|
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: 1021.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 1 MAKTLYEKLFDAHVVYEAENETPLLYIDRHLVHEVTSPQAFDGLRAHGRPVRQPGKTFATMDHNVSTQTKDINACGEMAR 80
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLPIADPVSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 81 IQMQELIKNCKEFGVELYDLNHPYQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQ 160
Cdd:PRK05478 81 IQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 161 GRAKTMKIEVQGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTF 240
Cdd:PRK05478 161 KKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 241 NYVKGRLHAPKGKDFDDAVAYWKTLQTDEGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDNIPDPASFADPVERASAE 320
Cdd:PRK05478 241 EYLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVKRASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 321 KALAYMGLKPGILLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGF 400
Cdd:PRK05478 321 RALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829330 401 EWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAVTGHFADIRNIK 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: 946.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 1 MAKTLYEKLFDAHVVYEAENETPLLYIDRHLVHEVTSPQAFDGLRAHGRPVRQPGKTFATMDHNVSTQTKDINACGEMAR 80
Cdd:TIGR00170 1 MPRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFNIKDEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 81 IQMQELIKNCKEFGVELYDLNHPYQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQ 160
Cdd:TIGR00170 81 IQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 161 GRAKTMKIEVQGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTF 240
Cdd:TIGR00170 161 ARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 241 NYVKGRLHAPKGKDFDDAVAYWKTLQTDEGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDNIPDPASFADPVERASAE 320
Cdd:TIGR00170 241 EYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 321 KALAYMGLKPGILLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGF 400
Cdd:TIGR00170 321 RALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829330 401 EWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAVTGHFADIRNI 465
Cdd:TIGR00170 401 EWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| 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: 713.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 1 MAKTLYEKLFDAHVVYEAE-NETPLLYIDRHLVHEVTSPQAFDGLRAHG-RPVRQPGKTFATMDHNVSTQTkdinacgEM 78
Cdd:COG0065 1 MGMTLAEKILARHAGREVEpGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPTKD-------PK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 79 ARIQMQELIKNCKEFGVELYDLNHPyqGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTL 158
Cdd:COG0065 74 SAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 159 KQGRAKTMKIEVQGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDET 238
Cdd:COG0065 152 WFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 239 TFNYVKGRLHAPkgkdfddavayWKTLQTDEGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDnipdpasfadpveras 318
Cdd:COG0065 232 TFEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE---------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 319 aekalaymglkpgilLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEA 398
Cdd:COG0065 285 ---------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEA 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829330 399 GFEWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGR-GGRTHLVSPAMAAAAAVTGHFADIRNI 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: 694.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 7 EKLFDAHVVYEAENEtpLLYI-DRHLVHEVTSPQAFDGLRAHGRPVRQPGKTFATMDHNVST--------QTKDINACGE 77
Cdd:pfam00330 1 EKIWDAHLVEELDGS--LLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTdlvidhapDALDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 78 MARI--QMQELIKNCKEFGVELYDlnhPYQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLAT 155
Cdd:pfam00330 79 ISRNkeQYDFLEWNAKKFGIRFVP---PGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 156 QTLKQGRAKTMKIEVQGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAP 235
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 236 DETTFNYVK--GRLHAPKGKDFDDAVAyWKTLQTDEGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDNIPDPasFADP 313
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDP--FADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 314 VERASAEKALAYMGLKPGILLTEVAIDKVFIGSCTNSRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAEA 388
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15829330 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: 611.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 29 RHLVHEVTSPQAFDGLRAHGRP-VRQPGKTFATMDHNVSTQtkdinacGEMARIQMQELIKNCKEFGVELYDLNhpYQGI 107
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREkVWDPEKIVAVFDHNVPTP-------DIKAAEQVKTLRKFAKEFGINFFDVG--RQGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 108 VHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVQGKAAPGITAKDIVLAI 187
Cdd:cd01583 72 CHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 188 IGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVKGRLHapkgkdfddavAYWKTLQT 267
Cdd:cd01583 152 IGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGK-----------AYWKELKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 268 DEGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDNIPdpasfadpverasaekalaymglkpgillteVAIDKVFIGSC 347
Cdd:cd01583 221 DEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQVFIGSC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 348 TNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNDRLNPGERCAST 427
Cdd:cd01583 270 TNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVST 349
|
410 420 430
....*....|....*....|....*....|...
gi 15829330 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 |
1.58e-87 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 273.94 E-value: 1.58e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 4 TLYEKLFDAHVVYEA-ENETPLLYIDRHLVHEVTSPQAFDGLRAHGRPVRQPGKTFATMDHNVSTQTkdINACgemariQ 82
Cdd:NF040615 2 TLAEKILSKKLGKEVyAGDTVEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPANT--VKAA------N 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 83 MQELIKN-CKEFGVELYDLNHpyQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQG 161
Cdd:NF040615 74 MQKITREfVKEQGIKNFYLGG--EGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 162 RAKTMKIEVQGKAaPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTFN 241
Cdd:NF040615 152 VPKTIRVNIVGKN-ENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 242 YVKgrlhapKGKDFDDAVAYWKTLQ---TDEGATFDTVVTLQAEEISPQVTWGTNPgqvisvnDNIpdpasfadpveras 318
Cdd:NF040615 231 YLR------KEGVSEEEIAELKKNRitvNEKEENYYKEIEIDITDMEEQVACPHHP-------DNV-------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 319 aekalaymglKPGILLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEA 398
Cdd:NF040615 284 ----------KPVSEVEGTEIDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKA 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829330 399 GFEWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGR-GGRTHLVSPAMAAAAAVTGH 458
Cdd:NF040615 354 GAMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGNiNSYIYLSSPKIAAKSAVKGY 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: 1021.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 1 MAKTLYEKLFDAHVVYEAENETPLLYIDRHLVHEVTSPQAFDGLRAHGRPVRQPGKTFATMDHNVSTQTKDINACGEMAR 80
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLPIADPVSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 81 IQMQELIKNCKEFGVELYDLNHPYQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQ 160
Cdd:PRK05478 81 IQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 161 GRAKTMKIEVQGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTF 240
Cdd:PRK05478 161 KKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 241 NYVKGRLHAPKGKDFDDAVAYWKTLQTDEGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDNIPDPASFADPVERASAE 320
Cdd:PRK05478 241 EYLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVKRASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 321 KALAYMGLKPGILLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGF 400
Cdd:PRK05478 321 RALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829330 401 EWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAVTGHFADIRNIK 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: 946.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 1 MAKTLYEKLFDAHVVYEAENETPLLYIDRHLVHEVTSPQAFDGLRAHGRPVRQPGKTFATMDHNVSTQTKDINACGEMAR 80
Cdd:TIGR00170 1 MPRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFNIKDEVAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 81 IQMQELIKNCKEFGVELYDLNHPYQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQ 160
Cdd:TIGR00170 81 IQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 161 GRAKTMKIEVQGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTF 240
Cdd:TIGR00170 161 ARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 241 NYVKGRLHAPKGKDFDDAVAYWKTLQTDEGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDNIPDPASFADPVERASAE 320
Cdd:TIGR00170 241 EYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKASAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 321 KALAYMGLKPGILLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGF 400
Cdd:TIGR00170 321 RALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829330 401 EWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAVTGHFADIRNI 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: 817.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 1 MAKTLYEKLFDAHVVYEAENETPLLYIDRHLVHEVTSPQAFDGLRAHGRPVRQPGKTFATMDHNVSTQTK-DINACGEMA 79
Cdd:PRK12466 2 MPRTLYDKLWDSHTVARLDDGHVLLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPTRPGrDRGITDPGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 80 RIQMQELIKNCKEFGVELYDLNHPYQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLK 159
Cdd:PRK12466 82 ALQVDYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQTLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 160 QGRAKTMKIEVQGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETT 239
Cdd:PRK12466 162 YRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 240 FNYVKGRLHAPKGKDFDDAVAYWKTLQTDEGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDNIPDPASFADPVERASA 319
Cdd:PRK12466 242 FDYLRGRPRAPKGALWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAAEADPARRAAM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 320 EKALAYMGLKPGILLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAG 399
Cdd:PRK12466 322 ERALDYMGLTPGTPLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAG 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829330 400 FEWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAVTGHFADIRNI 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: 713.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 1 MAKTLYEKLFDAHVVYEAE-NETPLLYIDRHLVHEVTSPQAFDGLRAHG-RPVRQPGKTFATMDHNVSTQTkdinacgEM 78
Cdd:COG0065 1 MGMTLAEKILARHAGREVEpGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPTKD-------PK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 79 ARIQMQELIKNCKEFGVELYDLNHPyqGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTL 158
Cdd:COG0065 74 SAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 159 KQGRAKTMKIEVQGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDET 238
Cdd:COG0065 152 WFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDET 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 239 TFNYVKGRLHAPkgkdfddavayWKTLQTDEGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDnipdpasfadpveras 318
Cdd:COG0065 232 TFEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE---------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 319 aekalaymglkpgilLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEA 398
Cdd:COG0065 285 ---------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEA 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829330 399 GFEWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGR-GGRTHLVSPAMAAAAAVTGHFADIRNI 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: 694.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 7 EKLFDAHVVYEAENEtpLLYI-DRHLVHEVTSPQAFDGLRAHGRPVRQPGKTFATMDHNVST--------QTKDINACGE 77
Cdd:pfam00330 1 EKIWDAHLVEELDGS--LLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTdlvidhapDALDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 78 MARI--QMQELIKNCKEFGVELYDlnhPYQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLAT 155
Cdd:pfam00330 79 ISRNkeQYDFLEWNAKKFGIRFVP---PGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 156 QTLKQGRAKTMKIEVQGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAP 235
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 236 DETTFNYVK--GRLHAPKGKDFDDAVAyWKTLQTDEGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDNIPDPasFADP 313
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDP--FADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 314 VERASAEKALAYMGLKPGILLTEVAIDKVFIGSCTNSRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAEA 388
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15829330 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: 611.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 29 RHLVHEVTSPQAFDGLRAHGRP-VRQPGKTFATMDHNVSTQtkdinacGEMARIQMQELIKNCKEFGVELYDLNhpYQGI 107
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREkVWDPEKIVAVFDHNVPTP-------DIKAAEQVKTLRKFAKEFGINFFDVG--RQGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 108 VHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVQGKAAPGITAKDIVLAI 187
Cdd:cd01583 72 CHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 188 IGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVKGRLHapkgkdfddavAYWKTLQT 267
Cdd:cd01583 152 IGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGK-----------AYWKELKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 268 DEGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDNIPdpasfadpverasaekalaymglkpgillteVAIDKVFIGSC 347
Cdd:cd01583 221 DEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQVFIGSC 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 348 TNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNDRLNPGERCAST 427
Cdd:cd01583 270 TNGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVST 349
|
410 420 430
....*....|....*....|....*....|...
gi 15829330 428 SNRNFEGRQG-RGGRTHLVSPAMAAAAAVTGHF 459
Cdd:cd01583 350 SNRNFKGRMGsPGARIYLASPATAAASAITGEI 382
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
1-465 |
2.69e-133 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 391.08 E-value: 2.69e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 1 MAKTLYEKLFDAHVVYEAE-NETPLLYIDRHLVHEVTSPQAFDGLRAHG-RPVRQPGKTFATMDHNVSTqtKDINAcgem 78
Cdd:PRK00402 1 MGMTLAEKILARHSGRDVSpGDIVEAKVDLVMAHDITGPLAIKEFEKIGgDKVFDPSKIVIVFDHFVPA--KDIKS---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 79 ARIQmqeliKNCKEFGVElYDLNHPY---QGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLAT 155
Cdd:PRK00402 75 AEQQ-----KILREFAKE-QGIPNFFdvgEGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 156 qtlkqGRA-----KTMKIEVQGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKA 230
Cdd:PRK00402 149 -----GKTwfkvpETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 231 GLVAPDETTFNYVKGRLHAPkgkdfddavayWKTLQTDEGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDnipdpasf 310
Cdd:PRK00402 224 GIFAPDEKTLEYLKERAGRD-----------YKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSE-------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 311 adpverasaekalaymglkpgilLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEG 390
Cdd:PRK00402 285 -----------------------VEGTKVDQVFIGSCTNGRLEDLRIAAEILKGRKVAPGVRLIVIPASQKIYLQALKEG 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829330 391 LDKIFIEAGFEWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQG-RGGRTHLVSPAMAAAAAVTGHFADIRNI 465
Cdd:PRK00402 342 LIEIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGsPESEVYLASPAVAAASAVTGKITDPREV 417
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
4-463 |
3.63e-110 |
|
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: 331.72 E-value: 3.63e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 4 TLYEKLFDAHVVYEA-ENETPLLYIDRHLVHEVTSPQAFDGLRAHGRP-VRQPGKTFATMDHNVSTqtKDINACgemari 81
Cdd:TIGR01343 1 TIAEKILSKKSGKEVyAGDLIEAEIDLAMVHDITAPLAIKTLEEYGIDkVWNPEKIVIVFDHQVPA--DTIKAA------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 82 QMQELIKN-CKEFGVElyDLNHPYQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQ 160
Cdd:TIGR01343 73 EMQKLAREfVKKQGIK--YFYDVGEGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 161 GRAKTMKIEVQGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTF 240
Cdd:TIGR01343 151 KVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 241 NYVKGRLHAPkgkdfddavayWKTLQTDEGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDnipdpasfadpverasae 320
Cdd:TIGR01343 231 QYLKERRKEP-----------FRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSE------------------ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 321 kalaymglkpgilLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGF 400
Cdd:TIGR01343 282 -------------VEGTEIDQVFIGSCTNGRLEDLRVAAKILKGRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGA 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829330 401 EWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQG-RGGRTHLVSPAMAAAAAVTGHFADIR 463
Cdd:TIGR01343 349 VVSTPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMGhPNAEIYLASPATAAASAVKGYIADPR 412
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
3-461 |
2.20e-96 |
|
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA family (Homoaconitate hydratase family, TIGR01343) and is most closely related to the 3-isopropylmalate dehydratase, large subunits which form TIGR00170. This subfamily includes the members of TIGR01343 which are gene clustered with other genes of leucine biosynthesis. The rest of the subfamily includes mainly archaeal species which exhibit two hits to this model. In these cases it is possible that one or the other of the hits does not have a 3-isopropylmalate dehydratase activity but rather one of the other related aconitase-like activities.
Pssm-ID: 273960 Cd Length: 413 Bit Score: 296.29 E-value: 2.20e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 3 KTLYEKLFDAHVVYEAE-NETPLLYIDRHLVHEVTSPQAFDGLRAHGR-PVRQPGKTFATMDHNVSTQTKdinacgEMAR 80
Cdd:TIGR02086 1 MTLAEKILSEKVGRPVCaGEIVEVEVDLAMTHDGTGPLAIKALRELGVaRVWDPEKIVIAFDHNVPPPTV------EAAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 81 IQmQELIKNCKEFGVELYDLNhpyQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQ 160
Cdd:TIGR02086 75 MQ-KEIREFAKRHGIKNFDVG---EGICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTWI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 161 GRAKTMKIEVQGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTF 240
Cdd:TIGR02086 151 KVPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEETY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 241 NYVKGRlhapKGKDFddavaywKTLQTDEGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDnipdpasfadpVErasae 320
Cdd:TIGR02086 231 EYLKKR----RGLEF-------RILVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVSD-----------VE----- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 321 kalaymGLKpgilltevaIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGF 400
Cdd:TIGR02086 284 ------GTE---------IDQVFIGSCTNGRLEDLRIAAEILKGRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAGA 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829330 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 |
1.58e-87 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 273.94 E-value: 1.58e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 4 TLYEKLFDAHVVYEA-ENETPLLYIDRHLVHEVTSPQAFDGLRAHGRPVRQPGKTFATMDHNVSTQTkdINACgemariQ 82
Cdd:NF040615 2 TLAEKILSKKLGKEVyAGDTVEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPANT--VKAA------N 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 83 MQELIKN-CKEFGVELYDLNHpyQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQG 161
Cdd:NF040615 74 MQKITREfVKEQGIKNFYLGG--EGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 162 RAKTMKIEVQGKAaPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTFN 241
Cdd:NF040615 152 VPKTIRVNIVGKN-ENISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 242 YVKgrlhapKGKDFDDAVAYWKTLQ---TDEGATFDTVVTLQAEEISPQVTWGTNPgqvisvnDNIpdpasfadpveras 318
Cdd:NF040615 231 YLR------KEGVSEEEIAELKKNRitvNEKEENYYKEIEIDITDMEEQVACPHHP-------DNV-------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 319 aekalaymglKPGILLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEA 398
Cdd:NF040615 284 ----------KPVSEVEGTEIDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKA 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829330 399 GFEWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGR-GGRTHLVSPAMAAAAAVTGH 458
Cdd:NF040615 354 GAMICTPGCGPCLGAHQGVLGDGEVCLSTTNRNFKGRMGNiNSYIYLSSPKIAAKSAVKGY 414
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
31-447 |
5.10e-69 |
|
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Aconitase catalytic domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. Aconitase, in its active form, contains a 4Fe-4S iron-sulfur cluster; three cysteine residues have been shown to be ligands of the 4Fe-4S cluster. This is the Aconitase core domain, including structural domains 1, 2 and 3, which binds the Fe-S cluster. The aconitase family also contains the following proteins: - Iron-responsive element binding protein (IRE-BP), a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid.
Pssm-ID: 153129 [Multi-domain] Cd Length: 389 Bit Score: 225.07 E-value: 5.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 31 LVHEVTSPQAFDGLRAHGRP--VRQPGKTFATMDHNVSTQtKDINACGEmariqmQELIKNCKEFGVELYDlnhPYQGIV 108
Cdd:cd01351 3 MLQDATGPMAMKAFEILAALgkVADPSQIACVHDHAVQLE-KPVNNEGH------KFLSFFAALQGIAFYR---PGVGII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 109 HVMGPEQGVtLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVQGKAAPGITAKDIVLAII 188
Cdd:cd01351 73 HQIMVENLA-LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 189 GKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVKGRLHaPKGKDFDDAvaYWKTLQTD 268
Cdd:cd01351 152 GIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGR-PLLKNLWLA--FPEELLAD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 269 EGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDnipdpasfadpverasaekalaymglkpgilLTEVAIDKVFIGSCT 348
Cdd:cd01351 229 EGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSE-------------------------------VEGTKIDQVLIGSCT 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 349 NSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNDRLNPGERCASTS 428
Cdd:cd01351 278 NNRYSDMLAAAKLLKGAKVAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLVADGEVGVSSG 357
|
410 420
....*....|....*....|
gi 15829330 429 NRNFEGRQGRG-GRTHLVSP 447
Cdd:cd01351 358 NRNFPGRLGTYeRHVYLASP 377
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
1-464 |
5.47e-51 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 183.04 E-value: 5.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 1 MAKTLYEKLFDAHVV---YEAENETpLLYIDRHLVHEVTSPQAFDGLRAHGRP-VRQPgKTFATMDHNVsTQTKDINAcg 76
Cdd:PRK07229 1 MGLTLTEKILYAHLVegeLEPGEEI-AIRIDQTLTQDATGTMAYLQFEAMGLDrVKTE-LSVQYVDHNL-LQADFENA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 77 emariqmqE----LIKNCKEFGVelyDLNHPYQGIVHVMGPEQ-GVtlPGMTIVCGDSHTATHGAFGALAFGIGTSEVEH 151
Cdd:PRK07229 76 --------DdhrfLQSVAAKYGI---YFSKPGNGICHQVHLERfAF--PGKTLLGSDSHTPTAGGLGMLAIGAGGLDVAL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 152 VLATQ--TLKQgrAKTMKIEVQGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAK 229
Cdd:PRK07229 143 AMAGGpyYLKM--PKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGAT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 230 AGLVAPDETTFNYVK--GRlhapkGKDfddavayWKTLQTDEGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDnipdp 307
Cdd:PRK07229 221 TSIFPSDERTREFLKaqGR-----EDD-------WVELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVSE----- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 308 asfadpverasaekalaymglkpgilLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAE 387
Cdd:PRK07229 284 --------------------------VAGIKVDQVLIGSCTNSSYEDLMRAASILKGKKVHPKVSLVINPGSRQVLEMLA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 388 AEGLDKIFIEAG---FEwrlPGCSMCLAMNNDrlnPGERCAS--TSNRNFEGRQG-RGGRTHLVSPAMAAAAAVTGHFAD 461
Cdd:PRK07229 338 RDGALADLIAAGariLE---NACGPCIGMGQA---PATGNVSlrTFNRNFPGRSGtKDAQVYLASPETAAASALTGVITD 411
|
...
gi 15829330 462 IRN 464
Cdd:PRK07229 412 PRT 414
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
103-459 |
5.23e-48 |
|
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: 169.17 E-value: 5.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 103 PYQGIVHVMGPEQgVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVQGKAAPGITAKD 182
Cdd:cd01585 66 PGNGICHQVHLER-FAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKD 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 183 IVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVkgrlhAPKGKDFDdavayW 262
Cdd:cd01585 145 VILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFL-----AAQGREDD-----W 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 263 KTLQTDEGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDnipdpasfadpVErasaekalaymGLKpgilltevaIDKV 342
Cdd:cd01585 215 VELAADADAEYDEEIEIDLSELEPLIARPHSPDNVVPVRE-----------VA-----------GIK---------VDQV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 343 FIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNdrlNPGE 422
Cdd:cd01585 264 AIGSCTNSSYEDLMTVAAILKGRRVHPHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQ---APPT 340
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15829330 423 RCAS--TSNRNFEGRQG-RGGRTHLVSPAMAAAAAVTGHF 459
Cdd:cd01585 341 GGVSvrTFNRNFEGRSGtKDDLVYLASPEVAAAAALTGVI 380
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
31-457 |
6.03e-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: 141.98 E-value: 6.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 31 LVHEVTSPQAFDGLRAHGRPVRQPGKTFATMDHNVSTQTKdinacgemARIQMQELIKN-CKEFGVELYDLNhpyQGIVH 109
Cdd:cd01582 3 MTHDNSWPVALKFMSIGATKIHNPDQIVMTLDHDVQNKSE--------KNLKKYKNIESfAKKHGIDFYPAG---RGIGH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 110 VMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLAT-QTLKQgRAKTMKIEVQGKAAPGITAKDIVLAII 188
Cdd:cd01582 72 QIMIEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATgQTWWQ-IPPVAKVELKGQLPKGVTGKDVIVALC 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 189 GKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDEttfnyvkgrlhapkgkdfddavaywKTLqtd 268
Cdd:cd01582 151 GLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDA-------------------------KHL--- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 269 egatfdtvvTLQAEEISPQVTWgtnpgqvisvndniPDPASFADPVERASAEkalaymglkpgilltEVAIDKVFIGSCT 348
Cdd:cd01582 203 ---------ILDLSTLSPYVSG--------------PNSVKVSTPLKELEAQ---------------NIKINKAYLVSCT 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 349 NSRIEDLRAAAEIAKGRK-------VAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNDRLNPG 421
Cdd:cd01582 245 NSRASDIAAAADVVKGKKekngkipVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQGLLEPG 324
|
410 420 430
....*....|....*....|....*....|....*..
gi 15829330 422 ERCASTSNRNFEGRQG-RGGRTHLVSPAMAAAAAVTG 457
Cdd:cd01582 325 EVGISATNRNFKGRMGsTEALAYLASPAVVAASAISG 361
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
90-447 |
1.81e-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: 122.16 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 90 CKEFGVELYdlnHPYQGIVHVMGPEQgVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIE 169
Cdd:cd01584 64 GAKYGIGFW---KPGSGIIHQIVLEN-YAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 170 VQGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVK--GRL 247
Cdd:cd01584 140 LTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKatGRA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 248 H-APKGKDFDDavaywKTLQTDEGATFDTVVTLQAEEISPQVtwgtnpgqvisvndNIPDPASFADPVER--ASAEKALA 324
Cdd:cd01584 220 EiADLADEFKD-----DLLVADEGAEYDQLIEINLSELEPHI--------------NGPFTPDLATPVSKfkEVAEKNGW 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 325 YMGLKPGIlltevaidkvfIGSCTNSRIEDLRAAAEIAK---GRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFE 401
Cdd:cd01584 281 PLDLRVGL-----------IGSCTNSSYEDMGRAASIAKqalAHGLKCKSIFTITPGSEQIRATIERDGLLQTFRDAGGI 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 15829330 402 WRLPGCSMCLAMNNDR-LNPGERCA--STSNRNFEGRQGRGGRTH--LVSP 447
Cdd:cd01584 350 VLANACGPCIGQWDRKdIKKGEKNTivTSYNRNFTGRNDANPATHafVASP 400
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
103-435 |
5.63e-28 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 117.81 E-value: 5.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 103 PYQGIVH----------VMGpEQGVTLPGmTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVQG 172
Cdd:PTZ00092 182 PGSGIVHqvnleylarvVFN-KDGLLYPD-SVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTG 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 173 KAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVK--GRlhaP 250
Cdd:PTZ00092 260 KLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKqtGR---S 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 251 KGK-DFDDAVAYWKTLQTDEGA--TFDTVVTLQAEEISPQVTWGTNPGQVISVNDNIPD-------PASF---ADPVERA 317
Cdd:PTZ00092 337 EEKvELIEKYLKANGLFRTYAEqiEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDftaclsaPVGFkgfGIPEEKH 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 318 SAEKALAYMGLKPGILLTEVAIDKvfIGSCTN-SRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAEAEGL 391
Cdd:PTZ00092 417 EKKVKFTYKGKEYTLTHGSVVIAA--ITSCTNtSNPSVMLAAGLLAKkavekGLKVPPYIKTSLSPGSKVVTKYLEASGL 494
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15829330 392 DKIFIEAGFEWRLPGCSMCLAMNNDRLNPGERCAS----------TSNRNFEGR 435
Cdd:PTZ00092 495 LKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITnndlvaaavlSGNRNFEGR 548
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
106-435 |
3.76e-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: 115.20 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 106 GIVH----------VMGPEQG---VTLPGmTIVCGDSHTATHGAFGALAFGIGTSEVEHVLAtqtlkqGRAKTMKI-EV- 170
Cdd:COG1048 176 GIVHqvnleylafvVWTREEDgetVAYPD-TLVGTDSHTTMINGLGVLGWGVGGIEAEAAML------GQPVSMLIpEVv 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 171 ----QGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVK-- 244
Cdd:COG1048 249 gvklTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRlt 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 245 GRlhapkGKDFDDAV-AY------WKTLQTDEgATFDTVVTLQAEEISPqvtwgtnpgqviSVN------DNIPDPASfa 311
Cdd:COG1048 329 GR-----SEEQIELVeAYakaqglWRDPDAPE-PYYSDVLELDLSTVEP------------SLAgpkrpqDRIPLSDL-- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 312 dpveRASAEKALAYMGLKPGILLTEVAIDKVF------------IGSCTNSRIED-LRAAAEIAK-----GRKVAPGVQA 373
Cdd:COG1048 389 ----KEAFRAALAAPVGEELDKPVRVEVDGEEfelghgavviaaITSCTNTSNPSvMIAAGLLAKkavekGLKVKPWVKT 464
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829330 374 LVVPGSGPVKAQAEAEGL----DKI-FIEAGFewrlpGCSMCLAmNNDRLNP---------GERCAS-TS-NRNFEGR 435
Cdd:COG1048 465 SLAPGSKVVTDYLERAGLlpylEALgFNVVGY-----GCTTCIG-NSGPLPPeiseaieenDLVVAAvLSgNRNFEGR 536
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
103-435 |
9.11e-25 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 107.71 E-value: 9.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 103 PYQGIVHVMGPEQ-------------GVTLPGmTIVCGDSHTATHGAFGALAFGIGTSEVEHVLAtqtlkqGRAKTMKI- 168
Cdd:PRK12881 175 PGTGIMHQVNLEYlarvvhtkeddgdTVAYPD-TLVGTDSHTTMINGIGVLGWGVGGIEAEAVML------GQPVYMLIp 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 169 -----EVQGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYV 243
Cdd:PRK12881 248 dvvgvELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 244 KGrlhapKGKDfDDAVA----YWKT----LQTDEGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDNipdPASFADPVE 315
Cdd:PRK12881 328 RL-----TGRT-EAQIAlveaYAKAqglwGDPKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNV---KSAFSDLFS 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 316 RASAEKALAYMG-LKPGILLTEVAIDKVFIGSCTN-SRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAEA 388
Cdd:PRK12881 399 KPVAENGFAKKAqTSNGVDLPDGAVAIAAITSCTNtSNPSVLIAAGLLAKkaverGLTVKPWVKTSLAPGSKVVTEYLER 478
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15829330 389 EGLDKIFIEAGFEWRLPGCSMCLAMNNDRLNPGER--------CAS--TSNRNFEGR 435
Cdd:PRK12881 479 AGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQaitkndlvAAAvlSGNRNFEGR 535
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
102-446 |
2.20e-23 |
|
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: 102.19 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 102 HPYQGIVHVMgpEQGVTLPGMTIVCGDSHTAthgaFG-ALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVQGKAAPGITA 180
Cdd:cd01581 90 RPGDGVIHSW--LNRMLLPDTVGTGGDSHTR----FPiGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 181 KDIVLAI--------IGKTGSAGG----TGHVVEFcgEAIRDLSMEGRMTLCNMAIEMGAKAGLV-APDETTFNYVKG-- 245
Cdd:cd01581 164 RDLVNAIpyyaiqqgLLTVEKKGKknvfNGRILEI--EGLPDLKVEQAFELTDASAERSAAACTVrLDKEPVIEYLESnv 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 246 -RLHAPKGKDFDDAvaywKTLQTDEGATFDTVVTLQAEEISPQVTWGTnpgqVISVN-DNIPDPAsFADPVERASAekal 323
Cdd:cd01581 242 vLMKIMIANGYDDA----RTLLRRIIAMEEWLANPPLLEPDADAEYAA----VIEIDlDDIKEPI-LACPNDPDDV---- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 324 aymglkpgILLTEVA---IDKVFIGSC-TNsrIEDLRAAAEIAKGRKVAPgVQALVVPGSGPVKAQAEAEGLDKIFIEAG 399
Cdd:cd01581 309 --------KLLSEVAgkkIDEVFIGSCmTN--IGHFRAAAKILRGKEFKP-TRLWVAPPTRMDWAILQEEGYYSIFGDAG 377
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15829330 400 FEWRLPGCSMCLAmNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVS 446
Cdd:cd01581 378 ARTEMPGCSLCMG-NQARVADGATVFSTSTRNFDNRVGKGAEVYLGS 423
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
103-435 |
2.89e-22 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 100.26 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 103 PYQGIVHVMGPE---------QGVTLPGmTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVQGK 173
Cdd:PLN00070 214 PGSGIVHQVNLEylgrvvfntDGILYPD-SVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 174 AAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVK--GR----- 246
Cdd:PLN00070 293 LRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKltGRsdetv 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 247 ------LHApkGKDFDDavayWKTLQTDEgaTFDTVVTLQAEEISPQVTWGTNPGQVISVNDNIPDPAS----------F 310
Cdd:PLN00070 373 amieayLRA--NKMFVD----YNEPQQER--VYSSYLELDLEDVEPCISGPKRPHDRVPLKEMKADWHScldnkvgfkgF 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 311 ADPVERASAEKALAYMGLKPGILLTEVAIdkVFIGSCTN-SRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKA 384
Cdd:PLN00070 445 AVPKEAQSKVAKFSFHGQPAELRHGSVVI--AAITSCTNtSNPSVMLGAGLVAKkacelGLEVKPWIKTSLAPGSGVVTK 522
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829330 385 QAEAEGLDKIFIEAGFEWRLPGCSMCLAmNNDRLNPGERCASTS-----------NRNFEGR 435
Cdd:PLN00070 523 YLLKSGLQKYLNQQGFHIVGYGCTTCIG-NSGELDESVASAITEndivaaavlsgNRNFEGR 583
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
118-446 |
5.56e-20 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 92.93 E-value: 5.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 118 TLPGMTIVCGDSHTATH-G-AFGA----LAFGIGTSEV-----EHVLATQTlkqgraktmkievqGKAAPGITAKDIVLA 186
Cdd:PRK09238 476 LLPDTVGTGGDSHTRFPiGiSFPAgsglVAFAAATGVMpldmpESVLVRFK--------------GEMQPGITLRDLVHA 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 187 I----IGK----TGSAGG----TGHVVEFcgEAIRDLSMEGRMTLCNMAIEMGAKAGLVA-PDETTFNYVK---GRLHAP 250
Cdd:PRK09238 542 IpyyaIKQglltVEKKGKknifSGRILEI--EGLPDLKVEQAFELTDASAERSAAGCTIKlSKEPIIEYLRsniVLLKWM 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 251 KGKDFDDAvaywKTLQTdegatfdtvvtlQAEEISpqvTWGTNPgQVISVNDNipdpASFADPVERASAEkalaymgLKP 330
Cdd:PRK09238 620 IAEGYGDA----RTLER------------RIAAME---EWLANP-ELLEADAD----AEYAAVIEIDLAE-------IKE 668
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 331 GIL-----------LTEVA---IDKVFIGSC-TNsrIEDLRAAAEIAKGRKVAPGVQALVVPgsgPVK---AQAEAEGLD 392
Cdd:PRK09238 669 PILacpndpddvrlLSEVAgtkIDEVFIGSCmTN--IGHFRAAGKLLEGKKGQLPTRLWVAP---PTKmdaDQLTEEGYY 743
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15829330 393 KIFIEAGFEWRLPGCSMCLAmNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVS 446
Cdd:PRK09238 744 SIFGKAGARIEMPGCSLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYLGS 796
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
106-435 |
1.77e-19 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 91.72 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 106 GIVH----------VMGPEQGVTL--PGmTIVCGDSHTaTH-GAFGALAFGIGTSEVEHVLatqtLkqGRAKTMKI---- 168
Cdd:PRK09277 179 GICHqvnleylapvVWTREDGELVayPD-TLVGTDSHT-TMiNGLGVLGWGVGGIEAEAAM----L--GQPSSMLIpevv 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 169 --EVQGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVK-- 244
Cdd:PRK09277 251 gvKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRlt 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 245 GRlhapkGKDFDDAV-AYWKT----LQTDEGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDNipdPASFADPVERASA 319
Cdd:PRK09277 331 GR-----DEEQVALVeAYAKAqglwRDPLEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDV---KEAFAKSAELGVQ 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 320 EKALAYMGLKPGILLTE--VAIDKvfIGSCTN-SRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAEAEG- 390
Cdd:PRK09277 403 GFGLDEAEEGEDYELPDgaVVIAA--ITSCTNtSNPSVMIAAGLLAKkavekGLKVKPWVKTSLAPGSKVVTDYLEKAGl 480
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 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 |
3.99e-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: 86.20 E-value: 3.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 103 PYQGIVH----------VMGPE---QGVTLPGmTIVCGDSHTATHGAFGALAFGIGTSEVEHVLAtqtlkqGRAKTMKI- 168
Cdd:cd01586 91 PGTGIIHqvnleylarvVFTSEedgDGVAYPD-SVVGTDSHTTMINGLGVLGWGVGGIEAEAVML------GQPISMLLp 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 169 -----EVQGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDettfnyv 243
Cdd:cd01586 164 evvgvKLTGKLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD------- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 244 kgrlhapkgkdfddavaywktlqtdegatfDTVVTLQAEEISPQVTWGTNPGQVISVNDNIPDPAsfadpverasaekal 323
Cdd:cd01586 237 ------------------------------TQVVELDLSTVEPSVSGPKRPQDRVPLHGSVVIAA--------------- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 324 aymglkpgilltevaidkvfIGSCTN-SRIEDLRAAAEIAK-----GRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIE 397
Cdd:cd01586 272 --------------------ITSCTNtSNPSVMLAAGLLAKkavelGLKVKPYVKTSLAPGSRVVTKYLEASGLLPYLEK 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15829330 398 AGFEWRLPGCSMCLAmNNDRLNP---------GERCAS--TSNRNFEGR 435
Cdd:cd01586 332 LGFHVVGYGCTTCIG-NSGPLPEeveeaikenDLVVAAvlSGNRNFEGR 379
|
|
| AcnB |
COG1049 |
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ... |
333-446 |
3.58e-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: 81.44 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 333 LLTEVA---IDKVFIGSC-TNsrIEDLRAAAEIAKGRKVAPgVQALVVPgsgPVK---AQAEAEGLDKIFIEAGFEWRLP 405
Cdd:COG1049 682 LLSEVAgtkIDEVFIGSCmTN--IGHFRAAGKLLEGKGNLP-TRLWIAP---PTKmdeAQLTEEGYYSIFGAAGARTEMP 755
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15829330 406 GCSMCLAmNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVS 446
Cdd:COG1049 756 GCSLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYLGS 795
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
119-446 |
6.80e-16 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 80.35 E-value: 6.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 119 LPGMTIVCGDSHTAthgaFG-ALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVQGKAAPGITAKDIVLAI---------- 187
Cdd:PLN00094 551 LPDTVGTGGDSHTR----FPiGISFPAGSGLVAFGAATGVIPLDMPESVLVRFTGTMQPGITLRDLVHAIpytaiqdgll 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 188 -IGKTGSAGG-TGHVVEFcgEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDEttfnyvkgrlhAPKGKDFDDAVAYWKTL 265
Cdd:PLN00094 627 tVEKKGKKNVfSGRILEI--EGLPHLKCEQAFELSDASAERSAAGCTIKLDK-----------EPIIEYLNSNVVMLKWM 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 266 QTDEgatFDTVVTLQaEEISPQVTWGTNP-----------GQVISVN-DNIPDP--ASFADPVERAsaekalaymglkpg 331
Cdd:PLN00094 694 IAEG---YGDRRTLE-RRIARMQQWLADPelleadpdaeyAAVIEIDmDEIKEPilCAPNDPDDAR-------------- 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 332 iLLTEVA---IDKVFIGSC-TNsrIEDLRAAAEIAKGRKVAPGVQALVVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGC 407
Cdd:PLN00094 756 -LLSEVTgdkIDEVFIGSCmTN--IGHFRAAGKLLNDNLSQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPGC 832
|
330 340 350
....*....|....*....|....*....|....*....
gi 15829330 408 SMCLAmNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVS 446
Cdd:PLN00094 833 SLCMG-NQARVAEKSTVVSTSTRNFPNRLGKGANVYLAS 870
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
121-437 |
3.56e-14 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 75.05 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 121 GMTIVCGDSHTaTHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVQGKAAPGITAKDIVLAIIGKTGSAGGTGH- 199
Cdd:PRK11413 142 GKMILGSDSHT-RYGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGYVKNk 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 200 VVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVKgrLHAPKGkdfddavAYwKTLQTDEGATFDTVVTL 279
Cdd:PRK11413 221 VMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLA--LHGRGQ-------DY-CELNPQPMAYYDGCISV 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 280 QAEEISPQVTWGTNPGQVISV---NDNIPDpasFADPVERASAEKAL--AYMGLKPGILLTEVAIDKVFIGSCTNSRIED 354
Cdd:PRK11413 291 DLSAIKPMIALPFHPSNVYEIdelNQNLTD---ILREVEIESERVAHgkAKLSLLDKIENGRLKVQQGIIAGCSGGNYEN 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829330 355 LRAAAEIAKGRKVAPGVQAL-VVPGSGPVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNDRLNPGERCASTSnRNFE 433
Cdd:PRK11413 368 VIAAANALRGQSCGNDTFSLsVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFGAGDTPANNGLSIRHTT-RNFP 446
|
....
gi 15829330 434 GRQG 437
Cdd:PRK11413 447 NREG 450
|
|
| |
