|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-450 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 848.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 1 MFDKIWQQHVVTGEPGEPQLMYVDLHLVHEVTSPQAFEGLRATHRRVRRPDKTFATMDHNVPTEDV-FNVKDVIARKQMQ 79
Cdd:PRK05478 5 LYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRdLPIADPVSRIQVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 80 TLQKNAAEFGVSLASVGQAEQGIIHVIGPQLGLTQPGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKPK 159
Cdd:PRK05478 85 TLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQKKPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 160 TMGIHIHGQLQPGVGAKDVIMVLIGQHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYLA 239
Cdd:PRK05478 165 TMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFEYLK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 240 GRKYAPK--DMATAIQYWSQFYTDDPTAYDEVIDFDVSDLAPYVTWGTNPGMAIPIDRTFPEPKDVND-------QKAYD 310
Cdd:PRK05478 245 GRPFAPKgeDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADpvkrasaERALA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 311 YVGLKPGDSPLNIPIGFAFFGSCTNGRLEDLRKAAHVLKGQHVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWRM 390
Cdd:PRK05478 325 YMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFEWRE 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 391 PGCSACLGMNPDRVPAGVHSASTSNRNFEGRQGAGSITHLASPEMVAAAAIHGHFVDIRK 450
Cdd:PRK05478 405 PGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRE 464
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-450 |
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: 664.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 1 MFDKIWQQHVV-TGEPGEPQLMYVDLHLVHEVTSPQAFEGLRATH-RRVRRPDKTFATMDHNVPTedvfnvKDVIARKQM 78
Cdd:COG0065 5 LAEKILARHAGrEVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPT------KDPKSAEQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 79 QTLQKNAAEFGVSLASVGQAeqGIIHVIGPQLGLTQPGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKP 158
Cdd:COG0065 79 KTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWFKVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 159 KTMGIHIHGQLQPGVGAKDVIMVLIGQHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYL 238
Cdd:COG0065 157 ETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFEYL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 239 AGRKYAPkdmataiqyWSQFYTDDPTAYDEVIDFDVSDLAPYVTWGTNPGMAIPIDrtfpepkDVNDqkaydyvglkpgd 318
Cdd:COG0065 237 KGRPFAP---------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVS-------ELEG------------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 319 splnIPIGFAFFGSCTNGRLEDLRKAAHVLKGQHVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWRMPGCSACLG 398
Cdd:COG0065 288 ----IKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLG 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2159755641 399 MNPDRVPAGVHSASTSNRNFEGRQG-AGSITHLASPEMVAAAAIHGHFVDIRK 450
Cdd:COG0065 364 MNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPRE 416
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
1-450 |
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: 659.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 1 MFDKIWQQHVVTGEPGEPQLMYVDLHLVHEVTSPQAFEGLRATHRRVRRPDKTFATMDHNVPTED-VFNVKDVIARKQMQ 79
Cdd:TIGR00170 5 LYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNrDFNIKDEVAKIQVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 80 TLQKNAAEFGVSLASVGQAEQGIIHVIGPQLGLTQPGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKPK 159
Cdd:TIGR00170 85 ELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQARAK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 160 TMGIHIHGQLQPGVGAKDVIMVLIGQHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYLA 239
Cdd:TIGR00170 165 TMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTFEYCK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 240 GRKYAPK--DMATAIQYWSQFYTDDPTAYDEVIDFDVSDLAPYVTWGTNPGMAIPIDRTFPEPKDVND-------QKAYD 310
Cdd:TIGR00170 245 GRPHAPKgkEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADpvdkasaERALA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 311 YVGLKPGDSPLNIPIGFAFFGSCTNGRLEDLRKAAHVLKGQHVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWRM 390
Cdd:TIGR00170 325 YMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGFEWRE 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 391 PGCSACLGMNPDRVPAGVHSASTSNRNFEGRQGAGSITHLASPEMVAAAAIHGHFVDIRK 450
Cdd:TIGR00170 405 PGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRK 464
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
3-443 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 621.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 3 DKIWQQHVVTGEPGEpqLMYV-DLHLVHEVTSPQAFEGLRATHRRVRRPDKTFATMDHNVPTEDV---------FNVKDV 72
Cdd:pfam00330 1 EKIWDAHLVEELDGS--LLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVidhapdaldKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 73 IAR--KQMQTLQKNAAEFGVSLASVGQaeqGIIHVIGPQLGLTQPGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFAT 150
Cdd:pfam00330 79 ISRnkEQYDFLEWNAKKFGIRFVPPGQ---GIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 151 QTIWQQKPKTMGIHIHGQLQPGVGAKDVIMVLIGQHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRP 230
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 231 DQTTFAYLA--GRKYAPK-DMATAIQYWSQFYTDDPTAYDEVIDFDVSDLAPYVTWGTNPGMAIPIDRTFPEP-----KD 302
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKgEAYDKAVAWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDPfadavKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 303 VNDQKAYDYVGLKPGDSPLNIPIGFAFFGSCTNGRLEDLRKAAHVLK-----GQHVAPGLTALVVPGSMAIKRAAEKEGL 377
Cdd:pfam00330 316 KAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEAEGL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159755641 378 DQIFKSAGCDWRMPGCSACLGmNPDRVPAGVHSASTSNRNFEGRQGAGSITHLASPEMVAAAAIHG 443
Cdd:pfam00330 396 DKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASPALVAAAAIAG 460
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
25-445 |
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: 560.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 25 LHLVHEVTSPQAFEGLR-ATHRRVRRPDKTFATMDHNVPTedvfnvKDVIARKQMQTLQKNAAEFGVSLASVGqaEQGII 103
Cdd:cd01583 1 LHLVHDVTSPQAFEGLReAGREKVWDPEKIVAVFDHNVPT------PDIKAAEQVKTLRKFAKEFGINFFDVG--RQGIC 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 104 HVIGPQLGLTQPGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKPKTMGIHIHGQLQPGVGAKDVIMVLI 183
Cdd:cd01583 73 HVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYII 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 184 GQHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYLAGRKYApkdmataiqYWSQFYTDDP 263
Cdd:cd01583 153 GKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKA---------YWKELKSDED 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 264 TAYDEVIDFDVSDLAPYVTWGTNPGMAIPIDRTFPepkdvndqkaydyvglkpgdsplnIPIGFAFFGSCTNGRLEDLRK 343
Cdd:cd01583 224 AEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG------------------------IKIDQVFIGSCTNGRLEDLRA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 344 AAHVLKGQHVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWRMPGCSACLGMNPDRVPAGVHSASTSNRNFEGRQG 423
Cdd:cd01583 280 AAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTSNRNFKGRMG 359
|
410 420
....*....|....*....|...
gi 2159755641 424 A-GSITHLASPEMVAAAAIHGHF 445
Cdd:cd01583 360 SpGARIYLASPATAAASAITGEI 382
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
14-444 |
3.46e-83 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 262.39 E-value: 3.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 14 EPGEPQLMYVDLHLVHEVTSPQAFEGLRATHRRVRRPDKTFATMDHNVPTedvfnvkDVIARKQMQTLQKN-AAEFGVSL 92
Cdd:NF040615 17 YAGDTVEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPA-------NTVKAANMQKITREfVKEQGIKN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 93 ASVGQaeQGIIHVIGPQLGLTQPGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKPKTMGIHIHGqLQPG 172
Cdd:NF040615 90 FYLGG--EGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVNIVG-KNEN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 173 VGAKDVIMVLIGQHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYLAGRKYAPKDMATaI 252
Cdd:NF040615 167 ISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEGVSEEEIAE-L 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 253 QYWSQFYTDDPTAYDEVIDFDVSDLAPYVTWGTNPGMAIPIdrtfpepkdvndqkaYDYVGLkpgdsplniPIGFAFFGS 332
Cdd:NF040615 246 KKNRITVNEKEENYYKEIEIDITDMEEQVACPHHPDNVKPV---------------SEVEGT---------EIDQVFIGS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 333 CTNGRLEDLRKAAHVLKGQHVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWRMPGCSACLGMNPDRVPAGVHSAS 412
Cdd:NF040615 302 CTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGEVCLS 381
|
410 420 430
....*....|....*....|....*....|...
gi 2159755641 413 TSNRNFEGRQG-AGSITHLASPEMVAAAAIHGH 444
Cdd:NF040615 382 TTNRNFKGRMGnINSYIYLSSPKIAAKSAVKGY 414
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
1-450 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 848.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 1 MFDKIWQQHVVTGEPGEPQLMYVDLHLVHEVTSPQAFEGLRATHRRVRRPDKTFATMDHNVPTEDV-FNVKDVIARKQMQ 79
Cdd:PRK05478 5 LYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRdLPIADPVSRIQVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 80 TLQKNAAEFGVSLASVGQAEQGIIHVIGPQLGLTQPGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKPK 159
Cdd:PRK05478 85 TLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQKKPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 160 TMGIHIHGQLQPGVGAKDVIMVLIGQHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYLA 239
Cdd:PRK05478 165 TMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFEYLK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 240 GRKYAPK--DMATAIQYWSQFYTDDPTAYDEVIDFDVSDLAPYVTWGTNPGMAIPIDRTFPEPKDVND-------QKAYD 310
Cdd:PRK05478 245 GRPFAPKgeDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADpvkrasaERALA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 311 YVGLKPGDSPLNIPIGFAFFGSCTNGRLEDLRKAAHVLKGQHVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWRM 390
Cdd:PRK05478 325 YMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFEWRE 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 391 PGCSACLGMNPDRVPAGVHSASTSNRNFEGRQGAGSITHLASPEMVAAAAIHGHFVDIRK 450
Cdd:PRK05478 405 PGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRE 464
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
1-453 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 681.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 1 MFDKIWQQHVVTGEPGEPQLMYVDLHLVHEVTSPQAFEGLRATHRRVRRPDKTFATMDHNVPTEDV--FNVKDVIARKQM 78
Cdd:PRK12466 6 LYDKLWDSHTVARLDDGHVLLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPTRPGrdRGITDPGGALQV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 79 QTLQKNAAEFGVSLASVGQAEQGIIHVIGPQLGLTQPGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKP 158
Cdd:PRK12466 86 DYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQTLVYRKP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 159 KTMGIHIHGQLQPGVGAKDVIMVLIGQHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYL 238
Cdd:PRK12466 166 KTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETTFDYL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 239 AGRKYAPK--DMATAIQYWSQFYTDDPTAYDEVIDFDVSDLAPYVTWGTNPGMAIPIDRTFPEPKDVND-------QKAY 309
Cdd:PRK12466 246 RGRPRAPKgaLWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAAEADparraamERAL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 310 DYVGLKPGDSPLNIPIGFAFFGSCTNGRLEDLRKAAHVLKGQHVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWR 389
Cdd:PRK12466 326 DYMGLTPGTPLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAGFEWR 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159755641 390 MPGCSACLGMNPDRVPAGVHSASTSNRNFEGRQGAGSITHLASPEMVAAAAIHGHFVDIRKEAI 453
Cdd:PRK12466 406 EPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHITDVRSLLQ 469
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
1-450 |
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: 664.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 1 MFDKIWQQHVV-TGEPGEPQLMYVDLHLVHEVTSPQAFEGLRATH-RRVRRPDKTFATMDHNVPTedvfnvKDVIARKQM 78
Cdd:COG0065 5 LAEKILARHAGrEVEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPT------KDPKSAEQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 79 QTLQKNAAEFGVSLASVGQAeqGIIHVIGPQLGLTQPGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKP 158
Cdd:COG0065 79 KTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWFKVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 159 KTMGIHIHGQLQPGVGAKDVIMVLIGQHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYL 238
Cdd:COG0065 157 ETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTFEYL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 239 AGRKYAPkdmataiqyWSQFYTDDPTAYDEVIDFDVSDLAPYVTWGTNPGMAIPIDrtfpepkDVNDqkaydyvglkpgd 318
Cdd:COG0065 237 KGRPFAP---------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVS-------ELEG------------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 319 splnIPIGFAFFGSCTNGRLEDLRKAAHVLKGQHVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWRMPGCSACLG 398
Cdd:COG0065 288 ----IKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGAEWREPGCGMCLG 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2159755641 399 MNPDRVPAGVHSASTSNRNFEGRQG-AGSITHLASPEMVAAAAIHGHFVDIRK 450
Cdd:COG0065 364 MNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPRE 416
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
1-450 |
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: 659.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 1 MFDKIWQQHVVTGEPGEPQLMYVDLHLVHEVTSPQAFEGLRATHRRVRRPDKTFATMDHNVPTED-VFNVKDVIARKQMQ 79
Cdd:TIGR00170 5 LYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNrDFNIKDEVAKIQVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 80 TLQKNAAEFGVSLASVGQAEQGIIHVIGPQLGLTQPGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKPK 159
Cdd:TIGR00170 85 ELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQARAK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 160 TMGIHIHGQLQPGVGAKDVIMVLIGQHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYLA 239
Cdd:TIGR00170 165 TMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTFEYCK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 240 GRKYAPK--DMATAIQYWSQFYTDDPTAYDEVIDFDVSDLAPYVTWGTNPGMAIPIDRTFPEPKDVND-------QKAYD 310
Cdd:TIGR00170 245 GRPHAPKgkEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADpvdkasaERALA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 311 YVGLKPGDSPLNIPIGFAFFGSCTNGRLEDLRKAAHVLKGQHVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWRM 390
Cdd:TIGR00170 325 YMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGFEWRE 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 391 PGCSACLGMNPDRVPAGVHSASTSNRNFEGRQGAGSITHLASPEMVAAAAIHGHFVDIRK 450
Cdd:TIGR00170 405 PGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRK 464
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
3-443 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 621.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 3 DKIWQQHVVTGEPGEpqLMYV-DLHLVHEVTSPQAFEGLRATHRRVRRPDKTFATMDHNVPTEDV---------FNVKDV 72
Cdd:pfam00330 1 EKIWDAHLVEELDGS--LLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVidhapdaldKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 73 IAR--KQMQTLQKNAAEFGVSLASVGQaeqGIIHVIGPQLGLTQPGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFAT 150
Cdd:pfam00330 79 ISRnkEQYDFLEWNAKKFGIRFVPPGQ---GIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 151 QTIWQQKPKTMGIHIHGQLQPGVGAKDVIMVLIGQHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRP 230
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 231 DQTTFAYLA--GRKYAPK-DMATAIQYWSQFYTDDPTAYDEVIDFDVSDLAPYVTWGTNPGMAIPIDRTFPEP-----KD 302
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKgEAYDKAVAWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDPfadavKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 303 VNDQKAYDYVGLKPGDSPLNIPIGFAFFGSCTNGRLEDLRKAAHVLK-----GQHVAPGLTALVVPGSMAIKRAAEKEGL 377
Cdd:pfam00330 316 KAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEAEGL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159755641 378 DQIFKSAGCDWRMPGCSACLGmNPDRVPAGVHSASTSNRNFEGRQGAGSITHLASPEMVAAAAIHG 443
Cdd:pfam00330 396 DKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASPALVAAAAIAG 460
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
25-445 |
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: 560.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 25 LHLVHEVTSPQAFEGLR-ATHRRVRRPDKTFATMDHNVPTedvfnvKDVIARKQMQTLQKNAAEFGVSLASVGqaEQGII 103
Cdd:cd01583 1 LHLVHDVTSPQAFEGLReAGREKVWDPEKIVAVFDHNVPT------PDIKAAEQVKTLRKFAKEFGINFFDVG--RQGIC 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 104 HVIGPQLGLTQPGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKPKTMGIHIHGQLQPGVGAKDVIMVLI 183
Cdd:cd01583 73 HVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYII 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 184 GQHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYLAGRKYApkdmataiqYWSQFYTDDP 263
Cdd:cd01583 153 GKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKA---------YWKELKSDED 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 264 TAYDEVIDFDVSDLAPYVTWGTNPGMAIPIDRTFPepkdvndqkaydyvglkpgdsplnIPIGFAFFGSCTNGRLEDLRK 343
Cdd:cd01583 224 AEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG------------------------IKIDQVFIGSCTNGRLEDLRA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 344 AAHVLKGQHVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWRMPGCSACLGMNPDRVPAGVHSASTSNRNFEGRQG 423
Cdd:cd01583 280 AAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTSNRNFKGRMG 359
|
410 420
....*....|....*....|...
gi 2159755641 424 A-GSITHLASPEMVAAAAIHGHF 445
Cdd:cd01583 360 SpGARIYLASPATAAASAITGEI 382
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
4-450 |
5.62e-131 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 384.53 E-value: 5.62e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 4 KIWQQHVV-TGEPGEPQLMYVDLHLVHEVTSPQAFEGLRAT-HRRVRRPDKTFATMDHNVPTedvfnvKDVIARKQMQTL 81
Cdd:PRK00402 8 KILARHSGrDVSPGDIVEAKVDLVMAHDITGPLAIKEFEKIgGDKVFDPSKIVIVFDHFVPA------KDIKSAEQQKIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 82 QKNAAEFGVSlaSVGQAEQGIIHVIGPQLGLTQPGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKPKTM 161
Cdd:PRK00402 82 REFAKEQGIP--NFFDVGEGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKTWFKVPETI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 162 GIHIHGQLQPGVGAKDVIMVLIGQHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYLAGR 241
Cdd:PRK00402 160 KVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEKTLEYLKER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 242 KYAPkdmataiqyWSQFYTDDPTAYDEVIDFDVSDLAPYVTWGTNPGMAIPIDRtfpepkdvndqkaydyVGlkpgdspl 321
Cdd:PRK00402 240 AGRD---------YKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSE----------------VE-------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 322 NIPIGFAFFGSCTNGRLEDLRKAAHVLKGQHVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWRMPGCSACLGMNP 401
Cdd:PRK00402 287 GTKVDQVFIGSCTNGRLEDLRIAAEILKGRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDAGAVVSTPTCGPCLGGHM 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2159755641 402 DRVPAGVHSASTSNRNFEGRQG-AGSITHLASPEMVAAAAIHGHFVDIRK 450
Cdd:PRK00402 367 GVLAPGEVCLSTTNRNFKGRMGsPESEVYLASPAVAAASAVTGKITDPRE 416
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
3-449 |
3.68e-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: 326.32 E-value: 3.68e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 3 DKIWQQHV-VTGEPGEPQLMYVDLHLVHEVTSPQAFEGL-RATHRRVRRPDKTFATMDHNVPTedvfnvKDVIARKQMQT 80
Cdd:TIGR01343 4 EKILSKKSgKEVYAGDLIEAEIDLAMVHDITAPLAIKTLeEYGIDKVWNPEKIVIVFDHQVPA------DTIKAAEMQKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 81 LQKNAAEFGV-SLASVGQaeqGIIHVIGPQLGLTQPGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKPK 159
Cdd:TIGR01343 78 AREFVKKQGIkYFYDVGE---GICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFKVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 160 TMGIHIHGQLQPGVGAKDVIMVLIGQHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYLA 239
Cdd:TIGR01343 155 TIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 240 grKYAPKDmataiqyWSQFYTDDPTAYDEVIDFDVSDLAPYVTWGTNPGMAIPIdrtfpepKDVNdqkaydyvglkpgds 319
Cdd:TIGR01343 235 --ERRKEP-------FRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPV-------SEVE--------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 320 plNIPIGFAFFGSCTNGRLEDLRKAAHVLKGQHVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWRMPGCSACLGM 399
Cdd:TIGR01343 284 --GTEIDQVFIGSCTNGRLEDLRVAAKILKGRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLGS 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2159755641 400 NPDRVPAGVHSASTSNRNFEGRQG-AGSITHLASPEMVAAAAIHGHFVDIR 449
Cdd:TIGR01343 362 HQGVLAPGEVCISTSNRNFKGRMGhPNAEIYLASPATAAASAVKGYIADPR 412
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
1-447 |
7.85e-93 |
|
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: 287.04 E-value: 7.85e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 1 MFDKIWQQHV-VTGEPGEPQLMYVDLHLVHEVTSPQAFEGLR-ATHRRVRRPDKTFATMDHNVPTEDVfnvkdVIARKQM 78
Cdd:TIGR02086 3 LAEKILSEKVgRPVCAGEIVEVEVDLAMTHDGTGPLAIKALReLGVARVWDPEKIVIAFDHNVPPPTV-----EAAEMQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 79 QTLqKNAAEFGVSLASVGQaeqGIIHVIGPQLGLTQPGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKP 158
Cdd:TIGR02086 78 EIR-EFAKRHGIKNFDVGE---GICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTWIKVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 159 KTMGIHIHGQLQPGVGAKDVIMVLIGQHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYL 238
Cdd:TIGR02086 154 ETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEETYEYL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 239 AGRKyapkdmataiQYWSQFYTDDPTA-YDEVIDFDVSDLAPYVTwgtnpgmaipidrtfpEPKDVNDQKAYDYV-GLKp 316
Cdd:TIGR02086 234 KKRR----------GLEFRILVPDPGAnYYKEIEIDLSDLEPQVA----------------VPHSVDNVKPVSDVeGTE- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 317 gdsplnipIGFAFFGSCTNGRLEDLRKAAHVLKGQHVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWRMPGCSAC 396
Cdd:TIGR02086 287 --------IDQVFIGSCTNGRLEDLRIAAEILKGRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAGAMICPPGCGPC 358
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2159755641 397 LGMNPDRVPAGVHSASTSNRNFEGRQGA-GSITHLASPEMVAAAAIHGHFVD 447
Cdd:TIGR02086 359 LGAHMGVLGDGEVCLSTTNRNFKGRMGSpNAEIYLASPATAAASAVEGYITD 410
|
|
| LEU2 |
TIGR02083 |
3-isopropylmalate dehydratase, large subunit; Homoaconitase, aconitase, and 3-isopropylmalate ... |
1-450 |
6.99e-88 |
|
3-isopropylmalate dehydratase, large subunit; 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 described by a separate model of subfamily (rather than equivalog) homology type (TIGR01343). This model along with TIGR00170 describe clades which consist only of LeuC sequences. Here, the genes from Pyrococcus furiosus, Clostridium acetobutylicum, Thermotoga maritima and others are gene clustered with related genes from the leucine biosynthesis pathway. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 131138 Cd Length: 419 Bit Score: 274.38 E-value: 6.99e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 1 MFDKIWQQHV--VTGEPGEPQLMYVDLHLVHEVTSPQAFEGLR-ATHRRVRRPDKTFATMDHNVPTedvfnvKDVIARKQ 77
Cdd:TIGR02083 3 MAEKILAQHAglESVEPGELILAKLDIVLGNDITTPLAIKAFKeYGGKKVFDPDRVALVPDHFTPN------KDIKSAEQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 78 MQTLQKNAAEFGVS-LASVGqaEQGIIHVIGPQLGLTQPGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQ 156
Cdd:TIGR02083 77 CKMMREFAREQGIEkFFEIG--NMGIEHALLPEEGIVKPGDLIIGADSHTCTYGALGAFATGVGSTDMAVGMATGKAWFR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 157 KPKTMGIHIHGQLQPGVGAKDVIMVLIGQHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFA 236
Cdd:TIGR02083 155 VPEAIKFVLKGKLKPWVTGKDLILHIIGIIGVDGALYKSMEFSGEGLKELSMDDRFTIANMAIEAGAKTGIFPVDEITIE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 237 YLAGRkyapkdmatAIQYWSQFYTDDPTAYDEVIDFDVSDLAPYVTWGTNPGMAIPIDRTfpepkdvndqkaydyvglkp 316
Cdd:TIGR02083 235 YEKGR---------GKREEKIYKADEDAKYVRVIEIDLSELEPQVAFPHLPENTKDISEA-------------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 317 gdSPLNIPIGFAFFGSCTNGRLEDLRKAAHVLKGQHVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWRMPGCSAC 396
Cdd:TIGR02083 286 --GKEEIKIDQVVIGSCTNGRLEDLRLAAEILKGKTVAPDVRCIIIPGSQNVYLEAMKEGLLEIFIEAGAVVSTPTCGPC 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2159755641 397 LGMNPDRVPAGVHSASTSNRNFEGRQG-AGSITHLASPEMVAAAAIHGHFVDIRK 450
Cdd:TIGR02083 364 LGGHMGILAEGERAISTTNRNFVGRMGhPKSEVYLASPAVAAASAIKGYIASPEE 418
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
14-444 |
3.46e-83 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 262.39 E-value: 3.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 14 EPGEPQLMYVDLHLVHEVTSPQAFEGLRATHRRVRRPDKTFATMDHNVPTedvfnvkDVIARKQMQTLQKN-AAEFGVSL 92
Cdd:NF040615 17 YAGDTVEVDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPA-------NTVKAANMQKITREfVKEQGIKN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 93 ASVGQaeQGIIHVIGPQLGLTQPGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKPKTMGIHIHGqLQPG 172
Cdd:NF040615 90 FYLGG--EGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVNIVG-KNEN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 173 VGAKDVIMVLIGQHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYLAGRKYAPKDMATaI 252
Cdd:NF040615 167 ISGKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEGVSEEEIAE-L 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 253 QYWSQFYTDDPTAYDEVIDFDVSDLAPYVTWGTNPGMAIPIdrtfpepkdvndqkaYDYVGLkpgdsplniPIGFAFFGS 332
Cdd:NF040615 246 KKNRITVNEKEENYYKEIEIDITDMEEQVACPHHPDNVKPV---------------SEVEGT---------EIDQVFIGS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 333 CTNGRLEDLRKAAHVLKGQHVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWRMPGCSACLGMNPDRVPAGVHSAS 412
Cdd:NF040615 302 CTNGRLSDLRIAAKYLKGKKVHKDVRLIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVLGDGEVCLS 381
|
410 420 430
....*....|....*....|....*....|...
gi 2159755641 413 TSNRNFEGRQG-AGSITHLASPEMVAAAAIHGH 444
Cdd:NF040615 382 TTNRNFKGRMGnINSYIYLSSPKIAAKSAVKGY 414
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
27-443 |
2.86e-75 |
|
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: 240.86 E-value: 2.86e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 27 LVHEVTSPQA---FEGLRAThRRVRRPDKTFATMDHNVPTEDVFNVKDviarkqMQTLQKNAAEFGVSLASVGQaeqGII 103
Cdd:cd01351 3 MLQDATGPMAmkaFEILAAL-GKVADPSQIACVHDHAVQLEKPVNNEG------HKFLSFFAALQGIAFYRPGV---GII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 104 HVIGPQLGLtQPGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKPKTMGIHIHGQLQPGVGAKDVIMVLI 183
Cdd:cd01351 73 HQIMVENLA-LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKDVVLKLG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 184 GQHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYLAGRKYaPKDMATAIQYWSQFYTDDP 263
Cdd:cd01351 152 GIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGR-PLLKNLWLAFPEELLADEG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 264 TAYDEVIDFDVSDLAPYVTwgtnpgmaipidrtfpEPKDVNDQKAYDYVGlkpgdsplNIPIGFAFFGSCTNGRLEDLRK 343
Cdd:cd01351 231 AEYDQVIEIDLSELEPDIS----------------GPNRPDDAVSVSEVE--------GTKIDQVLIGSCTNNRYSDMLA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 344 AAHVLKGQHVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWRMPGCSACLGMNPDRVPAGVHSASTSNRNFEGRQG 423
Cdd:cd01351 287 AAKLLKGAKVAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLVADGEVGVSSGNRNFPGRLG 366
|
410 420
....*....|....*....|.
gi 2159755641 424 AG-SITHLASPEMVAAAAIHG 443
Cdd:cd01351 367 TYeRHVYLASPELAAATAIAG 387
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
4-456 |
8.85e-64 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 217.32 E-value: 8.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 4 KIWQQHVVTGE--PGEPQLMYVDLHLVHEVTSPQA---FEGLRAThrRVRRPdKTFATMDHNVPTEDVFNvKDVIArkqm 78
Cdd:PRK07229 8 KILYAHLVEGElePGEEIAIRIDQTLTQDATGTMAylqFEAMGLD--RVKTE-LSVQYVDHNLLQADFEN-ADDHR---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 79 qTLQKNAAEFGVSLASVGQaeqGIIHvigpQLGLTQ---PGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQ 155
Cdd:PRK07229 80 -FLQSVAAKYGIYFSKPGN---GICH----QVHLERfafPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGGPYYL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 156 QKPKTMGIHIHGQLQPGVGAKDVIMVLIGQHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMviegGAKMG---QVRP-D 231
Cdd:PRK07229 152 KMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNM----GAELGattSIFPsD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 232 QTTFAYLA--GRKYApkdmataiqyWSQFYTDDPTAYDEVIDFDVSDLAPYVTWGTNPGMAIPIdrtfpepKDVNDqkay 309
Cdd:PRK07229 228 ERTREFLKaqGREDD----------WVELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPV-------SEVAG---- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 310 dyvglkpgdsplnIPIGFAFFGSCTNGRLEDLRKAAHVLKGQHVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWR 389
Cdd:PRK07229 287 -------------IKVDQVLIGSCTNSSYEDLMRAASILKGKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARIL 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2159755641 390 MPGCSACLGMNPDRVPAGVhSASTSNRNFEGRQGAGSiTH--LASPEMVAAAAIHGHFVDIRKEAIING 456
Cdd:PRK07229 354 ENACGPCIGMGQAPATGNV-SLRTFNRNFPGRSGTKD-AQvyLASPETAAASALTGVITDPRTLALENG 420
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
46-445 |
1.11e-59 |
|
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: 199.98 E-value: 1.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 46 RVRRPdKTFATMDHNVPTEDVFNVKDviarkqMQTLQKNAAEFGVSLASVGQaeqGIIHvigpQLGLTQ---PGKIIVCG 122
Cdd:cd01585 24 RVRTE-LSVSYVDHNTLQTDFENADD------HRFLQTVAARYGIYFSRPGN---GICH----QVHLERfavPGKTLLGS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 123 DSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKPKTMGIHIHGQLQPGVGAKDVIMVLIGQHGFSGFTGYAIEFYGDV 202
Cdd:cd01585 90 DSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVKGGVGKIFEYTGPG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 203 VENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYLA--GRKyapkdmataiQYWSQFYTDDPTAYDEVIDFDVSDLAPY 280
Cdd:cd01585 170 VATLSVPERATITNMGAELGATTSIFPSDERTREFLAaqGRE----------DDWVELAADADAEYDEEIEIDLSELEPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 281 VTWGTNPGMAIPIdrtfpepKDVNDQKAyDYVGLkpgdsplnipigfaffGSCTNGRLEDLRKAAHVLKGQHVAPGLTAL 360
Cdd:cd01585 240 IARPHSPDNVVPV-------REVAGIKV-DQVAI----------------GSCTNSSYEDLMTVAAILKGRRVHPHVSMV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 361 VVPGSMAIKRAAEKEGLDQIFKSAGCDWRMPGCSACLGMNPDRVPAGVhSASTSNRNFEGRQG-AGSITHLASPEMVAAA 439
Cdd:cd01585 296 VAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQAPPTGGV-SVRTFNRNFEGRSGtKDDLVYLASPEVAAAA 374
|
....*.
gi 2159755641 440 AIHGHF 445
Cdd:cd01585 375 ALTGVI 380
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
27-443 |
1.16e-45 |
|
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: 162.40 E-value: 1.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 27 LVHEVTSPQA--FEGLRAThrRVRRPDKTFATMDHNVPTEDVFNVKdviarkQMQTLQKNAAEFGVSLASVGQaeqGIIH 104
Cdd:cd01582 3 MTHDNSWPVAlkFMSIGAT--KIHNPDQIVMTLDHDVQNKSEKNLK------KYKNIESFAKKHGIDFYPAGR---GIGH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 105 VIGPQLGLTQPGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKPKTMGIHIHGQLQPGVGAKDVIMVLIG 184
Cdd:cd01582 72 QIMIEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVALCG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 185 QHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVrpdqttfaylagrkyapkdmataiqywsqfytddPT 264
Cdd:cd01582 152 LFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLF----------------------------------PT 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 265 AYDEVIdFDVSDLAPYVTWGTNPGMAIPIDrtfpepkDVNDQkaydyvglkpgdsplNIPIGFAFFGSCTNGRLEDLRKA 344
Cdd:cd01582 198 DAKHLI-LDLSTLSPYVSGPNSVKVSTPLK-------ELEAQ---------------NIKINKAYLVSCTNSRASDIAAA 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 345 AHVLKGQ-------HVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWRMPGCSACLGMNPDRVPAGVHSASTSNRN 417
Cdd:cd01582 255 ADVVKGKkekngkiPVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQGLLEPGEVGISATNRN 334
|
410 420
....*....|....*....|....*..
gi 2159755641 418 FEGRQGA-GSITHLASPEMVAAAAIHG 443
Cdd:cd01582 335 FKGRMGStEALAYLASPAVVAASAISG 361
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
81-443 |
1.98e-42 |
|
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: 154.91 E-value: 1.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 81 LQKNAAEFGVSLASVGQaeqGIIHvigpQLGLTQ---PGKIIVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTiWQQK 157
Cdd:cd01584 60 LASAGAKYGIGFWKPGS---GIIH----QIVLENyafPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIP-WELK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 158 -PKTMGIHIHGQLQPGVGAKDVIMVLIGQHGFSGFTGYAIEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFA 236
Cdd:cd01584 132 cPKVIGVKLTGKLSGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 237 YL--AGRKYApKDMATAIQYwSQFYTDDPTAYDEVIDFDVSDLAPYVTWGTNPGMAIPIDrtfpEPKDVNDQKAYdyvgl 314
Cdd:cd01584 212 YLkaTGRAEI-ADLADEFKD-DLLVADEGAEYDQLIEINLSELEPHINGPFTPDLATPVS----KFKEVAEKNGW----- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 315 kpgdsPLNIPIGfaFFGSCTNGRLEDLRKAAHVLKgQHVAPGLTA----LVVPGSMAIKRAAEKEGLDQIFKSAGCDWRM 390
Cdd:cd01584 281 -----PLDLRVG--LIGSCTNSSYEDMGRAASIAK-QALAHGLKCksifTITPGSEQIRATIERDGLLQTFRDAGGIVLA 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2159755641 391 PGCSACLGMnPDR--VPAGVHSA--STSNRNFEGRQGAGSITH--LASPEMVAAAAIHG 443
Cdd:cd01584 353 NACGPCIGQ-WDRkdIKKGEKNTivTSYNRNFTGRNDANPATHafVASPEIVTAMAIAG 410
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
123-456 |
6.44e-29 |
|
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle
Pssm-ID: 440669 [Multi-domain] Cd Length: 891 Bit Score: 120.21 E-value: 6.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 123 DSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKPKTMGIHIHGQLQPGVGAKDVIMVLIGQHGFSGFTGYAIEFYGDV 202
Cdd:COG1048 210 DSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVVGVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPG 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 203 VENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYLA--GR---------KYapkdmATAIQYWSQFYTDDPTaYDEVID 271
Cdd:COG1048 290 LASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRltGRseeqielveAY-----AKAQGLWRDPDAPEPY-YSDVLE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 272 FDVSDLAPYVTWGTNPGMAIPID-------RTFPEPKDVNDQKAydyVGLKPGDSPLNIPIGF---AFFGSCTNGRLEDL 341
Cdd:COG1048 364 LDLSTVEPSLAGPKRPQDRIPLSdlkeafrAALAAPVGEELDKP---VRVEVDGEEFELGHGAvviAAITSCTNTSNPSV 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 342 RKAAHVLKGQHVAPGLTA------LVVPGSMAIKRAAEKEGL----DQI-FKSAGCdwrmpGCSACLGM----------- 399
Cdd:COG1048 441 MIAAGLLAKKAVEKGLKVkpwvktSLAPGSKVVTDYLERAGLlpylEALgFNVVGY-----GCTTCIGNsgplppeisea 515
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2159755641 400 --NPDRVPAGVHSastSNRNFEGRQGAgSITH--LASPEMVAAAAIHGHF-VDIRKEAIING 456
Cdd:COG1048 516 ieENDLVVAAVLS---GNRNFEGRIHP-DVKAnfLASPPLVVAYALAGTVdIDLTTDPLGTD 573
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
119-453 |
4.57e-27 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 114.72 E-value: 4.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 119 IVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKPKTMGIHIHGQLQPGVGAKDVIMVLIGQHGFSGFTGYAIEF 198
Cdd:PTZ00092 211 VVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEF 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 199 YGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYLA--GRkyaPKDMATAIQYWSQ----FYTD-DPTAYDEVID 271
Cdd:PTZ00092 291 YGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKqtGR---SEEKVELIEKYLKanglFRTYaEQIEYSDVLE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 272 FDVSDLAPYVTwgtnpGMAIPIDRTFpepkdVNDQKaydyvglKPGDSPLNIPIGFAFFG-------------------- 331
Cdd:PTZ00092 368 LDLSTVVPSVA-----GPKRPHDRVP-----LSDLK-------KDFTACLSAPVGFKGFGipeekhekkvkftykgkeyt 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 332 ------------SCTN----------GRLEdlRKAahVLKGQHVAPGLTALVVPGSMAIKRAAEKEG----LDQI-FKSA 384
Cdd:PTZ00092 431 lthgsvviaaitSCTNtsnpsvmlaaGLLA--KKA--VEKGLKVPPYIKTSLSPGSKVVTKYLEASGllkyLEKLgFYTA 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 385 GCdwrmpGCSACLG-------------MNPDRVPAGVHSAstsNRNFEGR---QGAGSitHLASPEMVAAAAIHGHF-VD 447
Cdd:PTZ00092 507 GY-----GCMTCIGnsgdldpevseaiTNNDLVAAAVLSG---NRNFEGRvhpLTRAN--YLASPPLVVAYALAGRVnID 576
|
....*.
gi 2159755641 448 IRKEAI 453
Cdd:PTZ00092 577 FETEPL 582
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
123-453 |
2.25e-26 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 112.72 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 123 DSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKPKTMGIHIHGQLQPGVGAKDVIMVL---IGQHGFSG-FtgyaIEF 198
Cdd:PRK12881 212 DSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIPDVVGVELTGKLREGVTATDLVLTVtemLRKEGVVGkF----VEF 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 199 YGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYL--AGRkyaPKDMATAIQYWSQ----FYTDDPTA-YDEVID 271
Cdd:PRK12881 288 FGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLrlTGR---TEAQIALVEAYAKaqglWGDPKAEPrYTRTLE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 272 FDVSDLAPYVTWGTNPGMAIPIDRTFPEPKDV-NDQKAYDYVGLKPGDSPL----NIPIGFAFFGSCTN----------G 336
Cdd:PRK12881 365 LDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLfSKPVAENGFAKKAQTSNGvdlpDGAVAIAAITSCTNtsnpsvliaaG 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 337 RLEdlRKAahVLKGQHVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWRMPGCSACLGMN-------------PDR 403
Cdd:PRK12881 445 LLA--KKA--VERGLTVKPWVKTSLAPGSKVVTEYLERAGLLPYLEKLGFGIVGYGCTTCIGNSgpltpeieqaitkNDL 520
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2159755641 404 VPAGVHSAstsNRNFEGRqgagsiTH-------LASPEMVAAAAIHGHF-VDIRKEAI 453
Cdd:PRK12881 521 VAAAVLSG---NRNFEGR------IHpnikanfLASPPLVVAYALAGTVrRDLMTEPL 569
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
101-444 |
9.00e-25 |
|
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: 106.04 E-value: 9.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 101 GIIHVIGPQLGLtqPGKIIVCGDSHTSthgaFG-AIAFGIGTSEVEHVFATQTIWQQKPKTMGIHIHGQLQPGVGAKDVI 179
Cdd:cd01581 94 GVIHSWLNRMLL--PDTVGTGGDSHTR----FPiGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 180 ------------MVLIGQHGFSGFTGYAIEFYGdvVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFA-YLAGRKYAPK 246
Cdd:cd01581 168 naipyyaiqqglLTVEKKGKKNVFNGRILEIEG--LPDLKVEQAFELTDASAERSAAACTVRLDKEPVIeYLESNVVLMK 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 247 DM--------AT------AIQYW---SQFYTDDPTA-YDEVIDFDVSDLapyvtwgTNPGMAipidrtfpEPKDVNDQKA 308
Cdd:cd01581 246 IMiangyddaRTllrriiAMEEWlanPPLLEPDADAeYAAVIEIDLDDI-------KEPILA--------CPNDPDDVKL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 309 YDYVGLKPgdsplnipIGFAFFGSC-TNgrLEDLRKAAHVLKGQHVAPGLTALVVPGSMAIKRAAEkEGLDQIFKSAGCD 387
Cdd:cd01581 311 LSEVAGKK--------IDEVFIGSCmTN--IGHFRAAAKILRGKEFKPTRLWVAPPTRMDWAILQE-EGYYSIFGDAGAR 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2159755641 388 WRMPGCSACLGmNPDRVPAGVHSASTSNRNFEGRQGAGSITHLASPEMVAAAAIHGH 444
Cdd:cd01581 380 TEMPGCSLCMG-NQARVADGATVFSTSTRNFDNRVGKGAEVYLGSAELAAVCALLGR 435
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
119-453 |
3.00e-23 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 102.96 E-value: 3.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 119 IVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKPKTMGIHIHGQLQPGVGAKDVIMVLIGQHGFSGFTGYAIEF 198
Cdd:PLN00070 243 VVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRDGVTATDLVLTVTQMLRKHGVVGKFVEF 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 199 YGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYL--AGRKYAPKDMATAIQYWSQFYTD--DP---TAYDEVID 271
Cdd:PLN00070 323 YGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLklTGRSDETVAMIEAYLRANKMFVDynEPqqeRVYSSYLE 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 272 FDVSDLAPYVTWGTNPGMAIPID----------------RTFPEPKDVNDQKA-YDYVG----LKPGDsplnipIGFAFF 330
Cdd:PLN00070 403 LDLEDVEPCISGPKRPHDRVPLKemkadwhscldnkvgfKGFAVPKEAQSKVAkFSFHGqpaeLRHGS------VVIAAI 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 331 GSCTN-GRLEDLRKAAHVLK-----GQHVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWRMPGCSACLG------ 398
Cdd:PLN00070 477 TSCTNtSNPSVMLGAGLVAKkacelGLEVKPWIKTSLAPGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIGnsgeld 556
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159755641 399 -------MNPDRVPAGVHSAstsNRNFEGRQGAGS-ITHLASPEMVAAAAIHGHF-VDIRKEAI 453
Cdd:PLN00070 557 esvasaiTENDIVAAAVLSG---NRNFEGRVHPLTrANYLASPPLVVAYALAGTVdIDFEKEPI 617
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
101-444 |
3.37e-18 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 87.54 E-value: 3.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 101 GIIHVIGPQLGLtqPGKIIVCGDSHTSThgAFGaIAFGIGTSEVEHVFATQTIWQQKPKTMGIHIHGQLQPGVGAKDVI- 179
Cdd:PRK09238 466 GVIHSWLNRMLL--PDTVGTGGDSHTRF--PIG-ISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGEMQPGITLRDLVh 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 180 -----------MVLIGQHGFSGFTGYAIEFYGdvVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFA-YLAGRKYAPKD 247
Cdd:PRK09238 541 aipyyaikqglLTVEKKGKKNIFSGRILEIEG--LPDLKVEQAFELTDASAERSAAGCTIKLSKEPIIeYLRSNIVLLKW 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 248 M--------------ATAIQYWsqfyTDDPTA--------YDEVIDFDVSDLapyvtwgTNPGMAIPIDrtfpePKDVnd 305
Cdd:PRK09238 619 MiaegygdartlerrIAAMEEW----LANPELleadadaeYAAVIEIDLAEI-------KEPILACPND-----PDDV-- 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 306 qKAYDYVGlkpGDsplniPIGFAFFGSC-TNgrLEDLRKAAHVLKGQHVAPGlTALVV--PGSMAIKRAAEkEGLDQIFK 382
Cdd:PRK09238 681 -RLLSEVA---GT-----KIDEVFIGSCmTN--IGHFRAAGKLLEGKKGQLP-TRLWVapPTKMDADQLTE-EGYYSIFG 747
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2159755641 383 SAGCDWRMPGCSACLGmNPDRVPAGVHSASTSNRNFEGRQGAGSITHLASPEMVAAAAIHGH 444
Cdd:PRK09238 748 KAGARIEMPGCSLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYLGSAELAAVCALLGR 808
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
119-443 |
1.02e-17 |
|
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydrolyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes.
Pssm-ID: 153136 Cd Length: 404 Bit Score: 84.66 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 119 IVCGDSHTSTHGAFGAIAFGIGTSEVEHVFATQTIWQQKPKTMGIHIHGQLQPGVGAKDVIMvLIGQHGFS-GFTGYAIE 197
Cdd:cd01586 124 VVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTGKLRPGVTATDLVL-TVTQMLRKvGVVGKFVE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 198 FYGDVVENFSMAERMTLCNMVIEGGAKMGqvrpdqttfaylagrkYAPKDmataiqywsqfytddptayDEVIDFDVSDL 277
Cdd:cd01586 203 FFGPGVAKLSVADRATIANMAPEYGATCG----------------FFPVD-------------------TQVVELDLSTV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 278 APYVtwgtnPGMAIPIDRTfpepkdvndqkaydyvglkpgdsPLNIPIGFAFFGSCTN----------GRLEdlRKAahV 347
Cdd:cd01586 248 EPSV-----SGPKRPQDRV-----------------------PLHGSVVIAAITSCTNtsnpsvmlaaGLLA--KKA--V 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 348 LKGQHVAPGLTALVVPGSMAIKRAAEKEGLDQIFKSAGCDWRMPGCSACLG-------------MNPDRVPAGVHSAsts 414
Cdd:cd01586 296 ELGLKVKPYVKTSLAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGnsgplpeeveeaiKENDLVVAAVLSG--- 372
|
330 340 350
....*....|....*....|....*....|....*
gi 2159755641 415 NRNFEGRqgagsI------THLASPEMVAAAAIHG 443
Cdd:cd01586 373 NRNFEGR-----IhplvraNYLASPPLVVAYALAG 402
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
123-453 |
1.70e-17 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 85.18 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 123 DSHTsTH-GAFGAIAFGIGTSEVEHVFATQTIWQQKPKTMGIHIHGQLQPGVGAKDVimVL-----IGQHGFSG-Ftgya 195
Cdd:PRK09277 212 DSHT-TMiNGLGVLGWGVGGIEAEAAMLGQPSSMLIPEVVGVKLTGKLPEGVTATDL--VLtvtemLRKKGVVGkF---- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 196 IEFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYLA--GR---------KYApKdmATAIqywsqFYTDDPT 264
Cdd:PRK09277 285 VEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRltGRdeeqvalveAYA-K--AQGL-----WRDPLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 265 A-YDEVIDFDVSDLAPYVTWGTNPGMAIPID---RTFPEPKDVNDQKAYDyvGLKPGDSPLNIPIG---FAFFGSCTN-- 335
Cdd:PRK09277 357 PvYTDVLELDLSTVEPSLAGPKRPQDRIPLSdvkEAFAKSAELGVQGFGL--DEAEEGEDYELPDGavvIAAITSCTNts 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 336 --------GRLEdlRKAahVLKGQHVAPGL-TALvVPGSMAIKRAAEKEG----LDQI-FKSAGCdwrmpGCSACLGM-- 399
Cdd:PRK09277 435 npsvmiaaGLLA--KKA--VEKGLKVKPWVkTSL-APGSKVVTDYLEKAGllpyLEALgFNLVGY-----GCTTCIGNsg 504
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159755641 400 --NP---------DRVPAGVHSAstsNRNFEGRqgagsItH-------LASPEMVAAAAIHGHF-VDIRKEAI 453
Cdd:PRK09277 505 plPPeiekaindnDLVVTAVLSG---NRNFEGR-----I-HplvkanyLASPPLVVAYALAGTVdIDLEKDPL 568
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
112-443 |
2.51e-16 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 81.59 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 112 LTQPGKIIVCGDSHTStHGAFGAIAFGIGTSEVEHVFATQTIWQQKPKTMGIHIHGQLQPGVGAKDVIMVLIGQHGFSGF 191
Cdd:PRK11413 138 MAGGGKMILGSDSHTR-YGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVFKNGY 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 192 TGYAI-EFYGDVVENFSMAERMTLCNMVIEGGAKMGQVRPDQTTFAYLA--GRKYAPKDMATAiqywsqfytdDPTAYDE 268
Cdd:PRK11413 217 VKNKVmEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLAlhGRGQDYCELNPQ----------PMAYYDG 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 269 VIDFDVSDLAPYVTWGTNPGMAIPIDRTFPEPKDVNDQKAYDYVGLKPGDSPLN---------IPIGFAFFGSCTNGRLE 339
Cdd:PRK11413 287 CISVDLSAIKPMIALPFHPSNVYEIDELNQNLTDILREVEIESERVAHGKAKLSlldkiengrLKVQQGIIAGCSGGNYE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 340 DLRKAAHVLKGQHVAPGLTAL-VVPGSMAIKRAAEKEGLDQIFKSAGCDWRMPGCSACLGMNPdrVPA-GVHSASTSNRN 417
Cdd:PRK11413 367 NVIAAANALRGQSCGNDTFSLsVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFGAGD--TPAnNGLSIRHTTRN 444
|
330 340 350
....*....|....*....|....*....|..
gi 2159755641 418 FEGRQGA----GSITHLA--SPEMVAAAAIHG 443
Cdd:PRK11413 445 FPNREGSkpanGQMSAVAlmDARSIAATAANG 476
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
71-443 |
1.34e-15 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 79.58 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 71 DVIARKQMQTLQKNAAefGVSLasvgQAEQGIIHVIGPQLGLtqPGKIIVCGDSHTSthgaFG-AIAFGIGTSEVEHVFA 149
Cdd:PLN00094 516 DVVTHHTLPDFIRNRG--GVSL----RPGDGVIHSWLNRMLL--PDTVGTGGDSHTR----FPiGISFPAGSGLVAFGAA 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 150 TQTIWQQKPKTMGIHIHGQLQPGVGAKDVI------------MVLIGQHGFSGFTGYAIEFYGdvVENFSMAERMTLCNM 217
Cdd:PLN00094 584 TGVIPLDMPESVLVRFTGTMQPGITLRDLVhaipytaiqdglLTVEKKGKKNVFSGRILEIEG--LPHLKCEQAFELSDA 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 218 VIEGGAKMGQVRPDQTTFA-YLAGRKYAPKDMAT--------------AIQYW---SQFYTDDPTA-YDEVIDFDVSDLa 278
Cdd:PLN00094 662 SAERSAAGCTIKLDKEPIIeYLNSNVVMLKWMIAegygdrrtlerriaRMQQWladPELLEADPDAeYAAVIEIDMDEI- 740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 279 pyvtwgTNPGMAIPidrtfpepkdvNDQKAYDYVGLKPGDSplnipIGFAFFGSC-TNgrLEDLRKAAHVLKgQHVAPGL 357
Cdd:PLN00094 741 ------KEPILCAP-----------NDPDDARLLSEVTGDK-----IDEVFIGSCmTN--IGHFRAAGKLLN-DNLSQLP 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159755641 358 TAL-VVPGSMAIKRAAEKEGLDQIFKSAGCDWRMPGCSACLGmNPDRVPAGVHSASTSNRNFEGRQGAGSITHLASPEMV 436
Cdd:PLN00094 796 TRLwVAPPTKMDEAQLKAEGYYSTFGTVGARTEMPGCSLCMG-NQARVAEKSTVVSTSTRNFPNRLGKGANVYLASAELA 874
|
....*..
gi 2159755641 437 AAAAIHG 443
Cdd:PLN00094 875 AVAAILG 881
|
|
| |
