|
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: 1024.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 1 MAKTLYEKLFDAHVVYEAPNETPLLYIDRHLVHEVTSPQAFDGLRAHKRPVRQPGKTFATMDHNVSTQTKDINASGEMAR 80
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLPIADPVSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 81 IQMQELIKNCNEFGVELYDLNHPYQGIVHVMGPEQGITLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQ 160
Cdd:PRK05478 81 IQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 161 GRAKTMKIEVKGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDETTF 240
Cdd:PRK05478 161 KKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 241 NYVKGRLHAPKGQDFDDAVAYWKTLKTDDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDSIPDPASFADPVERASAE 320
Cdd:PRK05478 241 EYLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVKRASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 321 KALAYMGLKPGVPLTDVNIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGF 400
Cdd:PRK05478 321 RALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654547792 401 EWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAVTGHFADIRSLK 466
Cdd:PRK05478 401 EWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
1-463 |
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: 931.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 1 MAKTLYEKLFDAHVVYEAPNETPLLYIDRHLVHEVTSPQAFDGLRAHKRPVRQPGKTFATMDHNVSTQTKDINASGEMAR 80
Cdd:TIGR00170 1 MPRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFNIKDEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 81 IQMQELIKNCNEFGVELYDLNHPYQGIVHVMGPEQGITLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQ 160
Cdd:TIGR00170 81 IQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 161 GRAKTMKIEVKGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDETTF 240
Cdd:TIGR00170 161 ARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 241 NYVKGRLHAPKGQDFDDAVAYWKTLKTDDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDSIPDPASFADPVERASAE 320
Cdd:TIGR00170 241 EYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 321 KALAYMGLKPGVPLTDVNIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGF 400
Cdd:TIGR00170 321 RALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654547792 401 EWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAVTGHFADIR 463
Cdd:TIGR00170 401 EWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIR 463
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-465 |
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: 715.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 1 MAKTLYEKLFDAHVVYEA-PNETPLLYIDRHLVHEVTSPQAFDGLR-AHKRPVRQPGKTFATMDHNVSTQTkdinasgEM 78
Cdd:COG0065 1 MGMTLAEKILARHAGREVePGEIVLLYIDLHLVHDVTSPQAFEGLReAGGRKVWDPDRIVAVFDHNVPTKD-------PK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 79 ARIQMQELIKNCNEFGVELYDLNHPyqGIVHVMGPEQGITLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTL 158
Cdd:COG0065 74 SAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 159 KQGRAKTMKIEVKGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDET 238
Cdd:COG0065 152 WFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 239 TFNYVKGRLHAPkgqdfddavayWKTLKTDDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDsipdpasfadpveras 318
Cdd:COG0065 232 TFEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE---------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 319 aekalaymglkpgvpLTDVNIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEA 398
Cdd:COG0065 285 ---------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEA 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654547792 399 GFEWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGR-GGRTHLVSPAMAAAAAVTGHFADIRSL 465
Cdd:COG0065 350 GAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGSpGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-447 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 697.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 7 EKLFDAHVVYEApnETPLLYI-DRHLVHEVTSPQAFDGLRAHKRPVRQPGKTFATMDHNVST--------QTKDINASGE 77
Cdd:pfam00330 1 EKIWDAHLVEEL--DGSLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTdlvidhapDALDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 78 MARI--QMQELIKNCNEFGVELYDlnhPYQGIVHVMGPEQGITLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLAT 155
Cdd:pfam00330 79 ISRNkeQYDFLEWNAKKFGIRFVP---PGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 156 QTLKQGRAKTMKIEVKGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAP 235
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 236 DETTFNYVK--GRLHAPKGQDFDDAVAyWKTLKTDDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDSIPDPasFADP 313
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDP--FADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 314 VERASAEKALAYMGLKPGVPLTDVNIDKVFIGSCTNSRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAEA 388
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 654547792 389 EGLDKIFIEAGFEWRLPGCSMCLAmNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVSP 447
Cdd:pfam00330 393 EGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASP 450
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
29-459 |
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: 606.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 29 RHLVHEVTSPQAFDGLRAHKRP-VRQPGKTFATMDHNVSTqtkdinaSGEMARIQMQELIKNCNEFGVELYDLNhpYQGI 107
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREkVWDPEKIVAVFDHNVPT-------PDIKAAEQVKTLRKFAKEFGINFFDVG--RQGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 108 VHVMGPEQGITLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVKGKAAPGITAKDIVLAI 187
Cdd:cd01583 72 CHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 188 IGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVKGRLHapkgqdfddavAYWKTLKT 267
Cdd:cd01583 152 IGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGK-----------AYWKELKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 268 DDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDSIPdpasfadpverasaekalaymglkpgvpltdVNIDKVFIGSC 347
Cdd:cd01583 221 DEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQVFIGSC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 348 TNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNDRLNPGERCAST 427
Cdd:cd01583 270 TNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVST 349
|
410 420 430
....*....|....*....|....*....|...
gi 654547792 428 SNRNFEGRQG-RGGRTHLVSPAMAAAAAVTGHF 459
Cdd:cd01583 350 SNRNFKGRMGsPGARIYLASPATAAASAITGEI 382
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
4-458 |
8.21e-88 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 274.71 E-value: 8.21e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 4 TLYEKLFDAHVVYEA-PNETPLLYIDRHLVHEVTSPQAFDGLRAHKRPVRQPGKTFATMDHNVSTQTkdiNASGEMARIq 82
Cdd:NF040615 2 TLAEKILSKKLGKEVyAGDTVEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPANT---VKAANMQKI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 83 MQELIKncnEFGVELYDLNHpyQGIVHVMGPEQGITLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGR 162
Cdd:NF040615 78 TREFVK---EQGIKNFYLGG--EGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 163 AKTMKIEVKGKAaPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNY 242
Cdd:NF040615 153 PKTIRVNIVGKN-ENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 243 VKgrlhapKGQDFDDAVAYWKTLK---TDDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDsipdpasfadpVErasa 319
Cdd:NF040615 232 LR------KEGVSEEEIAELKKNRitvNEKEENYYKEIEIDITDMEEQVACPHHPDNVKPVSE-----------VE---- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 320 ekalaymglkpGVPltdvnIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAG 399
Cdd:NF040615 291 -----------GTE-----IDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAG 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 400 FEWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGR-GGRTHLVSPAMAAAAAVTGH 458
Cdd:NF040615 355 AMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGNiNSYIYLSSPKIAAKSAVKGY 414
|
|
| |
|
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: 1024.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 1 MAKTLYEKLFDAHVVYEAPNETPLLYIDRHLVHEVTSPQAFDGLRAHKRPVRQPGKTFATMDHNVSTQTKDINASGEMAR 80
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLPIADPVSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 81 IQMQELIKNCNEFGVELYDLNHPYQGIVHVMGPEQGITLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQ 160
Cdd:PRK05478 81 IQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 161 GRAKTMKIEVKGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDETTF 240
Cdd:PRK05478 161 KKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 241 NYVKGRLHAPKGQDFDDAVAYWKTLKTDDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDSIPDPASFADPVERASAE 320
Cdd:PRK05478 241 EYLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVKRASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 321 KALAYMGLKPGVPLTDVNIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGF 400
Cdd:PRK05478 321 RALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654547792 401 EWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAVTGHFADIRSLK 466
Cdd:PRK05478 401 EWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
1-463 |
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: 931.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 1 MAKTLYEKLFDAHVVYEAPNETPLLYIDRHLVHEVTSPQAFDGLRAHKRPVRQPGKTFATMDHNVSTQTKDINASGEMAR 80
Cdd:TIGR00170 1 MPRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFNIKDEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 81 IQMQELIKNCNEFGVELYDLNHPYQGIVHVMGPEQGITLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQ 160
Cdd:TIGR00170 81 IQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 161 GRAKTMKIEVKGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDETTF 240
Cdd:TIGR00170 161 ARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 241 NYVKGRLHAPKGQDFDDAVAYWKTLKTDDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDSIPDPASFADPVERASAE 320
Cdd:TIGR00170 241 EYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 321 KALAYMGLKPGVPLTDVNIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGF 400
Cdd:TIGR00170 321 RALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654547792 401 EWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAVTGHFADIR 463
Cdd:TIGR00170 401 EWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIR 463
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
1-465 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 817.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 1 MAKTLYEKLFDAHVVYEAPNETPLLYIDRHLVHEVTSPQAFDGLRAHKRPVRQPGKTFATMDHNVSTQTK-DINASGEMA 79
Cdd:PRK12466 2 MPRTLYDKLWDSHTVARLDDGHVLLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPTRPGrDRGITDPGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 80 RIQMQELIKNCNEFGVELYDLNHPYQGIVHVMGPEQGITLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLK 159
Cdd:PRK12466 82 ALQVDYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQTLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 160 QGRAKTMKIEVKGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDETT 239
Cdd:PRK12466 162 YRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 240 FNYVKGRLHAPKGQDFDDAVAYWKTLKTDDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDSIPDPASFADPVERASA 319
Cdd:PRK12466 242 FDYLRGRPRAPKGALWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAAEADPARRAAM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 320 EKALAYMGLKPGVPLTDVNIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAG 399
Cdd:PRK12466 322 ERALDYMGLTPGTPLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAG 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654547792 400 FEWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAVTGHFADIRSL 465
Cdd:PRK12466 402 FEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHITDVRSL 467
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-465 |
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: 715.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 1 MAKTLYEKLFDAHVVYEA-PNETPLLYIDRHLVHEVTSPQAFDGLR-AHKRPVRQPGKTFATMDHNVSTQTkdinasgEM 78
Cdd:COG0065 1 MGMTLAEKILARHAGREVePGEIVLLYIDLHLVHDVTSPQAFEGLReAGGRKVWDPDRIVAVFDHNVPTKD-------PK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 79 ARIQMQELIKNCNEFGVELYDLNHPyqGIVHVMGPEQGITLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTL 158
Cdd:COG0065 74 SAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 159 KQGRAKTMKIEVKGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDET 238
Cdd:COG0065 152 WFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 239 TFNYVKGRLHAPkgqdfddavayWKTLKTDDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDsipdpasfadpveras 318
Cdd:COG0065 232 TFEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE---------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 319 aekalaymglkpgvpLTDVNIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEA 398
Cdd:COG0065 285 ---------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEA 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654547792 399 GFEWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGR-GGRTHLVSPAMAAAAAVTGHFADIRSL 465
Cdd:COG0065 350 GAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGSpGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-447 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 697.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 7 EKLFDAHVVYEApnETPLLYI-DRHLVHEVTSPQAFDGLRAHKRPVRQPGKTFATMDHNVST--------QTKDINASGE 77
Cdd:pfam00330 1 EKIWDAHLVEEL--DGSLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTdlvidhapDALDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 78 MARI--QMQELIKNCNEFGVELYDlnhPYQGIVHVMGPEQGITLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLAT 155
Cdd:pfam00330 79 ISRNkeQYDFLEWNAKKFGIRFVP---PGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 156 QTLKQGRAKTMKIEVKGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAP 235
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 236 DETTFNYVK--GRLHAPKGQDFDDAVAyWKTLKTDDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDSIPDPasFADP 313
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDP--FADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 314 VERASAEKALAYMGLKPGVPLTDVNIDKVFIGSCTNSRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAEA 388
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 654547792 389 EGLDKIFIEAGFEWRLPGCSMCLAmNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVSP 447
Cdd:pfam00330 393 EGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASP 450
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
29-459 |
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: 606.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 29 RHLVHEVTSPQAFDGLRAHKRP-VRQPGKTFATMDHNVSTqtkdinaSGEMARIQMQELIKNCNEFGVELYDLNhpYQGI 107
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREkVWDPEKIVAVFDHNVPT-------PDIKAAEQVKTLRKFAKEFGINFFDVG--RQGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 108 VHVMGPEQGITLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVKGKAAPGITAKDIVLAI 187
Cdd:cd01583 72 CHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 188 IGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVKGRLHapkgqdfddavAYWKTLKT 267
Cdd:cd01583 152 IGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGK-----------AYWKELKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 268 DDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDSIPdpasfadpverasaekalaymglkpgvpltdVNIDKVFIGSC 347
Cdd:cd01583 221 DEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQVFIGSC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 348 TNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNDRLNPGERCAST 427
Cdd:cd01583 270 TNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVST 349
|
410 420 430
....*....|....*....|....*....|...
gi 654547792 428 SNRNFEGRQG-RGGRTHLVSPAMAAAAAVTGHF 459
Cdd:cd01583 350 SNRNFKGRMGsPGARIYLASPATAAASAITGEI 382
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
1-465 |
1.09e-133 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 391.85 E-value: 1.09e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 1 MAKTLYEKLFDAHVVYEA-PNETPLLYIDRHLVHEVTSPQAFDGLRAH-KRPVRQPGKTFATMDHNVSTqtKDINAsgem 78
Cdd:PRK00402 1 MGMTLAEKILARHSGRDVsPGDIVEAKVDLVMAHDITGPLAIKEFEKIgGDKVFDPSKIVIVFDHFVPA--KDIKS---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 79 ARIQmqeliKNCNEFGVElYDLNHPY---QGIVHVMGPEQGITLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLAT 155
Cdd:PRK00402 75 AEQQ-----KILREFAKE-QGIPNFFdvgEGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 156 qtlkqGRA-----KTMKIEVKGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKA 230
Cdd:PRK00402 149 -----GKTwfkvpETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 231 GLVAPDETTFNYVKGRLHAPkgqdfddavayWKTLKTDDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDsipdpasf 310
Cdd:PRK00402 224 GIFAPDEKTLEYLKERAGRD-----------YKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSE-------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 311 adpverasaekalaymglkpgvpLTDVNIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEG 390
Cdd:PRK00402 285 -----------------------VEGTKVDQVFIGSCTNGRLEDLRIAAEILKGRKVAPGVRLIVIPASQKIYLQALKEG 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654547792 391 LDKIFIEAGFEWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQG-RGGRTHLVSPAMAAAAAVTGHFADIRSL 465
Cdd:PRK00402 342 LIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGsPESEVYLASPAVAAASAVTGKITDPREV 417
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
4-463 |
2.58e-109 |
|
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: 329.41 E-value: 2.58e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 4 TLYEKLFDAHVVYEA-PNETPLLYIDRHLVHEVTSPQAFDGL-RAHKRPVRQPGKTFATMDHNVSTqtKDINASgEMARI 81
Cdd:TIGR01343 1 TIAEKILSKKSGKEVyAGDLIEAEIDLAMVHDITAPLAIKTLeEYGIDKVWNPEKIVIVFDHQVPA--DTIKAA-EMQKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 82 qMQELIKncnEFGVElyDLNHPYQGIVHVMGPEQGITLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQG 161
Cdd:TIGR01343 78 -AREFVK---KQGIK--YFYDVGEGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 162 RAKTMKIEVKGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDETTFN 241
Cdd:TIGR01343 152 VPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 242 YVKGRLHAPkgqdfddavayWKTLKTDDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDSipdpasfadpverasaek 321
Cdd:TIGR01343 232 YLKERRKEP-----------FRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSEV------------------ 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 322 alaymglkpgvplTDVNIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFE 401
Cdd:TIGR01343 283 -------------EGTEIDQVFIGSCTNGRLEDLRVAAKILKGRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAV 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654547792 402 WRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQG-RGGRTHLVSPAMAAAAAVTGHFADIR 463
Cdd:TIGR01343 350 VSTPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMGhPNAEIYLASPATAAASAVKGYIADPR 412
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
3-461 |
7.81e-97 |
|
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: 297.44 E-value: 7.81e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 3 KTLYEKLFDAHVVYE-APNETPLLYIDRHLVHEVTSPQAFDGLR-AHKRPVRQPGKTFATMDHNVSTQTKdinasgEMAR 80
Cdd:TIGR02086 1 MTLAEKILSEKVGRPvCAGEIVEVEVDLAMTHDGTGPLAIKALReLGVARVWDPEKIVIAFDHNVPPPTV------EAAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 81 IQmQELIKNCNEFGVELYDLNhpyQGIVHVMGPEQGITLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQ 160
Cdd:TIGR02086 75 MQ-KEIREFAKRHGIKNFDVG---EGICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTWI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 161 GRAKTMKIEVKGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDETTF 240
Cdd:TIGR02086 151 KVPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEETY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 241 NYVKGRlhapKGQDFddavaywKTLKTDDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDsipdpasfadpVErasae 320
Cdd:TIGR02086 231 EYLKKR----RGLEF-------RILVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVSD-----------VE----- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 321 kalaymGLKpgvpltdvnIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGF 400
Cdd:TIGR02086 284 ------GTE---------IDQVFIGSCTNGRLEDLRIAAEILKGRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAGA 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654547792 401 EWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQG-RGGRTHLVSPAMAAAAAVTGHFAD 461
Cdd:TIGR02086 349 MICPPGCGPCLGAHMGVLGDGEVCLSTTNRNFKGRMGsPNAEIYLASPATAAASAVEGYITD 410
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
4-458 |
8.21e-88 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 274.71 E-value: 8.21e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 4 TLYEKLFDAHVVYEA-PNETPLLYIDRHLVHEVTSPQAFDGLRAHKRPVRQPGKTFATMDHNVSTQTkdiNASGEMARIq 82
Cdd:NF040615 2 TLAEKILSKKLGKEVyAGDTVEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPANT---VKAANMQKI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 83 MQELIKncnEFGVELYDLNHpyQGIVHVMGPEQGITLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGR 162
Cdd:NF040615 78 TREFVK---EQGIKNFYLGG--EGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 163 AKTMKIEVKGKAaPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNY 242
Cdd:NF040615 153 PKTIRVNIVGKN-ENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 243 VKgrlhapKGQDFDDAVAYWKTLK---TDDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDsipdpasfadpVErasa 319
Cdd:NF040615 232 LR------KEGVSEEEIAELKKNRitvNEKEENYYKEIEIDITDMEEQVACPHHPDNVKPVSE-----------VE---- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 320 ekalaymglkpGVPltdvnIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAG 399
Cdd:NF040615 291 -----------GTE-----IDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAG 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 400 FEWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGR-GGRTHLVSPAMAAAAAVTGH 458
Cdd:NF040615 355 AMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGNiNSYIYLSSPKIAAKSAVKGY 414
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
31-447 |
1.12e-66 |
|
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: 218.91 E-value: 1.12e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 31 LVHEVTSPQAFDGLR--AHKRPVRQPGKTFATMDHNVSTQtKDINASGEmariqmQELIKNCNEFGVELYDlnhPYQGIV 108
Cdd:cd01351 3 MLQDATGPMAMKAFEilAALGKVADPSQIACVHDHAVQLE-KPVNNEGH------KFLSFFAALQGIAFYR---PGVGII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 109 HVMGPEQGItLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVKGKAAPGITAKDIVLAII 188
Cdd:cd01351 73 HQIMVENLA-LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 189 GKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVKGRLHaPKGQDFDDavAYWKTLKTD 268
Cdd:cd01351 152 GIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGR-PLLKNLWL--AFPEELLAD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 269 DGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDsipdpasfadpverasaekalaymglkpgvpLTDVNIDKVFIGSCT 348
Cdd:cd01351 229 EGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSE-------------------------------VEGTKIDQVLIGSCT 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 349 NSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNDRLNPGERCASTS 428
Cdd:cd01351 278 NNRYSDMLAAAKLLKGAKVAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLVADGEVGVSSG 357
|
410 420
....*....|....*....|
gi 654547792 429 NRNFEGRQGRG-GRTHLVSP 447
Cdd:cd01351 358 NRNFPGRLGTYeRHVYLASP 377
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
1-466 |
3.78e-50 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 180.73 E-value: 3.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 1 MAKTLYEKLFDAHVV---YEaPNETPLLYIDRHLVHEVTSPQAFDGLRAHKRP-VRQPgKTFATMDHNVsTQTKDINAsg 76
Cdd:PRK07229 1 MGLTLTEKILYAHLVegeLE-PGEEIAIRIDQTLTQDATGTMAYLQFEAMGLDrVKTE-LSVQYVDHNL-LQADFENA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 77 emariqmqE----LIKNCNEFGVelyDLNHPYQGIVH--VMgpeQGITLPGMTIVCGDSHTATHGAFGALAFGIGTSEVE 150
Cdd:PRK07229 76 --------DdhrfLQSVAAKYGI---YFSKPGNGICHqvHL---ERFAFPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 151 HVLATQ--TLKQgrAKTMKIEVKGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGA 228
Cdd:PRK07229 142 LAMAGGpyYLKM--PKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 229 KAGLVAPDETTFNYVK--GRlhapkGQDfddavayWKTLKTDDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVndsipd 306
Cdd:PRK07229 220 TTSIFPSDERTREFLKaqGR-----EDD-------WVELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPV------ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 307 pasfadpveRASAEKAlaymglkpgvpltdvnIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQA 386
Cdd:PRK07229 282 ---------SEVAGIK----------------VDQVLIGSCTNSSYEDLMRAASILKGKKVHPKVSLVINPGSRQVLEML 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 387 EAEGLDKIFIEAG---FEwrlPGCSMCLAMNNDrlnPGERCAS--TSNRNFEGRQG-RGGRTHLVSPAMAAAAAVTGHFA 460
Cdd:PRK07229 337 ARDGALADLIAAGariLE---NACGPCIGMGQA---PATGNVSlrTFNRNFPGRSGtKDAQVYLASPETAAASALTGVIT 410
|
....*.
gi 654547792 461 DIRSLK 466
Cdd:PRK07229 411 DPRTLA 416
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
103-459 |
1.56e-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: 1.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 103 PYQGIVHVMGPEQgITLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVKGKAAPGITAKD 182
Cdd:cd01585 66 PGNGICHQVHLER-FAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKD 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 183 IVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVkgrlhAPKGQDFDdavayW 262
Cdd:cd01585 145 VILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFL-----AAQGREDD-----W 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 263 KTLKTDDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDsipdpasfadpVErasaekalaymGLKpgvpltdvnIDKV 342
Cdd:cd01585 215 VELAADADAEYDEEIEIDLSELEPLIARPHSPDNVVPVRE-----------VA-----------GIK---------VDQV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 343 FIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNdrlNPGE 422
Cdd:cd01585 264 AIGSCTNSSYEDLMTVAAILKGRRVHPHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQ---APPT 340
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 654547792 423 RCAS--TSNRNFEGRQG-RGGRTHLVSPAMAAAAAVTGHF 459
Cdd:cd01585 341 GGVSvrTFNRNFEGRSGtKDDLVYLASPEVAAAAALTGVI 380
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
31-457 |
2.15e-38 |
|
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: 143.14 E-value: 2.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 31 LVHEVTSPQA--FDGLRAHKrpVRQPGKTFATMDHNVSTQTKdinasgemariQMQELIKNCNEF----GVELYDLNhpy 104
Cdd:cd01582 3 MTHDNSWPVAlkFMSIGATK--IHNPDQIVMTLDHDVQNKSE-----------KNLKKYKNIESFakkhGIDFYPAG--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 105 QGIVHVMGPEQGITLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLAT-QTLKQgRAKTMKIEVKGKAAPGITAKDI 183
Cdd:cd01582 67 RGIGHQIMIEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATgQTWWQ-IPPVAKVELKGQLPKGVTGKDV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 184 VLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDEttfnyvkgrlhapkgqdfddavaywK 263
Cdd:cd01582 146 IVALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDA-------------------------K 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 264 TLktddgatfdtvvTLQAEEIAPQVtwgtnpgqvisvndSIPDPASFADPVERASAEkalaymglkpgvpltDVNIDKVF 343
Cdd:cd01582 201 HL------------ILDLSTLSPYV--------------SGPNSVKVSTPLKELEAQ---------------NIKINKAY 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 344 IGSCTNSRIEDLRAAAEIAKGRK-------VAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNND 416
Cdd:cd01582 240 LVSCTNSRASDIAAAADVVKGKKekngkipVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQG 319
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 654547792 417 RLNPGERCASTSNRNFEGRQG-RGGRTHLVSPAMAAAAAVTG 457
Cdd:cd01582 320 LLEPGEVGISATNRNFKGRMGsTEALAYLASPAVVAASAISG 361
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
90-447 |
3.08e-31 |
|
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: 124.47 E-value: 3.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 90 CNEFGVELYdlnHPYQGIVHVMGPEQgITLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIE 169
Cdd:cd01584 64 GAKYGIGFW---KPGSGIIHQIVLEN-YAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 170 VKGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVK--GRl 247
Cdd:cd01584 140 LTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKatGR- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 248 hapkGQDFDDAVAY-WKTLKTDDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDsipdpasFADPVErasaekalaym 326
Cdd:cd01584 219 ----AEIADLADEFkDDLLVADEGAEYDQLIEINLSELEPHINGPFTPDLATPVSK-------FKEVAE----------- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 327 glKPGVPLtdvNIDKVFIGSCTNSRIEDLRAAAEIAK---GRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWR 403
Cdd:cd01584 277 --KNGWPL---DLRVGLIGSCTNSSYEDMGRAASIAKqalAHGLKCKSIFTITPGSEQIRATIERDGLLQTFRDAGGIVL 351
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 654547792 404 LPGCSMCLAMNNDR-LNPGERCA--STSNRNFEGRQGRGGRTH--LVSP 447
Cdd:cd01584 352 ANACGPCIGQWDRKdIKKGEKNTivTSYNRNFTGRNDANPATHafVASP 400
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
106-435 |
3.39e-28 |
|
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle
Pssm-ID: 440669 [Multi-domain] Cd Length: 891 Bit Score: 118.28 E-value: 3.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 106 GIVH----------VMGPEQGITL---PGmTIVCGDSHTATHGAFGALAFGIGTSEVEHVLAtqtlkqGRAKTMKI-EV- 170
Cdd:COG1048 176 GIVHqvnleylafvVWTREEDGETvayPD-TLVGTDSHTTMINGLGVLGWGVGGIEAEAAML------GQPVSMLIpEVv 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 171 ----KGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVK-- 244
Cdd:COG1048 249 gvklTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRlt 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 245 GRlhapkGQDFDDAV-AY------WKTLKTDDgATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDSipdPASFADPVERA 317
Cdd:COG1048 329 GR-----SEEQIELVeAYakaqglWRDPDAPE-PYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDL---KEAFRAALAAP 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 318 SAEKALAYMGLKPGVPLTDVNIDKVF---IGSCTNSRIED-LRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAEA 388
Cdd:COG1048 400 VGEELDKPVRVEVDGEEFELGHGAVViaaITSCTNTSNPSvMIAAGLLAKkavekGLKVKPWVKTSLAPGSKVVTDYLER 479
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654547792 389 EGL----DKI-FIEAGFewrlpGCSMCLAmNNDRLNP---------GERCAS-TS-NRNFEGR 435
Cdd:COG1048 480 AGLlpylEALgFNVVGY-----GCTTCIG-NSGPLPPeiseaieenDLVVAAvLSgNRNFEGR 536
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
103-435 |
9.41e-27 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 113.95 E-value: 9.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 103 PYQGIVH----------VMGpEQGITLPGmTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVKG 172
Cdd:PTZ00092 182 PGSGIVHqvnleylarvVFN-KDGLLYPD-SVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTG 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 173 KAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVK--GRlhaP 250
Cdd:PTZ00092 260 KLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKqtGR---S 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 251 KgQDFDDAVAYWKTLK----TDDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVND-------SIPDPASF---ADPVER 316
Cdd:PTZ00092 337 E-EKVELIEKYLKANGlfrtYAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDlkkdftaCLSAPVGFkgfGIPEEK 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 317 ASAEKALAYMGLKpgVPLTDVNIDKVFIGSCTN-SRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAEAEG 390
Cdd:PTZ00092 416 HEKKVKFTYKGKE--YTLTHGSVVIAAITSCTNtSNPSVMLAAGLLAKkavekGLKVPPYIKTSLSPGSKVVTKYLEASG 493
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 654547792 391 LDKIFIEAGFEWRLPGCSMCLAMNNDRLNPGERCAS----------TSNRNFEGR 435
Cdd:PTZ00092 494 LLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITnndlvaaavlSGNRNFEGR 548
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
123-435 |
8.41e-26 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 111.18 E-value: 8.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 123 TIVCGDSHTATHGAFGALAFGIGTSEVEHVLAtqtlkqGRAKTMKI------EVKGKAAPGITAKDIVLAIIGKTGSAGG 196
Cdd:PRK12881 207 TLVGTDSHTTMINGIGVLGWGVGGIEAEAVML------GQPVYMLIpdvvgvELTGKLREGVTATDLVLTVTEMLRKEGV 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 197 TGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVKGrlhapKGQDfDDAVA----YWKT--LKTDDG 270
Cdd:PRK12881 281 VGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLRL-----TGRT-EAQIAlveaYAKAqgLWGDPK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 271 AT--FDTVVTLQAEEIAPQVTWGTNPGQVISVNDSipdPASFADPVERASAEKALAYMG-LKPGVPLTDVNIDKVFIGSC 347
Cdd:PRK12881 355 AEprYTRTLELDLSTVAPSLAGPKRPQDRIALGNV---KSAFSDLFSKPVAENGFAKKAqTSNGVDLPDGAVAIAAITSC 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 348 TN-SRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNDRLNPG 421
Cdd:PRK12881 432 TNtSNPSVLIAAGLLAKkaverGLTVKPWVKTSLAPGSKVVTEYLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEI 511
|
330 340
....*....|....*....|....
gi 654547792 422 ER--------CAS--TSNRNFEGR 435
Cdd:PRK12881 512 EQaitkndlvAAAvlSGNRNFEGR 535
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
102-446 |
1.32e-22 |
|
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: 99.88 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 102 HPYQGIVHVMgpEQGITLPGMTIVCGDSHTAthgaFG-ALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVKGKAAPGITA 180
Cdd:cd01581 90 RPGDGVIHSW--LNRMLLPDTVGTGGDSHTR----FPiGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 181 KDIVLAI--------IGKTGSAGG----TGHVVEFcgEAIQALSMEGRMTLCNMAIEMGAKAGLV-APDETTFNYVKG-- 245
Cdd:cd01581 164 RDLVNAIpyyaiqqgLLTVEKKGKknvfNGRILEI--EGLPDLKVEQAFELTDASAERSAAACTVrLDKEPVIEYLESnv 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 246 -RLHAPKGQDFDDAvaywKTLKTDDGATFDTVVTLQAEEIAPQVTWGTnpgqVISVN-DSIPDPAsFADPVERASAeKAL 323
Cdd:cd01581 242 vLMKIMIANGYDDA----RTLLRRIIAMEEWLANPPLLEPDADAEYAA----VIEIDlDDIKEPI-LACPNDPDDV-KLL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 324 AYMglkpgvplTDVNIDKVFIGSC-TNsrIEDLRAAAEIAKGRKVAPgVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEW 402
Cdd:cd01581 312 SEV--------AGKKIDEVFIGSCmTN--IGHFRAAAKILRGKEFKP-TRLWVAPPTRMDWAILQEEGYYSIFGDAGART 380
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 654547792 403 RLPGCSMCLAmNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVS 446
Cdd:cd01581 381 EMPGCSLCMG-NQARVADGATVFSTSTRNFDNRVGKGAEVYLGS 423
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
103-435 |
1.45e-21 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 97.95 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 103 PYQGIVHVMGPE---------QGITLPGmTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVKGK 173
Cdd:PLN00070 214 PGSGIVHQVNLEylgrvvfntDGILYPD-SVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 174 AAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVKgrLHAPKGQ 253
Cdd:PLN00070 293 LRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLK--LTGRSDE 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 254 DFDDAVAYWKTLK-------TDDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDSIPDPAS----------FADPVER 316
Cdd:PLN00070 371 TVAMIEAYLRANKmfvdynePQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHScldnkvgfkgFAVPKEA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 317 ASAEKALAYMGLKPGVPLTDVNIdkVFIGSCTN-SRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAEAEG 390
Cdd:PLN00070 451 QSKVAKFSFHGQPAELRHGSVVI--AAITSCTNtSNPSVMLGAGLVAKkacelGLEVKPWIKTSLAPGSGVVTKYLLKSG 528
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 654547792 391 LDKIFIEAGFEWRLPGCSMCLAmNNDRLNPGERCASTS-----------NRNFEGR 435
Cdd:PLN00070 529 LQKYLNQQGFHIVGYGCTTCIG-NSGELDESVASAITEndivaaavlsgNRNFEGR 583
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
106-435 |
1.02e-19 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 92.49 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 106 GIVH----------VMGPEQGITL--PGmTIVCGDSHTaTH-GAFGALAFGIGTSEVEHVLatqtLkqGRAKTMKI---- 168
Cdd:PRK09277 179 GICHqvnleylapvVWTREDGELVayPD-TLVGTDSHT-TMiNGLGVLGWGVGGIEAEAAM----L--GQPSSMLIpevv 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 169 --EVKGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVK-- 244
Cdd:PRK09277 251 gvKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRlt 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 245 GRlhapkgqdfDDAV-----AYWKT----LKTDDGATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDSipdPASFAD--P 313
Cdd:PRK09277 331 GR---------DEEQvalveAYAKAqglwRDPLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDV---KEAFAKsaE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 314 VERASAEKALAYMGLKPGVPLTDVNIDKvfIGSCTN-SRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAE 387
Cdd:PRK09277 399 LGVQGFGLDEAEEGEDYELPDGAVVIAA--ITSCTNtSNPSVMIAAGLLAKkavekGLKVKPWVKTSLAPGSKVVTDYLE 476
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654547792 388 AEG----LDKI-FIEAGFewrlpGCSMCLAMNNDrLNPG------ER---CAS--TSNRNFEGR 435
Cdd:PRK09277 477 KAGllpyLEALgFNLVGY-----GCTTCIGNSGP-LPPEiekainDNdlvVTAvlSGNRNFEGR 534
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
117-446 |
3.61e-19 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 90.62 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 117 ITLPGMTIVCGDSHTATH-G-AFGA----LAFGIGTSEV-----EHVLATqtlkqgraktmkieVKGKAAPGITAKDIVL 185
Cdd:PRK09238 475 MLLPDTVGTGGDSHTRFPiGiSFPAgsglVAFAAATGVMpldmpESVLVR--------------FKGEMQPGITLRDLVH 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 186 AI----IGK----TGSAGG----TGHVVEFcgEAIQALSMEGRMTLCNMAIEMGAKAGLVA-PDETTFNYVKgrlhapkg 252
Cdd:PRK09238 541 AIpyyaIKQglltVEKKGKknifSGRILEI--EGLPDLKVEQAFELTDASAERSAAGCTIKlSKEPIIEYLR-------- 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 253 qdfdDAVAYWKTLkTDDGatFDTVVTLQAEeIAPQVTWGTNPgQVISvndsiPDP-ASFADPVERASA---EKALAymgl 328
Cdd:PRK09238 611 ----SNIVLLKWM-IAEG--YGDARTLERR-IAAMEEWLANP-ELLE-----ADAdAEYAAVIEIDLAeikEPILA---- 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 329 KPGVP-----LTDV---NIDKVFIGSC-TNsrIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAG 399
Cdd:PRK09238 673 CPNDPddvrlLSEVagtKIDEVFIGSCmTN--IGHFRAAGKLLEGKKGQLPTRLWVAPPTKMDADQLTEEGYYSIFGKAG 750
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 654547792 400 FEWRLPGCSMCLAmNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVS 446
Cdd:PRK09238 751 ARIEMPGCSLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYLGS 796
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
103-435 |
1.00e-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: 87.74 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 103 PYQGIVH----------VMGPE---QGITLPGmTIVCGDSHTATHGAFGALAFGIGTSEVEHVLAtqtlkqGRAKTMKI- 168
Cdd:cd01586 91 PGTGIIHqvnleylarvVFTSEedgDGVAYPD-SVVGTDSHTTMINGLGVLGWGVGGIEAEAVML------GQPISMLLp 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 169 -----EVKGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDettfnyv 243
Cdd:cd01586 164 evvgvKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD------- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 244 kgrlhapkgqdfddavaywktlktddgatfDTVVTLQAEEIAPQVTWGTNPGQVISVNDSIPDPAsfadpverasaekal 323
Cdd:cd01586 237 ------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPLHGSVVIAA--------------- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 324 aymglkpgvpltdvnidkvfIGSCTN-SRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIE 397
Cdd:cd01586 272 --------------------ITSCTNtSNPSVMLAAGLLAKkavelGLKVKPYVKTSLAPGSRVVTKYLEASGLLPYLEK 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 654547792 398 AGFEWRLPGCSMCLAmNNDRLNP---------GERCAS--TSNRNFEGR 435
Cdd:cd01586 332 LGFHVVGYGCTTCIG-NSGPLPEeveeaikenDLVVAAvlSGNRNFEGR 379
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
121-437 |
2.41e-15 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 78.51 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 121 GMTIVCGDSHTaTHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVKGKAAPGITAKDIVLAIIGKTGSAGGTGH- 199
Cdd:PRK11413 142 GKMILGSDSHT-RYGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVKNk 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 200 VVEFCGEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVKgrLHAPKGqdfddavAYwKTLKTDDGATFDTVVTL 279
Cdd:PRK11413 221 VMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLA--LHGRGQ-------DY-CELNPQPMAYYDGCISV 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 280 QAEEIAPQVTWGTNPGQVISVNDSIPDPASFADPVERASAEKALAYMGLKpgvpLTD------VNIDKVFIGSCTNSRIE 353
Cdd:PRK11413 291 DLSAIKPMIALPFHPSNVYEIDELNQNLTDILREVEIESERVAHGKAKLS----LLDkiengrLKVQQGIIAGCSGGNYE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 354 DLRAAAEIAKGRKVAPGVQAL-VVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNDRLNPGERCASTSnRNF 432
Cdd:PRK11413 367 NVIAAANALRGQSCGNDTFSLsVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFGAGDTPANNGLSIRHTT-RNF 445
|
....*
gi 654547792 433 EGRQG 437
Cdd:PRK11413 446 PNREG 450
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
91-446 |
2.43e-15 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 78.81 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 91 NEFGVELydlnHPYQGIVHVMgpEQGITLPGMTIVCGDSHTAthgaFG-ALAFGIGTSEVEHVLATQTLKQGRAKTMKIE 169
Cdd:PLN00094 529 NRGGVSL----RPGDGVIHSW--LNRMLLPDTVGTGGDSHTR----FPiGISFPAGSGLVAFGAATGVIPLDMPESVLVR 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 170 VKGKAAPGITAKDIVLAI-----------IGKTGSAGG-TGHVVEFcgEAIQALSMEGRMTLCNMAIEMGAKAGLVAPDE 237
Cdd:PLN00094 599 FTGTMQPGITLRDLVHAIpytaiqdglltVEKKGKKNVfSGRILEI--EGLPHLKCEQAFELSDASAERSAAGCTIKLDK 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 238 ttfnyvkgrlhAPKGQDFDDAVAYWKTLKTDDgatFDTVVTLQaEEIAPQVTWGTNP-----------GQVISVN-DSIP 305
Cdd:PLN00094 677 -----------EPIIEYLNSNVVMLKWMIAEG---YGDRRTLE-RRIARMQQWLADPelleadpdaeyAAVIEIDmDEIK 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 306 DP--ASFADPVERASAEKalaymglkpgvpLTDVNIDKVFIGSC-TNsrIEDLRAAAEIAKGRKVAPGVQALVVPGSGPV 382
Cdd:PLN00094 742 EPilCAPNDPDDARLLSE------------VTGDKIDEVFIGSCmTN--IGHFRAAGKLLNDNLSQLPTRLWVAPPTKMD 807
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654547792 383 KAQAEAEGLDKIFIEAGFEWRLPGCSMCLAmNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVS 446
Cdd:PLN00094 808 EAQLKAEGYYSTFGTVGARTEMPGCSLCMG-NQARVAEKSTVVSTSTRNFPNRLGKGANVYLAS 870
|
|
| AcnB |
COG1049 |
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ... |
333-446 |
3.86e-15 |
|
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: 77.97 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654547792 333 PLTDV---NIDKVFIGSC-TNsrIEDLRAAAEIAKGRKVAPgVQALVVPgsgPVK---AQAEAEGLDKIFIEAGFEWRLP 405
Cdd:COG1049 682 LLSEVagtKIDEVFIGSCmTN--IGHFRAAGKLLEGKGNLP-TRLWIAP---PTKmdeAQLTEEGYYSIFGAAGARTEMP 755
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 654547792 406 GCSMCLAmNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVS 446
Cdd:COG1049 756 GCSLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYLGS 795
|
|
| |
