKVADNIKqALIVPGSGLVKQQAEKEGLDKIFIDAG 400
Cdd:TIGR00170 321 RALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVK-ALVVPGSGLVKLQAEKEGLDKIFIEAG 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1120034798 401 FEWREPGCSMCLAMNNDRLKPGERCASTSNRNFEGRQGQGGRTHLVSPAMAAAAAVTGHFVDVR 464
Cdd:TIGR00170 400 FEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIR 463
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-466 |
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: 723.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 1 MAKTLYDKLWDAHLVHQD-DDGTALLYIDRQLLHEVTSPQAFEGLRLAG-RKPRRIDANLAVPDHNVPTDDrsseiadPV 78
Cdd:COG0065 1 MGMTLAEKILARHAGREVePGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPTKD-------PK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 79 SRLQVETLEKNCKEFGITMFAMNDPrqGIVHVIGPEQGATLPGMTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCL 158
Cdd:COG0065 74 SAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 159 IQKKSKTMLIEVNGELPSGLTAKDIVLAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQK 238
Cdd:COG0065 152 WFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 239 TIDYVEGRPFAPqgadwelavasWRQLKSDPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIADrvpspaeeadpvkqeg 318
Cdd:COG0065 232 TFEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE---------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 319 mqaalkymgLEpGTPInqikpDIVFIGSCTNGRIEDLRAVAAVAKGRKVADNIKqALIVPGSGLVKQQAEKEGLDKIFID 398
Cdd:COG0065 285 ---------LE-GIKI-----DQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVR-AIVVPGSQEVYRQAEAEGLDEIFIE 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1120034798 399 AGFEWREPGCSMCLAMNNDRLKPGERCASTSNRNFEGRQG-QGGRTHLVSPAMAAAAAVTGHFVDVRSL 466
Cdd:COG0065 349 AGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-448 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 707.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 7 DKLWDAHLVHQDDDgtALLYI-DRQLLHEVTSPQAFEGLRLAGRKPRRIDANLAVPDHNVPTD---DRSSE-----IADP 77
Cdd:pfam00330 1 EKIWDAHLVEELDG--SLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDlviDHAPDaldknIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 78 VSR--LQVETLEKNCKEFGITMFamnDPRQGIVHVIGPEQGATLPGMTVVCGDSHTATHGAFGALAFGIGTSEVEHVLAT 155
Cdd:pfam00330 79 ISRnkEQYDFLEWNAKKFGIRFV---PPGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 156 QCLIQKKSKTMLIEVNGELPSGLTAKDIVLAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAV 235
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 236 DQKTIDYVE--GRPFAPQGADWELAVAsWRQLKSDPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIADRVPSPaeEADP 313
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDP--FADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 314 VKQEGMQAALKYMGLEPGTPINQIKPDIVFIGSCTNGRIEDLRAVA-----AVAKGRKVADNIKqALIVPGSGLVKQQAE 388
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAgllkkAVEKGLKVAPGVK-ASVVPGSEVVRAYAE 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 389 KEGLDKIFIDAGFEWREPGCSMCLAmNNDRLKPGERCASTSNRNFEGRQGQGGRTHLVSP 448
Cdd:pfam00330 392 AEGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASP 450
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
29-460 |
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: 596.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 29 RQLLHEVTSPQAFEGLRLAGR-KPRRIDANLAVPDHNVPTDDrsseiadPVSRLQVETLEKNCKEFGITMFAMNdpRQGI 107
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPTPD-------IKAAEQVKTLRKFAKEFGINFFDVG--RQGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 108 VHVIGPEQGATLPGMTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCLIQKKSKTMLIEVNGELPSGLTAKDIVLAI 187
Cdd:cd01583 72 CHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 188 IGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTIDYVEGRPFAPqgadwelavasWRQLKS 267
Cdd:cd01583 152 IGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAY-----------WKELKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 268 DPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIADRVPspaeeadpvkqegmqaalkymglepgtpinqIKPDIVFIGSC 347
Cdd:cd01583 221 DEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQVFIGSC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 348 TNGRIEDLRAVAAVAKGRKVADNIKqALIVPGSGLVKQQAEKEGLDKIFIDAGFEWREPGCSMCLAMNNDRLKPGERCAS 427
Cdd:cd01583 270 TNGRLEDLRAAAEILKGRKVADGVR-LIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVS 348
|
410 420 430
....*....|....*....|....*....|....
gi 1120034798 428 TSNRNFEGRQG-QGGRTHLVSPAMAAAAAVTGHF 460
Cdd:cd01583 349 TSNRNFKGRMGsPGARIYLASPATAAASAITGEI 382
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
1-466 |
3.89e-132 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 388.00 E-value: 3.89e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 1 MAKTLYDKLWDAHLVHQDDDGTALLY-IDRQLLHEVTSPQAFEGLRLAGRK----PRRIdanLAVPDHNVPTDD-RSSEI 74
Cdd:PRK00402 1 MGMTLAEKILARHSGRDVSPGDIVEAkVDLVMAHDITGPLAIKEFEKIGGDkvfdPSKI---VIVFDHFVPAKDiKSAEQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 75 AdpvsrlqvetleKNCKEF----GITMFamNDPRQGIVHVIGPEQGATLPGMTVVCGDSHTATHGAFGALAFGIGTSEVE 150
Cdd:PRK00402 78 Q------------KILREFakeqGIPNF--FDVGEGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 151 HVLATQCLIQKKSKTMLIEVNGELPSGLTAKDIVLAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARA 230
Cdd:PRK00402 144 AAMATGKTWFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 231 GLIAVDQKTIDYVegrpfapqgadWELAVASWRQLKSDPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIADrvpspAEe 310
Cdd:PRK00402 224 GIFAPDEKTLEYL-----------KERAGRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSE-----VE- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 311 adpvkqegmqaalkymglepGTPINQikpdiVFIGSCTNGRIEDLRAVAAVAKGRKVADNIkQALIVPGSGLVKQQAEKE 390
Cdd:PRK00402 287 --------------------GTKVDQ-----VFIGSCTNGRLEDLRIAAEILKGRKVAPGV-RLIVIPASQKIYLQALKE 340
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1120034798 391 GLDKIFIDAGFEWREPGCSMCLAMNNDRLKPGERCASTSNRNFEGRQGQ-GGRTHLVSPAMAAAAAVTGHFVDVRSL 466
Cdd:PRK00402 341 GLIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGSpESEVYLASPAVAAASAVTGKITDPREV 417
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
27-464 |
2.94e-114 |
|
homoaconitate hydratase family protein; This model represents a subfamily of proteins consisting of aconitase, homoaconitase, 3-isopropylmalate dehydratase, and uncharacterized proteins. The majority of the members of this family have been designated as 3-isopropylmalate dehydratase large subunit (LeuC) in microbial genome annotation, but the only characterized member is Thermus thermophilus homoaconitase, an enzyme of a non-aspartate pathway of Lys biosynthesis.
Pssm-ID: 273563 Cd Length: 412 Bit Score: 342.12 E-value: 2.94e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 27 IDRQLLHEVTSPQAFEGL-RLAGRKPRRIDANLAVPDHNVPTDDRSseiadpVSRLQVETLEKnCKEFGITMFamNDPRQ 105
Cdd:TIGR01343 25 IDLAMVHDITAPLAIKTLeEYGIDKVWNPEKIVIVFDHQVPADTIK------AAEMQKLAREF-VKKQGIKYF--YDVGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 106 GIVHVIGPEQGATLPGMTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCLIQKKSKTMLIEVNGELPSGLTAKDIVL 185
Cdd:TIGR01343 96 GICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFKVPETIRVNITGKLNPGVTAKDVIL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 186 AIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTIDYVEgrpfapqgadwELAVASWRQL 265
Cdd:TIGR01343 176 EVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYLK-----------ERRKEPFRVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 266 KSDPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIADrvpspaeeadpvkqegmqaalkymglEPGTPINQikpdiVFIG 345
Cdd:TIGR01343 245 KSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSE--------------------------VEGTEIDQ-----VFIG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 346 SCTNGRIEDLRAVAAVAKGRKVADNIkQALIVPGSGLVKQQAEKEGLDKIFIDAGFEWREPGCSMCLAMNNDRLKPGERC 425
Cdd:TIGR01343 294 SCTNGRLEDLRVAAKILKGRKVAPDV-RLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLGSHQGVLAPGEVC 372
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1120034798 426 ASTSNRNFEGRQGQ-GGRTHLVSPAMAAAAAVTGHFVDVR 464
Cdd:TIGR01343 373 ISTSNRNFKGRMGHpNAEIYLASPATAAASAVKGYIADPR 412
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
27-464 |
5.53e-91 |
|
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: 282.42 E-value: 5.53e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 27 IDRQLLHEVTSPQAFEGLRLAG----RKPRRIdanLAVPDHNVPTDDRSseiadpVSRLQVETLEKnCKEFGITMFAMND 102
Cdd:TIGR02086 26 VDLAMTHDGTGPLAIKALRELGvarvWDPEKI---VIAFDHNVPPPTVE------AAEMQKEIREF-AKRHGIKNFDVGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 103 prqGIVHVIGPEQGATLPGMTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCLIQKKSKTMLIEVNGELPSGLTAKD 182
Cdd:TIGR02086 96 ---GICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTWIKVPETIRVVVEGKPEEGVTAKD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 183 IVLAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTIDYVEGRpfapqgadwelAVASW 262
Cdd:TIGR02086 173 VALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEETYEYLKKR-----------RGLEF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 263 RQLKSDPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIADrvpspaeeadpVKqegmqaalkymglepGTPINQikpdiV 342
Cdd:TIGR02086 242 RILVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVSD-----------VE---------------GTEIDQ-----V 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 343 FIGSCTNGRIEDLRAVAAVAKGRKVADNIKqALIVPGSGLVKQQAEKEGLDKIFIDAGFEWREPGCSMCLAMNNDRLKPG 422
Cdd:TIGR02086 291 FIGSCTNGRLEDLRIAAEILKGRRVHPDVR-LIVIPASRKVYLRALEEGIILTLVRAGAMICPPGCGPCLGAHMGVLGDG 369
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1120034798 423 ERCASTSNRNFEGRQGQ-GGRTHLVSPAMAAAAAVTGHFVDVR 464
Cdd:TIGR02086 370 EVCLSTTNRNFKGRMGSpNAEIYLASPATAAASAVEGYITDPE 412
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
27-459 |
9.12e-89 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 277.02 E-value: 9.12e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 27 IDRQLLHEVTSPQAFEGLRLAGRK---PRRIdanLAVPDHNVPTDDRSSeiadpvSRLQVETLEkNCKEFGITMFAMNDp 103
Cdd:NF040615 26 VDLAMTHDGTTPLTYKAFKEISDKvwdNEKI---VIVFDHNVPANTVKA------ANMQKITRE-FVKEQGIKNFYLGG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 104 rQGIVHVIGPEQGATLPGMTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCLIQKKSKTMLIEVNGELPSgLTAKDI 183
Cdd:NF040615 95 -EGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVNIVGKNEN-ISGKDI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 184 VLAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTIDYVEGRPFAPQGAdweLAVASWR 263
Cdd:NF040615 173 ILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEGVSEEEI---AELKKNR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 264 QLKSDPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIADRVpspaeeadpvkqegmqaalkymglepGTPINQikpdiVF 343
Cdd:NF040615 250 ITVNEKEENYYKEIEIDITDMEEQVACPHHPDNVKPVSEVE--------------------------GTEIDQ-----VF 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 344 IGSCTNGRIEDLRAVAAVAKGRKVADNIKqALIVPGSGLVKQQAEKEGLDKIFIDAGFEWREPGCSMCLAMNNDRLKPGE 423
Cdd:NF040615 299 IGSCTNGRLSDLRIAAKYLKGKKVHKDVR-LIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGE 377
|
410 420 430
....*....|....*....|....*....|....*..
gi 1120034798 424 RCASTSNRNFEGRQGQ-GGRTHLVSPAMAAAAAVTGH 459
Cdd:NF040615 378 VCLSTTNRNFKGRMGNiNSYIYLSSPKIAAKSAVKGY 414
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
29-448 |
5.92e-71 |
|
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: 230.08 E-value: 5.92e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 29 RQLLHEVTSPQA---FEGLRLAGR--KPRRIDAnlavpdhnvpTDDRSSEIADPVSRLQVETLEKNCKEFGItmfAMNDP 103
Cdd:cd01351 1 RVMLQDATGPMAmkaFEILAALGKvaDPSQIAC----------VHDHAVQLEKPVNNEGHKFLSFFAALQGI---AFYRP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 104 RQGIVHVIGPEQGAtLPGMTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCLIQKKSKTMLIEVNGELPSGLTAKDI 183
Cdd:cd01351 68 GVGIIHQIMVENLA-LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 184 VLAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTIDYVE--GRPFAPQgadweLAVAS 261
Cdd:cd01351 147 VLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEatGRPLLKN-----LWLAF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 262 WRQLKSDPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIADrvpspaeeadpvkqegmqaalkymglepgtpINQIKPDI 341
Cdd:cd01351 222 PEELLADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSE-------------------------------VEGTKIDQ 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 342 VFIGSCTNGRIEDLRAVAAVAKGRKVADNIkQALIVPGSGLVKQQAEKEGLDKIFIDAGFEWREPGCSMCLAMNNDRLKP 421
Cdd:cd01351 271 VLIGSCTNNRYSDMLAAAKLLKGAKVAPGV-RLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLVAD 349
|
410 420
....*....|....*....|....*...
gi 1120034798 422 GERCASTSNRNFEGRQGQG-GRTHLVSP 448
Cdd:cd01351 350 GEVGVSSGNRNFPGRLGTYeRHVYLASP 377
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
1-467 |
1.84e-55 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 195.37 E-value: 1.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 1 MAKTLYDKLWDAHLVhqddDGTAL------LYIDRQLLHEVTSPQA---FEGLRLAgrkprRIDANLAVP--DHNVP-TD 68
Cdd:PRK07229 1 MGLTLTEKILYAHLV----EGELEpgeeiaIRIDQTLTQDATGTMAylqFEAMGLD-----RVKTELSVQyvDHNLLqAD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 69 DRSSEIADpvsrlqveTLEKNCKEFGITmFAmnDPRQGIVHVIGPEQGATlPGMTVVCGDSHTATHGAFGALAFGIGTSE 148
Cdd:PRK07229 72 FENADDHR--------FLQSVAAKYGIY-FS--KPGNGICHQVHLERFAF-PGKTLLGSDSHTPTAGGLGMLAIGAGGLD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 149 VEHVLATQCLIQKKSKTMLIEVNGELPSGLTAKDIVLAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGA 228
Cdd:PRK07229 140 VALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 229 RAGLIAVDQKTIDYVE--GRpfapqGADWElavaswrQLKSDPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIADrvps 306
Cdd:PRK07229 220 TTSIFPSDERTREFLKaqGR-----EDDWV-------ELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSE---- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 307 paeeadpVKqegmqaalkymglepGTPINQikpdiVFIGSCTNGRIEDLRAVAAVAKGRKVADNIKqALIVPGSGLVKQQ 386
Cdd:PRK07229 284 -------VA---------------GIKVDQ-----VLIGSCTNSSYEDLMRAASILKGKKVHPKVS-LVINPGSRQVLEM 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 387 AEKEGLDKIFIDAGFEWREPGCSMCLAMNNDrlkPGERCAS--TSNRNFEGRQG-QGGRTHLVSPAMAAAAAVTGHFVDV 463
Cdd:PRK07229 336 LARDGALADLIAAGARILENACGPCIGMGQA---PATGNVSlrTFNRNFPGRSGtKDAQVYLASPETAAASALTGVITDP 412
|
....
gi 1120034798 464 RSLE 467
Cdd:PRK07229 413 RTLA 416
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
103-460 |
5.86e-53 |
|
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: 182.65 E-value: 5.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 103 PRQGIVHVIGPEQGAtLPGMTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCLIQKKSKTMLIEVNGELPSGLTAKD 182
Cdd:cd01585 66 PGNGICHQVHLERFA-VPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKD 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 183 IVLAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTIDYVE--GRPfapqgadwelavA 260
Cdd:cd01585 145 VILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAaqGRE------------D 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 261 SWRQLKSDPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIADrvpspaeeadpvkqegmqaalkymglepgtpINQIKPD 340
Cdd:cd01585 213 DWVELAADADAEYDEEIEIDLSELEPLIARPHSPDNVVPVRE-------------------------------VAGIKVD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 341 IVFIGSCTNGRIEDLRAVAAVAKGRKVADNIKQAlIVPGSGLVKQQAEKEGLDKIFIDAGFEWREPGCSMCLAMNNdrlK 420
Cdd:cd01585 262 QVAIGSCTNSSYEDLMTVAAILKGRRVHPHVSMV-VAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQ---A 337
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1120034798 421 PGERCAS--TSNRNFEGRQG-QGGRTHLVSPAMAAAAAVTGHF 460
Cdd:cd01585 338 PPTGGVSvrTFNRNFEGRSGtKDDLVYLASPEVAAAAALTGVI 380
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
86-448 |
2.43e-37 |
|
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: 141.42 E-value: 2.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 86 LEKNCKEFGITMFAmndPRQGIVHVIGPEQGAtLPGMTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCLIQKKSKT 165
Cdd:cd01584 60 LASAGAKYGIGFWK---PGSGIIHQIVLENYA-FPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 166 MLIEVNGELPSGLTAKDIVLAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTIDYVE- 244
Cdd:cd01584 136 IGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKa 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 245 -GRPFAPQGADwelaVASWRQLKSDPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIadrvpspAEEADPVKQEGMQAAL 323
Cdd:cd01584 216 tGRAEIADLAD----EFKDDLLVADEGAEYDQLIEINLSELEPHINGPFTPDLATPV-------SKFKEVAEKNGWPLDL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 324 KyMGLepgtpinqikpdivfIGSCTNGRIEDLRAVAAVAKgRKVADNIK---QALIVPGSGLVKQQAEKEGLDKIFIDAG 400
Cdd:cd01584 285 R-VGL---------------IGSCTNSSYEDMGRAASIAK-QALAHGLKcksIFTITPGSEQIRATIERDGLLQTFRDAG 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1120034798 401 FEWREPGCSMCLAMNNDR-LKPGERCA--STSNRNFEGRQGQGGRTH--LVSP 448
Cdd:cd01584 348 GIVLANACGPCIGQWDRKdIKKGEKNTivTSYNRNFTGRNDANPATHafVASP 400
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
105-458 |
2.01e-32 |
|
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: 126.57 E-value: 2.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 105 QGIVHVIGPEQGATLPGMTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCLIQKKSKTMLIEVNGELPSGLTAKDIV 184
Cdd:cd01582 67 RGIGHQIMIEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 185 LAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTIdyvegrpfapqgadwelavaswrq 264
Cdd:cd01582 147 VALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAKHL------------------------ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 265 lksdpdaefdkivRIDARDLNPQVtwgTSPEMVvsiadRVPSPAEEADpvKQEgmqaalkymglepgtpinqIKPDIVFI 344
Cdd:cd01582 203 -------------ILDLSTLSPYV---SGPNSV-----KVSTPLKELE--AQN-------------------IKINKAYL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 345 GSCTNGRIEDLRAVAAVAKGRKvaDNIKQALIVPG--------SGLVKQQAEKEGLDKIFIDAGFEWREPGCSMCLAMNN 416
Cdd:cd01582 241 VSCTNSRASDIAAAADVVKGKK--EKNGKIPVAPGvefyvaaaSSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQ 318
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1120034798 417 DRLKPGERCASTSNRNFEGRQG-QGGRTHLVSPAMAAAAAVTG 458
Cdd:cd01582 319 GLLEPGEVGISATNRNFKGRMGsTEALAYLASPAVVAASAISG 361
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
103-436 |
3.74e-31 |
|
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: 127.14 E-value: 3.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 103 PRQGIVH----------VIGPEQGATL---PGmTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCLiqkkskTMLI- 168
Cdd:COG1048 173 PGTGIVHqvnleylafvVWTREEDGETvayPD-TLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPV------SMLIp 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 169 EV-----NGELPSGLTAKDIVLAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTIDYV 243
Cdd:COG1048 246 EVvgvklTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 244 E--GRPfapqgadwELAVA----------SWRQlKSDPDAEFDKIVRIDARDLNPqvtwgtspemvvSIA------DRVP 305
Cdd:COG1048 326 RltGRS--------EEQIElveayakaqgLWRD-PDAPEPYYSDVLELDLSTVEP------------SLAgpkrpqDRIP 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 306 SPAeeadpVKQEGMQAALKYMGLEPGTPINQIKPDIVF-----------IGSCTNGRIED-LRA---VA--AVAKGRKVA 368
Cdd:COG1048 385 LSD-----LKEAFRAALAAPVGEELDKPVRVEVDGEEFelghgavviaaITSCTNTSNPSvMIAaglLAkkAVEKGLKVK 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 369 DNIKQALiVPGSGLVKQQAEKEGL----DKI-FIDAGFewrepGCSMCL------------AMNNDRLKPgerCASTS-N 430
Cdd:COG1048 460 PWVKTSL-APGSKVVTDYLERAGLlpylEALgFNVVGY-----GCTTCIgnsgplppeiseAIEENDLVV---AAVLSgN 530
|
....*.
gi 1120034798 431 RNFEGR 436
Cdd:COG1048 531 RNFEGR 536
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
48-436 |
1.24e-29 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 122.81 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 48 GRKPRRIdaNLAVP-----DHNVPTDDRSSEiaDPVSRLQVETLEKNCKEFGITMFAMND--------PRQGIVHVIGPE 114
Cdd:PTZ00092 118 GGDPAKI--NPLVPvdlviDHSVQVDFSRSP--DALELNQEIEFERNLERFEFLKWGSKAfknllivpPGSGIVHQVNLE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 115 --------QGATLPGMTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCLIQKKSKTMLIEVNGELPSGLTAKDIVLA 186
Cdd:PTZ00092 194 ylarvvfnKDGLLYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTGKLSEHVTATDLVLT 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 187 IIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTIDYVE--GRPfapqgadwELAVASWRQ 264
Cdd:PTZ00092 274 VTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKqtGRS--------EEKVELIEK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 265 -LK-------SDPDAEFDKIVRIDARDLNPQVTWGTSPEmvvsiaDRVPSPAEEADpvKQEGMQAALKYMGLepGTPINQ 336
Cdd:PTZ00092 346 yLKanglfrtYAEQIEYSDVLELDLSTVVPSVAGPKRPH------DRVPLSDLKKD--FTACLSAPVGFKGF--GIPEEK 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 337 IKPDIVF------------------IGSCTN----------GriedLRAVAAVAKGRKVADNIKQALiVPGSGLVKQQAE 388
Cdd:PTZ00092 416 HEKKVKFtykgkeytlthgsvviaaITSCTNtsnpsvmlaaG----LLAKKAVEKGLKVPPYIKTSL-SPGSKVVTKYLE 490
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1120034798 389 KEGLDKI-----FIDAGFewrepGCSMCLAMNNDRLKPGERCAS----------TSNRNFEGR 436
Cdd:PTZ00092 491 ASGLLKYleklgFYTAGY-----GCMTCIGNSGDLDPEVSEAITnndlvaaavlSGNRNFEGR 548
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
103-436 |
8.72e-27 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 114.26 E-value: 8.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 103 PRQGIVHVIGPEQGATL-------------PGmTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQcliqkkSKTMLI- 168
Cdd:PRK12881 175 PGTGIMHQVNLEYLARVvhtkeddgdtvayPD-TLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQ------PVYMLIp 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 169 -----EVNGELPSGLTAKDIVLAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTIDYV 243
Cdd:PRK12881 248 dvvgvELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 244 E--GRPfapqGADWELAVASWRQ--LKSDPDAE--FDKIVRIDARDLNPQVTWGTSPEmvvsiaDRVPSP--AEEADPVK 315
Cdd:PRK12881 328 RltGRT----EAQIALVEAYAKAqgLWGDPKAEprYTRTLELDLSTVAPSLAGPKRPQ------DRIALGnvKSAFSDLF 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 316 QEGMQAALKymgLEPGTPINQIK-PD----IVFIGSCTN----------GriedLRAVAAVAKGRKVADNIKQALiVPGS 380
Cdd:PRK12881 398 SKPVAENGF---AKKAQTSNGVDlPDgavaIAAITSCTNtsnpsvliaaG----LLAKKAVERGLTVKPWVKTSL-APGS 469
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1120034798 381 GLVKQQAEKEGLDKIFIDAGFEWREPGCSMCLAMNNDRLKPGER--------CAS--TSNRNFEGR 436
Cdd:PRK12881 470 KVVTEYLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQaitkndlvAAAvlSGNRNFEGR 535
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
60-436 |
5.29e-23 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 102.58 E-value: 5.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 60 VPDHNVPTDDRSSEIADPVSrLQVEtLEKNCKEFGITMFAMN--------DPRQGIVHVIGPE---------QGATLPGm 122
Cdd:PLN00070 165 VIDHSVQVDVARSENAVQAN-MELE-FQRNKERFAFLKWGSTafqnmlvvPPGSGIVHQVNLEylgrvvfntDGILYPD- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 123 TVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCLIQKKSKTMLIEVNGELPSGLTAKDIVLAIIGRIGTAGGTGYCVE 202
Cdd:PLN00070 242 SVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 203 FGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTIDYVE--GRpfapQGADWELAVASWRQLK-----SDPDAE--F 273
Cdd:PLN00070 322 FYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKltGR----SDETVAMIEAYLRANKmfvdyNEPQQErvY 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 274 DKIVRIDARDLNPQVTWGTSPEmvvsiaDRVPSPAEEAD----------------PVKQEGMQAALKYmglePGTPINQI 337
Cdd:PLN00070 398 SSYLELDLEDVEPCISGPKRPH------DRVPLKEMKADwhscldnkvgfkgfavPKEAQSKVAKFSF----HGQPAELR 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 338 KPDIVF--IGSCTNGRIEDLRAVAA-VAK-----GRKVADNIKQALiVPGSGLVKQQAEKEGLDKIFIDAGFEWREPGCS 409
Cdd:PLN00070 468 HGSVVIaaITSCTNTSNPSVMLGAGlVAKkacelGLEVKPWIKTSL-APGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCT 546
|
410 420 430
....*....|....*....|....*....|....*...
gi 1120034798 410 MCLAmNNDRLKPGERCASTS-----------NRNFEGR 436
Cdd:PLN00070 547 TCIG-NSGELDESVASAITEndivaaavlsgNRNFEGR 583
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
123-436 |
5.48e-22 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 99.43 E-value: 5.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 123 TVVCGDSHTaTH-GAFGALAFGIGTSEVEHVLATQCLiqkkskTMLI------EVNGELPSGLTAKDIVLAIIGRIGTAG 195
Cdd:PRK09277 207 TLVGTDSHT-TMiNGLGVLGWGVGGIEAEAAMLGQPS------SMLIpevvgvKLTGKLPEGVTATDLVLTVTEMLRKKG 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 196 GTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTIDYVE--GRPfapqgaDWELAVAS--------WRQl 265
Cdd:PRK09277 280 VVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRltGRD------EEQVALVEayakaqglWRD- 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 266 kSDPDAEFDKIVRIDARDLNPqvtwgtspemvvSIA------DRVpsPAEEADPVKQEGMQAALKYMGLEPGTPINQIK- 338
Cdd:PRK09277 353 -PLEEPVYTDVLELDLSTVEP------------SLAgpkrpqDRI--PLSDVKEAFAKSAELGVQGFGLDEAEEGEDYEl 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 339 PD----IVFIGSCTN----------GriedLRAVAAVAKGRKVADNIKQALiVPGSGLVKQQAEKEG----LDKI-FIDA 399
Cdd:PRK09277 418 PDgavvIAAITSCTNtsnpsvmiaaG----LLAKKAVEKGLKVKPWVKTSL-APGSKVVTDYLEKAGllpyLEALgFNLV 492
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1120034798 400 GFewrepGCSMCLAMNNDRLKPGERC------ASTS----NRNFEGR 436
Cdd:PRK09277 493 GY-----GCTTCIGNSGPLPPEIEKAindndlVVTAvlsgNRNFEGR 534
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
48-436 |
1.58e-20 |
|
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydrolyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes.
Pssm-ID: 153136 Cd Length: 404 Bit Score: 93.14 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 48 GRKPRRIdaNLAVP-----DHNVPTDDRSSEIAdpVSRLQVETLEKNCKEFGITMFAMN--------DPRQGIVHVIGPE 114
Cdd:cd01586 27 GGDPEKI--NPLIPvdlviDHSVQVDFYGTADA--LAKNMKLEFERNRERYEFLKWGQKafknlrvvPPGTGIIHQVNLE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 115 -------------QGATLPGmTVVCGDSHTATHGAFGALAFGIGTSEVEHVLATQCLiqkkskTMLI------EVNGELP 175
Cdd:cd01586 103 ylarvvftseedgDGVAYPD-SVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPI------SMLLpevvgvKLTGKLR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 176 SGLTAKDIVLAIIGRIGTAGGTGYCVEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTidyvegrpfapqgadw 255
Cdd:cd01586 176 PGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVDTQV---------------- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 256 elavaswrqlksdpdaefdkiVRIDARDLNPQVTWGTSPEmvvsiaDRVPspaeeadpvkqegmqaalkymglepgtpin 335
Cdd:cd01586 240 ---------------------VELDLSTVEPSVSGPKRPQ------DRVP------------------------------ 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 336 qIKPDIVF--IGSCTN----------GriedLRAVAAVAKGRKVADNIKQALiVPGSGLVKQQAEKEGLDKIFIDAGFEW 403
Cdd:cd01586 263 -LHGSVVIaaITSCTNtsnpsvmlaaG----LLAKKAVELGLKVKPYVKTSL-APGSRVVTKYLEASGLLPYLEKLGFHV 336
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1120034798 404 REPGCSMCLAmNNDRLKP---------GERCAS--TSNRNFEGR 436
Cdd:cd01586 337 VGYGCTTCIG-NSGPLPEeveeaikenDLVVAAvlSGNRNFEGR 379
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
118-447 |
1.02e-18 |
|
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle; Aconitase B catalytic domain. Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle. Aconitase has an active (4FE-4S) and an inactive (3FE-4S) form. The active cluster is part of the catalytic site that interconverts citrate, cis-aconitase and isocitrate. The domain architecture of aconitase B is different from other aconitases in that the catalytic domain is normally found at C-terminus for other aconitases, but it is at N-terminus for B family. It also has a HEAT domain before domain 4 which plays a role in protein-protein interaction. This alignment is the core domain including domains 1,2 and 3.
Pssm-ID: 153131 Cd Length: 436 Bit Score: 88.32 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 118 TLPGMTVVCGDSHTAthgaFG-ALAFGIGTSEVEHVLATQCLIQKKSKTMLIEVNGELPSGLTAKDIVLAI--------I 188
Cdd:cd01581 104 LLPDTVGTGGDSHTR----FPiGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVNAIpyyaiqqgL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 189 GRIGTAGG----TGYCVEFGGdaIRALSMEGRMTVCNMAIEAGARAGLIAVDQKT-IDYVE------------GRPFAPQ 251
Cdd:cd01581 180 LTVEKKGKknvfNGRILEIEG--LPDLKVEQAFELTDASAERSAAACTVRLDKEPvIEYLEsnvvlmkimianGYDDART 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 252 GADWELAVASWRQ----LKSDPDAEFDKIVRIDARDLN-PQVTWGTSPEMVVSIADRVpspaeeadpvkqegmqaalkym 326
Cdd:cd01581 258 LLRRIIAMEEWLAnpplLEPDADAEYAAVIEIDLDDIKePILACPNDPDDVKLLSEVA---------------------- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 327 glepGTPInqikpDIVFIGSC-TNgrIEDLRAVAAVAKGRKVADniKQALIVPGSGLVKQQAEKEGLDKIFIDAGFEWRE 405
Cdd:cd01581 316 ----GKKI-----DEVFIGSCmTN--IGHFRAAAKILRGKEFKP--TRLWVAPPTRMDWAILQEEGYYSIFGDAGARTEM 382
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1120034798 406 PGCSMCLAmNNDRLKPGERCASTSNRNFEGRQGQGGRTHLVS 447
Cdd:cd01581 383 PGCSLCMG-NQARVADGATVFSTSTRNFDNRVGKGAEVYLGS 423
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
331-447 |
9.45e-13 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 70.59 E-value: 9.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 331 GTPInqikpDIVFIGSC-TNgrIEDLRAVAAVAKGRKVadNIKQAL-IVPGSGLVKQQAEKEGLDKIFIDAGFEWREPGC 408
Cdd:PRK09238 688 GTKI-----DEVFIGSCmTN--IGHFRAAGKLLEGKKG--QLPTRLwVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGC 758
|
90 100 110
....*....|....*....|....*....|....*....
gi 1120034798 409 SMCLAmNNDRLKPGERCASTSNRNFEGRQGQGGRTHLVS 447
Cdd:PRK09238 759 SLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYLGS 796
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
119-447 |
1.01e-11 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 67.26 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 119 LPGMTVVCGDSHTAthgaFG-ALAFGIGTSEVEHVLATQCLIQKKSKTMLIEVNGELPSGLTAKDIVLAI------IGRI 191
Cdd:PLN00094 551 LPDTVGTGGDSHTR----FPiGISFPAGSGLVAFGAATGVIPLDMPESVLVRFTGTMQPGITLRDLVHAIpytaiqDGLL 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 192 gTAGGTGYCVEFGGdaiRALSMEGRMTV-CNMAIE---AGAR---AG-LIAVDQKTI-----------------DYVEGR 246
Cdd:PLN00094 627 -TVEKKGKKNVFSG---RILEIEGLPHLkCEQAFElsdASAErsaAGcTIKLDKEPIieylnsnvvmlkwmiaeGYGDRR 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 247 PFAPQGADWELAVASWRQLKSDPDAEFDKIVRIDARDLnpqvtwgtspemvvsiadRVPSPAEEADPvkqegMQAALKym 326
Cdd:PLN00094 703 TLERRIARMQQWLADPELLEADPDAEYAAVIEIDMDEI------------------KEPILCAPNDP-----DDARLL-- 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 327 glepgTPINQIKPDIVFIGSC-TNgrIEDLRAVAAVAKGRKvADNIKQALIVPGSGLVKQQAEKEGLDKIFIDAGFEWRE 405
Cdd:PLN00094 758 -----SEVTGDKIDEVFIGSCmTN--IGHFRAAGKLLNDNL-SQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEM 829
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1120034798 406 PGCSMCLAmNNDRLKPGERCASTSNRNFEGRQGQGGRTHLVS 447
Cdd:PLN00094 830 PGCSLCMG-NQARVAEKSTVVSTSTRNFPNRLGKGANVYLAS 870
|
|
| AcnB |
COG1049 |
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ... |
331-447 |
2.11e-11 |
|
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: 66.41 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 331 GTPInqikpDIVFIGSC-TNgrIEDLRAVAAVAKGRKvadNIKQAL-IVPGSGLVKQQAEKEGLDKIFIDAGFEWREPGC 408
Cdd:COG1049 688 GTKI-----DEVFIGSCmTN--IGHFRAAGKLLEGKG---NLPTRLwIAPPTKMDEAQLTEEGYYSIFGAAGARTEMPGC 757
|
90 100 110
....*....|....*....|....*....|....*....
gi 1120034798 409 SMCLAmNNDRLKPGERCASTSNRNFEGRQGQGGRTHLVS 447
Cdd:COG1049 758 SLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYLGS 795
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
103-438 |
4.07e-10 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 61.95 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 103 PRQGIVHVIGPEQGATLPGMtVVCGDSHTaTHGAFGALAFGIGTSEvehvLATQCLIQ----KKSKTMLIEVNGELPSGL 178
Cdd:PRK11413 125 PHIAVIHQYMREMMAGGGKM-ILGSDSHT-RYGALGTMAVGEGGGE----LVKQLLNDtydiDYPGVVAVYLTGKPAPGV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 179 TAKDIVLAIIGRIGtagGTGYC----VEFGGDAIRALSMEGRMTVCNMAIEAGARAGLIAVDQKTIDYVE--GRPFApqg 252
Cdd:PRK11413 199 GPQDVALAIIGAVF---KNGYVknkvMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLAlhGRGQD--- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 253 adwelavasWRQLKSDPDAEFDKIVRIDARDLNPQVTWGTSPEMVVSIADRVPSPAEEADPVKQEGMQAALKYMGLEPGT 332
Cdd:PRK11413 273 ---------YCELNPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDELNQNLTDILREVEIESERVAHGKAKLSLLD 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120034798 333 PI--NQIKPDIVFIGSCTNGRIEDLRAVAAVAKGRKVADNIKQALIVPGSGLVKQQAEKEGLDKIFIDAGFEWREPGCSM 410
Cdd:PRK11413 344 KIenGRLKVQQGIIAGCSGGNYENVIAAANALRGQSCGNDTFSLSVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGP 423
|
330 340 350
....*....|....*....|....*....|..
gi 1120034798 411 CLAM----NNDRLKpgercASTSNRNFEGRQG 438
Cdd:PRK11413 424 CFGAgdtpANNGLS-----IRHTTRNFPNREG 450
|
|
| |
