|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
2-473 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 994.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 2 AGKTLYDKLWDMHLVKQRDDGSALIYIDRHILHEVTSPQAFEGLRLAGRKPWRIDANIATPDHNVPTTRTERkggiaAIA 81
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDL-----PIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 82 DEVSRLQVQTLDENCDDFGITEFKMNDVRQGIVHVVGPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLAT 161
Cdd:PRK05478 76 DPVSRIQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 162 QCLVAKKMKNMLVKVEGRLPAGVTAKDIVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAV 241
Cdd:PRK05478 156 QTLLQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 242 DQKTIDYVKGRPFAPSAEQWDQAVACWQGLVSDADARFDTVVELDAAQIKPQVSWGTSPEMVLAVDQNVPDPARESDPIK 321
Cdd:PRK05478 236 DETTFEYLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 322 RGSIERALKYMGLRPNQAITDIQLDRVFIGSCTNSRIEDLRAAAEVARGRKVAATIkQALVVPGSGLVKEQAEKEGLDRI 401
Cdd:PRK05478 316 RASAERALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGV-RALVVPGSGLVKAQAEAEGLDKI 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22095867 402 FIEAGFEWREPGCSMCLAMNPDRLESGEHCASTSNRNFEGRQGAGGRTHLVSPAMAAAAAVNGRFIDVRELL 473
Cdd:PRK05478 395 FIEAGFEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
4-472 |
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: 733.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 4 KTLYDKLWDMHLVKQRDDGSALIYIDRHILHEVTSPQAFEGLRLAGRKPWRIDANIATPDHNVPTTRTErkggiAAIADE 83
Cdd:TIGR00170 3 RTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRD-----FNIKDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 84 VSRLQVQTLDENCDDFGITEFKMNDVRQGIVHVVGPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQC 163
Cdd:TIGR00170 78 VAKIQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 164 LVAKKMKNMLVKVEGRLPAGVTAKDIVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAVDQ 243
Cdd:TIGR00170 158 LKQARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 244 KTIDYVKGRPFAPSAEQWDQAVACWQGLVSDADARFDTVVELDAAQIKPQVSWGTSPEMVLAVDQNVPDPARESDPIKRG 323
Cdd:TIGR00170 238 TTFEYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 324 SIERALKYMGLRPNQAITDIQLDRVFIGSCTNSRIEDLRAAAEVARGRKVAATIKqALVVPGSGLVKEQAEKEGLDRIFI 403
Cdd:TIGR00170 318 SAERALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVK-ALVVPGSGLVKLQAEKEGLDKIFI 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22095867 404 EAGFEWREPGCSMCLAMNPDRLESGEHCASTSNRNFEGRQGAGGRTHLVSPAMAAAAAVNGRFIDVREL 472
Cdd:TIGR00170 397 EAGFEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
3-472 |
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: 697.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 3 GKTLYDKLWDMHLVKQ-RDDGSALIYIDRHILHEVTSPQAFEGLRLAG-RKPWRIDANIATPDHNVPTTrterkggiaai 80
Cdd:COG0065 2 GMTLAEKILARHAGREvEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPTK----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 81 aDEVSRLQVQTLDENCDDFGITEFKMNDVrqGIVHVVGPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLA 160
Cdd:COG0065 71 -DPKSAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 161 TQCLVAKKMKNMLVKVEGRLPAGVTAKDIVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVA 240
Cdd:COG0065 148 TGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 241 VDQKTIDYVKGRPFAPsaeqwdqavacWQGLVSDADARFDTVVELDAAQIKPQVSWGTSPEMVLAVDQnvpdparesdpi 320
Cdd:COG0065 228 PDETTFEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE------------ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 321 krgsieralkymglrpnqaITDIQLDRVFIGSCTNSRIEDLRAAAEVARGRKVAATIKqALVVPGSGLVKEQAEKEGLDR 400
Cdd:COG0065 285 -------------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVR-AIVVPGSQEVYRQAEAEGLDE 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22095867 401 IFIEAGFEWREPGCSMCLAMNPDRLESGEHCASTSNRNFEGRQG-AGGRTHLVSPAMAAAAAVNGRFIDVREL 472
Cdd:COG0065 345 IFIEAGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
8-454 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 693.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 8 DKLWDMHLVKQRDDgsALIYI-DRHILHEVTSPQAFEGLRLAGRKPWRIDANIATPDHNVPTTRT---ERKGGIAAIADE 83
Cdd:pfam00330 1 EKIWDAHLVEELDG--SLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVidhAPDALDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 84 VSR--LQVQTLDENCDDFGITEFKMNdvrQGIVHVVGPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLAT 161
Cdd:pfam00330 79 ISRnkEQYDFLEWNAKKFGIRFVPPG---QGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 162 QCLVAKKMKNMLVKVEGRLPAGVTAKDIVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAV 241
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 242 DQKTIDYVK--GRPFAPSAEQWDQAVAcWQGLVSDADARFDTVVELDAAQIKPQVSWGTSPEMVLAVDQNVPDParESDP 319
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDP--FADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 320 IKRGSIERALKYMGLRPNQAITDIQLDRVFIGSCTNSRIEDLRAAAEVAR-----GRKVAATIKqALVVPGSGLVKEQAE 394
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVK-ASVVPGSEVVRAYAE 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 395 KEGLDRIFIEAGFEWREPGCSMCLAmNPDRLESGEHCASTSNRNFEGRQGAGGRTHLVSP 454
Cdd:pfam00330 392 AEGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASP 450
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
30-466 |
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: 573.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 30 RHILHEVTSPQAFEGLRLAGR-KPWRIDANIATPDHNVPTtrterkggiaaiADEVSRLQVQTLDENCDDFGITEFKMNd 108
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPT------------PDIKAAEQVKTLRKFAKEFGINFFDVG- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 109 vRQGIVHVVGPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQCLVAKKMKNMLVKVEGRLPAGVTAKD 188
Cdd:cd01583 68 -RQGICHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 189 IVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAVDQKTIDYVKGRPFAPsaeqwdqavacW 268
Cdd:cd01583 147 VILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAY-----------W 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 269 QGLVSDADARFDTVVELDAAQIKPQVSWGTSPEMVLAVDQNVPdparesdpikrgsieralkymglrpnqaitdIQLDRV 348
Cdd:cd01583 216 KELKSDEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 349 FIGSCTNSRIEDLRAAAEVARGRKVAATIKqALVVPGSGLVKEQAEKEGLDRIFIEAGFEWREPGCSMCLAMNPDRLESG 428
Cdd:cd01583 265 FIGSCTNGRLEDLRAAAEILKGRKVADGVR-LIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPG 343
|
410 420 430
....*....|....*....|....*....|....*....
gi 22095867 429 EHCASTSNRNFEGRQGAGG-RTHLVSPAMAAAAAVNGRF 466
Cdd:cd01583 344 ERCVSTSNRNFKGRMGSPGaRIYLASPATAAASAITGEI 382
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
26-464 |
3.66e-76 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 244.67 E-value: 3.66e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 26 IYIDRHILHEVTSPQAFEGLRLAGRKPWRIDANIATPDHNVPttrterkggiaAIADEVSRLQVQTLdENCDDFGITEFK 105
Cdd:NF040615 24 VDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVP-----------ANTVKAANMQKITR-EFVKEQGIKNFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 106 MNDvrQGIVHVVGPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQCLVAKKMKNMLVKVEGRLPAgVT 185
Cdd:NF040615 92 LGG--EGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVNIVGKNEN-IS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 186 AKDIVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAVDQKTIDYVKGRPFApsaEQWDQAV 265
Cdd:NF040615 169 GKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEGVS---EEEIAEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 266 ACWQGLVSDADARFDTVVELDAAQIKPQVSWGTSPEMVlavdqnvpdparesdpikrgsieralkymglRPNQAITDIQL 345
Cdd:NF040615 246 KKNRITVNEKEENYYKEIEIDITDMEEQVACPHHPDNV-------------------------------KPVSEVEGTEI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 346 DRVFIGSCTNSRIEDLRAAAEVARGRKVAATIKqALVVPGSGLVKEQAEKEGLDRIFIEAGFEWREPGCSMCLAMNPDRL 425
Cdd:NF040615 295 DQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVR-LIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVL 373
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 22095867 426 ESGEHCASTSNRNFEGRQG-AGGRTHLVSPAMAAAAAVNG 464
Cdd:NF040615 374 GDGEVCLSTTNRNFKGRMGnINSYIYLSSPKIAAKSAVKG 413
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
2-473 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 994.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 2 AGKTLYDKLWDMHLVKQRDDGSALIYIDRHILHEVTSPQAFEGLRLAGRKPWRIDANIATPDHNVPTTRTERkggiaAIA 81
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDL-----PIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 82 DEVSRLQVQTLDENCDDFGITEFKMNDVRQGIVHVVGPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLAT 161
Cdd:PRK05478 76 DPVSRIQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 162 QCLVAKKMKNMLVKVEGRLPAGVTAKDIVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAV 241
Cdd:PRK05478 156 QTLLQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 242 DQKTIDYVKGRPFAPSAEQWDQAVACWQGLVSDADARFDTVVELDAAQIKPQVSWGTSPEMVLAVDQNVPDPARESDPIK 321
Cdd:PRK05478 236 DETTFEYLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 322 RGSIERALKYMGLRPNQAITDIQLDRVFIGSCTNSRIEDLRAAAEVARGRKVAATIkQALVVPGSGLVKEQAEKEGLDRI 401
Cdd:PRK05478 316 RASAERALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGV-RALVVPGSGLVKAQAEAEGLDKI 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22095867 402 FIEAGFEWREPGCSMCLAMNPDRLESGEHCASTSNRNFEGRQGAGGRTHLVSPAMAAAAAVNGRFIDVRELL 473
Cdd:PRK05478 395 FIEAGFEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVRELL 466
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
1-473 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 822.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 1 MAGKTLYDKLWDMHLVKQRDDGSALIYIDRHILHEVTSPQAFEGLRLAGRKPWRIDANIATPDHNVPTtrteRKGGIAAI 80
Cdd:PRK12466 1 MMPRTLYDKLWDSHTVARLDDGHVLLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPT----RPGRDRGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 81 ADEVSRLQVQTLDENCDDFGITEFKMNDVRQGIVHVVGPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLA 160
Cdd:PRK12466 77 TDPGGALQVDYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 161 TQCLVAKKMKNMLVKVEGRLPAGVTAKDIVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVA 240
Cdd:PRK12466 157 TQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 241 VDQKTIDYVKGRPFAPSAEQWDQAVACWQGLVSDADARFDTVVELDAAQIKPQVSWGTSPEMVLAVDQNVPDPARESDPI 320
Cdd:PRK12466 237 PDETTFDYLRGRPRAPKGALWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAAEADPA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 321 KRGSIERALKYMGLRPNQAITDIQLDRVFIGSCTNSRIEDLRAAAEVARGRKVAATIkQALVVPGSGLVKEQAEKEGLDR 400
Cdd:PRK12466 317 RRAAMERALDYMGLTPGTPLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGV-RAMVVPGSGAVRRQAEAEGLAR 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22095867 401 IFIEAGFEWREPGCSMCLAMNPDRLESGEHCASTSNRNFEGRQGAGGRTHLVSPAMAAAAAVNGRFIDVRELL 473
Cdd:PRK12466 396 IFIAAGFEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHITDVRSLL 468
|
|
| leuC |
TIGR00170 |
3-isopropylmalate dehydratase, large subunit; Members of this family are 3-isopropylmalate ... |
4-472 |
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: 733.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 4 KTLYDKLWDMHLVKQRDDGSALIYIDRHILHEVTSPQAFEGLRLAGRKPWRIDANIATPDHNVPTTRTErkggiAAIADE 83
Cdd:TIGR00170 3 RTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRD-----FNIKDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 84 VSRLQVQTLDENCDDFGITEFKMNDVRQGIVHVVGPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQC 163
Cdd:TIGR00170 78 VAKIQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 164 LVAKKMKNMLVKVEGRLPAGVTAKDIVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAVDQ 243
Cdd:TIGR00170 158 LKQARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 244 KTIDYVKGRPFAPSAEQWDQAVACWQGLVSDADARFDTVVELDAAQIKPQVSWGTSPEMVLAVDQNVPDPARESDPIKRG 323
Cdd:TIGR00170 238 TTFEYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 324 SIERALKYMGLRPNQAITDIQLDRVFIGSCTNSRIEDLRAAAEVARGRKVAATIKqALVVPGSGLVKEQAEKEGLDRIFI 403
Cdd:TIGR00170 318 SAERALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVK-ALVVPGSGLVKLQAEKEGLDKIFI 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22095867 404 EAGFEWREPGCSMCLAMNPDRLESGEHCASTSNRNFEGRQGAGGRTHLVSPAMAAAAAVNGRFIDVREL 472
Cdd:TIGR00170 397 EAGFEWREPGCSMCLGMNNDRLPEGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAIHGHFVDIRKF 465
|
|
| LeuC |
COG0065 |
Homoaconitase/3-isopropylmalate dehydratase large subunit [Amino acid transport and metabolism] ... |
3-472 |
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: 697.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 3 GKTLYDKLWDMHLVKQ-RDDGSALIYIDRHILHEVTSPQAFEGLRLAG-RKPWRIDANIATPDHNVPTTrterkggiaai 80
Cdd:COG0065 2 GMTLAEKILARHAGREvEPGEIVLLYIDLHLVHDVTSPQAFEGLREAGgRKVWDPDRIVAVFDHNVPTK----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 81 aDEVSRLQVQTLDENCDDFGITEFKMNDVrqGIVHVVGPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLA 160
Cdd:COG0065 71 -DPKSAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 161 TQCLVAKKMKNMLVKVEGRLPAGVTAKDIVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVA 240
Cdd:COG0065 148 TGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 241 VDQKTIDYVKGRPFAPsaeqwdqavacWQGLVSDADARFDTVVELDAAQIKPQVSWGTSPEMVLAVDQnvpdparesdpi 320
Cdd:COG0065 228 PDETTFEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE------------ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 321 krgsieralkymglrpnqaITDIQLDRVFIGSCTNSRIEDLRAAAEVARGRKVAATIKqALVVPGSGLVKEQAEKEGLDR 400
Cdd:COG0065 285 -------------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVR-AIVVPGSQEVYRQAEAEGLDE 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22095867 401 IFIEAGFEWREPGCSMCLAMNPDRLESGEHCASTSNRNFEGRQG-AGGRTHLVSPAMAAAAAVNGRFIDVREL 472
Cdd:COG0065 345 IFIEAGAEWREPGCGMCLGMNMGVLAPGERCASTSNRNFEGRMGsPGSRTYLASPATAAASAIAGRITDPREL 417
|
|
| Aconitase |
pfam00330 |
Aconitase family (aconitate hydratase); |
8-454 |
0e+00 |
|
Aconitase family (aconitate hydratase);
Pssm-ID: 459764 Cd Length: 460 Bit Score: 693.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 8 DKLWDMHLVKQRDDgsALIYI-DRHILHEVTSPQAFEGLRLAGRKPWRIDANIATPDHNVPTTRT---ERKGGIAAIADE 83
Cdd:pfam00330 1 EKIWDAHLVEELDG--SLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDLVidhAPDALDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 84 VSR--LQVQTLDENCDDFGITEFKMNdvrQGIVHVVGPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLAT 161
Cdd:pfam00330 79 ISRnkEQYDFLEWNAKKFGIRFVPPG---QGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 162 QCLVAKKMKNMLVKVEGRLPAGVTAKDIVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAV 241
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 242 DQKTIDYVK--GRPFAPSAEQWDQAVAcWQGLVSDADARFDTVVELDAAQIKPQVSWGTSPEMVLAVDQNVPDParESDP 319
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDP--FADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 320 IKRGSIERALKYMGLRPNQAITDIQLDRVFIGSCTNSRIEDLRAAAEVAR-----GRKVAATIKqALVVPGSGLVKEQAE 394
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVK-ASVVPGSEVVRAYAE 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 395 KEGLDRIFIEAGFEWREPGCSMCLAmNPDRLESGEHCASTSNRNFEGRQGAGGRTHLVSP 454
Cdd:pfam00330 392 AEGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASP 450
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
30-466 |
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: 573.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 30 RHILHEVTSPQAFEGLRLAGR-KPWRIDANIATPDHNVPTtrterkggiaaiADEVSRLQVQTLDENCDDFGITEFKMNd 108
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGReKVWDPEKIVAVFDHNVPT------------PDIKAAEQVKTLRKFAKEFGINFFDVG- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 109 vRQGIVHVVGPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQCLVAKKMKNMLVKVEGRLPAGVTAKD 188
Cdd:cd01583 68 -RQGICHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 189 IVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAVDQKTIDYVKGRPFAPsaeqwdqavacW 268
Cdd:cd01583 147 VILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGKAY-----------W 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 269 QGLVSDADARFDTVVELDAAQIKPQVSWGTSPEMVLAVDQNVPdparesdpikrgsieralkymglrpnqaitdIQLDRV 348
Cdd:cd01583 216 KELKSDEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 349 FIGSCTNSRIEDLRAAAEVARGRKVAATIKqALVVPGSGLVKEQAEKEGLDRIFIEAGFEWREPGCSMCLAMNPDRLESG 428
Cdd:cd01583 265 FIGSCTNGRLEDLRAAAEILKGRKVADGVR-LIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPG 343
|
410 420 430
....*....|....*....|....*....|....*....
gi 22095867 429 EHCASTSNRNFEGRQGAGG-RTHLVSPAMAAAAAVNGRF 466
Cdd:cd01583 344 ERCVSTSNRNFKGRMGSPGaRIYLASPATAAASAITGEI 382
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
3-473 |
2.63e-119 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 355.64 E-value: 2.63e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 3 GKTLYDKLWDMHLVKQRDDGSALIY-IDRHILHEVTSPQAFEGLRLAG-RKPWRIDANIATPDHNVPTtrterkggiaai 80
Cdd:PRK00402 2 GMTLAEKILARHSGRDVSPGDIVEAkVDLVMAHDITGPLAIKEFEKIGgDKVFDPSKIVIVFDHFVPA------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 81 ADEVSRLQVQTLDENCDDFGITEFkmNDVRQGIVHVVGPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLA 160
Cdd:PRK00402 70 KDIKSAEQQKILREFAKEQGIPNF--FDVGEGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAMA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 161 TQCLVAKKMKNMLVKVEGRLPAGVTAKDIVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVA 240
Cdd:PRK00402 148 TGKTWFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIFA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 241 VDQKTIDYVKGRPFAPsaeqwdqavacWQGLVSDADARFDTVVELDAAQIKPQVSWGTSPEMVLAVDQnvpdparesdpi 320
Cdd:PRK00402 228 PDEKTLEYLKERAGRD-----------YKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSE------------ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 321 krgsieralkymglrpnqaITDIQLDRVFIGSCTNSRIEDLRAAAEVARGRKVAATIkQALVVPGSGLVKEQAEKEGLDR 400
Cdd:PRK00402 285 -------------------VEGTKVDQVFIGSCTNGRLEDLRIAAEILKGRKVAPGV-RLIVIPASQKIYLQALKEGLIE 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22095867 401 IFIEAGFEWREPGCSMCLAMNPDRLESGEHCASTSNRNFEGRQG-AGGRTHLVSPAMAAAAAVNGRFIDVRELL 473
Cdd:PRK00402 345 IFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGsPESEVYLASPAVAAASAVTGKITDPREVL 418
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
28-470 |
4.68e-106 |
|
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: 321.32 E-value: 4.68e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 28 IDRHILHEVTSPQAFEGL-RLAGRKPWRIDANIATPDHNVPTTRTErkggiAAIADEVSRLQVQtldencdDFGITEFkm 106
Cdd:TIGR01343 25 IDLAMVHDITAPLAIKTLeEYGIDKVWNPEKIVIVFDHQVPADTIK-----AAEMQKLAREFVK-------KQGIKYF-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 107 NDVRQGIVHVVGPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQCLVAKKMKNMLVKVEGRLPAGVTA 186
Cdd:TIGR01343 91 YDVGEGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFKVPETIRVNITGKLNPGVTA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 187 KDIVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAVDQKTIDYVKGRPFAPsaeqwdqava 266
Cdd:TIGR01343 171 KDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYLKERRKEP---------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 267 cWQGLVSDADARFDTVVELDAAQIKPQVSWGTSPEMVlavdqnvpDPARESDPIKrgsieralkymglrpnqaitdiqLD 346
Cdd:TIGR01343 241 -FRVYKSDEDAEYAKEIEIDASQIEPVVACPHNVDNV--------KPVSEVEGTE-----------------------ID 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 347 RVFIGSCTNSRIEDLRAAAEVARGRKVAATIkQALVVPGSGLVKEQAEKEGLDRIFIEAGFEWREPGCSMCLAMNPDRLE 426
Cdd:TIGR01343 289 QVFIGSCTNGRLEDLRVAAKILKGRKVAPDV-RLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLGSHQGVLA 367
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 22095867 427 SGEHCASTSNRNFEGRQG-AGGRTHLVSPAMAAAAAVNGRFIDVR 470
Cdd:TIGR01343 368 PGEVCISTSNRNFKGRMGhPNAEIYLASPATAAASAVKGYIADPR 412
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
4-471 |
5.38e-83 |
|
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: 262.01 E-value: 5.38e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 4 KTLYDKLWDMHLVKQRDDGSALIY-IDRHILHEVTSPQAFEGLRLAGR-KPWRIDANIATPDHNVPTTRTErkggiaaia 81
Cdd:TIGR02086 1 MTLAEKILSEKVGRPVCAGEIVEVeVDLAMTHDGTGPLAIKALRELGVaRVWDPEKIVIAFDHNVPPPTVE--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 82 deVSRLQVQTLdENCDDFGITEFkmnDVRQGIVHVVGPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLAT 161
Cdd:TIGR02086 72 --AAEMQKEIR-EFAKRHGIKNF---DVGEGICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 162 QCLVAKKMKNMLVKVEGRLPAGVTAKDIVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAV 241
Cdd:TIGR02086 146 GKTWIKVPETIRVVVEGKPEEGVTAKDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 242 DQKTIDYVKGRPFAPSAEqwdqavacwqgLVSDADARFDTVVELDAAQIKPQVSWGTSPEMVLAVDQnvpdparesdpik 321
Cdd:TIGR02086 226 DEETYEYLKKRRGLEFRI-----------LVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPVSD------------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 322 rgsieralkymglrpnqaITDIQLDRVFIGSCTNSRIEDLRAAAEVARGRKVAATIKqALVVPGSGLVKEQAEKEGLDRI 401
Cdd:TIGR02086 282 ------------------VEGTEIDQVFIGSCTNGRLEDLRIAAEILKGRRVHPDVR-LIVIPASRKVYLRALEEGIILT 342
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22095867 402 FIEAGFEWREPGCSMCLAMNPDRLESGEHCASTSNRNFEGRQGA-GGRTHLVSPAMAAAAAVNGRFIDVRE 471
Cdd:TIGR02086 343 LVRAGAMICPPGCGPCLGAHMGVLGDGEVCLSTTNRNFKGRMGSpNAEIYLASPATAAASAVEGYITDPED 413
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
26-464 |
3.66e-76 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 244.67 E-value: 3.66e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 26 IYIDRHILHEVTSPQAFEGLRLAGRKPWRIDANIATPDHNVPttrterkggiaAIADEVSRLQVQTLdENCDDFGITEFK 105
Cdd:NF040615 24 VDVDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVP-----------ANTVKAANMQKITR-EFVKEQGIKNFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 106 MNDvrQGIVHVVGPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQCLVAKKMKNMLVKVEGRLPAgVT 185
Cdd:NF040615 92 LGG--EGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVNIVGKNEN-IS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 186 AKDIVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAVDQKTIDYVKGRPFApsaEQWDQAV 265
Cdd:NF040615 169 GKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEGVS---EEEIAEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 266 ACWQGLVSDADARFDTVVELDAAQIKPQVSWGTSPEMVlavdqnvpdparesdpikrgsieralkymglRPNQAITDIQL 345
Cdd:NF040615 246 KKNRITVNEKEENYYKEIEIDITDMEEQVACPHHPDNV-------------------------------KPVSEVEGTEI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 346 DRVFIGSCTNSRIEDLRAAAEVARGRKVAATIKqALVVPGSGLVKEQAEKEGLDRIFIEAGFEWREPGCSMCLAMNPDRL 425
Cdd:NF040615 295 DQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVR-LIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGVL 373
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 22095867 426 ESGEHCASTSNRNFEGRQG-AGGRTHLVSPAMAAAAAVNG 464
Cdd:NF040615 374 GDGEVCLSTTNRNFKGRMGnINSYIYLSSPKIAAKSAVKG 413
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
32-454 |
8.33e-69 |
|
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Aconitase catalytic domain. Aconitase (aconitate hydratase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. Aconitase, in its active form, contains a 4Fe-4S iron-sulfur cluster; three cysteine residues have been shown to be ligands of the 4Fe-4S cluster. This is the Aconitase core domain, including structural domains 1, 2 and 3, which binds the Fe-S cluster. The aconitase family also contains the following proteins: - Iron-responsive element binding protein (IRE-BP), a cytosolic protein that binds to iron-responsive elements (IREs). IREs are stem-loop structures found in the 5'UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'UTR of transferrin receptor mRNA. IRE-BP also express aconitase activity. - 3-isopropylmalate dehydratase (isopropylmalate isomerase), the enzyme that catalyzes the second step in the biosynthesis of leucine. - Homoaconitase (homoaconitate hydratase), an enzyme that participates in the alpha-aminoadipate pathway of lysine biosynthesis and that converts cis-homoaconitate into homoisocitric acid.
Pssm-ID: 153129 [Multi-domain] Cd Length: 389 Bit Score: 224.68 E-value: 8.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 32 ILHEVTSPQA---FEGLRLAGrKPWRIDANIATPDHNVPttrterkggiaaIADEVSRLQVQTLDENCDDFGITEFkmnD 108
Cdd:cd01351 3 MLQDATGPMAmkaFEILAALG-KVADPSQIACVHDHAVQ------------LEKPVNNEGHKFLSFFAALQGIAFY---R 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 109 VRQGIVHVVGPEQGAtLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQCLVAKKMKNMLVKVEGRLPAGVTAKD 188
Cdd:cd01351 67 PGVGIIHQIMVENLA-LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 189 IVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAVDQKTIDYVKGRPFAPSAEQWDqavACW 268
Cdd:cd01351 146 VVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWL---AFP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 269 QGLVSDADARFDTVVELDAAQIKPQVSWGTSPEMVlavdqnvpdparesdpikrgsieralkymglRPNQAITDIQLDRV 348
Cdd:cd01351 223 EELLADEGAEYDQVIEIDLSELEPDISGPNRPDDA-------------------------------VSVSEVEGTKIDQV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 349 FIGSCTNSRIEDLRAAAEVARGRKVAATIkQALVVPGSGLVKEQAEKEGLDRIFIEAGFEWREPGCSMCLAMNPDRLESG 428
Cdd:cd01351 272 LIGSCTNNRYSDMLAAAKLLKGAKVAPGV-RLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLVADG 350
|
410 420
....*....|....*....|....*..
gi 22095867 429 EHCASTSNRNFEGRQGAG-GRTHLVSP 454
Cdd:cd01351 351 EVGVSSGNRNFPGRLGTYeRHVYLASP 377
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
89-466 |
2.35e-50 |
|
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: 175.71 E-value: 2.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 89 VQTLDENCDD----------FGITEFKMNDvrqGIVHVVGPEQGAtLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHV 158
Cdd:cd01585 39 LQTDFENADDhrflqtvaarYGIYFSRPGN---GICHQVHLERFA-VPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 159 LATQCLVAKKMKNMLVKVEGRLPAGVTAKDIVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGL 238
Cdd:cd01585 115 MAGEPYYIPMPKVVGVRLTGELPPWVTAKDVILELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 239 VAVDQKTIDYVK--GRPfapsaeqwdqavACWQGLVSDADARFDTVVELDAAQIKPQVSWGTSPEMVLAVdqnvpdpaRE 316
Cdd:cd01585 195 FPSDERTREFLAaqGRE------------DDWVELAADADAEYDEEIEIDLSELEPLIARPHSPDNVVPV--------RE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 317 SDPIKrgsieralkymglrpnqaitdiqLDRVFIGSCTNSRIEDLRAAAEVARGRKVAATIKQAlVVPGSGLVKEQAEKE 396
Cdd:cd01585 255 VAGIK-----------------------VDQVAIGSCTNSSYEDLMTVAAILKGRRVHPHVSMV-VAPGSKQVLEMLARN 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22095867 397 GLDRIFIEAGFEWREPGCSMCLAMN--PdrlESGEHCASTSNRNFEGRQG-AGGRTHLVSPAMAAAAAVNGRF 466
Cdd:cd01585 311 GALADLLAAGARILESACGPCIGMGqaP---PTGGVSVRTFNRNFEGRSGtKDDLVYLASPEVAAAAALTGVI 380
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
112-472 |
7.79e-50 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 179.96 E-value: 7.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 112 GIVHVVGPEQGATlPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQCLVAKKMKNMLVKVEGRLPAGVTAKDIVL 191
Cdd:PRK07229 98 GICHQVHLERFAF-PGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVIL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 192 AVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAVDQKTIDYVK--GRpfapsAEQWDQavacwq 269
Cdd:PRK07229 177 ELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLKaqGR-----EDDWVE------ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 270 gLVSDADARFDTVVELDAAQIKPQVSWGTSPEMVlavdqnvpDPARESDPIKrgsieralkymglrpnqaitdiqLDRVF 349
Cdd:PRK07229 246 -LLADPDAEYDEVIEIDLSELEPLIAGPHSPDNV--------VPVSEVAGIK-----------------------VDQVL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 350 IGSCTNSRIEDLRAAAEVARGRKVAATIKqaLVV-PGSGLVKEQAEKEGLDRIFIEAGFEWREPGCSMCLAMN--PDrle 426
Cdd:PRK07229 294 IGSCTNSSYEDLMRAASILKGKKVHPKVS--LVInPGSRQVLEMLARDGALADLIAAGARILENACGPCIGMGqaPA--- 368
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 22095867 427 SGEHCASTSNRNFEGRQG-AGGRTHLVSPAMAAAAAVNGRFIDVREL 472
Cdd:PRK07229 369 TGNVSLRTFNRNFPGRSGtKDAQVYLASPETAAASALTGVITDPRTL 415
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
111-465 |
2.79e-36 |
|
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: 137.36 E-value: 2.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 111 QGIVHVVGPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQCLVAKKMKNMLVKVEGRLPAGVTAKDIV 190
Cdd:cd01582 67 RGIGHQIMIEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 191 LAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAVDQKTIdyvkgrpfapsaeqwdqavacwqg 270
Cdd:cd01582 147 VALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAKHL------------------------ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 271 lvsdadarfdtvvELDAAQIKPQVSWgtspemvlavdqnvPDPARESDPIKRGSIEralkymglrpnqaitDIQLDRVFI 350
Cdd:cd01582 203 -------------ILDLSTLSPYVSG--------------PNSVKVSTPLKELEAQ---------------NIKINKAYL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 351 GSCTNSRIEDLRAAAEVARGRKVAAtiKQALVVPG--------SGLVKEQAEKEGLDRIFIEAGFEWREPGCSMCLAMNP 422
Cdd:cd01582 241 VSCTNSRASDIAAAADVVKGKKEKN--GKIPVAPGvefyvaaaSSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQ 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 22095867 423 DRLESGEHCASTSNRNFEGRQGA-GGRTHLVSPAMAAAAAVNGR 465
Cdd:cd01582 319 GLLEPGEVGISATNRNFKGRMGStEALAYLASPAVVAASAISGK 362
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
112-442 |
2.71e-32 |
|
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: 130.61 E-value: 2.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 112 GIVH---------VV--GPEQGATL--PGmTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQCLvakkmkNML----- 173
Cdd:COG1048 176 GIVHqvnleylafVVwtREEDGETVayPD-TLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPV------SMLipevv 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 174 -VKVEGRLPAGVTAKDIVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAVDQKTIDYVK-- 250
Cdd:COG1048 249 gVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRlt 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 251 GRpfapSAEQWD--QAVACWQGLVSD---ADARFDTVVELDAAQIKPQVSwGTS--------PEMVLAVDQNVPDPAREs 317
Cdd:COG1048 329 GR----SEEQIElvEAYAKAQGLWRDpdaPEPYYSDVLELDLSTVEPSLA-GPKrpqdriplSDLKEAFRAALAAPVGE- 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 318 DPIKRGSIERALKYMGLrPNQAITdIQLdrvfIGSCTNSRIED-LRAAAEVAR-----GRKVAATIKQALvVPGSGLVKE 391
Cdd:COG1048 403 ELDKPVRVEVDGEEFEL-GHGAVV-IAA----ITSCTNTSNPSvMIAAGLLAKkavekGLKVKPWVKTSL-APGSKVVTD 475
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22095867 392 QAEKEGL----DRI-FIEAGFewrepGCSMCLAmNPDRL---------ESGEHCAS-TS-NRNFEGR 442
Cdd:COG1048 476 YLERAGLlpylEALgFNVVGY-----GCTTCIG-NSGPLppeiseaieENDLVVAAvLSgNRNFEGR 536
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
112-454 |
4.14e-31 |
|
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Mitochondrial aconitase A catalytic domain. Aconitase (also known as aconitate hydratase and citrate hydro-lyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediary product during the course of the reaction. In eukaryotes two isozymes of aconitase are known to exist: one found in the mitochondrial matrix and the other found in the cytoplasm. This is the mitochondrial form. The mitochondrial product is coded by a nuclear gene. Most members of this subfamily are mitochondrial but there are some bacterial members.
Pssm-ID: 153134 Cd Length: 412 Bit Score: 124.09 E-value: 4.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 112 GIVHVVGPEQGAtLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQCLVAKKMKNMLVKVEGRLPAGVTAKDIVL 191
Cdd:cd01584 77 GIIHQIVLENYA-FPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVIL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 192 AVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAVDQKTIDYVKGRPFAPSAEQWDQAVAcwQGL 271
Cdd:cd01584 156 KVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKATGRAEIADLADEFKD--DLL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 272 VSDADARFDTVVELDAAQIKPQVSWGTSPEMVLAVDQNVPDPARESDPIKrgsIERALkymglrpnqaitdiqldrvfIG 351
Cdd:cd01584 234 VADEGAEYDQLIEINLSELEPHINGPFTPDLATPVSKFKEVAEKNGWPLD---LRVGL--------------------IG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 352 SCTNSRIEDLRAAAEVAR-----GRKVAAtikQALVVPGSGLVKEQAEKEGLDRIFIEAGFEWREPGCSMCLAMnPDR-- 424
Cdd:cd01584 291 SCTNSSYEDMGRAASIAKqalahGLKCKS---IFTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQ-WDRkd 366
|
330 340 350
....*....|....*....|....*....|....
gi 22095867 425 LESGEHCA--STSNRNFEGRQGAGGRTH--LVSP 454
Cdd:cd01584 367 IKKGEKNTivTSYNRNFTGRNDANPATHafVASP 400
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
112-442 |
1.42e-29 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 122.81 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 112 GIVH---------VVGPEQGATLPGmTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQCLvakkmkNMLV------KV 176
Cdd:PTZ00092 185 GIVHqvnleylarVVFNKDGLLYPD-SVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPI------SMVLpevvgfKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 177 EGRLPAGVTAKDIVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAVDQKTIDYVK--GRPf 254
Cdd:PTZ00092 258 TGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKqtGRS- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 255 apsAEQWD--QAVACWQGL--VSDADARFDTVVELDAAQIKPQVSWGTSPEmvlavdQNVP--DPARE-----SDP---- 319
Cdd:PTZ00092 337 ---EEKVEliEKYLKANGLfrTYAEQIEYSDVLELDLSTVVPSVAGPKRPH------DRVPlsDLKKDftaclSAPvgfk 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 320 ---IKRGSIERALKYMGLRPNQAITDIQLDRVFIGSCTN-SRIEDLRAAAEVAR-----GRKVAATIKQALvVPGSGLVK 390
Cdd:PTZ00092 408 gfgIPEEKHEKKVKFTYKGKEYTLTHGSVVIAAITSCTNtSNPSVMLAAGLLAKkavekGLKVPPYIKTSL-SPGSKVVT 486
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22095867 391 EQAEKEGLDRIFIEAGFEWREPGCSMCLAMNPDRLESGEHCAS----------TSNRNFEGR 442
Cdd:PTZ00092 487 KYLEASGLLKYLEKLGFYTAGYGCMTCIGNSGDLDPEVSEAITnndlvaaavlSGNRNFEGR 548
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
112-442 |
6.46e-29 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 120.81 E-value: 6.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 112 GIVHVVGPEQGATL-------------PGmTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQCLVakkmknML----- 173
Cdd:PRK12881 178 GIMHQVNLEYLARVvhtkeddgdtvayPD-TLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVY------MLipdvv 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 174 -VKVEGRLPAGVTAKDIVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAVDQKTIDYVK-- 250
Cdd:PRK12881 251 gVELTGKLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLRlt 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 251 GRPFAPSA--EQWDQAvacwQGL--VSDADARFDTVVELDAAQIKPQVSWGTSPEMVLAVDQNvpdPARESDPIKRGSIE 326
Cdd:PRK12881 331 GRTEAQIAlvEAYAKA----QGLwgDPKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNV---KSAFSDLFSKPVAE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 327 RALKYmglrPNQAITDIQLDR--VFIG---SCTN-SRIEDLRAAAEVAR-----GRKVAATIKQALvVPGSGLVKEQAEK 395
Cdd:PRK12881 404 NGFAK----KAQTSNGVDLPDgaVAIAaitSCTNtSNPSVLIAAGLLAKkaverGLTVKPWVKTSL-APGSKVVTEYLER 478
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 22095867 396 EGLDRIFIEAGFEWREPGCSMCLAMN---PDRLES-----GEHCAS--TSNRNFEGR 442
Cdd:PRK12881 479 AGLLPYLEKLGFGIVGYGCTTCIGNSgplTPEIEQaitknDLVAAAvlSGNRNFEGR 535
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
124-453 |
3.16e-24 |
|
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: 104.50 E-value: 3.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 124 TLPGMTVVCGDSHT--STHGAFGAlahgiGTSEVEHVLATQCLVAKKMKNMLVKVEGRLPAGVTAKDIVLAV-------- 193
Cdd:cd01581 104 LLPDTVGTGGDSHTrfPIGISFPA-----GSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVNAIpyyaiqqg 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 194 IGRIGTAGG----NGHAIEFAGsaIRDLSIEGRMTICNMSIEAGARVGLVAVDQKT-IDYV------------KGRPFAP 256
Cdd:cd01581 179 LLTVEKKGKknvfNGRILEIEG--LPDLKVEQAFELTDASAERSAAACTVRLDKEPvIEYLesnvvlmkimiaNGYDDAR 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 257 SAEQWDQAVACWQG----LVSDADARFDTVVELDAAQIKpqvswgtspEMVLAvDQNVPDPAResdpikrgsieralkym 332
Cdd:cd01581 257 TLLRRIIAMEEWLAnpplLEPDADAEYAAVIEIDLDDIK---------EPILA-CPNDPDDVK----------------- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 333 glrPNQAITDIQLDRVFIGSC-TNsrIEDLRAAAEVARGRKVAATikQALVVPGSGLVKEQAEKEGLDRIFIEAGFEWRE 411
Cdd:cd01581 310 ---LLSEVAGKKIDEVFIGSCmTN--IGHFRAAAKILRGKEFKPT--RLWVAPPTRMDWAILQEEGYYSIFGDAGARTEM 382
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 22095867 412 PGCSMCLAmNPDRLESGEHCASTSNRNFEGRQGAGGRTHLVS 453
Cdd:cd01581 383 PGCSLCMG-NQARVADGATVFSTSTRNFDNRVGKGAEVYLGS 423
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
129-442 |
1.06e-23 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 104.82 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 129 TVVCGDSHTsTH-GAFGALAHGIGTSEVEHVLATQCLVakkmknML------VKVEGRLPAGVTAKDIVLAVIGRIGTAG 201
Cdd:PRK09277 207 TLVGTDSHT-TMiNGLGVLGWGVGGIEAEAAMLGQPSS------MLipevvgVKLTGKLPEGVTATDLVLTVTEMLRKKG 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 202 GNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAVDQKTIDYVK--GRpfapSAEQWD--QAVACWQGL--VSDA 275
Cdd:PRK09277 280 VVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRltGR----DEEQVAlvEAYAKAQGLwrDPLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 276 DARFDTVVELDAAQIKPQVSWGTSPEMVLAVDQnvpdpARESdpiKRGSIERALKYMGLRPNQAITDIQLDR--VFIG-- 351
Cdd:PRK09277 356 EPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSD-----VKEA---FAKSAELGVQGFGLDEAEEGEDYELPDgaVVIAai 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 352 -SCTN-SRIEDLRAAAEVAR-----GRKVAATIKQALvVPGSGLVKEQAEKEG----LDRI-FIEAGFewrepGCSMCLA 419
Cdd:PRK09277 428 tSCTNtSNPSVMIAAGLLAKkavekGLKVKPWVKTSL-APGSKVVTDYLEKAGllpyLEALgFNLVGY-----GCTTCIG 501
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 22095867 420 MN---PDRLE--------------SGehcastsNRNFEGR 442
Cdd:PRK09277 502 NSgplPPEIEkaindndlvvtavlSG-------NRNFEGR 534
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
113-442 |
1.20e-22 |
|
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: 99.69 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 113 IVHVVGPEQGATLPGMTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQCLVAKKMKNMLVKVEGRLPAGVTAKDIVLA 192
Cdd:cd01586 107 VVFTSEEDGDGVAYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTGKLRPGVTATDLVLT 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 193 VIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAVDqktidyvkgrpfapsaeqwdqavacwqglv 272
Cdd:cd01586 187 VTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVD------------------------------ 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 273 sdadarfDTVVELDAAQIKPQVSWGTSPEMVLAVDqnvpdparesdpikrGSIERAlkymglrpnqAITdiqldrvfigS 352
Cdd:cd01586 237 -------TQVVELDLSTVEPSVSGPKRPQDRVPLH---------------GSVVIA----------AIT----------S 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 353 CTN-SRIEDLRAAAEVAR-----GRKVAATIKQALvVPGSGLVKEQAEKEGLDRIFIEAGFEWREPGCSMCLAMN---PD 423
Cdd:cd01586 275 CTNtSNPSVMLAAGLLAKkavelGLKVKPYVKTSL-APGSRVVTKYLEASGLLPYLEKLGFHVVGYGCTTCIGNSgplPE 353
|
330 340
....*....|....*....|....*.
gi 22095867 424 RLESG--EH----CASTS-NRNFEGR 442
Cdd:cd01586 354 EVEEAikENdlvvAAVLSgNRNFEGR 379
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
112-454 |
1.72e-22 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 101.04 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 112 GIVHVVGPE---------QGATLPGmTVVCGDSHTSTHGAFGALAHGIGTSEVEHVLATQclvakKMKNML-----VKVE 177
Cdd:PLN00070 217 GIVHQVNLEylgrvvfntDGILYPD-SVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQ-----PMSMVLpgvvgFKLS 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 178 GRLPAGVTAKDIVLAVIGRIGTAGGNGHAIEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAVDQKTIDYVK--GRPfa 255
Cdd:PLN00070 291 GKLRDGVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKltGRS-- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 256 psaeqwDQAVACWQGLV-----------SDADARFDTVVELDAAQIKPQVSWGTSP-------EMV-------------- 303
Cdd:PLN00070 369 ------DETVAMIEAYLrankmfvdynePQQERVYSSYLELDLEDVEPCISGPKRPhdrvplkEMKadwhscldnkvgfk 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 304 -LAVDQNVPDPARESD------PIKRGSIERAlkymglrpnqAITdiqldrvfigSCTN-SRIEDLRAAAEVAR-----G 370
Cdd:PLN00070 443 gFAVPKEAQSKVAKFSfhgqpaELRHGSVVIA----------AIT----------SCTNtSNPSVMLGAGLVAKkacelG 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 371 RKVAATIKQALvVPGSGLVKEQAEKEGLDRIFIEAGFEWREPGCSMCLAMNPDRLESGEHCAS----------TSNRNFE 440
Cdd:PLN00070 503 LEVKPWIKTSL-APGSGVVTKYLLKSGLQKYLNQQGFHIVGYGCTTCIGNSGELDESVASAITendivaaavlSGNRNFE 581
|
410
....*....|....*
gi 22095867 441 GRQGAGGR-THLVSP 454
Cdd:PLN00070 582 GRVHPLTRaNYLASP 596
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
133-453 |
7.27e-17 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 83.69 E-value: 7.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 133 GDSHTSTH-G-AFGAlahGIGTseVEHVLATqclvaKKMK-NM----LVKVEGRLPAGVTAKDIVLAV----IGR----I 197
Cdd:PRK09238 485 GDSHTRFPiGiSFPA---GSGL--VAFAAAT-----GVMPlDMpesvLVRFKGEMQPGITLRDLVHAIpyyaIKQglltV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 198 GTAGG----NGHAIEFAGsaIRDLSIEGRMTICNMSIEAGARVGLVAVDQKT-IDYV------------KGRPFAPSAEQ 260
Cdd:PRK09238 555 EKKGKknifSGRILEIEG--LPDLKVEQAFELTDASAERSAAGCTIKLSKEPiIEYLrsnivllkwmiaEGYGDARTLER 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 261 WDQAVACWQG----LVSDADARFDTVVELDAAQIKpqvswgtspEMVLAvDQNVPDPAResdpikrgsieralkymglrP 336
Cdd:PRK09238 633 RIAAMEEWLAnpelLEADADAEYAAVIEIDLAEIK---------EPILA-CPNDPDDVR--------------------L 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 337 NQAITDIQLDRVFIGSC-TNsrIEDLRAAAEVARGRKVaaTIKQALVV-PGSGLVKEQAEKEGLDRIFIEAGFEWREPGC 414
Cdd:PRK09238 683 LSEVAGTKIDEVFIGSCmTN--IGHFRAAGKLLEGKKG--QLPTRLWVaPPTKMDADQLTEEGYYSIFGKAGARIEMPGC 758
|
330 340 350
....*....|....*....|....*....|....*....
gi 22095867 415 SMCLAmNPDRLESGEHCASTSNRNFEGRQGAGGRTHLVS 453
Cdd:PRK09238 759 SLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYLGS 796
|
|
| AcnB |
COG1049 |
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ... |
271-453 |
1.96e-13 |
|
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: 72.58 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 271 LVSDADARFDTVVELDAAQIKpqvswgtspEMVLAVdQNVPDPAR-----ESDPIkrgsieralkymglrpnqaitdiql 345
Cdd:COG1049 647 LEADADAEYAAVIEIDLNEIK---------EPILAC-PNDPDDVKllsevAGTKI------------------------- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 346 DRVFIGSC-TNsrIEDLRAAAEVARGRKVAATikQALVVPGSGLVKEQAEKEGLDRIFIEAGFEWREPGCSMCLAmNPDR 424
Cdd:COG1049 692 DEVFIGSCmTN--IGHFRAAGKLLEGKGNLPT--RLWIAPPTKMDEAQLTEEGYYSIFGAAGARTEMPGCSLCMG-NQAR 766
|
170 180
....*....|....*....|....*....
gi 22095867 425 LESGEHCASTSNRNFEGRQGAGGRTHLVS 453
Cdd:COG1049 767 VADGATVFSTSTRNFPNRLGKGANVYLGS 795
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
125-474 |
3.81e-13 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 71.88 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 125 LPGMTVVCGDSHTSthgafgaLAHGI----GTSEVEHVLATQCLVAKKMKNMLVKVEGRLPAGVTAKDIVLAV------I 194
Cdd:PLN00094 551 LPDTVGTGGDSHTR-------FPIGIsfpaGSGLVAFGAATGVIPLDMPESVLVRFTGTMQPGITLRDLVHAIpytaiqD 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 195 GRIgTAGGNGHAIEFAGsaiRDLSIEG--------RMTICNMSIEAGARVGLVAVDQKTI-----------------DYV 249
Cdd:PLN00094 624 GLL-TVEKKGKKNVFSG---RILEIEGlphlkceqAFELSDASAERSAAGCTIKLDKEPIieylnsnvvmlkwmiaeGYG 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 250 KGRPFAPSAEQWDQAVACWQGLVSDADARFDTVVELDAAQIKpqvswgtspEMVLAVdQNVPDPARESdpikrgsieral 329
Cdd:PLN00094 700 DRRTLERRIARMQQWLADPELLEADPDAEYAAVIEIDMDEIK---------EPILCA-PNDPDDARLL------------ 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 330 kymglrpnQAITDIQLDRVFIGSC-TNsrIEDLRAAAEVARGRKvaATIKQAL-VVPGSGLVKEQAEKEGLDRIFIEAGF 407
Cdd:PLN00094 758 --------SEVTGDKIDEVFIGSCmTN--IGHFRAAGKLLNDNL--SQLPTRLwVAPPTKMDEAQLKAEGYYSTFGTVGA 825
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22095867 408 EWREPGCSMCLAmNPDRLESGEHCASTSNRNFEGRQGAGGRTHLVSPAMAAAAAVNGRFIDVRELLA 474
Cdd:PLN00094 826 RTEMPGCSLCMG-NQARVAEKSTVVSTSTRNFPNRLGKGANVYLASAELAAVAAILGRLPTVEEYLS 891
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
128-444 |
1.21e-08 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 57.33 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 128 MTVVCG------DSHTStHGAFGALAHGIGTSEVEHVLATQCLVAKKMKNMLVKVEGRLPAGVTAKDIVLAVIGRIGtag 201
Cdd:PRK11413 137 MMAGGGkmilgsDSHTR-YGALGTMAVGEGGGELVKQLLNDTYDIDYPGVVAVYLTGKPAPGVGPQDVALAIIGAVF--- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 202 GNGHA----IEFAGSAIRDLSIEGRMTICNMSIEAGARVGLVAVDQKTIDYVK--GRPFApsaeqwdqavacWQGLVSDA 275
Cdd:PRK11413 213 KNGYVknkvMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLAlhGRGQD------------YCELNPQP 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 276 DARFDTVVELDAAQIKPQVSWGTSPEMVLAVDQ---NVPDPAREsdpIKRGSIERALKYMGLRPNQAITD--IQLDRVFI 350
Cdd:PRK11413 281 MAYYDGCISVDLSAIKPMIALPFHPSNVYEIDElnqNLTDILRE---VEIESERVAHGKAKLSLLDKIENgrLKVQQGII 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22095867 351 GSCTNSRIEDLRAAAEVARGRKVAATIKQALVVPGSGLVKEQAEKEGLDRIFIEAGFEWREPGCSMCLAMNpDRLESGEH 430
Cdd:PRK11413 358 AGCSGGNYENVIAAANALRGQSCGNDTFSLSVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFGAG-DTPANNGL 436
|
330
....*....|....
gi 22095867 431 CASTSNRNFEGRQG 444
Cdd:PRK11413 437 SIRHTTRNFPNREG 450
|
|
| |
