SitesBLAST
Comparing 15516 b1394 enoyl-CoA hydratase (NCBI) to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
45% identity, 99% coverage: 4:262/262 of query aligns to 4:257/257 of 6slbAAA
- active site: Q64 (= Q64), F69 (vs. gap), L80 (≠ V84), N84 (= N89), A108 (= A113), S111 (≠ T116), A130 (= A135), F131 (= F136), L136 (= L141), P138 (= P143), D139 (= D144), A224 (≠ D229), G234 (= G239)
- 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 (= R58), A62 (= A62), Q64 (= Q64), D65 (= D65), L66 (= L66), Y76 (≠ L80), A108 (= A113), F131 (= F136), D139 (= D144)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
44% identity, 99% coverage: 4:262/262 of query aligns to 1:245/245 of 6slaAAA
- active site: Q61 (= Q64), L68 (≠ V71), N72 (= N89), A96 (= A113), S99 (≠ T116), A118 (= A135), F119 (= F136), L124 (= L141), P126 (= P143), N127 (≠ D144), A212 (≠ D229), G222 (= G239)
- 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 (= L24), A59 (= A62), Q61 (= Q64), D62 (= D65), L63 (= L66), L68 (≠ V71), Y71 (= Y88), A94 (= A111), G95 (= G112), A96 (= A113), F119 (= F136), I122 (≠ L139), L124 (= L141), N127 (≠ D144), F234 (= F251), K237 (= K254)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
35% identity, 100% coverage: 2:262/262 of query aligns to 1:259/259 of 5zaiC
- active site: A65 (≠ Q64), F70 (≠ R69), S82 (≠ E85), R86 (≠ N89), G110 (≠ A113), E113 (≠ T116), P132 (≠ A135), E133 (≠ F136), I138 (≠ L141), P140 (= P143), G141 (≠ D144), A226 (≠ D229), F236 (≠ G239)
- binding coenzyme a: K24 (≠ R23), L25 (= L24), A63 (= A62), G64 (= G63), A65 (≠ Q64), D66 (= D65), I67 (≠ L66), P132 (≠ A135), R166 (≠ Q169), F248 (= F251), K251 (= K254)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 98% coverage: 3:260/262 of query aligns to 3:250/250 of 3q0gD
- active site: A64 (≠ Q64), M69 (≠ R69), T75 (≠ S83), F79 (= F87), G103 (≠ A113), E106 (≠ T116), P125 (≠ A135), E126 (≠ F136), V131 (≠ L141), P133 (= P143), G134 (≠ D144), L219 (≠ D229), F229 (≠ G239)
- binding Butyryl Coenzyme A: F225 (≠ Q235), F241 (= F251)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
32% identity, 93% coverage: 16:259/262 of query aligns to 20:257/260 of 2hw5C
- active site: A68 (≠ Q64), M73 (≠ R69), S83 (≠ N89), L87 (≠ R93), G111 (≠ A113), E114 (≠ T116), P133 (≠ A135), E134 (≠ F136), T139 (≠ L141), P141 (= P143), G142 (≠ D144), K227 (≠ D229), F237 (≠ G239)
- binding crotonyl coenzyme a: K26 (≠ E22), A27 (≠ R23), L28 (= L24), A30 (≠ S26), K62 (≠ R58), I70 (≠ L66), F109 (≠ A111)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
33% identity, 98% coverage: 3:260/262 of query aligns to 4:255/255 of 3q0jC
- active site: A65 (≠ Q64), M70 (≠ R69), T80 (≠ Y88), F84 (≠ V92), G108 (≠ A113), E111 (≠ T116), P130 (≠ A135), E131 (≠ F136), V136 (≠ L141), P138 (= P143), G139 (≠ D144), L224 (≠ D229), F234 (≠ G239)
- binding acetoacetyl-coenzyme a: Q23 (≠ E22), A24 (≠ R23), L25 (= L24), A27 (≠ S26), A63 (= A62), G64 (= G63), A65 (≠ Q64), D66 (= D65), I67 (≠ L66), K68 (≠ N67), M70 (≠ R69), F84 (≠ V92), G107 (= G112), G108 (≠ A113), E111 (≠ T116), P130 (≠ A135), E131 (≠ F136), P138 (= P143), G139 (≠ D144), M140 (≠ C145)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 98% coverage: 3:260/262 of query aligns to 4:255/255 of 3q0gC
- active site: A65 (≠ Q64), M70 (≠ R69), T80 (≠ Y88), F84 (≠ V92), G108 (≠ A113), E111 (≠ T116), P130 (≠ A135), E131 (≠ F136), V136 (≠ L141), P138 (= P143), G139 (≠ D144), L224 (≠ D229), F234 (≠ G239)
- binding coenzyme a: L25 (= L24), A63 (= A62), I67 (≠ L66), K68 (≠ N67), Y104 (≠ V109), P130 (≠ A135), E131 (≠ F136), L134 (= L139)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
32% identity, 99% coverage: 3:262/262 of query aligns to 3:256/256 of 3h81A
- active site: A64 (≠ Q64), M69 (≠ R69), T79 (≠ Y88), F83 (≠ V92), G107 (≠ A113), E110 (≠ T116), P129 (≠ A135), E130 (≠ F136), V135 (≠ L141), P137 (= P143), G138 (≠ D144), L223 (≠ D229), F233 (≠ G239)
- binding calcium ion: F233 (≠ G239), Q238 (≠ Y244)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
32% identity, 93% coverage: 16:259/262 of query aligns to 20:255/258 of 1mj3A
- active site: A68 (≠ Q64), M73 (≠ R69), S83 (≠ N89), L85 (= L91), G109 (≠ A113), E112 (≠ T116), P131 (≠ A135), E132 (≠ F136), T137 (≠ L141), P139 (= P143), G140 (≠ D144), K225 (≠ D229), F235 (≠ G239)
- binding hexanoyl-coenzyme a: K26 (≠ E22), A27 (≠ R23), L28 (= L24), A30 (≠ S26), A66 (= A62), G67 (= G63), A68 (≠ Q64), D69 (= D65), I70 (≠ L66), G109 (≠ A113), P131 (≠ A135), E132 (≠ F136), L135 (= L139), G140 (≠ D144)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
32% identity, 93% coverage: 16:259/262 of query aligns to 19:251/254 of 2dubA
- active site: A67 (≠ Q64), M72 (= M82), S82 (≠ V92), G105 (≠ A113), E108 (≠ T116), P127 (≠ A135), E128 (≠ F136), T133 (≠ L141), P135 (= P143), G136 (≠ D144), K221 (≠ D229), F231 (≠ G239)
- binding octanoyl-coenzyme a: K25 (≠ E22), A26 (≠ R23), L27 (= L24), A29 (≠ S26), A65 (= A62), A67 (≠ Q64), D68 (= D65), I69 (≠ L66), K70 (≠ N67), G105 (≠ A113), E108 (≠ T116), P127 (≠ A135), E128 (≠ F136), G136 (≠ D144), A137 (≠ C145)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
32% identity, 93% coverage: 16:259/262 of query aligns to 20:257/260 of 1dubA
- active site: A68 (≠ Q64), M73 (≠ R69), S83 (≠ L80), L87 (≠ V84), G111 (≠ A113), E114 (≠ T116), P133 (≠ A135), E134 (≠ F136), T139 (≠ L141), P141 (= P143), G142 (≠ D144), K227 (≠ D229), F237 (≠ G239)
- binding acetoacetyl-coenzyme a: K26 (≠ E22), A27 (≠ R23), L28 (= L24), A30 (≠ S26), A66 (= A62), A68 (≠ Q64), D69 (= D65), I70 (≠ L66), Y107 (≠ V109), G110 (= G112), G111 (≠ A113), E114 (≠ T116), P133 (≠ A135), E134 (≠ F136), L137 (= L139), G142 (≠ D144), F233 (≠ Q235), F249 (= F251)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
32% identity, 93% coverage: 16:259/262 of query aligns to 18:255/258 of 1ey3A
- active site: A66 (≠ Q64), M71 (≠ R69), S81 (≠ L80), L85 (≠ V84), G109 (≠ A113), E112 (≠ T116), P131 (≠ A135), E132 (≠ F136), T137 (≠ L141), P139 (= P143), G140 (≠ D144), K225 (≠ D229), F235 (≠ G239)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E22), L26 (= L24), A28 (≠ S26), A64 (= A62), G65 (= G63), A66 (≠ Q64), D67 (= D65), I68 (≠ L66), L85 (≠ V84), W88 (≠ F87), G109 (≠ A113), P131 (≠ A135), L135 (= L139), G140 (≠ D144)
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)
32% identity, 93% coverage: 16:259/262 of query aligns to 50:287/290 of P14604
- E144 (≠ T116) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ F136) 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
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
30% identity, 88% coverage: 1:231/262 of query aligns to 1:232/269 of 1nzyB
- active site: C61 (= C61), F64 (≠ Q64), I69 (≠ R69), A86 (≠ E85), H90 (≠ N89), G114 (≠ A113), G117 (≠ T116), A136 (= A135), W137 (≠ F136), I142 (≠ L141), N144 (≠ P143), D145 (= D144), E230 (≠ D229)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ E22), H23 (≠ R23), R24 (≠ L24), A62 (= A62), F64 (≠ Q64), Y65 (≠ D65), L66 (= L66), R67 (≠ N67), W89 (≠ Y88), G113 (= G112), G114 (≠ A113), A136 (= A135), W137 (≠ F136), D145 (= D144), T146 (≠ C145)
- binding calcium ion: G49 (≠ R49), L202 (= L201), A203 (= A202), A205 (≠ Q204), T207 (= T206), Q210 (≠ L209)
- binding phosphate ion: E57 (≠ G57), N108 (= N107), K188 (≠ D187), R192 (≠ A191)
Sites not aligning to the query:
1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
30% identity, 88% coverage: 1:231/262 of query aligns to 1:232/269 of 1jxzB
- active site: C61 (= C61), F64 (≠ Q64), I69 (≠ R69), A86 (≠ E85), Q90 (≠ N89), G113 (= G112), G114 (≠ A113), G117 (≠ T116), A136 (= A135), W137 (≠ F136), I142 (≠ L141), N144 (≠ P143), D145 (= D144), E230 (≠ D229)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ E22), H23 (≠ R23), R24 (≠ L24), A62 (= A62), F64 (≠ Q64), Y65 (≠ D65), L66 (= L66), R67 (≠ N67), W89 (≠ Y88), G113 (= G112), A136 (= A135), W137 (≠ F136), I142 (≠ L141), D145 (= D144), T146 (≠ C145)
- binding calcium ion: G49 (≠ R49), L202 (= L201), A203 (= A202), A205 (≠ Q204), T207 (= T206), Q210 (≠ L209)
Sites not aligning to the query:
A5JTM5 4-chlorobenzoyl coenzyme A dehalogenase; 4-CBA-CoA dehalogenase; 4-CBCoA dehalogenase; 4-chlorobenzoyl-CoA dehalogenase; EC 3.8.1.7 from Pseudomonas sp. (strain CBS-3) (see 7 papers)
30% identity, 88% coverage: 1:231/262 of query aligns to 1:232/269 of A5JTM5
- R24 (≠ L24) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (≠ Q34) mutation to T: Forms inclusion bodies.
- E43 (= E43) mutation to A: No effect on catalytic activity.
- D45 (= D45) mutation to A: No effect on catalytic activity.
- D46 (= D46) mutation to A: No effect on catalytic activity.
- G63 (= G63) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ Q64) mutation to A: 30-fold reduction in catalytic activity, substrate benzoyl group binding is unaffected.; mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to P: Severely reduces catalytic activity. Arylated intermediate does not accumulate.
- Y65 (≠ D65) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (≠ N67) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (≠ D68) mutation to T: No effect on catalytic activity.
- H81 (≠ L80) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ G81) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (≠ Y88) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ N89) active site, Proton acceptor; mutation to Q: Complete loss of catalytic activity (PubMed:8718880, PubMed:9063883). Significantly reduced activity (PubMed:11695894). Substrate binding is not significantly affected. Reduced arylated intermediate formation.
- H94 (≠ R93) mutation to Q: No effect on catalytic activity.
- A112 (= A111) mutation to G: Yields insoluble protein.; mutation to S: Protein precipitates upon purification.; mutation to V: Catalytic activity is almost as efficient as wild type.
- G113 (= G112) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding. Arylated intermediate does not accumulate.; mutation G->N,S: Strongly reduced catalytic activity. Arylated intermediate does not accumulate.; mutation to V: Protein precipitates upon purification.
- G114 (≠ A113) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G114) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D122) mutation to T: No effect on catalytic activity.
- D129 (≠ R128) mutation to T: No effect on catalytic activity.
- W137 (≠ F136) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D144) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (≠ G162) mutation to T: No effect on catalytic activity.
- E175 (≠ Q174) mutation to D: No effect on catalytic activity.
- W179 (= W178) mutation to F: No effect on catalytic activity.
- H208 (≠ F207) mutation to Q: No effect on catalytic activity.
- R216 (≠ A215) mutation R->E,K,L: Yields insoluble protein.
- E232 (= E231) mutation E->A,N,Q,R: Yields insoluble protein.; mutation to D: Reduced catalytic activity, increased substrate binding.
Sites not aligning to the query:
- 257 R→K: Retains catalytic activity and substrate CoA binding.; R→L: Significantly reduces catalytic activity and substrate CoA binding.
7borA Structure of pseudomonas aeruginosa coa-bound odaa (see paper)
34% identity, 96% coverage: 3:254/262 of query aligns to 2:247/247 of 7borA
- active site: N63 (≠ Q64), F68 (≠ R69), D77 (≠ M82), G81 (≠ E85), I105 (≠ A113), T108 (= T116), F128 (= F136), L133 (= L141), P135 (= P143), E136 (≠ D144), A222 (≠ D229), L232 (≠ G239)
- binding coenzyme a: D21 (≠ E22), K22 (≠ R23), A25 (≠ S26), S61 (≠ A62), I65 (≠ L66), V103 (≠ A111), F128 (= F136), L131 (= L139), F244 (= F251), R247 (≠ K254)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
31% identity, 95% coverage: 13:262/262 of query aligns to 18:266/266 of O53561
- K135 (= K131) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 131:138, 38% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (= K138) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
32% identity, 94% coverage: 17:262/262 of query aligns to 19:261/261 of 5jbxB
- active site: A67 (≠ Q64), R72 (= R69), L84 (≠ Y88), R88 (≠ V92), G112 (≠ A113), E115 (≠ T116), T134 (≠ A135), E135 (≠ F136), I140 (≠ L141), P142 (= P143), G143 (≠ D144), A228 (≠ D229), L238 (≠ A238)
- binding coenzyme a: S24 (≠ E22), R25 (= R23), R26 (≠ L24), A28 (≠ S26), A65 (= A62), D68 (= D65), L69 (= L66), K70 (≠ N67), L110 (≠ A111), G111 (= G112), T134 (≠ A135), E135 (≠ F136), L138 (= L139), R168 (≠ Q169)
Q9P4U9 Enoyl-CoA hydratase AKT3-1; AF-toxin biosynthesis protein 3-1; EC 4.2.1.17 from Alternaria alternata (Alternaria rot fungus) (Torula alternata) (see paper)
29% identity, 95% coverage: 12:259/262 of query aligns to 24:268/296 of Q9P4U9
Sites not aligning to the query:
- 294:296 Peroxisomal targeting signal type 1
Query Sequence
>15516 b1394 enoyl-CoA hydratase (NCBI)
MMEFILSHVEKGVMTLTLNRPERLNSFNDEMHAQLAECLKQVERDDTIRCLLLTGAGRGF
CAGQDLNDRNVDPTGPAPDLGMSVERFYNPLVRRLAKLPKPVICAVNGVAAGAGATLALG
GDIVIAARSAKFVMAFSKLGLIPDCGGTWLLPRVAGRARAMGLALLGNQLSAEQAHEWGM
IWQVVDDETLADTAQQLARHLATQPTFGLGLIKQAINSAETNTLDTQLDLERDYQRLAGR
SADYREGVSAFLAKRSPQFTGK
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