|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
4-466 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 917.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 4 PQTIVEKIWDTHVIHQEENKPDLLYIDLHLVHEVTSPQAFEGLRMKNRKVRRPDRTFATMDHNVPTIARHF-ISDPVSRK 82
Cdd:PRK05478 2 GKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLpIADPVSRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 83 QMETLYDNCQEFDIPLADINHPDQGIVHVIGPQLGLTQPGKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSIWQA 162
Cdd:PRK05478 82 QVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 163 RPKTMNVKVNGRLSPSVTAKDLILAIIGKFGVRFGTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTTVE 242
Cdd:PRK05478 162 KPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 243 FLRGRRHAPEGAAFEEAAASWKALATDDGAAYDAVVSIDAEEVEPQVTWGINPGMCLPVSGTVPSPAQAETDAEREEIER 322
Cdd:PRK05478 242 YLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVKRASAER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 323 ALDYMGLEAGQAITSVPIQHVFIGSCTNSRLSDLERAAEVIRGQQVHEDVRALVVPGSQTVKQQAEEKGIDKIFTDAGFE 402
Cdd:PRK05478 322 ALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFE 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 651990612 403 WREAGCSMCLAMNDDVVPPGERCASTSNRNFEGRQGNGARTHLVAPEMAAAAAVEGRFTDVRKF 466
Cdd:PRK05478 402 WREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVREL 465
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
4-466 |
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: 752.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 4 PQTIVEKIWDTHVIHQEENKPDLLYIDLHLVHEVTSPQAFEGLRMKNRKVRRPDRTFATMDHNVPTIARHF-ISDPVSRK 82
Cdd:TIGR00170 2 PRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFnIKDEVAKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 83 QMETLYDNCQEFDIPLADINHPDQGIVHVIGPQLGLTQPGKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSIWQA 162
Cdd:TIGR00170 82 QVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 163 RPKTMNVKVNGRLSPSVTAKDLILAIIGKFGVRFGTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTTVE 242
Cdd:TIGR00170 162 RAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTFE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 243 FLRGRRHAPEGAAFEEAAASWKALATDDGAAYDAVVSIDAEEVEPQVTWGINPGMCLPVSGTVPSPAQAETDAEREEIER 322
Cdd:TIGR00170 242 YCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKASAER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 323 ALDYMGLEAGQAITSVPIQHVFIGSCTNSRLSDLERAAEVIRGQQVHEDVRALVVPGSQTVKQQAEEKGIDKIFTDAGFE 402
Cdd:TIGR00170 322 ALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGFE 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 651990612 403 WREAGCSMCLAMNDDVVPPGERCASTSNRNFEGRQGNGARTHLVAPEMAAAAAVEGRFTDVRKF 466
Cdd:TIGR00170 402 WREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
4-466 |
0e+00 |
|
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism]; Homoaconitase/3-isopropylmalate dehydratase large subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439835 Cd Length: 417 Bit Score: 703.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 4 PQTIVEKIWDTHVIHQ-EENKPDLLYIDLHLVHEVTSPQAFEGLR-MKNRKVRRPDRTFATMDHNVPTiarhfiSDPVSR 81
Cdd:COG0065 2 GMTLAEKILARHAGREvEPGEIVLLYIDLHLVHDVTSPQAFEGLReAGGRKVWDPDRIVAVFDHNVPT------KDPKSA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 82 KQMETLYDNCQEFDIPLADINHPdqGIVHVIGPQLGLTQPGKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSIWQ 161
Cdd:COG0065 76 EQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 162 ARPKTMNVKVNGRLSPSVTAKDLILAIIGKFGVRFGTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTTV 241
Cdd:COG0065 154 KVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 242 EFLRGRRHAPegaafeeaaasWKALATDDGAAYDAVVSIDAEEVEPQVTWGINPGMCLPVSGtvpspaqaetdaereeie 321
Cdd:COG0065 234 EYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE------------------ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 322 raldymgleagqaITSVPIQHVFIGSCTNSRLSDLERAAEVIRGQQVHEDVRALVVPGSQTVKQQAEEKGIDKIFTDAGF 401
Cdd:COG0065 285 -------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGA 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 651990612 402 EWREAGCSMCLAMNDDVVPPGERCASTSNRNFEGRQGN-GARTHLVAPEMAAAAAVEGRFTDVRKF 466
Cdd:COG0065 352 EWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGSpGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
9-450 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 659.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 9 EKIWDTHVIHQEENkpDLLYI-DLHLVHEVTSPQAFEGLRMKNRKVRRPDRTFATMDHNVPTI---------ARHFISDP 78
Cdd:pfam00330 1 EKIWDAHLVEELDG--SLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDlvidhapdaLDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 79 VSR--KQMETLYDNCQEFDIPLADinhPDQGIVHVIGPQLGLTQPGKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAA 156
Cdd:pfam00330 79 ISRnkEQYDFLEWNAKKFGIRFVP---PGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 157 QSIWQARPKTMNVKVNGRLSPSVTAKDLILAIIGKFGVRFGTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISP 236
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 237 DDTTVEFLR--GRRHaPEGAAFEEAAASWKALATDDGAAYDAVVSIDAEEVEPQVTWGINPGMCLPVSGTVPSPaqAETD 314
Cdd:pfam00330 236 DETTFEYLRatGRPE-APKGEAYDKAVAWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDP--FADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 315 AEREEIERALDYMGLEAGQAITSVPIQHVFIGSCTNSRLSDLERAAEVIR-----GQQVHEDVRALVVPGSQTVKQQAEE 389
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 651990612 390 KGIDKIFTDAGFEWREAGCSMCLAmNDDVVPPGERCASTSNRNFEGRQGNGARTHLVAPEM 450
Cdd:pfam00330 393 EGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASPAL 452
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
31-460 |
0e+00 |
|
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate; Aconatase-like catalytic domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes.
Pssm-ID: 153133 Cd Length: 382 Bit Score: 584.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 31 LHLVHEVTSPQAFEGLRMKNR-KVRRPDRTFATMDHNVPTiarhfiSDPVSRKQMETLYDNCQEFDIPLADINhpDQGIV 109
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPT------PDIKAAEQVKTLRKFAKEFGINFFDVG--RQGIC 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 110 HVIGPQLGLTQPGKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSIWQARPKTMNVKVNGRLSPSVTAKDLILAII 189
Cdd:cd01583 73 HVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYII 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 190 GKFGVRFGTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTTVEFLRGRRHAPegaafeeaaasWKALATD 269
Cdd:cd01583 153 GKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAY-----------WKELKSD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 270 DGAAYDAVVSIDAEEVEPQVTWGINPGMCLPVSGTVPspaqaetdaereeieraldymgleagqaitsVPIQHVFIGSCT 349
Cdd:cd01583 222 EDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQVFIGSCT 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 350 NSRLSDLERAAEVIRGQQVHEDVRALVVPGSQTVKQQAEEKGIDKIFTDAGFEWREAGCSMCLAMNDDVVPPGERCASTS 429
Cdd:cd01583 271 NGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTS 350
|
410 420 430
....*....|....*....|....*....|..
gi 651990612 430 NRNFEGRQGN-GARTHLVAPEMAAAAAVEGRF 460
Cdd:cd01583 351 NRNFKGRMGSpGARIYLASPATAAASAITGEI 382
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
4-466 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 917.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 4 PQTIVEKIWDTHVIHQEENKPDLLYIDLHLVHEVTSPQAFEGLRMKNRKVRRPDRTFATMDHNVPTIARHF-ISDPVSRK 82
Cdd:PRK05478 2 GKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDLpIADPVSRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 83 QMETLYDNCQEFDIPLADINHPDQGIVHVIGPQLGLTQPGKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSIWQA 162
Cdd:PRK05478 82 QVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 163 RPKTMNVKVNGRLSPSVTAKDLILAIIGKFGVRFGTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTTVE 242
Cdd:PRK05478 162 KPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAPDETTFE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 243 FLRGRRHAPEGAAFEEAAASWKALATDDGAAYDAVVSIDAEEVEPQVTWGINPGMCLPVSGTVPSPAQAETDAEREEIER 322
Cdd:PRK05478 242 YLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVKRASAER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 323 ALDYMGLEAGQAITSVPIQHVFIGSCTNSRLSDLERAAEVIRGQQVHEDVRALVVPGSQTVKQQAEEKGIDKIFTDAGFE 402
Cdd:PRK05478 322 ALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGVRALVVPGSGLVKAQAEAEGLDKIFIEAGFE 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 651990612 403 WREAGCSMCLAMNDDVVPPGERCASTSNRNFEGRQGNGARTHLVAPEMAAAAAVEGRFTDVRKF 466
Cdd:PRK05478 402 WREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVREL 465
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
3-469 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 759.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 3 RPQTIVEKIWDTHVIHQEENKPDLLYIDLHLVHEVTSPQAFEGLRMKNRKVRRPDRTFATMDHNVPT--IARHFISDPVS 80
Cdd:PRK12466 2 MPRTLYDKLWDSHTVARLDDGHVLLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPTrpGRDRGITDPGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 81 RKQMETLYDNCQEFDIPLADINHPDQGIVHVIGPQLGLTQPGKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSIW 160
Cdd:PRK12466 82 ALQVDYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLATQTLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 161 QARPKTMNVKVNGRLSPSVTAKDLILAIIGKFGVRFGTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTT 240
Cdd:PRK12466 162 YRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIAPDETT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 241 VEFLRGRRHAPEGAAFEEAAASWKALATDDGAAYDAVVSIDAEEVEPQVTWGINPGMCLPVSGTVPSPAQAETDAEREEI 320
Cdd:PRK12466 242 FDYLRGRPRAPKGALWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAAEADPARRAAM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 321 ERALDYMGLEAGQAITSVPIQHVFIGSCTNSRLSDLERAAEVIRGQQVHEDVRALVVPGSQTVKQQAEEKGIDKIFTDAG 400
Cdd:PRK12466 322 ERALDYMGLTPGTPLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGVRAMVVPGSGAVRRQAEAEGLARIFIAAG 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 651990612 401 FEWREAGCSMCLAMNDDVVPPGERCASTSNRNFEGRQGNGARTHLVAPEMAAAAAVEGRFTDVRKFQQT 469
Cdd:PRK12466 402 FEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHITDVRSLLQA 470
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
4-466 |
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: 752.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 4 PQTIVEKIWDTHVIHQEENKPDLLYIDLHLVHEVTSPQAFEGLRMKNRKVRRPDRTFATMDHNVPTIARHF-ISDPVSRK 82
Cdd:TIGR00170 2 PRTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFnIKDEVAKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 83 QMETLYDNCQEFDIPLADINHPDQGIVHVIGPQLGLTQPGKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSIWQA 162
Cdd:TIGR00170 82 QVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLKQA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 163 RPKTMNVKVNGRLSPSVTAKDLILAIIGKFGVRFGTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTTVE 242
Cdd:TIGR00170 162 RAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDETTFE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 243 FLRGRRHAPEGAAFEEAAASWKALATDDGAAYDAVVSIDAEEVEPQVTWGINPGMCLPVSGTVPSPAQAETDAEREEIER 322
Cdd:TIGR00170 242 YCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKASAER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 323 ALDYMGLEAGQAITSVPIQHVFIGSCTNSRLSDLERAAEVIRGQQVHEDVRALVVPGSQTVKQQAEEKGIDKIFTDAGFE 402
Cdd:TIGR00170 322 ALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVKALVVPGSGLVKLQAEKEGLDKIFIEAGFE 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 651990612 403 WREAGCSMCLAMNDDVVPPGERCASTSNRNFEGRQGNGARTHLVAPEMAAAAAVEGRFTDVRKF 466
Cdd:TIGR00170 402 WREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
4-466 |
0e+00 |
|
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism]; Homoaconitase/3-isopropylmalate dehydratase large subunit is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439835 Cd Length: 417 Bit Score: 703.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 4 PQTIVEKIWDTHVIHQ-EENKPDLLYIDLHLVHEVTSPQAFEGLR-MKNRKVRRPDRTFATMDHNVPTiarhfiSDPVSR 81
Cdd:COG0065 2 GMTLAEKILARHAGREvEPGEIVLLYIDLHLVHDVTSPQAFEGLReAGGRKVWDPDRIVAVFDHNVPT------KDPKSA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 82 KQMETLYDNCQEFDIPLADINHPdqGIVHVIGPQLGLTQPGKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSIWQ 161
Cdd:COG0065 76 EQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLATGTLWF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 162 ARPKTMNVKVNGRLSPSVTAKDLILAIIGKFGVRFGTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTTV 241
Cdd:COG0065 154 KVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIAPDETTF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 242 EFLRGRRHAPegaafeeaaasWKALATDDGAAYDAVVSIDAEEVEPQVTWGINPGMCLPVSGtvpspaqaetdaereeie 321
Cdd:COG0065 234 EYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE------------------ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 322 raldymgleagqaITSVPIQHVFIGSCTNSRLSDLERAAEVIRGQQVHEDVRALVVPGSQTVKQQAEEKGIDKIFTDAGF 401
Cdd:COG0065 285 -------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVRAIVVPGSQEVYRQAEAEGLDEIFIEAGA 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 651990612 402 EWREAGCSMCLAMNDDVVPPGERCASTSNRNFEGRQGN-GARTHLVAPEMAAAAAVEGRFTDVRKF 466
Cdd:COG0065 352 EWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGSpGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
9-450 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 659.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 9 EKIWDTHVIHQEENkpDLLYI-DLHLVHEVTSPQAFEGLRMKNRKVRRPDRTFATMDHNVPTI---------ARHFISDP 78
Cdd:pfam00330 1 EKIWDAHLVEELDG--SLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDlvidhapdaLDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 79 VSR--KQMETLYDNCQEFDIPLADinhPDQGIVHVIGPQLGLTQPGKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAA 156
Cdd:pfam00330 79 ISRnkEQYDFLEWNAKKFGIRFVP---PGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 157 QSIWQARPKTMNVKVNGRLSPSVTAKDLILAIIGKFGVRFGTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISP 236
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 237 DDTTVEFLR--GRRHaPEGAAFEEAAASWKALATDDGAAYDAVVSIDAEEVEPQVTWGINPGMCLPVSGTVPSPaqAETD 314
Cdd:pfam00330 236 DETTFEYLRatGRPE-APKGEAYDKAVAWKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDP--FADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 315 AEREEIERALDYMGLEAGQAITSVPIQHVFIGSCTNSRLSDLERAAEVIR-----GQQVHEDVRALVVPGSQTVKQQAEE 389
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVKASVVPGSEVVRAYAEA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 651990612 390 KGIDKIFTDAGFEWREAGCSMCLAmNDDVVPPGERCASTSNRNFEGRQGNGARTHLVAPEM 450
Cdd:pfam00330 393 EGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASPAL 452
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
31-460 |
0e+00 |
|
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate; Aconatase-like catalytic domain of 3-isopropylmalate dehydratase and related uncharacterized proteins. 3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate 3-isopropylmalate. IPMI is involved in fungal and bacterial leucine biosynthesis and is also found in eukaryotes.
Pssm-ID: 153133 Cd Length: 382 Bit Score: 584.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 31 LHLVHEVTSPQAFEGLRMKNR-KVRRPDRTFATMDHNVPTiarhfiSDPVSRKQMETLYDNCQEFDIPLADINhpDQGIV 109
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPT------PDIKAAEQVKTLRKFAKEFGINFFDVG--RQGIC 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 110 HVIGPQLGLTQPGKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSIWQARPKTMNVKVNGRLSPSVTAKDLILAII 189
Cdd:cd01583 73 HVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKDVILYII 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 190 GKFGVRFGTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTTVEFLRGRRHAPegaafeeaaasWKALATD 269
Cdd:cd01583 153 GKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAY-----------WKELKSD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 270 DGAAYDAVVSIDAEEVEPQVTWGINPGMCLPVSGTVPspaqaetdaereeieraldymgleagqaitsVPIQHVFIGSCT 349
Cdd:cd01583 222 EDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQVFIGSCT 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 350 NSRLSDLERAAEVIRGQQVHEDVRALVVPGSQTVKQQAEEKGIDKIFTDAGFEWREAGCSMCLAMNDDVVPPGERCASTS 429
Cdd:cd01583 271 NGRLEDLRAAAEILKGRKVADGVRLIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPGERCVSTS 350
|
410 420 430
....*....|....*....|....*....|..
gi 651990612 430 NRNFEGRQGN-GARTHLVAPEMAAAAAVEGRF 460
Cdd:cd01583 351 NRNFKGRMGSpGARIYLASPATAAASAITGEI 382
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
4-466 |
1.85e-136 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 399.17 E-value: 1.85e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 4 PQTIVEKIWDTHVIHQEEnKPDLLY--IDLHLVHEVTSPQAFEGLR-MKNRKVRRPDRTFATMDHNVPTiarhfiSDPVS 80
Cdd:PRK00402 2 GMTLAEKILARHSGRDVS-PGDIVEakVDLVMAHDITGPLAIKEFEkIGGDKVFDPSKIVIVFDHFVPA------KDIKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 81 RKQMETLYDNCQEFDIP-LADINhpdQGIVHVIGPQLGLTQPGKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSI 159
Cdd:PRK00402 75 AEQQKILREFAKEQGIPnFFDVG---EGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMATGKT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 160 WQARPKTMNVKVNGRLSPSVTAKDLILAIIGKFGVRFGTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDT 239
Cdd:PRK00402 152 WFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFAPDEK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 240 TVEFLRGRRhapegaafeeaAASWKALATDDGAAYDAVVSIDAEEVEPQVTWGINPGMCLPVSgtvpspaqaetdaereE 319
Cdd:PRK00402 232 TLEYLKERA-----------GRDYKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVS----------------E 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 320 IERaldymgleagqaitsVPIQHVFIGSCTNSRLSDLERAAEVIRGQQVHEDVRALVVPGSQTVKQQAEEKGIDKIFTDA 399
Cdd:PRK00402 285 VEG---------------TKVDQVFIGSCTNGRLEDLRIAAEILKGRKVAPGVRLIVIPASQKIYLQALKEGLIEIFVDA 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 651990612 400 GFEWREAGCSMCLAMNDDVVPPGERCASTSNRNFEGRQGN-GARTHLVAPEMAAAAAVEGRFTDVRKF 466
Cdd:PRK00402 350 GAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGSpESEVYLASPAVAAASAVTGKITDPREV 417
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
6-464 |
1.47e-116 |
|
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: 348.28 E-value: 1.47e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 6 TIVEKIWDTHVIHqEENKPDLLY--IDLHLVHEVTSPQAFEGL-RMKNRKVRRPDRTFATMDHNVPtiarhfiSDPVSRK 82
Cdd:TIGR01343 1 TIAEKILSKKSGK-EVYAGDLIEaeIDLAMVHDITAPLAIKTLeEYGIDKVWNPEKIVIVFDHQVP-------ADTIKAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 83 QMETL-YDNCQEFDIplADINHPDQGIVHVIGPQLGLTQPGKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSIWQ 161
Cdd:TIGR01343 73 EMQKLaREFVKKQGI--KYFYDVGEGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 162 ARPKTMNVKVNGRLSPSVTAKDLILAIIGKFGVRFGTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTTV 241
Cdd:TIGR01343 151 KVPETIRVNITGKLNPGVTAKDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 242 EFLRGRRhapegaafeeaAASWKALATDDGAAYDAVVSIDAEEVEPQVTWGINPGMCLPVSGtvpspaqaetdaereeie 321
Cdd:TIGR01343 231 QYLKERR-----------KEPFRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSE------------------ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 322 raldymgleagqaITSVPIQHVFIGSCTNSRLSDLERAAEVIRGQQVHEDVRALVVPGSQTVKQQAEEKGIDKIFTDAGF 401
Cdd:TIGR01343 282 -------------VEGTEIDQVFIGSCTNGRLEDLRVAAKILKGRKVAPDVRLIVIPASRAVYLQALKEGLIEIFVKAGA 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 651990612 402 EWREAGCSMCLAMNDDVVPPGERCASTSNRNFEGRQGN-GARTHLVAPEMAAAAAVEGRFTDVR 464
Cdd:TIGR01343 349 VVSTPGCGPCLGSHQGVLAPGEVCISTSNRNFKGRMGHpNAEIYLASPATAAASAVKGYIADPR 412
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
5-464 |
1.43e-102 |
|
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: 312.47 E-value: 1.43e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 5 QTIVEKIWDTHVihQEENKP-DLLY--IDLHLVHEVTSPQAFEGLR-MKNRKVRRPDRTFATMDHNVPTIarhfiSDPVS 80
Cdd:TIGR02086 1 MTLAEKILSEKV--GRPVCAgEIVEveVDLAMTHDGTGPLAIKALReLGVARVWDPEKIVIAFDHNVPPP-----TVEAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 81 RKQMETLyDNCQEFDIPLADINhpdQGIVHVIGPQLGLTQPGKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSIW 160
Cdd:TIGR02086 74 EMQKEIR-EFAKRHGIKNFDVG---EGICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTW 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 161 QARPKTMNVKVNGRLSPSVTAKDLILAIIGKFGVRFGTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTT 240
Cdd:TIGR02086 150 IKVPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEET 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 241 VEFLRGRRhapegaafeeaAASWKALATDDGAAYDAVVSIDAEEVEPQVTWGINPGMCLPVSgtvpspaqaetDAEREEI 320
Cdd:TIGR02086 230 YEYLKKRR-----------GLEFRILVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVS-----------DVEGTEI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 321 ERaldymgleagqaitsvpiqhVFIGSCTNSRLSDLERAAEVIRGQQVHEDVRALVVPGSQTVKQQAEEKGIDKIFTDAG 400
Cdd:TIGR02086 288 DQ--------------------VFIGSCTNGRLEDLRIAAEILKGRRVHPDVRLIVIPASRKVYLRALEEGIILTLVRAG 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 651990612 401 FEWREAGCSMCLAMNDDVVPPGERCASTSNRNFEGRQGN-GARTHLVAPEMAAAAAVEGRFTDVR 464
Cdd:TIGR02086 348 AMICPPGCGPCLGAHMGVLGDGEVCLSTTNRNFKGRMGSpNAEIYLASPATAAASAVEGYITDPE 412
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
104-466 |
1.14e-65 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 222.71 E-value: 1.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 104 PDQGIVHvigpQLGLTQ---PGKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSIWQARPKTMNVKVNGRLSPSVT 180
Cdd:PRK07229 95 PGNGICH----QVHLERfafPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVS 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 181 AKDLILAIIGKFGVRFGTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTTVEFLR--GRRHApegaafee 258
Cdd:PRK07229 171 AKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLKaqGREDD-------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 259 aaasWKALATDDGAAYDAVVSIDAEEVEPQVTWGINPGMCLPVSgtvpspaqaetdaereEIERaldymgleagqaitsV 338
Cdd:PRK07229 243 ----WVELLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVS----------------EVAG---------------I 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 339 PIQHVFIGSCTNSRLSDLERAAEVIRGQQVHEDVRALVVPGSQTVKQQAEEKGIDKIFTDAGFEWREAGCSMCLAMNDDv 418
Cdd:PRK07229 288 KVDQVLIGSCTNSSYEDLMRAASILKGKKVHPKVSLVINPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMGQA- 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 651990612 419 vpPGERCAS--TSNRNFEGRQGN-GARTHLVAPEMAAAAAVEGRFTDVRKF 466
Cdd:PRK07229 367 --PATGNVSlrTFNRNFPGRSGTkDAQVYLASPETAAASALTGVITDPRTL 415
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
104-450 |
3.77e-65 |
|
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Aconitase catalytic domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. Aconitase, in its active form, contains a 4Fe-4S iron-sulfur cluster; three cysteine residues have been shown to be ligands of the 4Fe-4S cluster. This is the Aconitase core domain, including structural domains 1, 2 and 3, which binds the Fe-S cluster. The aconitase family also contains the following proteins: - Iron-responsive element binding protein (IRE-BP), a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid.
Pssm-ID: 153129 [Multi-domain] Cd Length: 389 Bit Score: 215.05 E-value: 3.77e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 104 PDQGIVHVIGPQLGLtQPGKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSIWQARPKTMNVKVNGRLSPSVTAKD 183
Cdd:cd01351 67 PGVGIIHQIMVENLA-LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 184 LILAIIGKFGVRFGTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTTVEFLrgrRHAPEGAAFEEAAASW 263
Cdd:cd01351 146 VVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWL---EATGRPLLKNLWLAFP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 264 KALATDDGAAYDAVVSIDAEEVEPQVtwginpgmCLPVSgtvPSPAQAETDAEREEIERaldymgleagqaitsvpiqhV 343
Cdd:cd01351 223 EELLADEGAEYDQVIEIDLSELEPDI--------SGPNR---PDDAVSVSEVEGTKIDQ--------------------V 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 344 FIGSCTNSRLSDLERAAEVIRGQQVHEDVRALVVPGSQTVKQQAEEKGIDKIFTDAGFEWREAGCSMCLAMNDDVVPPGE 423
Cdd:cd01351 272 LIGSCTNNRYSDMLAAAKLLKGAKVAPGVRLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLVADGE 351
|
330 340
....*....|....*....|....*...
gi 651990612 424 RCASTSNRNFEGRQGNG-ARTHLVAPEM 450
Cdd:cd01351 352 VGVSSGNRNFPGRLGTYeRHVYLASPEL 379
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
104-460 |
4.01e-60 |
|
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: 201.52 E-value: 4.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 104 PDQGIVHvigpQLGLTQ---PGKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSIWQARPKTMNVKVNGRLSPSVT 180
Cdd:cd01585 66 PGNGICH----QVHLERfavPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 181 AKDLILAIIGKFGVRFGTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTTVEFLR--GRrhapegaafee 258
Cdd:cd01585 142 AKDVILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAaqGR----------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 259 aAASWKALATDDGAAYDAVVSIDAEEVEPQVTWGINPGMCLPVsgtvpspaqaetdaerEEIEraldymGLEAGQaitsv 338
Cdd:cd01585 211 -EDDWVELAADADAEYDEEIEIDLSELEPLIARPHSPDNVVPV----------------REVA------GIKVDQ----- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 339 piqhVFIGSCTNSRLSDLERAAEVIRGQQVHEDVRALVVPGSQTVKQQAEEKGIDKIFTDAGFEWREAGCSMCLAMNDdv 418
Cdd:cd01585 263 ----VAIGSCTNSSYEDLMTVAAILKGRRVHPHVSMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQ-- 336
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 651990612 419 VPP-GERCASTSNRNFEGRQGN-GARTHLVAPEMAAAAAVEGRF 460
Cdd:cd01585 337 APPtGGVSVRTFNRNFEGRSGTkDDLVYLASPEVAAAAALTGVI 380
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
104-459 |
9.94e-40 |
|
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: 147.97 E-value: 9.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 104 PDQGIVHvigpQLGLTQ---PGKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSiWQAR-PKTMNVKVNGRLSPSV 179
Cdd:cd01584 74 PGSGIIH----QIVLENyafPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIP-WELKcPKVIGVKLTGKLSGWT 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 180 TAKDLILAIIGKFGVRFGTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTTVEFLR--GRrhapEGAAFE 257
Cdd:cd01584 149 SPKDVILKVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKatGR----AEIADL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 258 EAAASWKALATDDGAAYDAVVSIDAEEVEPQVTWGINPGMCLPVSgtvpspaqaETDAEREEIERALDymgLEAGqaits 337
Cdd:cd01584 225 ADEFKDDLLVADEGAEYDQLIEINLSELEPHINGPFTPDLATPVS---------KFKEVAEKNGWPLD---LRVG----- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 338 vpiqhvFIGSCTNSRLSDLERAAEVIRGQQVHE-DVRAL--VVPGSQTVKQQAEEKGIDKIFTDAGFEWREAGCSMCLAM 414
Cdd:cd01584 288 ------LIGSCTNSSYEDMGRAASIAKQALAHGlKCKSIftITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQ 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 651990612 415 NDDV-VPPGERCA--STSNRNFEGRQGNGARTH--LVAPEMAAAAAVEGR 459
Cdd:cd01584 362 WDRKdIKKGEKNTivTSYNRNFTGRNDANPATHafVASPEIVTAMAIAGT 411
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
33-459 |
1.21e-38 |
|
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase catalytic domain. Homoaconitase and other uncharacterized proteins of the Aconitase family. Homoaconitase is part of an unusual lysine biosynthesis pathway found only in filamentous fungi, in which lysine is synthesized via the alpha-aminoadipate pathway. In this pathway, homoaconitase catalyzes the conversion of cis-homoaconitic acid into homoisocitric acid. The reaction mechanism is believed to be similar to that of other aconitases.
Pssm-ID: 153132 [Multi-domain] Cd Length: 363 Bit Score: 143.91 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 33 LVHEVTSPQAFEGLRMKNRKVRRPDRTFATMDHNVPTiarhfisdpVSRKQMETlYDNCQEFdiplADINHPD-----QG 107
Cdd:cd01582 3 MTHDNSWPVALKFMSIGATKIHNPDQIVMTLDHDVQN---------KSEKNLKK-YKNIESF----AKKHGIDfypagRG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 108 IVHVIGPQLGLTQPGKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSIWQARPKTMNVKVNGRLSPSVTAKDLILA 187
Cdd:cd01582 69 IGHQIMIEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVIVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 188 IIGKFGVRFGTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLIsPDDTTVEFLRgrrhapegaafeeaaaswkaLA 267
Cdd:cd01582 149 LCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLF-PTDAKHLILD--------------------LS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 268 TddgaaydavvsidaeevepqvtwgINPGMCLPVSGTVPSPAQaetDAEREEIEraldymgleagqaitsvpIQHVFIGS 347
Cdd:cd01582 208 T------------------------LSPYVSGPNSVKVSTPLK---ELEAQNIK------------------INKAYLVS 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 348 CTNSRLSDLERAAEVIRGQ-------QVHEDVRALVVPGSQTVKQQAEEKGIDKIFTDAGFEWREAGCSMCLAMNDDVVP 420
Cdd:cd01582 243 CTNSRASDIAAAADVVKGKkekngkiPVAPGVEFYVAAASSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQGLLE 322
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 651990612 421 PGERCASTSNRNFEGRQGN-GARTHLVAPEMAAAAAVEGR 459
Cdd:cd01582 323 PGEVGISATNRNFKGRMGStEALAYLASPAVVAASAISGK 362
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
104-436 |
1.53e-26 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 113.57 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 104 PDQGIVH---------VIGPQLGLTQPgKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSIWQARPKTMNVKVNGR 174
Cdd:PTZ00092 182 PGSGIVHqvnleylarVVFNKDGLLYP-DSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMVLPEVVGFKLTGK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 175 LSPSVTAKDLILAI---IGKFGVrfgTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTTVEFLR--GRRH 249
Cdd:PTZ00092 261 LSEHVTATDLVLTVtsmLRKRGV---VGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKqtGRSE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 250 APEGAAFEEAAASWKALATDDGAAYDAVVSIDAEEVEPQVTWGINPGMCLPVSGTVPSPAQAETD----------AEREE 319
Cdd:PTZ00092 338 EKVELIEKYLKANGLFRTYAEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDLKKDFTACLSApvgfkgfgipEEKHE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 320 IERALDYMGLEAGQAITSVPIQHvfIGSCTNSRLSD-------LERAAeVIRGQQVHEDVRALVVPGSQTVKQQAEEKGI 392
Cdd:PTZ00092 418 KKVKFTYKGKEYTLTHGSVVIAA--ITSCTNTSNPSvmlaaglLAKKA-VEKGLKVPPYIKTSLSPGSKVVTKYLEASGL 494
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 651990612 393 DKI-----FTDAGFewreaGCSMCLAMNDDVVPPGERCAS----------TSNRNFEGR 436
Cdd:PTZ00092 495 LKYleklgFYTAGY-----GCMTCIGNSGDLDPEVSEAITnndlvaaavlSGNRNFEGR 548
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
104-450 |
1.57e-25 |
|
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: 110.19 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 104 PDQGIVHvigpQLGL----------TQPGKTIVCG------DSHTSTHGAFGALAFGIGTSEVEHVLAAQSIWQARPKTM 167
Cdd:COG1048 173 PGTGIVH----QVNLeylafvvwtrEEDGETVAYPdtlvgtDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVV 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 168 NVKVNGRLSPSVTAKDLILAIIG---KFGVrfgTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTTVEFL 244
Cdd:COG1048 249 GVKLTGKLPEGVTATDLVLTVTEmlrKKGV---VGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 245 R--GR--RHAPEGAAFEEAAASWKALATDDgAAYDAVVSIDAEEVEPQVTWGINPGMCLPVSGTVPSPAQAETDAEREEI 320
Cdd:COG1048 326 RltGRseEQIELVEAYAKAQGLWRDPDAPE-PYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAAPVGEEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 321 ERALDYMGLEAGQAIT--SVPIqhVFIGSCTNSRLSDLERAA------EVIRGQQVHEDVRALVVPGSQTVKQQAEEKGI 392
Cdd:COG1048 405 DKPVRVEVDGEEFELGhgAVVI--AAITSCTNTSNPSVMIAAgllakkAVEKGLKVKPWVKTSLAPGSKVVTDYLERAGL 482
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 651990612 393 ----DKI-FTDAGFewreaGCSMCLAMNDDVVPPGER---------CASTS-NRNFEGRQGNGARTHLVA-PEM 450
Cdd:COG1048 483 lpylEALgFNVVGY-----GCTTCIGNSGPLPPEISEaieendlvvAAVLSgNRNFEGRIHPDVKANFLAsPPL 551
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
104-436 |
1.17e-23 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 104.63 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 104 PDQGIVHvigpQLGLTQPGK----------------TIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSIWQARPKTM 167
Cdd:PRK12881 175 PGTGIMH----QVNLEYLARvvhtkeddgdtvaypdTLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIPDVV 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 168 NVKVNGRLSPSVTAKDLILAI---------IGKFgvrfgtgyvLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDD 238
Cdd:PRK12881 251 GVELTGKLREGVTATDLVLTVtemlrkegvVGKF---------VEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 239 TTVEFLRGRRHAPEGAAFEEAAASWKALATDDGAA--YDAVVSIDAEEVEPQVTWGINPGMCLPVSGTVPSPAQAETDAE 316
Cdd:PRK12881 322 QTLDYLRLTGRTEAQIALVEAYAKAQGLWGDPKAEprYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAFSDLFSKPV 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 317 REEieralDYMGLEAGQAITSVPIQHVFIG---SCTNSrlSD---------LERAAeVIRGQQVHEDVRALVVPGSQTVK 384
Cdd:PRK12881 402 AEN-----GFAKKAQTSNGVDLPDGAVAIAaitSCTNT--SNpsvliaaglLAKKA-VERGLTVKPWVKTSLAPGSKVVT 473
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 651990612 385 QQAEEKGIDKIFTDAGFEWREAGCSMCLAMNDDVVPPGER--------CAS--TSNRNFEGR 436
Cdd:PRK12881 474 EYLERAGLLPYLEKLGFGIVGYGCTTCIGNSGPLTPEIEQaitkndlvAAAvlSGNRNFEGR 535
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
103-459 |
2.39e-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: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 103 HPDQGIVHVIGPQLGLtqPGKTIVCGDSHTSthgaFG-ALAFGIGTSEVEHVLAAQSIWQARPKTMNVKVNGRLSPSVTA 181
Cdd:cd01581 90 RPGDGVIHSWLNRMLL--PDTVGTGGDSHTR----FPiGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 182 KDLILAI------------IGKFGVRFGTGYVLEFtgEAIENLTMEERMTICNMSIEAGARAGLISPDDTTV-EFLR--- 245
Cdd:cd01581 164 RDLVNAIpyyaiqqglltvEKKGKKNVFNGRILEI--EGLPDLKVEQAFELTDASAERSAAACTVRLDKEPViEYLEsnv 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 246 ---------GRRHAPEGAAFEEAAASW----KALATDDGAAYDAVVSIDAEEV-EPqvtwginpgmclpvsgTVPSPAQA 311
Cdd:cd01581 242 vlmkimianGYDDARTLLRRIIAMEEWlanpPLLEPDADAEYAAVIEIDLDDIkEP----------------ILACPNDP 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 312 ETDAEREEIeraldymgleAGQaitsvPIQHVFIGSC-TNsrLSDLERAAEVIRGQQvHEDVRALVVPGSQTVKQQAEEK 390
Cdd:cd01581 306 DDVKLLSEV----------AGK-----KIDEVFIGSCmTN--IGHFRAAAKILRGKE-FKPTRLWVAPPTRMDWAILQEE 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 651990612 391 GIDKIFTDAGFEWREAGCSMCLAmNDDVVPPGERCASTSNRNFEGRQGNGARTHLVAPEMAAAAAVEGR 459
Cdd:cd01581 368 GYYSIFGDAGARTEMPGCSLCMG-NQARVADGATVFSTSTRNFDNRVGKGAEVYLGSAELAAVCALLGR 435
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
104-436 |
7.20e-21 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 96.03 E-value: 7.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 104 PDQGIVH---------VIGPQLGLTQPgKTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSIWQARPKTMNVKVNGR 174
Cdd:PLN00070 214 PGSGIVHqvnleylgrVVFNTDGILYP-DSVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 175 LSPSVTAKDLILA---IIGKFGVrfgTGYVLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTTVEFLR--GRRH 249
Cdd:PLN00070 293 LRDGVTATDLVLTvtqMLRKHGV---VGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKltGRSD 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 250 APEGAAFEEAAAS-----WKALATDDgaAYDAVVSIDAEEVEPQVTWGINPGMCLPVSG------------------TVP 306
Cdd:PLN00070 370 ETVAMIEAYLRANkmfvdYNEPQQER--VYSSYLELDLEDVEPCISGPKRPHDRVPLKEmkadwhscldnkvgfkgfAVP 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 307 SPAQAETdAEreeieraLDYMGLEAGQAITSVPIqhVFIGSCTN-SRLSDLERAAEVIR-----GQQVHEDVRALVVPGS 380
Cdd:PLN00070 448 KEAQSKV-AK-------FSFHGQPAELRHGSVVI--AAITSCTNtSNPSVMLGAGLVAKkacelGLEVKPWIKTSLAPGS 517
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 651990612 381 QTVKQQAEEKGIDKIFTDAGFEWREAGCSMCLAMNDDVvppGERCAS-------------TSNRNFEGR 436
Cdd:PLN00070 518 GVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIGNSGEL---DESVASaitendivaaavlSGNRNFEGR 583
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
124-436 |
2.37e-20 |
|
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydrolyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes.
Pssm-ID: 153136 Cd Length: 404 Bit Score: 92.75 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 124 TIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAAQSIWQARPKTMNVKVNGRLSPSVTAKDLILAI---IGKFGVrfgTGY 200
Cdd:cd01586 123 SVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTGKLRPGVTATDLVLTVtqmLRKVGV---VGK 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 201 VLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTTVEflrgrrhapegaafeeaaaswkalatddgaaydavvsI 280
Cdd:cd01586 200 FVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVDTQVVE-------------------------------------L 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 281 DAEEVEPQVTWGINPGMCLPVSGTVpspaqaetdaereeieraldymgleAGQAITsvpiqhvfigSCTN-SRLSDLERA 359
Cdd:cd01586 243 DLSTVEPSVSGPKRPQDRVPLHGSV-------------------------VIAAIT----------SCTNtSNPSVMLAA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 360 A-----EVIRGQQVHEDVRALVVPGSQTVKQQAEEKGIDKIFTDAGFEWREAGCSMCLAMNDDVVPPGER---------C 425
Cdd:cd01586 288 GllakkAVELGLKVKPYVKTSLAPGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGNSGPLPEEVEEaikendlvvA 367
|
330
....*....|..
gi 651990612 426 ASTS-NRNFEGR 436
Cdd:cd01586 368 AVLSgNRNFEGR 379
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
118-438 |
6.04e-20 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 93.15 E-value: 6.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 118 LTQPGKTIVCGDSHTStHGAFGALAFGIGTSEVEHVLAAQSIWQARPKTMNVKVNGRLSPSVTAKDLILAIIGKFgvrFG 197
Cdd:PRK11413 138 MAGGGKMILGSDSHTR-YGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAV---FK 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 198 TGY----VLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTTVEFLR--GRRhapegaafeeaaASWKALATDDG 271
Cdd:PRK11413 214 NGYvknkVMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLAlhGRG------------QDYCELNPQPM 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 272 AAYDAVVSIDAEEVEPQVTWGINPGMCLPVSGTVPSPAQAETDAEREEIERALDYMGLEAGQAITS--VPIQHVFIGSCT 349
Cdd:PRK11413 282 AYYDGCISVDLSAIKPMIALPFHPSNVYEIDELNQNLTDILREVEIESERVAHGKAKLSLLDKIENgrLKVQQGIIAGCS 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 350 NSRLSDLERAAEVIRGQQVHEDVRAL-VVPGSQTVKQQAEEKGIDKIFTDAGFEWREAGCSMCLAMNDdvvPPGERCAST 428
Cdd:PRK11413 362 GGNYENVIAAANALRGQSCGNDTFSLsVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFGAGD---TPANNGLSI 438
|
330
....*....|..
gi 651990612 429 --SNRNFEGRQG 438
Cdd:PRK11413 439 rhTTRNFPNREG 450
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
124-436 |
3.65e-19 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 90.57 E-value: 3.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 124 TIVCGDSHTsTH-GAFGALAFGIGTSEVEHVLAAQSIWQARPKTMNVKVNGRLSPSVTAKDLILAI---------IGKFg 193
Cdd:PRK09277 207 TLVGTDSHT-TMiNGLGVLGWGVGGIEAEAAMLGQPSSMLIPEVVGVKLTGKLPEGVTATDLVLTVtemlrkkgvVGKF- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 194 vrfgtgyvLEFTGEAIENLTMEERMTICNMSIEAGARAGLISPDDTTVEFLR--GRRHAPEgaafeeaaaswkAL----- 266
Cdd:PRK09277 285 --------VEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRltGRDEEQV------------ALveaya 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 267 -------ATDDGAAYDAVVSIDAEEVEPQvtwginpgmclpVSGtvPSPAQ---AETDAE---REEIERALDYMGLEAGQ 333
Cdd:PRK09277 345 kaqglwrDPLEEPVYTDVLELDLSTVEPS------------LAG--PKRPQdriPLSDVKeafAKSAELGVQGFGLDEAE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 334 AITSVPIQH--VFIG---SCTNSrlSD---------LERAAeVIRGQQVHEDVRALVVPGSQTVKQQAEEKG----IDKI 395
Cdd:PRK09277 411 EGEDYELPDgaVVIAaitSCTNT--SNpsvmiaaglLAKKA-VEKGLKVKPWVKTSLAPGSKVVTDYLEKAGllpyLEAL 487
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 651990612 396 -FTDAGFewreaGCSMCLAMNDDVVPPGERC------ASTS----NRNFEGR 436
Cdd:PRK09277 488 gFNLVGY-----GCTTCIGNSGPLPPEIEKAindndlVVTAvlsgNRNFEGR 534
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
103-445 |
3.89e-16 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 81.38 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 103 HPDQGIVHVIGPQLGLtqPGKTIVCGDSHTSTH-G-AFGA----LAFGIGTSEV-----EHVLaaqsiwqarpktmnVKV 171
Cdd:PRK09238 462 RPGDGVIHSWLNRMLL--PDTVGTGGDSHTRFPiGiSFPAgsglVAFAAATGVMpldmpESVL--------------VRF 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 172 NGRLSPSVTAKDLILAI------------IGKFGVRFGTGYVLEFtgEAIENLTMEERMTICNMSIEAGARAGLI-SPDD 238
Cdd:PRK09238 526 KGEMQPGITLRDLVHAIpyyaikqglltvEKKGKKNIFSGRILEI--EGLPDLKVEQAFELTDASAERSAAGCTIkLSKE 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 239 TTVEFLR------------GRRHAPEGAAFEEAAASW----KALATDDGAAYDAVVSIDAEEV-EPQVtwginpgmCLP- 300
Cdd:PRK09238 604 PIIEYLRsnivllkwmiaeGYGDARTLERRIAAMEEWlanpELLEADADAEYAAVIEIDLAEIkEPIL--------ACPn 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 301 ----------VSGTvpspaqaetdaereeieraldymgleagqaitsvPIQHVFIGSC-TNsrLSDLERAAEVIRGQQVH 369
Cdd:PRK09238 676 dpddvrllseVAGT----------------------------------KIDEVFIGSCmTN--IGHFRAAGKLLEGKKGQ 719
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 651990612 370 EDVRALVVPGSQTVKQQAEEKGIDKIFTDAGFEWREAGCSMCLAmNDDVVPPGERCASTSNRNFEGRQGNGARTHL 445
Cdd:PRK09238 720 LPTRLWVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYL 794
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
104-466 |
4.53e-16 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 81.12 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 104 PDQGIVHVIGPQLGLtqPGKTIVCGDSHT------STHGAFGALAFGIGTSEVEHVLaaqsiwqarPKTMNVKVNGRLSP 177
Cdd:PLN00094 537 PGDGVIHSWLNRMLL--PDTVGTGGDSHTrfpigiSFPAGSGLVAFGAATGVIPLDM---------PESVLVRFTGTMQP 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 178 SVTAKDLILAI-----------IGKFG-VRFGTGYVLEFtgEAIENLTMEERMTICNMSIEAGARAGLISPDDTTV-EFL 244
Cdd:PLN00094 606 GITLRDLVHAIpytaiqdglltVEKKGkKNVFSGRILEI--EGLPHLKCEQAFELSDASAERSAAGCTIKLDKEPIiEYL 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 245 R------------GRRHAPEGAAFEEAAASWKA----LATDDGAAYDAVVSIDAEEVEpqvtwgiNPGMCLPvsgtvPSP 308
Cdd:PLN00094 684 NsnvvmlkwmiaeGYGDRRTLERRIARMQQWLAdpelLEADPDAEYAAVIEIDMDEIK-------EPILCAP-----NDP 751
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 309 AQAETDAEreeieraldymgleagqaITSVPIQHVFIGSC-TNsrLSDLERAAEVIRGQQVHEDVRALVVPGSQTVKQQA 387
Cdd:PLN00094 752 DDARLLSE------------------VTGDKIDEVFIGSCmTN--IGHFRAAGKLLNDNLSQLPTRLWVAPPTKMDEAQL 811
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 651990612 388 EEKGIDKIFTDAGFEWREAGCSMCLAmNDDVVPPGERCASTSNRNFEGRQGNGARTHLVAPEMAAAAAVEGRFTDVRKF 466
Cdd:PLN00094 812 KAEGYYSTFGTVGARTEMPGCSLCMG-NQARVAEKSTVVSTSTRNFPNRLGKGANVYLASAELAAVAAILGRLPTVEEY 889
|
|
| AcnB |
COG1049 |
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ... |
128-459 |
8.84e-11 |
|
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440670 [Multi-domain] Cd Length: 852 Bit Score: 64.49 E-value: 8.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 128 GDSHT------STHGAFGALAFGIGTSEV-----EHVLaaqsiwqarpktmnVKVNGRLSPSVTAKDLILAI----I--- 189
Cdd:COG1049 485 GDSHTrfpigiSFPAGSGLVAFAAATGVMpldmpESVL--------------VRFKGEMQPGITLRDLVNAIpyyaIkqg 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 190 -------GKFGVrFgTGYVLEFtgEAIENLTMEERMTICNMSIEAGARAGLISPDDTTV-EFLR------------GRRH 249
Cdd:COG1049 551 lltvekkGKKNI-F-SGRILEI--EGLPDLKVEQAFELSDASAERSAAGCTIKLSKEPViEYLRsniallkwmiaeGYGD 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 250 APEGAAFEEAAASWKA----LATDDGAAYDAVVSIDAEEV-EPQVtwginpgmCLPvsgtvPSPAQAETDAEreeieral 324
Cdd:COG1049 627 ARTLERRIAAMEEWLAnpelLEADADAEYAAVIEIDLNEIkEPIL--------ACP-----NDPDDVKLLSE-------- 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651990612 325 dymgleagqaITSVPIQHVFIGSC-TNsrLSDLERAAEVIRGQQvHEDVRALVVPGSQTVKQQAEEKGIDKIFTDAGFEW 403
Cdd:COG1049 686 ----------VAGTKIDEVFIGSCmTN--IGHFRAAGKLLEGKG-NLPTRLWIAPPTKMDEAQLTEEGYYSIFGAAGART 752
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 651990612 404 REAGCSMCLAmNDDVVPPGERCASTSNRNFEGRQGNGARTHLVAPEMAAAAAVEGR 459
Cdd:COG1049 753 EMPGCSLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYLGSAELAAVCALLGR 807
|
|
| |
