SitesBLAST
Comparing CCNA_00006 CCNA_00006 enoyl-CoA hydratase 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)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
60% identity, 98% coverage: 4:259/262 of query aligns to 2:253/256 of 3h81A
- active site: A64 (= A69), M69 (= M74), T79 (≠ K84), F83 (= F88), G107 (= G113), E110 (= E116), P129 (= P135), E130 (= E136), V135 (= V141), P137 (= P143), G138 (= G144), L223 (≠ A229), F233 (= F239)
- binding calcium ion: R171 (= R177), S172 (= S178), F233 (= F239), Q238 (= Q244)
3q0jA Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
60% identity, 98% coverage: 4:259/262 of query aligns to 3:254/255 of 3q0jA
- active site: A65 (= A69), M70 (= M74), T80 (≠ K84), F84 (= F88), G108 (= G113), E111 (= E116), P130 (= P135), E131 (= E136), V136 (= V141), P138 (= P143), G139 (= G144), L224 (≠ A229), F234 (= F239)
- binding acetoacetyl-coenzyme a: F246 (= F251), K249 (= K254)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
60% identity, 98% coverage: 4:259/262 of query aligns to 3:254/255 of 3q0gC
- active site: A65 (= A69), M70 (= M74), T80 (≠ K84), F84 (= F88), G108 (= G113), E111 (= E116), P130 (= P135), E131 (= E136), V136 (= V141), P138 (= P143), G139 (= G144), L224 (≠ A229), F234 (= F239)
- binding coenzyme a: A24 (= A28), L25 (= L29), A27 (= A31), A63 (= A67), A65 (= A69), D66 (= D70), I67 (= I71), K68 (= K72), Y104 (= Y109), P130 (= P135), E131 (= E136), L134 (= L139)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
59% identity, 98% coverage: 4:259/262 of query aligns to 2:249/250 of 3q0gD
- active site: A64 (= A69), M69 (= M74), T75 (≠ K84), F79 (= F88), G103 (= G113), E106 (= E116), P125 (= P135), E126 (= E136), V131 (= V141), P133 (= P143), G134 (= G144), L219 (≠ A229), F229 (= F239)
- binding Butyryl Coenzyme A: F225 (= F235), F241 (= F251), K244 (= K254)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
57% identity, 99% coverage: 2:260/262 of query aligns to 1:258/260 of 1dubA
- active site: A68 (= A69), M73 (= M74), S83 (≠ K84), L87 (≠ F88), G111 (= G113), E114 (= E116), P133 (= P135), E134 (= E136), T139 (≠ V141), P141 (= P143), G142 (= G144), K227 (≠ A229), F237 (= F239)
- binding acetoacetyl-coenzyme a: K26 (≠ E27), A27 (= A28), L28 (= L29), A30 (= A31), K62 (= K63), A66 (= A67), G67 (= G68), A68 (= A69), D69 (= D70), I70 (= I71), K71 (= K72), M73 (= M74), Y107 (= Y109), L109 (= L111), G110 (= G112), G111 (= G113), E114 (= E116), P133 (= P135), E134 (= E136), L137 (= L139), G142 (= G144), F233 (= F235), F249 (= F251), K252 (= K254)
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)
57% identity, 99% coverage: 2:260/262 of query aligns to 31:288/290 of P14604
- E144 (= E116) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E136) 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
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
57% identity, 98% coverage: 4:260/262 of query aligns to 1:256/258 of 1ey3A
- active site: A66 (= A69), M71 (= M74), S81 (≠ K84), L85 (≠ F88), G109 (= G113), E112 (= E116), P131 (= P135), E132 (= E136), T137 (≠ V141), P139 (= P143), G140 (= G144), K225 (≠ A229), F235 (= F239)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E27), A25 (= A28), L26 (= L29), A28 (= A31), A64 (= A67), G65 (= G68), A66 (= A69), D67 (= D70), I68 (= I71), K69 (= K72), L85 (≠ F88), W88 (≠ G91), Y105 (= Y109), L107 (= L111), G108 (= G112), G109 (= G113), P131 (= P135), E132 (= E136), L135 (= L139), G140 (= G144), A141 (≠ I145), R165 (≠ M169), F231 (= F235), F247 (= F251), K250 (= K254)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
57% identity, 99% coverage: 2:260/262 of query aligns to 1:256/258 of 1mj3A
- active site: A68 (= A69), M73 (= M74), S83 (≠ K84), L85 (≠ T89), G109 (= G113), E112 (= E116), P131 (= P135), E132 (= E136), T137 (≠ V141), P139 (= P143), G140 (= G144), K225 (≠ A229), F235 (= F239)
- binding hexanoyl-coenzyme a: K26 (≠ E27), A27 (= A28), L28 (= L29), A30 (= A31), K62 (= K63), A66 (= A67), G67 (= G68), A68 (= A69), D69 (= D70), I70 (= I71), K71 (= K72), M73 (= M74), W88 (≠ A92), Y105 (= Y109), L107 (= L111), G108 (= G112), G109 (= G113), E112 (= E116), P131 (= P135), E132 (= E136), L135 (= L139), G140 (= G144), A141 (≠ I145), F231 (= F235), F247 (= F251), K250 (= K254)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
57% identity, 98% coverage: 3:260/262 of query aligns to 1:252/254 of 2dubA
- active site: A67 (= A69), M72 (= M74), S82 (≠ A90), G105 (= G113), E108 (= E116), P127 (= P135), E128 (= E136), T133 (≠ V141), P135 (= P143), G136 (= G144), K221 (≠ A229), F231 (= F239)
- binding octanoyl-coenzyme a: K25 (≠ E27), A26 (= A28), L27 (= L29), A29 (= A31), K61 (= K63), A65 (= A67), G66 (= G68), A67 (= A69), D68 (= D70), I69 (= I71), K70 (= K72), Y101 (= Y109), G104 (= G112), G105 (= G113), E108 (= E116), P127 (= P135), E128 (= E136), L131 (= L139), P135 (= P143), G136 (= G144), A137 (≠ I145)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
56% identity, 99% coverage: 2:260/262 of query aligns to 1:258/260 of 2hw5C
- active site: A68 (= A69), M73 (= M74), S83 (≠ K84), L87 (≠ F88), G111 (= G113), E114 (= E116), P133 (= P135), E134 (= E136), T139 (≠ V141), P141 (= P143), G142 (= G144), K227 (≠ A229), F237 (= F239)
- binding crotonyl coenzyme a: K26 (≠ E27), A27 (= A28), L28 (= L29), A30 (= A31), K62 (= K63), A66 (= A67), A68 (= A69), D69 (= D70), I70 (= I71), K71 (= K72), Y107 (= Y109), F109 (≠ L111)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
48% identity, 92% coverage: 20:261/262 of query aligns to 16:258/259 of 5zaiC
- active site: A65 (= A69), F70 (≠ M74), S82 (≠ T89), R86 (= R93), G110 (= G113), E113 (= E116), P132 (= P135), E133 (= E136), I138 (≠ V141), P140 (= P143), G141 (= G144), A226 (= A229), F236 (= F239)
- binding coenzyme a: D23 (≠ E27), K24 (≠ A28), L25 (= L29), A27 (= A31), A63 (= A67), G64 (= G68), A65 (= A69), D66 (= D70), I67 (= I71), L108 (= L111), G109 (= G112), P132 (= P135), E133 (= E136), R166 (≠ M169), F248 (= F251), K251 (= K254)
5jbxC Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
40% identity, 89% coverage: 30:261/262 of query aligns to 27:260/261 of 5jbxC
- active site: A67 (= A69), R72 (≠ M74), L84 (≠ M82), R88 (≠ T89), G112 (= G113), E115 (= E116), T134 (≠ P135), E135 (= E136), I140 (≠ V141), P142 (= P143), G143 (= G144), A228 (= A229), L238 (≠ F239)
- binding coenzyme a: F250 (= F251), K253 (= K254)
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)
35% identity, 94% coverage: 16:260/262 of query aligns to 19:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 95% coverage: 13:261/262 of query aligns to 8:256/257 of 6slbAAA
- active site: Q64 (≠ A69), F69 (≠ M74), L80 (≠ A85), N84 (≠ T89), A108 (≠ G113), S111 (≠ E116), A130 (≠ P135), F131 (≠ E136), L136 (≠ V141), P138 (= P143), D139 (≠ G144), A224 (= A229), G234 (≠ F239)
- 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 (= L29), A26 (= A31), R58 (≠ K63), A62 (= A67), G63 (= G68), Q64 (≠ A69), D65 (= D70), L66 (≠ I71), Y76 (≠ Q81), H79 (≠ K84), Y83 (≠ F88), V104 (≠ Y109), A106 (≠ L111), G107 (= G112), A108 (≠ G113), A130 (≠ P135), F131 (≠ E136), I134 (≠ L139), D139 (≠ G144)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 95% coverage: 13:261/262 of query aligns to 5:244/245 of 6slaAAA
- active site: Q61 (≠ A69), L68 (≠ D76), N72 (≠ A80), A96 (≠ G113), S99 (≠ E116), A118 (≠ P135), F119 (≠ E136), L124 (≠ V141), P126 (= P143), N127 (≠ G144), A212 (= A229), G222 (≠ F239)
- 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 (≠ A28), L21 (= L29), A23 (= A31), R55 (≠ K63), A59 (= A67), G60 (= G68), Q61 (≠ A69), D62 (= D70), L63 (≠ I71), L68 (≠ D76), Y71 (= Y79), V92 (≠ Y109), A94 (≠ L111), G95 (= G112), A96 (≠ G113), A118 (≠ P135), F119 (≠ E136), I122 (≠ L139), L124 (≠ V141), N127 (≠ G144), F234 (= F251), K237 (= K254)
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
35% identity, 96% coverage: 9:259/262 of query aligns to 22:260/267 of 4elwA