|
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: 1015.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 1 MAKTLYEKLFDAHVVFEAQNETPLLYIDRHLVHEVTSPQAFDGLRAHGRQVRQPGKTFATMDHNVSTQTKDINASGEMAR 80
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLPIADPVSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 81 IQMQELIKNCNEFGVELYDLNHPYQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQ 160
Cdd:PRK05478 81 IQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 161 GRAKTMKIEVNGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETTF 240
Cdd:PRK05478 161 KKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 241 NYVQGRLHAPKGEDFTHAVEYWKTLKTDDNATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDNIPDPASFVDPVERASAE 320
Cdd:PRK05478 241 EYLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVKRASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 321 KALAYMGLKPGIPLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGF 400
Cdd:PRK05478 321 RALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489108948 401 EWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAVTGHFADIRSIK 466
Cdd:PRK05478 401 EWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
1-465 |
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: 926.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 1 MAKTLYEKLFDAHVVFEAQNETPLLYIDRHLVHEVTSPQAFDGLRAHGRQVRQPGKTFATMDHNVSTQTKDINASGEMAR 80
Cdd:TIGR00170 1 MPRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFNIKDEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 81 IQMQELIKNCNEFGVELYDLNHPYQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQ 160
Cdd:TIGR00170 81 IQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 161 GRAKTMKIEVNGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETTF 240
Cdd:TIGR00170 161 ARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 241 NYVQGRLHAPKGEDFTHAVEYWKTLKTDDNATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDNIPDPASFVDPVERASAE 320
Cdd:TIGR00170 241 EYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 321 KALAYMGLKPGIPLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGF 400
Cdd:TIGR00170 321 RALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489108948 401 EWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAVTGHFADIRSI 465
Cdd:TIGR00170 401 EWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-463 |
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: 709.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 1 MAKTLYEKLFDAHVVFEAQ-NETPLLYIDRHLVHEVTSPQAFDGLRAHG-RQVRQPGKTFATMDHNVSTQTkdinasgEM 78
Cdd:COG0065 1 MGMTLAEKILARHAGREVEpGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPTKD-------PK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 79 ARIQMQELIKNCNEFGVELYDLNHPyqGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTL 158
Cdd:COG0065 74 SAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 159 KQGRAKTMKIEVNGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDET 238
Cdd:COG0065 152 WFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 239 TFNYVQGRLHAPkgedfthaveyWKTLKTDDNATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDnipdpasfvdpveras 318
Cdd:COG0065 232 TFEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE---------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 319 aekalaymglkpgipLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEA 398
Cdd:COG0065 285 ---------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEA 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489108948 399 GFEWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGR-GGRTHLVSPAMAAAAAVTGHFADIR 463
Cdd:COG0065 350 GAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGSpGSRTYLASPATAAASAIAGRITDPR 415
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-447 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 694.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 7 EKLFDAHVVfeAQNETPLLYI-DRHLVHEVTSPQAFDGLRAHGRQVRQPGKTFATMDHNVST--------QTKDINASGE 77
Cdd:pfam00330 1 EKIWDAHLV--EELDGSLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTdlvidhapDALDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 78 MARI--QMQELIKNCNEFGVELYDlnhPYQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLAT 155
Cdd:pfam00330 79 ISRNkeQYDFLEWNAKKFGIRFVP---PGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 156 QTLKQGRAKTMKIEVNGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAP 235
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 236 DETTFNYVQ--GRLHAPKGEDFTHAVEyWKTLKTDDNATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDNIPDPasFVDP 313
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDP--FADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 314 VERASAEKALAYMGLKPGIPLTEVAIDKVFIGSCTNSRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAEA 388
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 489108948 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: 608.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 29 RHLVHEVTSPQAFDGLRAHGRQ-VRQPGKTFATMDHNVSTqtkdinaSGEMARIQMQELIKNCNEFGVELYDLNhpYQGI 107
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREkVWDPEKIVAVFDHNVPT-------PDIKAAEQVKTLRKFAKEFGINFFDVG--RQGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 108 VHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVNGKAAPGITAKDIVLAI 187
Cdd:cd01583 72 CHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 188 IGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVQGRLHApkgedfthaveYWKTLKT 267
Cdd:cd01583 152 IGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKA-----------YWKELKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 268 DDNATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDNIPdpasfvdpverasaekalaymglkpgiplteVAIDKVFIGSC 347
Cdd:cd01583 221 DEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQVFIGSC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 348 TNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNDRLNPGERCAST 427
Cdd:cd01583 270 TNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVST 349
|
410 420 430
....*....|....*....|....*....|...
gi 489108948 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 |
2.80e-88 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 275.87 E-value: 2.80e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 4 TLYEKLFDAHVVFEA-QNETPLLYIDRHLVHEVTSPQAFDGLRAHGRQVRQPGKTFATMDHNVSTQTkdiNASGEMARIq 82
Cdd:NF040615 2 TLAEKILSKKLGKEVyAGDTVEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPANT---VKAANMQKI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 83 MQELIKncnEFGVELYDLNHpyQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGR 162
Cdd:NF040615 78 TREFVK---EQGIKNFYLGG--EGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 163 AKTMKIEVNGKAaPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNY 242
Cdd:NF040615 153 PKTIRVNIVGKN-ENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 243 VQgrlHAPKGEDFTHAVEYWKTLKTDDNATFDTVVTLQAEEIAPQVTWGTNPgqvisvnDNIPDpasfVDPVErasaeka 322
Cdd:NF040615 232 LR---KEGVSEEEIAELKKNRITVNEKEENYYKEIEIDITDMEEQVACPHHP-------DNVKP----VSEVE------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 323 laymglkpGIPltevaIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEW 402
Cdd:NF040615 291 --------GTE-----IDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAMI 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 489108948 403 RLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGR-GGRTHLVSPAMAAAAAVTGH 458
Cdd:NF040615 358 CTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGNiNSYIYLSSPKIAAKSAVKGY 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: 1015.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 1 MAKTLYEKLFDAHVVFEAQNETPLLYIDRHLVHEVTSPQAFDGLRAHGRQVRQPGKTFATMDHNVSTQTKDINASGEMAR 80
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLPIADPVSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 81 IQMQELIKNCNEFGVELYDLNHPYQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQ 160
Cdd:PRK05478 81 IQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 161 GRAKTMKIEVNGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETTF 240
Cdd:PRK05478 161 KKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 241 NYVQGRLHAPKGEDFTHAVEYWKTLKTDDNATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDNIPDPASFVDPVERASAE 320
Cdd:PRK05478 241 EYLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVKRASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 321 KALAYMGLKPGIPLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGF 400
Cdd:PRK05478 321 RALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489108948 401 EWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAVTGHFADIRSIK 466
Cdd:PRK05478 401 EWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
1-465 |
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: 926.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 1 MAKTLYEKLFDAHVVFEAQNETPLLYIDRHLVHEVTSPQAFDGLRAHGRQVRQPGKTFATMDHNVSTQTKDINASGEMAR 80
Cdd:TIGR00170 1 MPRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFNIKDEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 81 IQMQELIKNCNEFGVELYDLNHPYQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQ 160
Cdd:TIGR00170 81 IQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 161 GRAKTMKIEVNGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETTF 240
Cdd:TIGR00170 161 ARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 241 NYVQGRLHAPKGEDFTHAVEYWKTLKTDDNATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDNIPDPASFVDPVERASAE 320
Cdd:TIGR00170 241 EYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 321 KALAYMGLKPGIPLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGF 400
Cdd:TIGR00170 321 RALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489108948 401 EWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAVTGHFADIRSI 465
Cdd:TIGR00170 401 EWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
1-465 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 814.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 1 MAKTLYEKLFDAHVVFEAQNETPLLYIDRHLVHEVTSPQAFDGLRAHGRQVRQPGKTFATMDHNVSTQTK-DINASGEMA 79
Cdd:PRK12466 2 MPRTLYDKLWDSHTVARLDDGHVLLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPTRPGrDRGITDPGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 80 RIQMQELIKNCNEFGVELYDLNHPYQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLK 159
Cdd:PRK12466 82 ALQVDYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQTLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 160 QGRAKTMKIEVNGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETT 239
Cdd:PRK12466 162 YRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 240 FNYVQGRLHAPKGEDFTHAVEYWKTLKTDDNATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDNIPDPASFVDPVERASA 319
Cdd:PRK12466 242 FDYLRGRPRAPKGALWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAAEADPARRAAM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 320 EKALAYMGLKPGIPLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAG 399
Cdd:PRK12466 322 ERALDYMGLTPGTPLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAG 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489108948 400 FEWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAVTGHFADIRSI 465
Cdd:PRK12466 402 FEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHITDVRSL 467
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-463 |
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: 709.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 1 MAKTLYEKLFDAHVVFEAQ-NETPLLYIDRHLVHEVTSPQAFDGLRAHG-RQVRQPGKTFATMDHNVSTQTkdinasgEM 78
Cdd:COG0065 1 MGMTLAEKILARHAGREVEpGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPTKD-------PK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 79 ARIQMQELIKNCNEFGVELYDLNHPyqGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTL 158
Cdd:COG0065 74 SAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 159 KQGRAKTMKIEVNGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDET 238
Cdd:COG0065 152 WFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 239 TFNYVQGRLHAPkgedfthaveyWKTLKTDDNATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDnipdpasfvdpveras 318
Cdd:COG0065 232 TFEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE---------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 319 aekalaymglkpgipLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEA 398
Cdd:COG0065 285 ---------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEA 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489108948 399 GFEWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGR-GGRTHLVSPAMAAAAAVTGHFADIR 463
Cdd:COG0065 350 GAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGSpGSRTYLASPATAAASAIAGRITDPR 415
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
7-447 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 694.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 7 EKLFDAHVVfeAQNETPLLYI-DRHLVHEVTSPQAFDGLRAHGRQVRQPGKTFATMDHNVST--------QTKDINASGE 77
Cdd:pfam00330 1 EKIWDAHLV--EELDGSLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTdlvidhapDALDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 78 MARI--QMQELIKNCNEFGVELYDlnhPYQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLAT 155
Cdd:pfam00330 79 ISRNkeQYDFLEWNAKKFGIRFVP---PGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 156 QTLKQGRAKTMKIEVNGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAP 235
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 236 DETTFNYVQ--GRLHAPKGEDFTHAVEyWKTLKTDDNATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDNIPDPasFVDP 313
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDP--FADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 314 VERASAEKALAYMGLKPGIPLTEVAIDKVFIGSCTNSRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAEA 388
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 489108948 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: 608.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 29 RHLVHEVTSPQAFDGLRAHGRQ-VRQPGKTFATMDHNVSTqtkdinaSGEMARIQMQELIKNCNEFGVELYDLNhpYQGI 107
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREkVWDPEKIVAVFDHNVPT-------PDIKAAEQVKTLRKFAKEFGINFFDVG--RQGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 108 VHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVNGKAAPGITAKDIVLAI 187
Cdd:cd01583 72 CHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 188 IGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVQGRLHApkgedfthaveYWKTLKT 267
Cdd:cd01583 152 IGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKA-----------YWKELKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 268 DDNATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDNIPdpasfvdpverasaekalaymglkpgiplteVAIDKVFIGSC 347
Cdd:cd01583 221 DEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQVFIGSC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 348 TNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNDRLNPGERCAST 427
Cdd:cd01583 270 TNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVST 349
|
410 420 430
....*....|....*....|....*....|...
gi 489108948 428 SNRNFEGRQG-RGGRTHLVSPAMAAAAAVTGHF 459
Cdd:cd01583 350 SNRNFKGRMGsPGARIYLASPATAAASAITGEI 382
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
1-465 |
2.15e-132 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 388.77 E-value: 2.15e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 1 MAKTLYEKLFDAHVVFEAQ-NETPLLYIDRHLVHEVTSPQAFDGLRAHG-RQVRQPGKTFATMDHNVSTqtKDINAsgem 78
Cdd:PRK00402 1 MGMTLAEKILARHSGRDVSpGDIVEAKVDLVMAHDITGPLAIKEFEKIGgDKVFDPSKIVIVFDHFVPA--KDIKS---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 79 ARIQmqeliKNCNEFGVElYDLNHPY---QGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLAT 155
Cdd:PRK00402 75 AEQQ-----KILREFAKE-QGIPNFFdvgEGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 156 qtlkqGRA-----KTMKIEVNGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKA 230
Cdd:PRK00402 149 -----GKTwfkvpETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 231 GLVAPDETTFNYVQGRLHAPkgedfthaveyWKTLKTDDNATFDTVVTLQAEEIAPQVTWGTNPgqvisvnDNipdpasf 310
Cdd:PRK00402 224 GIFAPDEKTLEYLKERAGRD-----------YKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLP-------DN------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 311 VDPVERAsaekalaymglkpgiplTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEG 390
Cdd:PRK00402 279 VKPVSEV-----------------EGTKVDQVFIGSCTNGRLEDLRIAAEILKGRKVAPGVRLIVIPASQKIYLQALKEG 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489108948 391 LDKIFIEAGFEWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQG-RGGRTHLVSPAMAAAAAVTGHFADIRSI 465
Cdd:PRK00402 342 LIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGsPESEVYLASPAVAAASAVTGKITDPREV 417
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
4-463 |
1.31e-108 |
|
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: 327.87 E-value: 1.31e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 4 TLYEKLFDAHVVFEA-QNETPLLYIDRHLVHEVTSPQAFDGLRAHGR-QVRQPGKTFATMDHNVSTqtKDINASgEMARI 81
Cdd:TIGR01343 1 TIAEKILSKKSGKEVyAGDLIEAEIDLAMVHDITAPLAIKTLEEYGIdKVWNPEKIVIVFDHQVPA--DTIKAA-EMQKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 82 qMQELIKncnEFGVElyDLNHPYQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQG 161
Cdd:TIGR01343 78 -AREFVK---KQGIK--YFYDVGEGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 162 RAKTMKIEVNGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETTFN 241
Cdd:TIGR01343 152 VPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 242 YVQGRLHAPkgedfthaveyWKTLKTDDNATFDTVVTLQAEEIAPQVTWGTNPgqvisvnDNIpDPASFVDpverasaek 321
Cdd:TIGR01343 232 YLKERRKEP-----------FRVYKSDEDAEYAKEIEIDASQIEPVVACPHNV-------DNV-KPVSEVE--------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 322 alaymglkpGIPltevaIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFE 401
Cdd:TIGR01343 284 ---------GTE-----IDQVFIGSCTNGRLEDLRVAAKILKGRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAV 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489108948 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 |
6.49e-95 |
|
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: 292.44 E-value: 6.49e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 3 KTLYEKLFDAHVVFE-AQNETPLLYIDRHLVHEVTSPQAFDGLRAHGR-QVRQPGKTFATMDHNVSTQTKdinasgEMAR 80
Cdd:TIGR02086 1 MTLAEKILSEKVGRPvCAGEIVEVEVDLAMTHDGTGPLAIKALRELGVaRVWDPEKIVIAFDHNVPPPTV------EAAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 81 IQmQELIKNCNEFGVELYDLNhpyQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQ 160
Cdd:TIGR02086 75 MQ-KEIREFAKRHGIKNFDVG---EGICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTWI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 161 GRAKTMKIEVNGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETTF 240
Cdd:TIGR02086 151 KVPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEETY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 241 NYVQGRlhapKGEDFthaveywKTLKTDDNATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDnipdpasfvdpVErasae 320
Cdd:TIGR02086 231 EYLKKR----RGLEF-------RILVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVSD-----------VE----- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 321 kalaymGLKpgipltevaIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGF 400
Cdd:TIGR02086 284 ------GTE---------IDQVFIGSCTNGRLEDLRIAAEILKGRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAGA 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489108948 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 |
2.80e-88 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 275.87 E-value: 2.80e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 4 TLYEKLFDAHVVFEA-QNETPLLYIDRHLVHEVTSPQAFDGLRAHGRQVRQPGKTFATMDHNVSTQTkdiNASGEMARIq 82
Cdd:NF040615 2 TLAEKILSKKLGKEVyAGDTVEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPANT---VKAANMQKI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 83 MQELIKncnEFGVELYDLNHpyQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGR 162
Cdd:NF040615 78 TREFVK---EQGIKNFYLGG--EGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 163 AKTMKIEVNGKAaPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNY 242
Cdd:NF040615 153 PKTIRVNIVGKN-ENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 243 VQgrlHAPKGEDFTHAVEYWKTLKTDDNATFDTVVTLQAEEIAPQVTWGTNPgqvisvnDNIPDpasfVDPVErasaeka 322
Cdd:NF040615 232 LR---KEGVSEEEIAELKKNRITVNEKEENYYKEIEIDITDMEEQVACPHHP-------DNVKP----VSEVE------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 323 laymglkpGIPltevaIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEW 402
Cdd:NF040615 291 --------GTE-----IDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAMI 357
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 489108948 403 RLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGR-GGRTHLVSPAMAAAAAVTGH 458
Cdd:NF040615 358 CTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGNiNSYIYLSSPKIAAKSAVKGY 414
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
31-447 |
2.28e-65 |
|
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: 215.44 E-value: 2.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 31 LVHEVTSPQAFDGLRAHG--RQVRQPGKTFATMDHNVSTQtKDINASGEmariqmQELIKNCNEFGVELYDlnhPYQGIV 108
Cdd:cd01351 3 MLQDATGPMAMKAFEILAalGKVADPSQIACVHDHAVQLE-KPVNNEGH------KFLSFFAALQGIAFYR---PGVGII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 109 HVMGPEQGVtLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVNGKAAPGITAKDIVLAII 188
Cdd:cd01351 73 HQIMVENLA-LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 189 GKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYV--QGRLHAPKGEDfthavEYWKTLK 266
Cdd:cd01351 152 GIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLeaTGRPLLKNLWL-----AFPEELL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 267 TDDNATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDnipdpasfvdpverasaekalaymglkpgipLTEVAIDKVFIGS 346
Cdd:cd01351 227 ADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSE-------------------------------VEGTKIDQVLIGS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 347 CTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNDRLNPGERCAS 426
Cdd:cd01351 276 CTNNRYSDMLAAAKLLKGAKVAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLVADGEVGVS 355
|
410 420
....*....|....*....|..
gi 489108948 427 TSNRNFEGRQGRG-GRTHLVSP 447
Cdd:cd01351 356 SGNRNFPGRLGTYeRHVYLASP 377
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
1-463 |
6.17e-51 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 182.65 E-value: 6.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 1 MAKTLYEKLFDAHVV---FEAQNETpLLYIDRHLVHEVTSPQAFDGLRAHGR-QVRQPgKTFATMDHNVsTQTKDINAsg 76
Cdd:PRK07229 1 MGLTLTEKILYAHLVegeLEPGEEI-AIRIDQTLTQDATGTMAYLQFEAMGLdRVKTE-LSVQYVDHNL-LQADFENA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 77 emariqmqE----LIKNCNEFGVelyDLNHPYQGIVHVMGPEQ-GVtlPGMTIVCGDSHTATHGAFGALAFGIGTSEVEH 151
Cdd:PRK07229 76 --------DdhrfLQSVAAKYGI---YFSKPGNGICHQVHLERfAF--PGKTLLGSDSHTPTAGGLGMLAIGAGGLDVAL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 152 VLATQ--TLKQgrAKTMKIEVNGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAK 229
Cdd:PRK07229 143 AMAGGpyYLKM--PKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGAT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 230 AGLVAPDETTFNYV--QGRlhapkGEDfthaveyWKTLKTDDNATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDnipdp 307
Cdd:PRK07229 221 TSIFPSDERTREFLkaQGR-----EDD-------WVELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSE----- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 308 asfvdpverasaekalaymglkpgipLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAE 387
Cdd:PRK07229 284 --------------------------VAGIKVDQVLIGSCTNSSYEDLMRAASILKGKKVHPKVSLVINPGSRQVLEMLA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 388 AEGLDKIFIEAG---FEwrlPGCSMCLAMNNDrlnPGERCAS--TSNRNFEGRQG-RGGRTHLVSPAMAAAAAVTGHFAD 461
Cdd:PRK07229 338 RDGALADLIAAGariLE---NACGPCIGMGQA---PATGNVSlrTFNRNFPGRSGtKDAQVYLASPETAAASALTGVITD 411
|
..
gi 489108948 462 IR 463
Cdd:PRK07229 412 PR 413
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
103-459 |
4.26e-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: 166.86 E-value: 4.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 103 PYQGIVHVMGPEQgVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVNGKAAPGITAKD 182
Cdd:cd01585 66 PGNGICHQVHLER-FAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKD 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 183 IVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYV--QGRlhapkGEDfthave 260
Cdd:cd01585 145 VILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLaaQGR-----EDD------ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 261 yWKTLKTDDNATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDnipdpasfvdpVErasaekalaymGLKpgipltevaID 340
Cdd:cd01585 214 -WVELAADADAEYDEEIEIDLSELEPLIARPHSPDNVVPVRE-----------VA-----------GIK---------VD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 341 KVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNdrlNP 420
Cdd:cd01585 262 QVAIGSCTNSSYEDLMTVAAILKGRRVHPHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQ---AP 338
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 489108948 421 GERCAS--TSNRNFEGRQG-RGGRTHLVSPAMAAAAAVTGHF 459
Cdd:cd01585 339 PTGGVSvrTFNRNFEGRSGtKDDLVYLASPEVAAAAALTGVI 380
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
31-457 |
3.80e-37 |
|
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase catalytic domain. Homoaconitase and other uncharacterized proteins of the Aconitase family. Homoaconitase is part of an unusual lysine biosynthesis pathway found only in filamentous fungi, in which lysine is synthesized via the alpha-aminoadipate pathway. In this pathway, homoaconitase catalyzes the conversion of cis-homoaconitic acid into homoisocitric acid. The reaction mechanism is believed to be similar to that of other aconitases.
Pssm-ID: 153132 [Multi-domain] Cd Length: 363 Bit Score: 139.67 E-value: 3.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 31 LVHEVTSPQAFDGLRAHGRQVRQPGKTFATMDHNVSTQTKdinasgemariQMQELIKNCNEF----GVELYDLNhpyQG 106
Cdd:cd01582 3 MTHDNSWPVALKFMSIGATKIHNPDQIVMTLDHDVQNKSE-----------KNLKKYKNIESFakkhGIDFYPAG---RG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 107 IVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLAT-QTLKQgRAKTMKIEVNGKAAPGITAKDIVL 185
Cdd:cd01582 69 IGHQIMIEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATgQTWWQ-IPPVAKVELKGQLPKGVTGKDVIV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 186 AIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDEttfnyvqgrlhapkgedfthaveywKTL 265
Cdd:cd01582 148 ALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDA-------------------------KHL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 266 ktddnatfdtvvTLQAEEIAPQVTWgtnpgqvisvndniPDPASFVDPVERASAEkalaymglkpgipltEVAIDKVFIG 345
Cdd:cd01582 203 ------------ILDLSTLSPYVSG--------------PNSVKVSTPLKELEAQ---------------NIKINKAYLV 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 346 SCTNSRIEDLRAAAEIAKGRK-------VAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNDRL 418
Cdd:cd01582 242 SCTNSRASDIAAAADVVKGKKekngkipVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQGLL 321
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 489108948 419 NPGERCASTSNRNFEGRQG-RGGRTHLVSPAMAAAAAVTG 457
Cdd:cd01582 322 EPGEVGISATNRNFKGRMGsTEALAYLASPAVVAASAISG 361
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
90-447 |
6.29e-30 |
|
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: 120.62 E-value: 6.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 90 CNEFGVELYdlnHPYQGIVHVMGPEQgVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIE 169
Cdd:cd01584 64 GAKYGIGFW---KPGSGIIHQIVLEN-YAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 170 VNGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVQ--GRL 247
Cdd:cd01584 140 LTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKatGRA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 248 HAPKGEDFTHAveywKTLKTDDNATFDTVVTLQAEEIAPQVTwgtnpgqvisvNDNIPDPASFVDPVeRASAEKALAYMG 327
Cdd:cd01584 220 EIADLADEFKD----DLLVADEGAEYDQLIEINLSELEPHIN-----------GPFTPDLATPVSKF-KEVAEKNGWPLD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 328 LKPGIpltevaidkvfIGSCTNSRIEDLRAAAEIAK---GRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWRL 404
Cdd:cd01584 284 LRVGL-----------IGSCTNSSYEDMGRAASIAKqalAHGLKCKSIFTITPGSEQIRATIERDGLLQTFRDAGGIVLA 352
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 489108948 405 PGCSMCLAMNNDR-LNPGERCA--STSNRNFEGRQGRGGRTH--LVSP 447
Cdd:cd01584 353 NACGPCIGQWDRKdIKKGEKNTivTSYNRNFTGRNDANPATHafVASP 400
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
103-435 |
1.21e-27 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 116.65 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 103 PYQGIVH----------VMGpEQGVTLPGmTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVNG 172
Cdd:PTZ00092 182 PGSGIVHqvnleylarvVFN-KDGLLYPD-SVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTG 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 173 KAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVQ--GR--LH 248
Cdd:PTZ00092 260 KLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKqtGRseEK 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 249 APKGEDFTHAVEYWKTlkTDDNATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDNIPD-------PASFVD---PVERAS 318
Cdd:PTZ00092 340 VELIEKYLKANGLFRT--YAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDftaclsaPVGFKGfgiPEEKHE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 319 AEKALAYMGLKPGIPLTEVAIDKvfIGSCTN-SRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAEAEGLD 392
Cdd:PTZ00092 418 KKVKFTYKGKEYTLTHGSVVIAA--ITSCTNtSNPSVMLAAGLLAKkavekGLKVPPYIKTSLSPGSKVVTKYLEASGLL 495
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489108948 393 KIFIEAGFEWRLPGCSMCLAMNNDRLNPGERCAS----------TSNRNFEGR 435
Cdd:PTZ00092 496 KYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITnndlvaaavlSGNRNFEGR 548
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
106-435 |
2.15e-27 |
|
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: 115.97 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 106 GIVH----------VMGPEQG---VTLPGmTIVCGDSHTATHGAFGALAFGIGTSEVEHVLAtqtlkqGRAKTMKI-EV- 170
Cdd:COG1048 176 GIVHqvnleylafvVWTREEDgetVAYPD-TLVGTDSHTTMINGLGVLGWGVGGIEAEAAML------GQPVSMLIpEVv 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 171 ----NGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVQ-- 244
Cdd:COG1048 249 gvklTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRlt 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 245 GR--LHAPKGEDFTHAVEYWKTLKTDDnATFDTVVTLQAEEIAPqvtwgtnpgqviSVN------DNIPDPASfvdpveR 316
Cdd:COG1048 329 GRseEQIELVEAYAKAQGLWRDPDAPE-PYYSDVLELDLSTVEP------------SLAgpkrpqDRIPLSDL------K 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 317 ASAEKALAYMGLKPGIPLTEVAIDKVF------------IGSCTNSRIED-LRAAAEIAK-----GRKVAPGVQALVVPG 378
Cdd:COG1048 390 EAFRAALAAPVGEELDKPVRVEVDGEEfelghgavviaaITSCTNTSNPSvMIAAGLLAKkavekGLKVKPWVKTSLAPG 469
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489108948 379 SGPVKAQAEAEGL----DKI-FIEAGFewrlpGCSMCLAmNNDRLNP---------GERCAS-TS-NRNFEGR 435
Cdd:COG1048 470 SKVVTDYLERAGLlpylEALgFNVVGY-----GCTTCIG-NSGPLPPeiseaieenDLVVAAvLSgNRNFEGR 536
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
103-435 |
9.98e-25 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 107.71 E-value: 9.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 103 PYQGIVHVMGPEQ-------------GVTLPGmTIVCGDSHTATHGAFGALAFGIGTSEVEHVLAtqtlkqGRAKTMKI- 168
Cdd:PRK12881 175 PGTGIMHQVNLEYlarvvhtkeddgdTVAYPD-TLVGTDSHTTMINGIGVLGWGVGGIEAEAVML------GQPVYMLIp 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 169 -----EVNGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYV 243
Cdd:PRK12881 248 dvvgvELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 244 Q--GRlhapkGEDFTHAVE-YWKTLK----TDDNATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDNipdPASFVDPVER 316
Cdd:PRK12881 328 RltGR-----TEAQIALVEaYAKAQGlwgdPKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNV---KSAFSDLFSK 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 317 ASAEKALAYMG---LKPGIPLTEVAIdkVFIGSCTN-SRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAE 387
Cdd:PRK12881 400 PVAENGFAKKAqtsNGVDLPDGAVAI--AAITSCTNtSNPSVLIAAGLLAKkaverGLTVKPWVKTSLAPGSKVVTEYLE 477
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 489108948 388 AEGLDKIFIEAGFEWRLPGCSMCLAMNNDRLNPGER--------CAS--TSNRNFEGR 435
Cdd:PRK12881 478 RAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQaitkndlvAAAvlSGNRNFEGR 535
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
102-446 |
1.62e-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: 99.50 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 102 HPYQGIVHVMgpEQGVTLPGMTIVCGDSHTAthgaFG-ALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVNGKAAPGITA 180
Cdd:cd01581 90 RPGDGVIHSW--LNRMLLPDTVGTGGDSHTR----FPiGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 181 KDIVLAI--------IGKTGSAGG----TGHVVEFcgEAIRALSMEGRMTLCNMAIEMGAKAGLV-APDETTFNYVQ--- 244
Cdd:cd01581 164 RDLVNAIpyyaiqqgLLTVEKKGKknvfNGRILEI--EGLPDLKVEQAFELTDASAERSAAACTVrLDKEPVIEYLEsnv 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 245 ---------GRLHAPKGEDFTHAVEYW----KTLKTDDNATFDTVVTLQAEEIapqvtwgTNPgqvISVNDNIPDPAsfv 311
Cdd:cd01581 242 vlmkimianGYDDARTLLRRIIAMEEWlanpPLLEPDADAEYAAVIEIDLDDI-------KEP---ILACPNDPDDV--- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 312 dpverasaekalaymglkpgIPLTEVA---IDKVFIGSC-TNsrIEDLRAAAEIAKGRKVAPgVQALVVPGSGPVKAQAE 387
Cdd:cd01581 309 --------------------KLLSEVAgkkIDEVFIGSCmTN--IGHFRAAAKILRGKEFKP-TRLWVAPPTRMDWAILQ 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 489108948 388 AEGLDKIFIEAGFEWRLPGCSMCLAmNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVS 446
Cdd:cd01581 366 EEGYYSIFGDAGARTEMPGCSLCMG-NQARVADGATVFSTSTRNFDNRVGKGAEVYLGS 423
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
103-435 |
2.92e-21 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 97.18 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 103 PYQGIVHVMGPE---------QGVTLPGmTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVNGK 173
Cdd:PLN00070 214 PGSGIVHQVNLEylgrvvfntDGILYPD-SVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 174 AAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVqgRLHAPKGE 253
Cdd:PLN00070 293 LRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYL--KLTGRSDE 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 254 DFTHAVEYWKTLK-------TDDNATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDNIPDPASFVD----------PVER 316
Cdd:PLN00070 371 TVAMIEAYLRANKmfvdynePQQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHSCLDnkvgfkgfavPKEA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 317 ASAEKALAYMGLKPGIPLTEVAIdkVFIGSCTN-SRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAEAEG 390
Cdd:PLN00070 451 QSKVAKFSFHGQPAELRHGSVVI--AAITSCTNtSNPSVMLGAGLVAKkacelGLEVKPWIKTSLAPGSGVVTKYLLKSG 528
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 489108948 391 LDKIFIEAGFEWRLPGCSMCLAmNNDRLNPGERCASTS-----------NRNFEGR 435
Cdd:PLN00070 529 LQKYLNQQGFHIVGYGCTTCIG-NSGELDESVASAITEndivaaavlsgNRNFEGR 583
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
118-446 |
4.47e-19 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 90.24 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 118 TLPGMTIVCGDSHTATH-G-AFGA----LAFGIGTSEV-----EHVLATQTlkqgraktmkievnGKAAPGITAKDIVLA 186
Cdd:PRK09238 476 LLPDTVGTGGDSHTRFPiGiSFPAgsglVAFAAATGVMpldmpESVLVRFK--------------GEMQPGITLRDLVHA 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 187 I----IGK----TGSAGG----TGHVVEFcgEAIRALSMEGRMTLCNMAIEMGAKAGLVA-PDETTFNYVQ--------- 244
Cdd:PRK09238 542 IpyyaIKQglltVEKKGKknifSGRILEI--EGLPDLKVEQAFELTDASAERSAAGCTIKlSKEPIIEYLRsnivllkwm 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 245 ---GRLHAPKGEDFTHAVEYW----KTLKTDDNATFDTVVTLQAEEI------APqvtwgtnpgqvisvNDniPDPASfv 311
Cdd:PRK09238 620 iaeGYGDARTLERRIAAMEEWlanpELLEADADAEYAAVIEIDLAEIkepilaCP--------------ND--PDDVR-- 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 312 dpverasaekalaymglkpgiPLTEVA---IDKVFIGSC-TNsrIEDLRAAAEIAKGRKVAPGVQALVVPgsgPVK---A 384
Cdd:PRK09238 682 ---------------------LLSEVAgtkIDEVFIGSCmTN--IGHFRAAGKLLEGKKGQLPTRLWVAP---PTKmdaD 735
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489108948 385 QAEAEGLDKIFIEAGFEWRLPGCSMCLAmNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVS 446
Cdd:PRK09238 736 QLTEEGYYSIFGKAGARIEMPGCSLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYLGS 796
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
106-435 |
4.77e-19 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 90.18 E-value: 4.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 106 GIVH----------VMGPEQGVTL--PGmTIVCGDSHTaTH-GAFGALAFGIGTSEVEHVLatqtLkqGRAKTMKI---- 168
Cdd:PRK09277 179 GICHqvnleylapvVWTREDGELVayPD-TLVGTDSHT-TMiNGLGVLGWGVGGIEAEAAM----L--GQPSSMLIpevv 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 169 --EVNGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVQ-- 244
Cdd:PRK09277 251 gvKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRlt 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 245 GRlhapkGEDFTHAVE-YWKT----LKTDDNATFDTVVTLQAEEIAPQVTWGTNPGQVISVNDNipdPASF--VDPVERA 317
Cdd:PRK09277 331 GR-----DEEQVALVEaYAKAqglwRDPLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDV---KEAFakSAELGVQ 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 318 SAEKALAYMGLKPGIPLTEVAIDKvfIGSCTN-SRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAEAEG- 390
Cdd:PRK09277 403 GFGLDEAEEGEDYELPDGAVVIAA--ITSCTNtSNPSVMIAAGLLAKkavekGLKVKPWVKTSLAPGSKVVTDYLEKAGl 480
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 391 ---LDKI-FIEAGFewrlpGCSMCLAMNNDrLNPG------ER---CAS--TSNRNFEGR 435
Cdd:PRK09277 481 lpyLEALgFNLVGY-----GCTTCIGNSGP-LPPEiekainDNdlvVTAvlSGNRNFEGR 534
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
103-435 |
7.18e-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: 85.43 E-value: 7.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 103 PYQGIVH----------VMGPE---QGVTLPGmTIVCGDSHTATHGAFGALAFGIGTSEVEHVLAtqtlkqGRAKTMKI- 168
Cdd:cd01586 91 PGTGIIHqvnleylarvVFTSEedgDGVAYPD-SVVGTDSHTTMINGLGVLGWGVGGIEAEAVML------GQPISMLLp 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 169 -----EVNGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDettfnyv 243
Cdd:cd01586 164 evvgvKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD------- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 244 qgrlhapkgedfthaveywktlktddnatfDTVVTLQAEEIAPQVTWGTNPgqvisvNDNIPDPASFVdpverasaekaL 323
Cdd:cd01586 237 ------------------------------TQVVELDLSTVEPSVSGPKRP------QDRVPLHGSVV-----------I 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 324 AYmglkpgipltevaidkvfIGSCTN-SRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIE 397
Cdd:cd01586 270 AA------------------ITSCTNtSNPSVMLAAGLLAKkavelGLKVKPYVKTSLAPGSRVVTKYLEASGLLPYLEK 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 489108948 398 AGFEWRLPGCSMCLAmNNDRLNP---------GERCAS--TSNRNFEGR 435
Cdd:cd01586 332 LGFHVVGYGCTTCIG-NSGPLPEeveeaikenDLVVAAvlSGNRNFEGR 379
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
91-446 |
3.41e-16 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 81.51 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 91 NEFGVELydlnHPYQGIVHVMgpEQGVTLPGMTIVCGDSHTAthgaFG-ALAFGIGTSEVEHVLATQTLKQGRAKTMKIE 169
Cdd:PLN00094 529 NRGGVSL----RPGDGVIHSW--LNRMLLPDTVGTGGDSHTR----FPiGISFPAGSGLVAFGAATGVIPLDMPESVLVR 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 170 VNGKAAPGITAKDIVLAI-----------IGKTGSAGG-TGHVVEFcgEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDE 237
Cdd:PLN00094 599 FTGTMQPGITLRDLVHAIpytaiqdglltVEKKGKKNVfSGRILEI--EGLPHLKCEQAFELSDASAERSAAGCTIKLDK 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 238 TTF-NYVQGRLHAPK-------GEDFT-----HAVEYW----KTLKTDDNATFDTVVTLQAEEIapqvtwgTNPgqvISV 300
Cdd:PLN00094 677 EPIiEYLNSNVVMLKwmiaegyGDRRTlerriARMQQWladpELLEADPDAEYAAVIEIDMDEI-------KEP---ILC 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 301 NDNIPDPASFvdpverasaekalaymglkpgipLTEVA---IDKVFIGSC-TNsrIEDLRAAAEIAKGRKVAPGVQALVV 376
Cdd:PLN00094 747 APNDPDDARL-----------------------LSEVTgdkIDEVFIGSCmTN--IGHFRAAGKLLNDNLSQLPTRLWVA 801
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 377 PGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAmNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVS 446
Cdd:PLN00094 802 PPTKMDEAQLKAEGYYSTFGTVGARTEMPGCSLCMG-NQARVAEKSTVVSTSTRNFPNRLGKGANVYLAS 870
|
|
| AcnB |
COG1049 |
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ... |
333-446 |
4.84e-16 |
|
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440670 [Multi-domain] Cd Length: 852 Bit Score: 81.05 E-value: 4.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 333 PLTEVA---IDKVFIGSC-TNsrIEDLRAAAEIAKGRKVAPgVQALVVPgsgPVK---AQAEAEGLDKIFIEAGFEWRLP 405
Cdd:COG1049 682 LLSEVAgtkIDEVFIGSCmTN--IGHFRAAGKLLEGKGNLP-TRLWIAP---PTKmdeAQLTEEGYYSIFGAAGARTEMP 755
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489108948 406 GCSMCLAmNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVS 446
Cdd:COG1049 756 GCSLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYLGS 795
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
121-437 |
2.54e-15 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 78.51 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 121 GMTIVCGDSHTaTHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVNGKAAPGITAKDIVLAIIGKTGSAGGTGH- 199
Cdd:PRK11413 142 GKMILGSDSHT-RYGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVKNk 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 200 VVEFCGEAIRALSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVqgRLHApKGEDFthaveywKTLKTDDNATFDTVVTL 279
Cdd:PRK11413 221 VMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWL--ALHG-RGQDY-------CELNPQPMAYYDGCISV 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 280 QAEEIAPQVTWGTNPGQVISV---NDNIPDPASFVDPVERASAEKALAYmGLKPGIPLTEVAIDKVFIGSCTNSRIEDLR 356
Cdd:PRK11413 291 DLSAIKPMIALPFHPSNVYEIdelNQNLTDILREVEIESERVAHGKAKL-SLLDKIENGRLKVQQGIIAGCSGGNYENVI 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108948 357 AAAEIAKGRKVAPGVQAL-VVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNDRLNPGERCASTSnRNFEGR 435
Cdd:PRK11413 370 AAANALRGQSCGNDTFSLsVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFGAGDTPANNGLSIRHTT-RNFPNR 448
|
..
gi 489108948 436 QG 437
Cdd:PRK11413 449 EG 450
|
|
| |
