SitesBLAST
Comparing 14182 FitnessBrowser__Keio:14182 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
38% identity, 99% coverage: 3:261/261 of query aligns to 4:259/259 of 5zaiC
- active site: A65 (≠ W64), F70 (≠ A69), S82 (≠ G80), R86 (≠ F84), G110 (= G108), E113 (= E111), P132 (= P130), E133 (= E131), I138 (= I136), P140 (= P138), G141 (≠ D139), A226 (≠ R224), F236 (≠ L238)
- binding coenzyme a: K24 (= K22), L25 (≠ A23), A63 (= A62), G64 (= G63), A65 (≠ W64), D66 (= D65), I67 (≠ L66), P132 (= P130), R166 (= R164), F248 (= F250), K251 (= K253)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
39% identity, 92% coverage: 22:261/261 of query aligns to 25:261/261 of 5jbxB
- active site: A67 (≠ W64), R72 (≠ A69), L84 (≠ G80), R88 (≠ F84), G112 (= G108), E115 (= E111), T134 (≠ P130), E135 (= E131), I140 (= I136), P142 (= P138), G143 (≠ D139), A228 (≠ R224), L238 (= L238)
- binding coenzyme a: R25 (≠ K22), R26 (≠ A23), A28 (= A25), A65 (= A62), D68 (= D65), L69 (= L66), K70 (= K67), L110 (≠ F106), G111 (= G107), T134 (≠ P130), E135 (= E131), L138 (= L134), R168 (= R164)
Sites not aligning to the query:
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
36% identity, 97% coverage: 9:261/261 of query aligns to 14:266/266 of O53561
- K135 (≠ S126) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 126:133, 50% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (= K133) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
Q4WF54 Mevalonyl-coenzyme A hydratase sidH; Siderophore biosynthesis protein H; EC 4.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
38% identity, 99% coverage: 1:259/261 of query aligns to 1:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
37% identity, 99% coverage: 3:261/261 of query aligns to 3:256/256 of 3h81A
- active site: A64 (≠ W64), M69 (≠ A69), T79 (≠ G80), F83 (= F84), G107 (= G108), E110 (= E111), P129 (= P130), E130 (= E131), V135 (≠ I136), P137 (= P138), G138 (≠ D139), L223 (≠ R224), F233 (≠ L238)
- binding calcium ion: F233 (≠ L238), Q238 (≠ A243)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
37% identity, 98% coverage: 3:258/261 of query aligns to 4:254/255 of 3q0jC
- active site: A65 (≠ W64), M70 (≠ A69), T80 (≠ G80), F84 (= F84), G108 (= G108), E111 (= E111), P130 (= P130), E131 (= E131), V136 (≠ I136), P138 (= P138), G139 (≠ D139), L224 (≠ R224), F234 (≠ L238)
- binding acetoacetyl-coenzyme a: Q23 (≠ K22), A24 (= A23), L25 (vs. gap), A27 (= A25), A63 (= A62), G64 (= G63), A65 (≠ W64), D66 (= D65), I67 (≠ L66), K68 (= K67), M70 (≠ A69), F84 (= F84), G107 (= G107), G108 (= G108), E111 (= E111), P130 (= P130), E131 (= E131), P138 (= P138), G139 (≠ D139), M140 (≠ S140)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
37% identity, 98% coverage: 3:258/261 of query aligns to 4:254/255 of 3q0gC
- active site: A65 (≠ W64), M70 (≠ A69), T80 (≠ G80), F84 (= F84), G108 (= G108), E111 (= E111), P130 (= P130), E131 (= E131), V136 (≠ I136), P138 (= P138), G139 (≠ D139), L224 (≠ R224), F234 (≠ L238)
- binding coenzyme a: L25 (vs. gap), A63 (= A62), I67 (≠ L66), K68 (= K67), Y104 (= Y104), P130 (= P130), E131 (= E131), L134 (= L134)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
35% identity, 96% coverage: 9:259/261 of query aligns to 13:256/258 of 1mj3A
- active site: A68 (≠ W64), M73 (≠ A69), S83 (≠ A85), L85 (= L87), G109 (= G108), E112 (= E111), P131 (= P130), E132 (= E131), T137 (≠ I136), P139 (= P138), G140 (≠ D139), K225 (≠ R224), F235 (≠ L238)
- binding hexanoyl-coenzyme a: K26 (= K22), A27 (= A23), L28 (vs. gap), A30 (= A25), A66 (= A62), G67 (= G63), A68 (≠ W64), D69 (= D65), I70 (≠ L66), G109 (= G108), P131 (= P130), E132 (= E131), L135 (= L134), G140 (≠ D139)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
35% identity, 96% coverage: 9:259/261 of query aligns to 12:252/254 of 2dubA
- active site: A67 (≠ W64), M72 (≠ A69), S82 (≠ A85), G105 (= G108), E108 (= E111), P127 (= P130), E128 (= E131), T133 (≠ I136), P135 (= P138), G136 (≠ D139), K221 (≠ R224), F231 (≠ L238)
- binding octanoyl-coenzyme a: K25 (= K22), A26 (= A23), L27 (vs. gap), A29 (= A25), A65 (= A62), A67 (≠ W64), D68 (= D65), I69 (≠ L66), K70 (= K67), G105 (= G108), E108 (= E111), P127 (= P130), E128 (= E131), G136 (≠ D139), A137 (≠ S140)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
35% identity, 96% coverage: 9:259/261 of query aligns to 13:258/260 of 1dubA
- active site: A68 (≠ W64), M73 (≠ A69), S83 (≠ F79), L87 (≠ F84), G111 (= G108), E114 (= E111), P133 (= P130), E134 (= E131), T139 (≠ I136), P141 (= P138), G142 (≠ D139), K227 (≠ R224), F237 (≠ L238)
- binding acetoacetyl-coenzyme a: K26 (= K22), A27 (= A23), L28 (vs. gap), A30 (= A25), A66 (= A62), A68 (≠ W64), D69 (= D65), I70 (≠ L66), Y107 (= Y104), G110 (= G107), G111 (= G108), E114 (= E111), P133 (= P130), E134 (= E131), L137 (= L134), G142 (≠ D139), F233 (≠ Y234), F249 (= F250)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
35% identity, 96% coverage: 9:259/261 of query aligns to 11:256/258 of 1ey3A
- active site: A66 (≠ W64), M71 (≠ A69), S81 (≠ F79), L85 (≠ F84), G109 (= G108), E112 (= E111), P131 (= P130), E132 (= E131), T137 (≠ I136), P139 (= P138), G140 (≠ D139), K225 (≠ R224), F235 (≠ L238)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K22), L26 (vs. gap), A28 (= A25), A64 (= A62), G65 (= G63), A66 (≠ W64), D67 (= D65), I68 (≠ L66), L85 (≠ F84), W88 (≠ L87), G109 (= G108), P131 (= P130), L135 (= L134), G140 (≠ D139)
P14604 Enoyl-CoA hydratase, mitochondrial; mECH; mECH1; Enoyl-CoA hydratase 1; ECHS1; Short-chain enoyl-CoA hydratase; SCEH; EC 4.2.1.17; EC 5.3.3.8 from Rattus norvegicus (Rat) (see 3 papers)
35% identity, 96% coverage: 9:259/261 of query aligns to 43:288/290 of P14604
- E144 (= E111) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E131) mutation to D: Reduces activity 1250-fold.; mutation to Q: Reduces activity 330000-fold.
Sites not aligning to the query:
- 1:29 modified: transit peptide, Mitochondrion
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
37% identity, 98% coverage: 3:258/261 of query aligns to 3:249/250 of 3q0gD
- active site: A64 (≠ W64), M69 (≠ A69), T75 (≠ D76), F79 (= F84), G103 (= G108), E106 (= E111), P125 (= P130), E126 (= E131), V131 (≠ I136), P133 (= P138), G134 (≠ D139), L219 (≠ R224), F229 (≠ L238)
- binding Butyryl Coenzyme A: F225 (≠ Y234), F241 (= F250)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
33% identity, 97% coverage: 9:261/261 of query aligns to 13:260/260 of 2hw5C
- active site: A68 (≠ W64), M73 (≠ A69), S83 (≠ G80), L87 (≠ F84), G111 (= G108), E114 (= E111), P133 (= P130), E134 (= E131), T139 (≠ I136), P141 (= P138), G142 (≠ D139), K227 (≠ R224), F237 (≠ L238)
- binding crotonyl coenzyme a: K26 (= K22), A27 (= A23), L28 (vs. gap), A30 (= A25), K62 (= K58), I70 (≠ L66), F109 (= F106)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 97% coverage: 9:261/261 of query aligns to 9:257/257 of 6slbAAA
- active site: Q64 (≠ W64), F69 (≠ A69), L80 (≠ P81), N84 (≠ A85), A108 (≠ G108), S111 (≠ E111), A130 (≠ P130), F131 (≠ E131), L136 (≠ I136), P138 (= P138), D139 (= D139), A224 (≠ R224), G234 (≠ S236)
- binding (~{E})-6-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethylsulfanyl]-6-oxidanylidene-hex-3-enoic acid: R58 (≠ K58), A62 (= A62), Q64 (≠ W64), D65 (= D65), L66 (= L66), Y76 (≠ A77), A108 (≠ G108), F131 (≠ E131), D139 (= D139)
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
32% identity, 97% coverage: 3:255/261 of query aligns to 55:318/327 of Q62651
- D176 (≠ E111) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (= E131) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (= D139) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
34% identity, 97% coverage: 9:261/261 of query aligns to 6:245/245 of 6slaAAA
- active site: Q61 (≠ W64), L68 (≠ E71), N72 (≠ A85), A96 (≠ G108), S99 (≠ E111), A118 (≠ P130), F119 (≠ E131), L124 (≠ I136), P126 (= P138), N127 (≠ D139), A212 (≠ R224), G222 (≠ S236)
- binding ~{S}-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethyl] 2-(2,5-dihydrooxepin-7-yl)ethanethioate: L21 (≠ A23), A59 (= A62), Q61 (≠ W64), D62 (= D65), L63 (= L66), L68 (≠ E71), Y71 (≠ F84), A94 (≠ F106), G95 (= G107), A96 (≠ G108), F119 (≠ E131), I122 (≠ L134), L124 (≠ I136), N127 (≠ D139), F234 (= F250), K237 (= K253)
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
36% identity, 72% coverage: 9:195/261 of query aligns to 9:201/707 of 6yswA
- active site: A66 (≠ W64), I71 (vs. gap), A84 (≠ G80), Q88 (≠ F84), G112 (= G108), E115 (= E111), P136 (= P130), E137 (= E131), G145 (≠ D139)
- binding coenzyme a: E23 (vs. gap), M25 (≠ A23), A66 (≠ W64), D67 (= D65), I68 (≠ L66), P136 (= P130), E137 (= E131), L140 (= L134)
Sites not aligning to the query:
1ef9A The crystal structure of methylmalonyl coa decarboxylase complexed with 2s-carboxypropyl coa (see paper)
32% identity, 83% coverage: 45:261/261 of query aligns to 46:261/261 of 1ef9A
- active site: H66 (≠ W64), L71 (≠ A69), D82 (≠ G80), R86 (≠ F84), G110 (= G108), E113 (= E111), P133 (≠ E131), V138 (≠ I136), Y140 (≠ P138), N141 (≠ D139), E228 (≠ I226), Y238 (≠ L238)
- binding 2-carboxypropyl-coenzyme a: A64 (= A62), H66 (≠ W64), D67 (= D65), I68 (≠ L66), H69 (≠ K67), W108 (≠ F106), G110 (= G108), T132 (≠ P130), P133 (≠ E131), K253 (= K253)
P52045 Methylmalonyl-CoA decarboxylase; MMCD; Transcarboxylase; EC 4.1.1.- from Escherichia coli (strain K12) (see paper)
32% identity, 83% coverage: 45:261/261 of query aligns to 46:261/261 of P52045
- G110 (= G108) binding substrate
- T132 (≠ P130) binding substrate
- K253 (= K253) binding substrate
Query Sequence
>14182 FitnessBrowser__Keio:14182
MSESLHLTRNGSILEITLDRPKANAIDAKTSFEMGEVFLNFRDDPQLRVAIITGAGEKFF
SAGWDLKAAAEGEAPDADFGPGGFAGLTEIFNLDKPVIAAVNGYAFGGGFELALAADFIV
CADNASFALPEAKLGIVPDSGGVLRLPKILPPAIVNEMVMTGRRMGAEEALRWGIVNRVV
SQAELMDNARELAQQLVNSAPLAIAALKEIYRTTSEMPVEEAYRYIRSGVLKHYPSVLHS
EDAIEGPLAFAEKRDPVWKGR
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory