SitesBLAST
Comparing BPHYT_RS17335 BPHYT_RS17335 enoyl-CoA hydratase 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)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
64% identity, 99% coverage: 3:258/258 of query aligns to 2:256/256 of 3h81A
- active site: A64 (= A65), M69 (= M70), T79 (≠ K80), F83 (≠ I84), G107 (= G109), E110 (= E112), P129 (= P131), E130 (= E132), V135 (≠ I137), P137 (= P139), G138 (= G140), L223 (≠ H225), F233 (= F235)
- binding calcium ion: R171 (= R173), S172 (≠ A174), F233 (= F235), Q238 (= Q240)
3q0jA Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
64% identity, 99% coverage: 1:255/258 of query aligns to 1:254/255 of 3q0jA
- active site: A65 (= A65), M70 (= M70), T80 (≠ K80), F84 (≠ I84), G108 (= G109), E111 (= E112), P130 (= P131), E131 (= E132), V136 (≠ I137), P138 (= P139), G139 (= G140), L224 (≠ H225), F234 (= F235)
- binding acetoacetyl-coenzyme a: F246 (= F247), K249 (= K250)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
64% identity, 99% coverage: 1:255/258 of query aligns to 1:254/255 of 3q0gC
- active site: A65 (= A65), M70 (= M70), T80 (≠ K80), F84 (≠ I84), G108 (= G109), E111 (= E112), P130 (= P131), E131 (= E132), V136 (≠ I137), P138 (= P139), G139 (= G140), L224 (≠ H225), F234 (= F235)
- binding coenzyme a: A24 (= A24), L25 (= L25), A27 (= A27), A63 (= A63), A65 (= A65), D66 (= D66), I67 (= I67), K68 (≠ G68), Y104 (≠ F105), P130 (= P131), E131 (= E132), L134 (= L135)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
63% identity, 98% coverage: 3:255/258 of query aligns to 2:249/250 of 3q0gD
- active site: A64 (= A65), M69 (= M70), T75 (≠ K80), F79 (≠ I84), G103 (= G109), E106 (= E112), P125 (= P131), E126 (= E132), V131 (≠ I137), P133 (= P139), G134 (= G140), L219 (≠ H225), F229 (= F235)
- binding Butyryl Coenzyme A: F225 (= F231), F241 (= F247), K244 (= K250)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
56% identity, 98% coverage: 3:256/258 of query aligns to 3:258/260 of 1dubA
- active site: A68 (= A65), M73 (= M70), S83 (≠ K80), L87 (≠ I84), G111 (= G109), E114 (= E112), P133 (= P131), E134 (= E132), T139 (≠ I137), P141 (= P139), G142 (= G140), K227 (≠ H225), F237 (= F235)
- binding acetoacetyl-coenzyme a: K26 (= K23), A27 (= A24), L28 (= L25), A30 (= A27), K62 (= K59), A66 (= A63), G67 (= G64), A68 (= A65), D69 (= D66), I70 (= I67), K71 (≠ G68), M73 (= M70), Y107 (≠ F105), L109 (= L107), G110 (= G108), G111 (= G109), E114 (= E112), P133 (= P131), E134 (= E132), L137 (= L135), G142 (= G140), F233 (= F231), F249 (= F247), K252 (= K250)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
56% identity, 98% coverage: 3:256/258 of query aligns to 1:256/258 of 1ey3A
- active site: A66 (= A65), M71 (= M70), S81 (≠ K80), L85 (≠ I84), G109 (= G109), E112 (= E112), P131 (= P131), E132 (= E132), T137 (≠ I137), P139 (= P139), G140 (= G140), K225 (≠ H225), F235 (= F235)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K23), A25 (= A24), L26 (= L25), A28 (= A27), A64 (= A63), G65 (= G64), A66 (= A65), D67 (= D66), I68 (= I67), K69 (≠ G68), L85 (≠ I84), W88 (= W88), Y105 (≠ F105), L107 (= L107), G108 (= G108), G109 (= G109), P131 (= P131), E132 (= E132), L135 (= L135), G140 (= G140), A141 (= A141), R165 (≠ F165), F231 (= F231), F247 (= F247), K250 (= K250)
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)
56% identity, 98% coverage: 3:256/258 of query aligns to 33:288/290 of P14604
- E144 (= E112) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E132) 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
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
55% identity, 99% coverage: 3:258/258 of query aligns to 3:260/260 of 2hw5C
- active site: A68 (= A65), M73 (= M70), S83 (≠ K80), L87 (≠ I84), G111 (= G109), E114 (= E112), P133 (= P131), E134 (= E132), T139 (≠ I137), P141 (= P139), G142 (= G140), K227 (≠ H225), F237 (= F235)
- binding crotonyl coenzyme a: K26 (= K23), A27 (= A24), L28 (= L25), A30 (= A27), K62 (= K59), A66 (= A63), A68 (= A65), D69 (= D66), I70 (= I67), K71 (≠ G68), Y107 (≠ F105), F109 (≠ L107)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
56% identity, 98% coverage: 3:256/258 of query aligns to 3:256/258 of 1mj3A
- active site: A68 (= A65), M73 (= M70), S83 (≠ K80), L85 (≠ T85), G109 (= G109), E112 (= E112), P131 (= P131), E132 (= E132), T137 (≠ I137), P139 (= P139), G140 (= G140), K225 (≠ H225), F235 (= F235)
- binding hexanoyl-coenzyme a: K26 (= K23), A27 (= A24), L28 (= L25), A30 (= A27), K62 (= K59), A66 (= A63), G67 (= G64), A68 (= A65), D69 (= D66), I70 (= I67), K71 (≠ G68), M73 (= M70), W88 (= W88), Y105 (≠ F105), L107 (= L107), G108 (= G108), G109 (= G109), E112 (= E112), P131 (= P131), E132 (= E132), L135 (= L135), G140 (= G140), A141 (= A141), F231 (= F231), F247 (= F247), K250 (= K250)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
56% identity, 98% coverage: 3:256/258 of query aligns to 2:252/254 of 2dubA
- active site: A67 (= A65), M72 (= M70), S82 (≠ K80), G105 (= G109), E108 (= E112), P127 (= P131), E128 (= E132), T133 (≠ I137), P135 (= P139), G136 (= G140), K221 (≠ H225), F231 (= F235)
- binding octanoyl-coenzyme a: K25 (= K23), A26 (= A24), L27 (= L25), A29 (= A27), K61 (= K59), A65 (= A63), G66 (= G64), A67 (= A65), D68 (= D66), I69 (= I67), K70 (≠ G68), Y101 (≠ F105), G104 (= G108), G105 (= G109), E108 (= E112), P127 (= P131), E128 (= E132), L131 (= L135), P135 (= P139), G136 (= G140), A137 (= A141)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
42% identity, 100% coverage: 1:258/258 of query aligns to 1:259/259 of 5zaiC
- active site: A65 (= A65), F70 (≠ M70), S82 (≠ D82), R86 (= R86), G110 (= G109), E113 (= E112), P132 (= P131), E133 (= E132), I138 (= I137), P140 (= P139), G141 (= G140), A226 (≠ H225), F236 (= F235)
- binding coenzyme a: D23 (≠ K23), K24 (≠ A24), L25 (= L25), A27 (= A27), A63 (= A63), G64 (= G64), A65 (= A65), D66 (= D66), I67 (= I67), L108 (= L107), G109 (= G108), P132 (= P131), E133 (= E132), R166 (≠ F165), F248 (= F247), K251 (= K250)
5jbxC Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
39% identity, 97% coverage: 8:258/258 of query aligns to 9:261/261 of 5jbxC
- active site: A67 (= A65), R72 (≠ M70), L84 (≠ I84), R88 (≠ W88), G112 (= G109), E115 (= E112), T134 (≠ P131), E135 (= E132), I140 (= I137), P142 (= P139), G143 (= G140), A228 (≠ H225), L238 (≠ F235)
- binding coenzyme a: F250 (= F247), K253 (= K250)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 98% coverage: 6:258/258 of query aligns to 2:245/245 of 6slaAAA
- active site: Q61 (≠ A65), L68 (≠ M76), N72 (≠ T85), A96 (≠ G109), S99 (≠ E112), A118 (≠ P131), F119 (≠ E132), L124 (≠ I137), P126 (= P139), N127 (≠ G140), A212 (≠ H225), G222 (≠ F235)
- 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: K20 (≠ A24), L21 (= L25), A23 (= A27), R55 (≠ K59), A59 (= A63), G60 (= G64), Q61 (≠ A65), D62 (= D66), L63 (≠ I67), L68 (≠ M76), Y71 (= Y79), V92 (≠ F105), A94 (≠ L107), G95 (= G108), A96 (≠ G109), A118 (≠ P131), F119 (≠ E132), I122 (≠ L135), L124 (≠ I137), N127 (≠ G140), F234 (= F247), K237 (= K250)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 98% coverage: 6:258/258 of query aligns to 5:257/257 of 6slbAAA
- active site: Q64 (≠ A65), F69 (≠ M76), L80 (vs. gap), N84 (≠ T85), A108 (≠ G109), S111 (≠ E112), A130 (≠ P131), F131 (≠ E132), L136 (≠ I137), P138 (= P139), D139 (≠ G140), A224 (≠ H225), G234 (≠ F235)
- 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: L24 (= L25), A26 (= A27), R58 (≠ K59), A62 (= A63), G63 (= G64), Q64 (≠ A65), D65 (= D66), L66 (≠ I67), Y76 (= Y83), H79 (vs. gap), Y83 (≠ I84), V104 (≠ F105), A106 (≠ L107), G107 (= G108), A108 (≠ G109), A130 (≠ P131), F131 (≠ E132), I134 (≠ L135), D139 (≠ G140)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
35% identity, 98% coverage: 7:258/258 of query aligns to 11:266/266 of O53561
- K135 (= K127) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 127:134, 63% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (= K134) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
5wydA Structural of pseudomonas aeruginosa dspi (see paper)
35% identity, 98% coverage: 4:256/258 of query aligns to 9:262/262 of 5wydA