|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
2-472 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 985.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 2 AGKTLYDKLWDDHVVSQRDDGSCLLYIDRHLLHEVTSPQAFEGLQLADRQPWRLSANVATPDHNVPTSKKERdqgiaGIE 81
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDL-----PIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 82 DDTSRIQVQTLDDNCKAFNIVEFSINDIRQGIVHVVGPEQGLTLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLAT 161
Cdd:PRK05478 76 DPVSRIQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 162 QCLIQKKSKNMLVRVDGVLGKGVTPKDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAV 241
Cdd:PRK05478 156 QTLLQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 242 DDKTIEYVKGRSYAPKGEQWEQAVAYWNTLHSDEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEAVPTLEQAKDDVQ 321
Cdd:PRK05478 236 DETTFEYLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 322 RNDWTRAYQYMGLNAGQALADIQLDRVFIGSCTNSRIEDIRAAAEVVKGRKVASTIkQAMIVPGSGLVKQQAEKEGLDKI 401
Cdd:PRK05478 316 RASAERALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGV-RALVVPGSGLVKAQAEAEGLDKI 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488043610 402 FLEAGFEWREPGCSMCLAMNADKLQPGEHCASTSNRNFEGRQGNGGRTHLVSPAMAAAAAIAGHFVDVRSF 472
Cdd:PRK05478 395 FIEAGFEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVREL 465
|
|
| 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: 735.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 4 KTLYDKLWDDHVVSQRDDGSCLLYIDRHLLHEVTSPQAFEGLQLADRQPWRLSANVATPDHNVPTSKKERDqgiagIEDD 83
Cdd:TIGR00170 3 RTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFN-----IKDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 84 TSRIQVQTLDDNCKAFNIVEFSINDIRQGIVHVVGPEQGLTLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLATQC 163
Cdd:TIGR00170 78 VAKIQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 164 LIQKKSKNMLVRVDGVLGKGVTPKDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAVDD 243
Cdd:TIGR00170 158 LKQARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 244 KTIEYVKGRSYAPKGEQWEQAVAYWNTLHSDEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEAVPTLEQAKDDVQRN 323
Cdd:TIGR00170 238 TTFEYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 324 DWTRAYQYMGLNAGQALADIQLDRVFIGSCTNSRIEDIRAAAEVVKGRKVASTIKqAMIVPGSGLVKQQAEKEGLDKIFL 403
Cdd:TIGR00170 318 SAERALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVK-ALVVPGSGLVKLQAEKEGLDKIFI 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488043610 404 EAGFEWREPGCSMCLAMNADKLQPGEHCASTSNRNFEGRQGNGGRTHLVSPAMAAAAAIAGHFVDVRSF 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: 698.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 3 GKTLYDKLWDDHVVSQ-RDDGSCLLYIDRHLLHEVTSPQAFEGLQLA-DRQPWRLSANVATPDHNVPTSkkerdqgiagi 80
Cdd:COG0065 2 GMTLAEKILARHAGREvEPGEIVLLYIDLHLVHDVTSPQAFEGLREAgGRKVWDPDRIVAVFDHNVPTK----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 81 eDDTSRIQVQTLDDNCKAFNIVEFSINDIrqGIVHVVGPEQGLTLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLA 160
Cdd:COG0065 71 -DPKSAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 161 TQCLIQKKSKNMLVRVDGVLGKGVTPKDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVA 240
Cdd:COG0065 148 TGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 241 VDDKTIEYVKGRSYAPkgeqweqavayWNTLHSDEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEavptleqakddv 320
Cdd:COG0065 228 PDETTFEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE------------ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 321 qrndwtrayqymglnagqaLADIQLDRVFIGSCTNSRIEDIRAAAEVVKGRKVASTIKqAMIVPGSGLVKQQAEKEGLDK 400
Cdd:COG0065 285 -------------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVR-AIVVPGSQEVYRQAEAEGLDE 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488043610 401 IFLEAGFEWREPGCSMCLAMNADKLQPGEHCASTSNRNFEGRQGN-GGRTHLVSPAMAAAAAIAGHFVDVRSF 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: 691.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 8 DKLWDDHVVSQRDDgsCLLYI-DRHLLHEVTSPQAFEGLQLADRQPWRLSANVATPDHNVPTS---KKERDQGIAGIEDD 83
Cdd:pfam00330 1 EKIWDAHLVEELDG--SLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDlviDHAPDALDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 84 TSRI--QVQTLDDNCKAFNIVEFsinDIRQGIVHVVGPEQGLTLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLAT 161
Cdd:pfam00330 79 ISRNkeQYDFLEWNAKKFGIRFV---PPGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 162 QCLIQKKSKNMLVRVDGVLGKGVTPKDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAV 241
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 242 DDKTIEYVK--GRSYAPKGEQWEQAVAyWNTLHSDEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEAVPTLEqaKDD 319
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDPF--ADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 320 VQRNDWTRAYQYMGLNAGQALADIQLDRVFIGSCTNSRIEDIRAAAEVVK-----GRKVASTIKqAMIVPGSGLVKQQAE 394
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVK-ASVVPGSEVVRAYAE 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 395 KEGLDKIFLEAGFEWREPGCSMCLAmNADKLQPGEHCASTSNRNFEGRQGNGGRTHLVSP 454
Cdd:pfam00330 392 AEGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASP 450
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
30-454 |
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: 572.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 30 RHLLHEVTSPQAFEGLQLADRQ-PWRLSANVATPDHNVPTSkkerdqgiagieDDTSRIQVQTLDDNCKAFNIVEFSINd 108
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREkVWDPEKIVAVFDHNVPTP------------DIKAAEQVKTLRKFAKEFGINFFDVG- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 109 iRQGIVHVVGPEQGLTLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLATQCLIQKKSKNMLVRVDGVLGKGVTPKD 188
Cdd:cd01583 68 -RQGICHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 189 VVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAVDDKTIEYVKGRSYapkgeqweqavAYW 268
Cdd:cd01583 147 VILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGK-----------AYW 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 269 NTLHSDEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEAVPtleqakddvqrndwtrayqymglnagqaladIQLDRV 348
Cdd:cd01583 216 KELKSDEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 349 FIGSCTNSRIEDIRAAAEVVKGRKVASTIKqAMIVPGSGLVKQQAEKEGLDKIFLEAGFEWREPGCSMCLAMNADKLQPG 428
Cdd:cd01583 265 FIGSCTNGRLEDLRAAAEILKGRKVADGVR-LIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPG 343
|
410 420
....*....|....*....|....*..
gi 488043610 429 EHCASTSNRNFEGRQGNGG-RTHLVSP 454
Cdd:cd01583 344 ERCVSTSNRNFKGRMGSPGaRIYLASP 370
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
28-454 |
2.05e-80 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 255.45 E-value: 2.05e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 28 IDRHLLHEVTSPQAFEGLQLADRQPWRLSANVATPDHNVP--TSKKERDQGIAgieddtsriqvqtlDDNCKAFNIVEFS 105
Cdd:NF040615 26 VDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPanTVKAANMQKIT--------------REFVKEQGIKNFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 106 INDirQGIVHVVGPEQGLTLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLATQCLIQKKSKNMLVRVDGvLGKGVT 185
Cdd:NF040615 92 LGG--EGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVNIVG-KNENIS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 186 PKDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAVDDKTIEYVKGRSYAPKgeqwEQAV 265
Cdd:NF040615 169 GKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEGVSEE----EIAE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 266 AYWNTLHSDED-AVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEAVPTleqakddvqrndwtrayqymglnagqaladiQ 344
Cdd:NF040615 245 LKKNRITVNEKeENYYKEIEIDITDMEEQVACPHHPDNVKPVSEVEGT-------------------------------E 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 345 LDRVFIGSCTNSRIEDIRAAAEVVKGRKVASTIKqAMIVPGSGLVKQQAEKEGLDKIFLEAGFEWREPGCSMCLAMNADK 424
Cdd:NF040615 294 IDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVR-LIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGV 372
|
410 420 430
....*....|....*....|....*....|.
gi 488043610 425 LQPGEHCASTSNRNFEGRQGN-GGRTHLVSP 454
Cdd:NF040615 373 LGDGEVCLSTTNRNFKGRMGNiNSYIYLSSP 403
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05478 |
PRK05478 |
3-isopropylmalate dehydratase large subunit; |
2-472 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 235490 Cd Length: 466 Bit Score: 985.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 2 AGKTLYDKLWDDHVVSQRDDGSCLLYIDRHLLHEVTSPQAFEGLQLADRQPWRLSANVATPDHNVPTSKKERdqgiaGIE 81
Cdd:PRK05478 1 MGKTLYDKLWDAHVVHEEEDGPDLLYIDRHLVHEVTSPQAFEGLRLAGRKVRRPDLTFATMDHNVPTTDRDL-----PIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 82 DDTSRIQVQTLDDNCKAFNIVEFSINDIRQGIVHVVGPEQGLTLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLAT 161
Cdd:PRK05478 76 DPVSRIQVETLEKNCKEFGITLFDLGDPRQGIVHVVGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 162 QCLIQKKSKNMLVRVDGVLGKGVTPKDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAV 241
Cdd:PRK05478 156 QTLLQKKPKTMKIEVDGKLPPGVTAKDIILAIIGKIGTAGGTGYVIEFAGEAIRALSMEGRMTICNMSIEAGARAGLVAP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 242 DDKTIEYVKGRSYAPKGEQWEQAVAYWNTLHSDEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEAVPTLEQAKDDVQ 321
Cdd:PRK05478 236 DETTFEYLKGRPFAPKGEDWDKAVAYWKTLKSDEDAVFDKVVTLDAADIEPQVTWGTNPGQVISIDGKVPDPEDFADPVK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 322 RNDWTRAYQYMGLNAGQALADIQLDRVFIGSCTNSRIEDIRAAAEVVKGRKVASTIkQAMIVPGSGLVKQQAEKEGLDKI 401
Cdd:PRK05478 316 RASAERALAYMGLKPGTPITDIKIDKVFIGSCTNSRIEDLRAAAAVVKGRKVAPGV-RALVVPGSGLVKAQAEAEGLDKI 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488043610 402 FLEAGFEWREPGCSMCLAMNADKLQPGEHCASTSNRNFEGRQGNGGRTHLVSPAMAAAAAIAGHFVDVRSF 472
Cdd:PRK05478 395 FIEAGFEWREPGCSMCLAMNPDKLPPGERCASTSNRNFEGRQGKGGRTHLVSPAMAAAAAITGHFVDVREL 465
|
|
| PRK12466 |
PRK12466 |
3-isopropylmalate dehydratase large subunit; |
1-472 |
0e+00 |
|
3-isopropylmalate dehydratase large subunit;
Pssm-ID: 183543 Cd Length: 471 Bit Score: 811.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 1 MAGKTLYDKLWDDHVVSQRDDGSCLLYIDRHLLHEVTSPQAFEGLQLADRQPWRLSANVATPDHNVPTskkeRDQGIAGI 80
Cdd:PRK12466 1 MMPRTLYDKLWDSHTVARLDDGHVLLYIDRHLLNEYTSPQAFSGLRARGRTVRRPDLTLAVVDHVVPT----RPGRDRGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 81 EDDTSRIQVQTLDDNCKAFNIVEFSINDIRQGIVHVVGPEQGLTLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLA 160
Cdd:PRK12466 77 TDPGGALQVDYLRENCADFGIRLFDVDDPRQGIVHVVAPELGLTLPGMVIVCGDSHTTTYGALGALAFGIGTSEVEHVLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 161 TQCLIQKKSKNMLVRVDGVLGKGVTPKDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVA 240
Cdd:PRK12466 157 TQTLVYRKPKTMRVRVDGELPPGVTAKDLILALIARIGADGATGYAIEFAGEAIRALSMEGRMTLCNMAVEAGARGGLIA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 241 VDDKTIEYVKGRSYAPKGEQWEQAVAYWNTLHSDEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEAVPTLEQAKDDV 320
Cdd:PRK12466 237 PDETTFDYLRGRPRAPKGALWDAALAYWRTLRSDADAVFDREVEIDAADIAPQVTWGTSPDQAVPITGRVPDPAAEADPA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 321 QRNDWTRAYQYMGLNAGQALADIQLDRVFIGSCTNSRIEDIRAAAEVVKGRKVASTIkQAMIVPGSGLVKQQAEKEGLDK 400
Cdd:PRK12466 317 RRAAMERALDYMGLTPGTPLAGIPIDRVFIGSCTNGRIEDLRAAAAVLRGRKVAPGV-RAMVVPGSGAVRRQAEAEGLAR 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488043610 401 IFLEAGFEWREPGCSMCLAMNADKLQPGEHCASTSNRNFEGRQGNGGRTHLVSPAMAAAAAIAGHFVDVRSF 472
Cdd:PRK12466 396 IFIAAGFEWREPGCSMCLAMNDDVLAPGERCASTTNRNFEGRQGPGARTHLMSPAMVAAAAVAGHITDVRSL 467
|
|
| 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: 735.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 4 KTLYDKLWDDHVVSQRDDGSCLLYIDRHLLHEVTSPQAFEGLQLADRQPWRLSANVATPDHNVPTSKKERDqgiagIEDD 83
Cdd:TIGR00170 3 RTLYEKLFDAHIVYEAEGETPLLYIDRHLIHEVTSPQAFEGLRQAGRKVRRPQKTFATMDHNIPTQNRDFN-----IKDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 84 TSRIQVQTLDDNCKAFNIVEFSINDIRQGIVHVVGPEQGLTLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLATQC 163
Cdd:TIGR00170 78 VAKIQVTELEKNCKEFGVRLFDLHSVDQGIVHVMGPEQGLTLPGMTIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 164 LIQKKSKNMLVRVDGVLGKGVTPKDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAVDD 243
Cdd:TIGR00170 158 LKQARAKTMKIEVDGKLAPGITAKDIILAIIGKTGVAGGTGHVIEFCGEAIRDLSMEGRMTVCNMAIEAGARAGLIAPDE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 244 KTIEYVKGRSYAPKGEQWEQAVAYWNTLHSDEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEAVPTLEQAKDDVQRN 323
Cdd:TIGR00170 238 TTFEYCKGRPHAPKGKEFDKAVAYWKTLKTDEGAVFDTVITLEANDISPQVTWGTNPGQVLPVNSEVPDPESFADPVDKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 324 DWTRAYQYMGLNAGQALADIQLDRVFIGSCTNSRIEDIRAAAEVVKGRKVASTIKqAMIVPGSGLVKQQAEKEGLDKIFL 403
Cdd:TIGR00170 318 SAERALAYMGLEPGTPLKDIKVDKVFIGSCTNSRIEDLRAAAAVIKGRKVADNVK-ALVVPGSGLVKLQAEKEGLDKIFI 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488043610 404 EAGFEWREPGCSMCLAMNADKLQPGEHCASTSNRNFEGRQGNGGRTHLVSPAMAAAAAIAGHFVDVRSF 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: 698.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 3 GKTLYDKLWDDHVVSQ-RDDGSCLLYIDRHLLHEVTSPQAFEGLQLA-DRQPWRLSANVATPDHNVPTSkkerdqgiagi 80
Cdd:COG0065 2 GMTLAEKILARHAGREvEPGEIVLLYIDLHLVHDVTSPQAFEGLREAgGRKVWDPDRIVAVFDHNVPTK----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 81 eDDTSRIQVQTLDDNCKAFNIVEFSINDIrqGIVHVVGPEQGLTLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLA 160
Cdd:COG0065 71 -DPKSAEQVKTLREFAKEFGITFFDVGDP--GICHVVLPEQGLVLPGMTIVGGDSHTCTHGAFGAFAFGIGTTDVAHVLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 161 TQCLIQKKSKNMLVRVDGVLGKGVTPKDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVA 240
Cdd:COG0065 148 TGTLWFKVPETMRIEVTGKLPPGVTAKDLILAIIGKIGADGATGKAIEFAGEAIRALSMEERMTLCNMAIEAGAKAGIIA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 241 VDDKTIEYVKGRSYAPkgeqweqavayWNTLHSDEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEavptleqakddv 320
Cdd:COG0065 228 PDETTFEYLKGRPFAP-----------WRTLKSDEDAVYDKEVEIDASDLEPQVAWPHSPDNVVPVSE------------ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 321 qrndwtrayqymglnagqaLADIQLDRVFIGSCTNSRIEDIRAAAEVVKGRKVASTIKqAMIVPGSGLVKQQAEKEGLDK 400
Cdd:COG0065 285 -------------------LEGIKIDQVFIGSCTNGRIEDLRAAAEILKGRKVAPGVR-AIVVPGSQEVYRQAEAEGLDE 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488043610 401 IFLEAGFEWREPGCSMCLAMNADKLQPGEHCASTSNRNFEGRQGN-GGRTHLVSPAMAAAAAIAGHFVDVRSF 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: 691.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 8 DKLWDDHVVSQRDDgsCLLYI-DRHLLHEVTSPQAFEGLQLADRQPWRLSANVATPDHNVPTS---KKERDQGIAGIEDD 83
Cdd:pfam00330 1 EKIWDAHLVEELDG--SLLYIpDRVLMHDVTSPQAFVDLRAAGRAVRRPGGTPATIDHLVPTDlviDHAPDALDKNIEDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 84 TSRI--QVQTLDDNCKAFNIVEFsinDIRQGIVHVVGPEQGLTLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLAT 161
Cdd:pfam00330 79 ISRNkeQYDFLEWNAKKFGIRFV---PPGQGIVHQVGLEYGLALPGMTIVGTDSHTTTHGGLGALAFGVGGSEAEHVLAT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 162 QCLIQKKSKNMLVRVDGVLGKGVTPKDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAV 241
Cdd:pfam00330 156 QPLEMKKPKVVGVKLTGKLPPGVTAKDVILAIIGKLGVKGGTGKVVEFFGPGVRSLSMEGRATICNMAIEYGATAGLFPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 242 DDKTIEYVK--GRSYAPKGEQWEQAVAyWNTLHSDEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEAVPTLEqaKDD 319
Cdd:pfam00330 236 DETTFEYLRatGRPEAPKGEAYDKAVA-WKTLASDPGAEYDKVVEIDLSTIEPMVTGPTRPQDAVPLSELVPDPF--ADA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 320 VQRNDWTRAYQYMGLNAGQALADIQLDRVFIGSCTNSRIEDIRAAAEVVK-----GRKVASTIKqAMIVPGSGLVKQQAE 394
Cdd:pfam00330 313 VKRKAAERALEYMGLGPGTPLSDGKVDIAFIGSCTNSSIEDLRAAAGLLKkavekGLKVAPGVK-ASVVPGSEVVRAYAE 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 395 KEGLDKIFLEAGFEWREPGCSMCLAmNADKLQPGEHCASTSNRNFEGRQGNGGRTHLVSP 454
Cdd:pfam00330 392 AEGLDKILEEAGFEWRGPGCSMCIG-NSDRLPPGERCVSSSNRNFEGRQGPGGRTHLASP 450
|
|
| IPMI |
cd01583 |
3-isopropylmalate dehydratase catalyzes the isomerization between 2-isopropylmalate and ... |
30-454 |
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: 572.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 30 RHLLHEVTSPQAFEGLQLADRQ-PWRLSANVATPDHNVPTSkkerdqgiagieDDTSRIQVQTLDDNCKAFNIVEFSINd 108
Cdd:cd01583 1 LHLVHDVTSPQAFEGLREAGREkVWDPEKIVAVFDHNVPTP------------DIKAAEQVKTLRKFAKEFGINFFDVG- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 109 iRQGIVHVVGPEQGLTLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLATQCLIQKKSKNMLVRVDGVLGKGVTPKD 188
Cdd:cd01583 68 -RQGICHVILPEKGLTLPGMTIVGGDSHTCTHGAFGAFATGIGTTDVAHVLATGKLWFRVPETMRVNVEGKLPPGVTAKD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 189 VVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAVDDKTIEYVKGRSYapkgeqweqavAYW 268
Cdd:cd01583 147 VILYIIGKIGVDGATYKAMEFAGEAIESLSMEERMTLCNMAIEAGAKAGIVAPDETTFEYLKGRGK-----------AYW 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 269 NTLHSDEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEAVPtleqakddvqrndwtrayqymglnagqaladIQLDRV 348
Cdd:cd01583 216 KELKSDEDAEYDKVVEIDASELEPQVAWPHSPDNVVPVSEVEG-------------------------------IKIDQV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 349 FIGSCTNSRIEDIRAAAEVVKGRKVASTIKqAMIVPGSGLVKQQAEKEGLDKIFLEAGFEWREPGCSMCLAMNADKLQPG 428
Cdd:cd01583 265 FIGSCTNGRLEDLRAAAEILKGRKVADGVR-LIVVPASQRVYKQAEKEGLIEIFIEAGAEVRPPGCGACLGGHMGVLAPG 343
|
410 420
....*....|....*....|....*..
gi 488043610 429 EHCASTSNRNFEGRQGNGG-RTHLVSP 454
Cdd:cd01583 344 ERCVSTSNRNFKGRMGSPGaRIYLASP 370
|
|
| PRK00402 |
PRK00402 |
3-isopropylmalate dehydratase large subunit; Reviewed |
3-454 |
1.46e-121 |
|
3-isopropylmalate dehydratase large subunit; Reviewed
Pssm-ID: 234748 Cd Length: 418 Bit Score: 361.42 E-value: 1.46e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 3 GKTLYDKLWDDHVVSQRDDGSCLLY-IDRHLLHEVTSPQAFEGLQ--LADRqPWRLSANVATPDHNVPTSkkerdqgiag 79
Cdd:PRK00402 2 GMTLAEKILARHSGRDVSPGDIVEAkVDLVMAHDITGPLAIKEFEkiGGDK-VFDPSKIVIVFDHFVPAK---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 80 ieDDTSRIQVQTLDDNCKAFNIVEFSinDIRQGIVHVVGPEQGLTLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVL 159
Cdd:PRK00402 71 --DIKSAEQQKILREFAKEQGIPNFF--DVGEGICHQVLPEKGLVRPGDVVVGADSHTCTYGALGAFATGMGSTDMAAAM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 160 ATQCLIQKKSKNMLVRVDGVLGKGVTPKDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMV 239
Cdd:PRK00402 147 ATGKTWFKVPETIKVVLEGKLPPGVTAKDVILHIIGDIGVDGATYKALEFTGETIEALSMDERMTLANMAIEAGAKAGIF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 240 AVDDKTIEYVKGRSYAPkgeqweqavayWNTLHSDEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEAvptleqakdd 319
Cdd:PRK00402 227 APDEKTLEYLKERAGRD-----------YKPWKSDEDAEYEEVYEIDLSKLEPQVAAPHLPDNVKPVSEV---------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 320 vqrndwtrayqymglnagqalADIQLDRVFIGSCTNSRIEDIRAAAEVVKGRKVASTIkQAMIVPGSGLVKQQAEKEGLD 399
Cdd:PRK00402 286 ---------------------EGTKVDQVFIGSCTNGRLEDLRIAAEILKGRKVAPGV-RLIVIPASQKIYLQALKEGLI 343
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 488043610 400 KIFLEAGFEWREPGCSMCLAMNADKLQPGEHCASTSNRNFEGRQGN-GGRTHLVSP 454
Cdd:PRK00402 344 EIFVDAGAVVSTPTCGPCLGGHMGVLAPGEVCLSTTNRNFKGRMGSpESEVYLASP 399
|
|
| hacA_fam |
TIGR01343 |
homoaconitate hydratase family protein; This model represents a subfamily of proteins ... |
28-470 |
5.16e-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: 5.16e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 28 IDRHLLHEVTSPQAFEGL-QLADRQPWRLSANVATPDHNVPTSKKERDQgiagieddtsriQVQTLDDNCKAFNIVEFsi 106
Cdd:TIGR01343 25 IDLAMVHDITAPLAIKTLeEYGIDKVWNPEKIVIVFDHQVPADTIKAAE------------MQKLAREFVKKQGIKYF-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 107 NDIRQGIVHVVGPEQGLTLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLATQCLIQKKSKNMLVRVDGVLGKGVTP 186
Cdd:TIGR01343 91 YDVGEGICHQVLPEKGLVKPGDLVVGADSHTCTYGAFGAFATGMGSTDMAYAIATGKTWFKVPETIRVNITGKLNPGVTA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 187 KDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAVDDKTIEYVKGRSyapkGEQWEQAVa 266
Cdd:TIGR01343 171 KDVILEVIGEIGVDGATYMAMEFGGETVKNMDMEGRLTLANMAIEAGGKTGIIEPDEKTIQYLKERR----KEPFRVYK- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 267 ywntlhSDEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEavptleqakddvqrndwtrayqymglnagqaLADIQLD 346
Cdd:TIGR01343 246 ------SDEDAEYAKEIEIDASQIEPVVACPHNVDNVKPVSE-------------------------------VEGTEID 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 347 RVFIGSCTNSRIEDIRAAAEVVKGRKVASTIkQAMIVPGSGLVKQQAEKEGLDKIFLEAGFEWREPGCSMCLAMNADKLQ 426
Cdd:TIGR01343 289 QVFIGSCTNGRLEDLRVAAKILKGRKVAPDV-RLIVIPASRAVYLQALKEGLIEIFVKAGAVVSTPGCGPCLGSHQGVLA 367
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 488043610 427 PGEHCASTSNRNFEGRQGN-GGRTHLVSPAMAAAAAIAGHFVDVR 470
Cdd:TIGR01343 368 PGEVCISTSNRNFKGRMGHpNAEIYLASPATAAASAVKGYIADPR 412
|
|
| IPMI_arch |
TIGR02086 |
3-isopropylmalate dehydratase, large subunit; This subfamily is a subset of the larger HacA ... |
28-470 |
6.22e-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: 6.22e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 28 IDRHLLHEVTSPQAFEGLQ-LADRQPWRLSANVATPDHNVPTSKKErdqgiagieddTSRIQVQTLDdNCKAFNIVEFSI 106
Cdd:TIGR02086 26 VDLAMTHDGTGPLAIKALReLGVARVWDPEKIVIAFDHNVPPPTVE-----------AAEMQKEIRE-FAKRHGIKNFDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 107 NDirqGIVHVVGPEQGLTLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLATQCLIQKKSKNMLVRVDGVLGKGVTP 186
Cdd:TIGR02086 94 GE---GICHQILAEEGYALPGMVVVGGDSHTCTSGAFGAFATGMGATDMAIALATGKTWIKVPETIRVVVEGKPEEGVTA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 187 KDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAVDDKTIEYVKGRsyapKGEQweqava 266
Cdd:TIGR02086 171 KDVALHIVGELGADGATYMAIEFFGLPIENMDMDGRLTLCNMAVEMGAKAGIIEPDEETYEYLKKR----RGLE------ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 267 yWNTLHSDEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVteavptleqakDDVQRndwtrayqymglnagqaladIQLD 346
Cdd:TIGR02086 241 -FRILVPDPGANYYKEIEIDLSDLEPQVAVPHSVDNVKPV-----------SDVEG--------------------TEID 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 347 RVFIGSCTNSRIEDIRAAAEVVKGRKVASTIKqAMIVPGSGLVKQQAEKEGLDKIFLEAGFEWREPGCSMCLAMNADKLQ 426
Cdd:TIGR02086 289 QVFIGSCTNGRLEDLRIAAEILKGRRVHPDVR-LIVIPASRKVYLRALEEGIILTLVRAGAMICPPGCGPCLGAHMGVLG 367
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 488043610 427 PGEHCASTSNRNFEGRQGN-GGRTHLVSPAMAAAAAIAGHFVDVR 470
Cdd:TIGR02086 368 DGEVCLSTTNRNFKGRMGSpNAEIYLASPATAAASAVEGYITDPE 412
|
|
| HacA_Meth |
NF040615 |
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens |
28-454 |
2.05e-80 |
|
homoaconitase large subunit; Part of the 2-oxosuberate biosynthesis pathway in methangoens
Pssm-ID: 468587 Cd Length: 419 Bit Score: 255.45 E-value: 2.05e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 28 IDRHLLHEVTSPQAFEGLQLADRQPWRLSANVATPDHNVP--TSKKERDQGIAgieddtsriqvqtlDDNCKAFNIVEFS 105
Cdd:NF040615 26 VDLAMTHDGTTPLTYKAFKEISDKVWDNEKIVIVFDHNVPanTVKAANMQKIT--------------REFVKEQGIKNFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 106 INDirQGIVHVVGPEQGLTLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLATQCLIQKKSKNMLVRVDGvLGKGVT 185
Cdd:NF040615 92 LGG--EGICHQVLPEKGHVLPNMVIAGGDSHTCTHGAFGAFATGFGATDMGYIYATGKTWIKVPKTIRVNIVG-KNENIS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 186 PKDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAVDDKTIEYVKGRSYAPKgeqwEQAV 265
Cdd:NF040615 169 GKDIILKVCKEIGRRGATYMAIEYGGEVVKNMDMDGRMVLCNMAIEMGGKTGIIEADEITYEYLRKEGVSEE----EIAE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 266 AYWNTLHSDED-AVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEAVPTleqakddvqrndwtrayqymglnagqaladiQ 344
Cdd:NF040615 245 LKKNRITVNEKeENYYKEIEIDITDMEEQVACPHHPDNVKPVSEVEGT-------------------------------E 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 345 LDRVFIGSCTNSRIEDIRAAAEVVKGRKVASTIKqAMIVPGSGLVKQQAEKEGLDKIFLEAGFEWREPGCSMCLAMNADK 424
Cdd:NF040615 294 IDQVFIGSCTNGRLSDLRIAAKYLKGKKVHKDVR-LIVIPASKKVFKQALKEGLIEIFVKAGAMICTPGCGPCLGAHQGV 372
|
410 420 430
....*....|....*....|....*....|.
gi 488043610 425 LQPGEHCASTSNRNFEGRQGN-GGRTHLVSP 454
Cdd:NF040615 373 LGDGEVCLSTTNRNFKGRMGNiNSYIYLSSP 403
|
|
| Aconitase |
cd01351 |
Aconitase catalytic domain; Aconitase catalyzes the reversible isomerization of citrate and ... |
32-454 |
7.73e-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: 7.73e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 32 LLHEVTSPQA---FEGLQLADRqPWRLSANVATPDHNVPtskkerdqgiagIEDDTSRIQVQTLDDNCKAFNIVEFSIND 108
Cdd:cd01351 3 MLQDATGPMAmkaFEILAALGK-VADPSQIACVHDHAVQ------------LEKPVNNEGHKFLSFFAALQGIAFYRPGV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 109 irqGIVHVVGPEQGLtLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLATQCLIQKKSKNMLVRVDGVLGKGVTPKD 188
Cdd:cd01351 70 ---GIIHQIMVENLA-LPGDLLVGSDSHTTSYGGLGAISTGAGGGDVAFVMAGGPAWLKKPEVVGVNLTGKLSPGVTGKD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 189 VVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAVDDKTIEYVKGRSYAPKGEQWEqavAYW 268
Cdd:cd01351 146 VVLKLGGIVGVDGVLNRIVEFYGEGVSSLSIEDRLTICNMMAELGATTGIFPEDKTTLKWLEATGRPLLKNLWL---AFP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 269 NTLHSDEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEavptleqakddvqrndwtrayqymglnagqaLADIQLDRV 348
Cdd:cd01351 223 EELLADEGAEYDQVIEIDLSELEPDISGPNRPDDAVSVSE-------------------------------VEGTKIDQV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 349 FIGSCTNSRIEDIRAAAEVVKGRKVASTIkQAMIVPGSGLVKQQAEKEGLDKIFLEAGFEWREPGCSMCLAMNADKLQPG 428
Cdd:cd01351 272 LIGSCTNNRYSDMLAAAKLLKGAKVAPGV-RLIVTPGSRMVYATLSREGYYEILVDSGARILPPGCGPCMGNGARLVADG 350
|
410 420
....*....|....*....|....*..
gi 488043610 429 EHCASTSNRNFEGRQGNG-GRTHLVSP 454
Cdd:cd01351 351 EVGVSSGNRNFPGRLGTYeRHVYLASP 377
|
|
| PRK07229 |
PRK07229 |
aconitate hydratase; Validated |
3-454 |
1.64e-48 |
|
aconitate hydratase; Validated
Pssm-ID: 235974 [Multi-domain] Cd Length: 646 Bit Score: 176.11 E-value: 1.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 3 GKTLYDKLWDDHVVSQR-DDGSCL-LYIDRHLLHEVTSPQA---FEGLQLaDRqpwrlsanVATP------DHNVPTSKK 71
Cdd:PRK07229 2 GLTLTEKILYAHLVEGElEPGEEIaIRIDQTLTQDATGTMAylqFEAMGL-DR--------VKTElsvqyvDHNLLQADF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 72 ERdqgiagiEDDTSRIQvqtldDNCKAFNIVeFSindiR--QGIVHVVGPEQgLTLPGMTVVCGDSHTATHGAFGCLAHG 149
Cdd:PRK07229 73 EN-------ADDHRFLQ-----SVAAKYGIY-FS----KpgNGICHQVHLER-FAFPGKTLLGSDSHTPTAGGLGMLAIG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 150 IGTSEVEHVLATQCLIQKKSKNMLVRVDGVLGKGVTPKDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMA 229
Cdd:PRK07229 135 AGGLDVALAMAGGPYYLKMPKVVGVKLTGKLPPWVSAKDVILELLRRLTVKGGVGKIIEYFGPGVATLSVPERATITNMG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 230 IEAGARVGMVAVDDKTIEYVK--GRsyapkGEQWEQavaywntLHSDEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVT 307
Cdd:PRK07229 215 AELGATTSIFPSDERTREFLKaqGR-----EDDWVE-------LLADPDAEYDEVIEIDLSELEPLIAGPHSPDNVVPVS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 308 EavptleqakddvqrndwtrayqymglnagqaLADIQLDRVFIGSCTNSRIEDIRAAAEVVKGRKVASTIKqAMIVPGSG 387
Cdd:PRK07229 283 E-------------------------------VAGIKVDQVLIGSCTNSSYEDLMRAASILKGKKVHPKVS-LVINPGSR 330
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 388 LVKQQAEKEGLDKIFLEAGFEWREPGCSMCLAMNADklqPGEHCAS--TSNRNFEGRQGN-GGRTHLVSP 454
Cdd:PRK07229 331 QVLEMLARDGALADLIAAGARILENACGPCIGMGQA---PATGNVSlrTFNRNFPGRSGTkDAQVYLASP 397
|
|
| AcnA_Bact |
cd01585 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
112-454 |
8.99e-48 |
|
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle; Bacterial Aconitase-like catalytic domain. Aconitase (aconitate hydratase or citrate hydrolyase) catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA cycle. Cis-aconitate is formed as an intermediate product during the course of the reaction. This distinct subfamily is found only in bacteria and Archaea. Its exact characteristics are not known.
Pssm-ID: 153135 Cd Length: 380 Bit Score: 168.78 E-value: 8.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 112 GIVHVVGPEQgLTLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLATQCLIQKKSKNMLVRVDGVLGKGVTPKDVVL 191
Cdd:cd01585 69 GICHQVHLER-FAVPGKTLLGSDSHTPTAGGLGMLAIGAGGLDVALAMAGEPYYIPMPKVVGVRLTGELPPWVTAKDVIL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 192 AIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAVDDKTIEYVK--GRSyapkgeqweqavAYWN 269
Cdd:cd01585 148 ELLRRLTVKGGVGKIFEYTGPGVATLSVPERATITNMGAELGATTSIFPSDERTREFLAaqGRE------------DDWV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 270 TLHSDEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEavptleqakddvqrndwtrayqymglnagqaLADIQLDRVF 349
Cdd:cd01585 216 ELAADADAEYDEEIEIDLSELEPLIARPHSPDNVVPVRE-------------------------------VAGIKVDQVA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 350 IGSCTNSRIEDIRAAAEVVKGRKVASTIkQAMIVPGSGLVKQQAEKEGLDKIFLEAGFEWREPGCSMCLAMNAdklQPGE 429
Cdd:cd01585 265 IGSCTNSSYEDLMTVAAILKGRRVHPHV-SMVVAPGSKQVLEMLARNGALADLLAAGARILESACGPCIGMGQ---APPT 340
|
330 340
....*....|....*....|....*...
gi 488043610 430 HCAS--TSNRNFEGRQGN-GGRTHLVSP 454
Cdd:cd01585 341 GGVSvrTFNRNFEGRSGTkDDLVYLASP 368
|
|
| AcnA_Mitochondrial |
cd01584 |
Aconitase catalyzes the reversible isomerization of citrate and isocitrate as part of the TCA ... |
112-454 |
3.28e-37 |
|
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: 141.04 E-value: 3.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 112 GIVHVVGPEQgLTLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLATQCLIQKKSKNMLVRVDGVLGKGVTPKDVVL 191
Cdd:cd01584 77 GIIHQIVLEN-YAFPGLLMIGTDSHTPNAGGLGGIAIGVGGADAVDVMAGIPWELKCPKVIGVKLTGKLSGWTSPKDVIL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 192 AIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAVDDKTIEYVK--GRSYAPKGEQWEQAvaywN 269
Cdd:cd01584 156 KVAGILTVKGGTGAIVEYFGPGVDSLSCTGMGTICNMGAEIGATTSVFPYNERMKKYLKatGRAEIADLADEFKD----D 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 270 TLHSDEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEavptleqAKDDVQRNDWTrayqyMGLNAGqaladiqldrvF 349
Cdd:cd01584 232 LLVADEGAEYDQLIEINLSELEPHINGPFTPDLATPVSK-------FKEVAEKNGWP-----LDLRVG-----------L 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 350 IGSCTNSRIEDIRAAAEVVK-----GRKVAStikQAMIVPGSGLVKQQAEKEGLDKIFLEAGFEWREPGCSMCLAM-NAD 423
Cdd:cd01584 289 IGSCTNSSYEDMGRAASIAKqalahGLKCKS---IFTITPGSEQIRATIERDGLLQTFRDAGGIVLANACGPCIGQwDRK 365
|
330 340 350
....*....|....*....|....*....|....*
gi 488043610 424 KLQPGEHCA--STSNRNFEGRQGNGGRTH--LVSP 454
Cdd:cd01584 366 DIKKGEKNTivTSYNRNFTGRNDANPATHafVASP 400
|
|
| Homoaconitase |
cd01582 |
Homoaconitase and other uncharacterized proteins of the Aconitase family; Homoaconitase ... |
111-454 |
2.38e-34 |
|
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: 131.97 E-value: 2.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 111 QGIVHVVGPEQGLTLPGMTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLATQCLIQKKSKNMLVRVDGVLGKGVTPKDVV 190
Cdd:cd01582 67 RGIGHQIMIEEGYAFPGTLAVASDSHSNMYGGVGCLGTPIVRTDAAAIWATGQTWWQIPPVAKVELKGQLPKGVTGKDVI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 191 LAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAVDDKTIEyvkgrsyapkgeqweqavaywnt 270
Cdd:cd01582 147 VALCGLFNKDQVLNHAIEFTGSGLNSLSVDTRLTIANMTTEWGALSGLFPTDAKHLI----------------------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 271 lhsdedavfdavveLNGAEIEPQVSWGTSpemvIPVTEAVPTLEQAkddvqrndwtrayqymglnagqalaDIQLDRVFI 350
Cdd:cd01582 204 --------------LDLSTLSPYVSGPNS----VKVSTPLKELEAQ-------------------------NIKINKAYL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 351 GSCTNSRIEDIRAAAEVVKGRKVAStiKQAMIVPG--------SGLVKQQAEKEGLDKIFLEAGFEWREPGCSMCLAMNA 422
Cdd:cd01582 241 VSCTNSRASDIAAAADVVKGKKEKN--GKIPVAPGvefyvaaaSSEVQAAAEKNGDWQTLLEAGATPLPAGCGPCIGLGQ 318
|
330 340 350
....*....|....*....|....*....|...
gi 488043610 423 DKLQPGEHCASTSNRNFEGRQGN-GGRTHLVSP 454
Cdd:cd01582 319 GLLEPGEVGISATNRNFKGRMGStEALAYLASP 351
|
|
| AcnA |
COG1048 |
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: ... |
112-442 |
1.17e-29 |
|
Aconitase A [Energy production and conversion]; Aconitase A is part of the Pathway/BioSystem: Lysine biosynthesisTCA cycle
Pssm-ID: 440669 [Multi-domain] Cd Length: 891 Bit Score: 122.91 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 112 GIVH---------VV--GPEQGLTL--PGmTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLATQCLiqkkskNML----- 173
Cdd:COG1048 176 GIVHqvnleylafVVwtREEDGETVayPD-TLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPV------SMLipevv 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 174 -VRVDGVLGKGVTPKDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAVDDKTIEYVK-- 250
Cdd:COG1048 249 gVKLTGKLPEGVTATDLVLTVTEMLRKKGVVGKFVEFFGPGLASLSLADRATIANMAPEYGATCGFFPVDEETLDYLRlt 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 251 GRSyapkGEQWEQAVAY------WNTlHSDEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEAVPTLEQAKDDVQRND 324
Cdd:COG1048 329 GRS----EEQIELVEAYakaqglWRD-PDAPEPYYSDVLELDLSTVEPSLAGPKRPQDRIPLSDLKEAFRAALAAPVGEE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 325 WTRAYQYMGLNAGQALAD----IQLdrvfIGSCTNSRIEDI-RAAA-----EVVKGRKVASTIKqAMIVPGSGLVKQQAE 394
Cdd:COG1048 404 LDKPVRVEVDGEEFELGHgavvIAA----ITSCTNTSNPSVmIAAGllakkAVEKGLKVKPWVK-TSLAPGSKVVTDYLE 478
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488043610 395 KEGLDKiFLEA------GFewrepGCSMCLAMNADKLQPGEH---------CASTS-NRNFEGR 442
Cdd:COG1048 479 RAGLLP-YLEAlgfnvvGY-----GCTTCIGNSGPLPPEISEaieendlvvAAVLSgNRNFEGR 536
|
|
| PTZ00092 |
PTZ00092 |
aconitate hydratase-like protein; Provisional |
112-454 |
1.21e-27 |
|
aconitate hydratase-like protein; Provisional
Pssm-ID: 240263 [Multi-domain] Cd Length: 898 Bit Score: 116.65 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 112 GIVH---------VVGPEQGLTLPGmTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLATQCLiqkkskNMLV------RV 176
Cdd:PTZ00092 185 GIVHqvnleylarVVFNKDGLLYPD-SVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPI------SMVLpevvgfKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 177 DGVLGKGVTPKDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAVDDKTIEYVK--GRSy 254
Cdd:PTZ00092 258 TGKLSEHVTATDLVLTVTSMLRKRGVVGKFVEFYGPGVKTLSLADRATIANMAPEYGATMGFFPIDEKTLDYLKqtGRS- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 255 apkGEQWEQAVAYW--NTLHSD--EDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTE------------------AVPT 312
Cdd:PTZ00092 337 ---EEKVELIEKYLkaNGLFRTyaEQIEYSDVLELDLSTVVPSVAGPKRPHDRVPLSDlkkdftaclsapvgfkgfGIPE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 313 LEQAKddvqrndwTRAYQYMG----LNAGQ-ALADIQldrvfigSCTNSRIEDIRAAA------EVVKGRKVASTIKQAM 381
Cdd:PTZ00092 414 EKHEK--------KVKFTYKGkeytLTHGSvVIAAIT-------SCTNTSNPSVMLAAgllakkAVEKGLKVPPYIKTSL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 382 iVPGSGLVKQQAEKEGLDKiFLEA-GFEWREPGCSMCLAmNADKLQPGEH---------CAS--TSNRNFEGR-----QG 444
Cdd:PTZ00092 479 -SPGSKVVTKYLEASGLLK-YLEKlGFYTAGYGCMTCIG-NSGDLDPEVSeaitnndlvAAAvlSGNRNFEGRvhpltRA 555
|
410
....*....|
gi 488043610 445 NggrtHLVSP 454
Cdd:PTZ00092 556 N----YLASP 561
|
|
| PLN00070 |
PLN00070 |
aconitate hydratase |
112-442 |
1.03e-23 |
|
aconitate hydratase
Pssm-ID: 215047 [Multi-domain] Cd Length: 936 Bit Score: 104.89 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 112 GIVHVVGPE---------QGLTLPGmTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLATQCLIQKKSKNMLVRVDGVLGK 182
Cdd:PLN00070 217 GIVHQVNLEylgrvvfntDGILYPD-SVVGTDSHTTMIDGLGVAGWGVGGIEAEAAMLGQPMSMVLPGVVGFKLSGKLRD 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 183 GVTPKDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAVDDKTIEYVK--GRSyapkGEQ 260
Cdd:PLN00070 296 GVTATDLVLTVTQMLRKHGVVGKFVEFYGEGMSELSLADRATIANMSPEYGATMGFFPVDHVTLQYLKltGRS----DET 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 261 WEQAVAYW--NTLHSD-----EDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTE------------------AVPTLEQ 315
Cdd:PLN00070 372 VAMIEAYLraNKMFVDynepqQERVYSSYLELDLEDVEPCISGPKRPHDRVPLKEmkadwhscldnkvgfkgfAVPKEAQ 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 316 AKddvqrndwTRAYQYMGLNAGQALADIQLdrVFIGSCTN-SRIEDIRAAAEVVK-----GRKVASTIKQAMiVPGSGLV 389
Cdd:PLN00070 452 SK--------VAKFSFHGQPAELRHGSVVI--AAITSCTNtSNPSVMLGAGLVAKkacelGLEVKPWIKTSL-APGSGVV 520
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488043610 390 KQQAEKEGLDKIFLEAGFEWREPGCSMCLAmNADKLQPGEHCASTS-----------NRNFEGR 442
Cdd:PLN00070 521 TKYLLKSGLQKYLNQQGFHIVGYGCTTCIG-NSGELDESVASAITEndivaaavlsgNRNFEGR 583
|
|
| AcnB |
cd01581 |
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA ... |
123-453 |
3.40e-22 |
|
Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle; Aconitase B catalytic domain. Aconitate hydratase B catalyses the formation of cis-aconitate from citrate as part of the TCA cycle. Aconitase has an active (4FE-4S) and an inactive (3FE-4S) form. The active cluster is part of the catalytic site that interconverts citrate, cis-aconitase and isocitrate. The domain architecture of aconitase B is different from other aconitases in that the catalytic domain is normally found at C-terminus for other aconitases, but it is at N-terminus for B family. It also has a HEAT domain before domain 4 which plays a role in protein-protein interaction. This alignment is the core domain including domains 1,2 and 3.
Pssm-ID: 153131 Cd Length: 436 Bit Score: 98.72 E-value: 3.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 123 LTLPGMTVVCGDSHTAThgAFGClAHGIGTSEVEHVLATQCLIQKKSKNMLVRVDGVLGKGVTPKDVVLAI------IGK 196
Cdd:cd01581 103 MLLPDTVGTGGDSHTRF--PIGI-SFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVNAIpyyaiqQGL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 197 IGTAGGTGYAIeFGGQVFR-----DMSIEGRMTVCNMAIEAGARVGMVAVDDKT-IEYV------------KGRSYAPKG 258
Cdd:cd01581 180 LTVEKKGKKNV-FNGRILEieglpDLKVEQAFELTDASAERSAAACTVRLDKEPvIEYLesnvvlmkimiaNGYDDARTL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 259 EQWEQAVAYW--NT--LHSDEDAVFDAVVELNGAEI-EPQVswgtspemvipvteAVPtleqakdDVQRNDWTRAYqymg 333
Cdd:cd01581 259 LRRIIAMEEWlaNPplLEPDADAEYAAVIEIDLDDIkEPIL--------------ACP-------NDPDDVKLLSE---- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 334 lnagqaLADIQLDRVFIGSC-TNsrIEDIRAAAEVVKGRKVASTikQAMIVPGSGLVKQQAEKEGLDKIFLEAGFEWREP 412
Cdd:cd01581 314 ------VAGKKIDEVFIGSCmTN--IGHFRAAAKILRGKEFKPT--RLWVAPPTRMDWAILQEEGYYSIFGDAGARTEMP 383
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 488043610 413 GCSMCLAmNADKLQPGEHCASTSNRNFEGRQGNGGRTHLVS 453
Cdd:cd01581 384 GCSLCMG-NQARVADGATVFSTSTRNFDNRVGKGAEVYLGS 423
|
|
| acnA |
PRK12881 |
aconitate hydratase AcnA; |
112-442 |
1.67e-21 |
|
aconitate hydratase AcnA;
Pssm-ID: 237246 [Multi-domain] Cd Length: 889 Bit Score: 98.08 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 112 GIVHVVGPEQ-------------GLTLPGmTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLATQCLIQKKSKNMLVRVDG 178
Cdd:PRK12881 178 GIMHQVNLEYlarvvhtkeddgdTVAYPD-TLVGTDSHTTMINGIGVLGWGVGGIEAEAVMLGQPVYMLIPDVVGVELTG 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 179 VLGKGVTPKDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAVDDKTIEYVK--GRSyap 256
Cdd:PRK12881 257 KLREGVTATDLVLTVTEMLRKEGVVGKFVEFFGEGVASLTLGDRATIANMAPEYGATMGFFPVDEQTLDYLRltGRT--- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 257 kGEQWEQAVAY------WntLHSDEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEAVPTLeqaKDDVQRNDWTRAYQ 330
Cdd:PRK12881 334 -EAQIALVEAYakaqglW--GDPKAEPRYTRTLELDLSTVAPSLAGPKRPQDRIALGNVKSAF---SDLFSKPVAENGFA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 331 YmglnAGQALADIQLDR--VFIG---SCTNSRIEDIRAAAEVV------KGRKVASTIKQAMiVPGSGLVKQQAEKEGLD 399
Cdd:PRK12881 408 K----KAQTSNGVDLPDgaVAIAaitSCTNTSNPSVLIAAGLLakkaveRGLTVKPWVKTSL-APGSKVVTEYLERAGLL 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 488043610 400 KiFLEA-GFEWREPGCSMCLAMNADKLQPGE--------HCAS--TSNRNFEGR 442
Cdd:PRK12881 483 P-YLEKlGFGIVGYGCTTCIGNSGPLTPEIEqaitkndlVAAAvlSGNRNFEGR 535
|
|
| PRK09277 |
PRK09277 |
aconitate hydratase AcnA; |
129-442 |
1.24e-17 |
|
aconitate hydratase AcnA;
Pssm-ID: 236445 [Multi-domain] Cd Length: 888 Bit Score: 85.95 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 129 TVVCGDSHTaTH-GAFGCLAHGIGTSEVEHVLatqcLIQKKSknML------VRVDGVLGKGVTPKDVVLAIIGKIGTAG 201
Cdd:PRK09277 207 TLVGTDSHT-TMiNGLGVLGWGVGGIEAEAAM----LGQPSS--MLipevvgVKLTGKLPEGVTATDLVLTVTEMLRKKG 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 202 GTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAVDDKTIEYVK--GRSyapkGEQWEQAVAY------WNTlhS 273
Cdd:PRK09277 280 VVGKFVEFFGEGLASLSLADRATIANMAPEYGATCGFFPIDEETLDYLRltGRD----EEQVALVEAYakaqglWRD--P 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 274 DEDAVFDAVVELNGAEIEPQVSWGTSPEMVIPVTEAVPTLEQAkddvqrndWTRAYQYMGLNAGQALADIQLDR--VFIG 351
Cdd:PRK09277 354 LEEPVYTDVLELDLSTVEPSLAGPKRPQDRIPLSDVKEAFAKS--------AELGVQGFGLDEAEEGEDYELPDgaVVIA 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 352 ---SCTN-SRIEDIRAAA-----EVVKGRKVASTIKQAMiVPGSGLVKQQAEKEGLDKiFLEA------GFewrepGCSM 416
Cdd:PRK09277 426 aitSCTNtSNPSVMIAAGllakkAVEKGLKVKPWVKTSL-APGSKVVTDYLEKAGLLP-YLEAlgfnlvGY-----GCTT 498
|
330 340 350
....*....|....*....|....*....|....*..
gi 488043610 417 CLAMNADkLQPG------EH---CAS--TSNRNFEGR 442
Cdd:PRK09277 499 CIGNSGP-LPPEiekainDNdlvVTAvlSGNRNFEGR 534
|
|
| AcnA_IRP |
cd01586 |
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA ... |
112-442 |
1.62e-17 |
|
Aconitase A catalytic domain; Aconitase A catalytic domain. This is the major form of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydrolyase. It includes bacterial and archaeal aconitase A, and the eukaryotic cytosolic form of aconitase. This group also includes sequences that have been shown to act as an iron-responsive element (IRE) binding protein in animals and may have the same role in other eukaryotes.
Pssm-ID: 153136 Cd Length: 404 Bit Score: 84.28 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 112 GIVHVVGPE-------------QGLTLPGmTVVCGDSHTATHGAFGCLAHGIGTSEVEHVLATQCLIQKKSKNMLVRVDG 178
Cdd:cd01586 94 GIIHQVNLEylarvvftseedgDGVAYPD-SVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQPISMLLPEVVGVKLTG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 179 VLGKGVTPKDVVLAIIGKIGTAGGTGYAIEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAVDDKtieyvkgrsyapkg 258
Cdd:cd01586 173 KLRPGVTATDLVLTVTQMLRKVGVVGKFVEFFGPGVAKLSVADRATIANMAPEYGATCGFFPVDTQ-------------- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 259 eqweqavaywntlhsdedavfdaVVELNGAEIEPQVSWGTSPEMVIPVTEAVptleqakddvqrndwtrayqymglnagq 338
Cdd:cd01586 239 -----------------------VVELDLSTVEPSVSGPKRPQDRVPLHGSV---------------------------- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 339 ALADIQldrvfigSCTN-SRIEDIRAAAEVVK-----GRKVASTIKQAMiVPGSGLVKQQAEKEGLDKiFLEA-GFEWRE 411
Cdd:cd01586 268 VIAAIT-------SCTNtSNPSVMLAAGLLAKkavelGLKVKPYVKTSL-APGSRVVTKYLEASGLLP-YLEKlGFHVVG 338
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 488043610 412 PGCSMCLAmNADKLQP------GEH----CASTS-NRNFEGR 442
Cdd:cd01586 339 YGCTTCIG-NSGPLPEeveeaiKENdlvvAAVLSgNRNFEGR 379
|
|
| PRK09238 |
PRK09238 |
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated |
173-453 |
3.35e-15 |
|
bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase; Validated
Pssm-ID: 236424 [Multi-domain] Cd Length: 835 Bit Score: 78.30 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 173 LVRVDGVLGKGVTPKDVVLAIigkigtaggTGYAIEFGG---------QVF--RDMSIEG--------RMTVCNMAIEAG 233
Cdd:PRK09238 522 LVRFKGEMQPGITLRDLVHAI---------PYYAIKQGLltvekkgkkNIFsgRILEIEGlpdlkveqAFELTDASAERS 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 234 ARVGMVAVDDKT-IEYV------------KGRSYAPKGEQWEQAVAYWNT----LHSDEDAVFDAVVELNGAEI-EPQVS 295
Cdd:PRK09238 593 AAGCTIKLSKEPiIEYLrsnivllkwmiaEGYGDARTLERRIAAMEEWLAnpelLEADADAEYAAVIEIDLAEIkEPILA 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 296 WGTSPEMVIPVTEavptleqakddvqrndwtrayqymglnagqaLADIQLDRVFIGSC-TNsrIEDIRAAAEVVKGRKVa 374
Cdd:PRK09238 673 CPNDPDDVRLLSE-------------------------------VAGTKIDEVFIGSCmTN--IGHFRAAGKLLEGKKG- 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 375 sTIKQAM-IVPGSGLVKQQAEKEGLDKIFLEAGFEWREPGCSMCLAmNADKLQPGEHCASTSNRNFEGRQGNGGRTHLVS 453
Cdd:PRK09238 719 -QLPTRLwVAPPTKMDADQLTEEGYYSIFGKAGARIEMPGCSLCMG-NQARVADGATVFSTSTRNFPNRLGKGANVYLGS 796
|
|
| AcnB |
COG1049 |
Aconitase B [Energy production and conversion]; Aconitase B is part of the Pathway/BioSystem: ... |
271-453 |
3.79e-14 |
|
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: 74.89 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 271 LHSDEDAVFDAVVELNGAEI-EPQVSWGTSPemvipvteavptleqakDDVQRndwtrayqymglnagqaLADIQ---LD 346
Cdd:COG1049 647 LEADADAEYAAVIEIDLNEIkEPILACPNDP-----------------DDVKL-----------------LSEVAgtkID 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 347 RVFIGSC-TNsrIEDIRAAAEVVKGRKVASTikQAMIVPGSGLVKQQAEKEGLDKIFLEAGFEWREPGCSMCLAmNADKL 425
Cdd:COG1049 693 EVFIGSCmTN--IGHFRAAGKLLEGKGNLPT--RLWIAPPTKMDEAQLTEEGYYSIFGAAGARTEMPGCSLCMG-NQARV 767
|
170 180
....*....|....*....|....*...
gi 488043610 426 QPGEHCASTSNRNFEGRQGNGGRTHLVS 453
Cdd:COG1049 768 ADGATVFSTSTRNFPNRLGKGANVYLGS 795
|
|
| PLN00094 |
PLN00094 |
aconitate hydratase 2; Provisional |
125-453 |
6.55e-12 |
|
aconitate hydratase 2; Provisional
Pssm-ID: 215053 [Multi-domain] Cd Length: 938 Bit Score: 68.03 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 125 LPGMTVVCGDSHTAthgafgcLAHGI----GTSEVEHVLATQCLIQKKSKNMLVRVDGVLGKGVTPKDVVLAIIGKIGTA 200
Cdd:PLN00094 551 LPDTVGTGGDSHTR-------FPIGIsfpaGSGLVAFGAATGVIPLDMPESVLVRFTGTMQPGITLRDLVHAIPYTAIQD 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 201 GGTGYAIEFGGQVF--RDMSIEGRMTV-CNMAIE---AGAR---VGMVAVDDK--TIEYVKG----------------RS 253
Cdd:PLN00094 624 GLLTVEKKGKKNVFsgRILEIEGLPHLkCEQAFElsdASAErsaAGCTIKLDKepIIEYLNSnvvmlkwmiaegygdrRT 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 254 YAPKGEQWEQAVAYWNTLHSDEDAVFDAVVELNGAEI-EPQVSWGTSPEmvipvteAVPTLEQAKDDvqrndwtrayqym 332
Cdd:PLN00094 704 LERRIARMQQWLADPELLEADPDAEYAAVIEIDMDEIkEPILCAPNDPD-------DARLLSEVTGD------------- 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 333 glnagqaladiQLDRVFIGSC-TNsrIEDIRAAAEVVKGRKvASTIKQAMIVPGSGLVKQQAEKEGLDKIFLEAGFEWRE 411
Cdd:PLN00094 764 -----------KIDEVFIGSCmTN--IGHFRAAGKLLNDNL-SQLPTRLWVAPPTKMDEAQLKAEGYYSTFGTVGARTEM 829
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 488043610 412 PGCSMCLAmNADKLQPGEHCASTSNRNFEGRQGNGGRTHLVS 453
Cdd:PLN00094 830 PGCSLCMG-NQARVAEKSTVVSTSTRNFPNRLGKGANVYLAS 870
|
|
| PRK11413 |
PRK11413 |
putative hydratase; Provisional |
128-444 |
5.90e-11 |
|
putative hydratase; Provisional
Pssm-ID: 183125 [Multi-domain] Cd Length: 751 Bit Score: 64.65 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 128 MTVVCG------DSHTaTHGAFGCLAHGIGTSEvehvLATQCLIQ----KKSKNMLVRVDGVLGKGVTPKDVVLAIIGKI 197
Cdd:PRK11413 137 MMAGGGkmilgsDSHT-RYGALGTMAVGEGGGE----LVKQLLNDtydiDYPGVVAVYLTGKPAPGVGPQDVALAIIGAV 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 198 gtaGGTGYA----IEFGGQVFRDMSIEGRMTVCNMAIEAGARVGMVAVDDKTIEYVK--GRSYAPKgEQWEQAVAYwntl 271
Cdd:PRK11413 212 ---FKNGYVknkvMEFVGPGVSALSTDFRNGVDVMTTETTCLSSIWQTDEEVHNWLAlhGRGQDYC-ELNPQPMAY---- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 272 hsdedavFDAVVELNGAEIEPQVSWGTSPEMVIPVTEavptLEQAKDDVQRNDWTRAYQYMGLNAGQALAD------IQL 345
Cdd:PRK11413 284 -------YDGCISVDLSAIKPMIALPFHPSNVYEIDE----LNQNLTDILREVEIESERVAHGKAKLSLLDkiengrLKV 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488043610 346 DRVFIGSCTNSRIEDIRAAAEVVKGRKVASTIKQAMIVPGSGLVKQQAEKEGLDKIFLEAGFEWREPGCSMCL------A 419
Cdd:PRK11413 353 QQGIIAGCSGGNYENVIAAANALRGQSCGNDTFSLSVYPSSQPVFMDLAKKGVVADLMGAGAIIRTAFCGPCFgagdtpA 432
|
330 340
....*....|....*....|....*
gi 488043610 420 MNADKLQpgeHcastSNRNFEGRQG 444
Cdd:PRK11413 433 NNGLSIR---H----TTRNFPNREG 450
|
|
| |
