SitesBLAST
Comparing Ga0059261_3986 Ga0059261_3986 Enoyl-CoA hydratase/carnithine racemase 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, 98% coverage: 6:259/259 of query aligns to 5:257/257 of 6slbAAA
- active site: Q64 (≠ A64), F69 (≠ R69), L80 (vs. gap), N84 (= N86), A108 (= A110), S111 (≠ G113), A130 (= A132), F131 (= F133), L136 (= L138), P138 (= P140), D139 (= D141), A224 (≠ S226), G234 (= G236)
- 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 (≠ S62), Q64 (≠ A64), D65 (= D65), L66 (= L66), Y76 (≠ L81), A108 (= A110), F131 (= F133), D139 (= D141)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
43% identity, 98% coverage: 6:259/259 of query aligns to 2:245/245 of 6slaAAA
- active site: Q61 (≠ A64), L68 (vs. gap), N72 (= N86), A96 (= A110), S99 (≠ G113), A118 (= A132), F119 (= F133), L124 (= L138), P126 (= P140), N127 (≠ D141), A212 (≠ S226), G222 (= G236)
- 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 (= L25), A59 (≠ S62), Q61 (≠ A64), D62 (= D65), L63 (= L66), L68 (vs. gap), Y71 (= Y85), A94 (= A108), G95 (= G109), A96 (= A110), F119 (= F133), I122 (= I136), L124 (= L138), N127 (≠ D141), F234 (= F248), K237 (= K251)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
35% identity, 100% coverage: 1:259/259 of query aligns to 1:259/259 of 5zaiC
- active site: A65 (= A64), F70 (≠ G72), S82 (≠ H84), R86 (vs. gap), G110 (≠ A110), E113 (≠ G113), P132 (≠ A132), E133 (≠ F133), I138 (≠ L138), P140 (= P140), G141 (≠ D141), A226 (≠ S226), F236 (≠ G236)
- binding coenzyme a: K24 (≠ R24), L25 (= L25), A63 (≠ S62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (≠ L66), P132 (≠ A132), R166 (≠ K166), F248 (= F248), K251 (= K251)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
31% identity, 96% coverage: 11:259/259 of query aligns to 14:260/260 of 2hw5C
- active site: A68 (= A64), M73 (= M70), S83 (≠ N80), L87 (vs. gap), G111 (≠ A110), E114 (≠ G113), P133 (≠ A132), E134 (≠ F133), T139 (≠ L138), P141 (= P140), G142 (≠ D141), K227 (≠ S226), F237 (≠ G236)
- binding crotonyl coenzyme a: K26 (≠ D23), A27 (≠ R24), L28 (= L25), A30 (= A27), K62 (≠ R58), I70 (≠ V67), F109 (≠ A108)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
31% identity, 94% coverage: 14:257/259 of query aligns to 15:256/258 of 1ey3A
- active site: A66 (= A64), M71 (= M70), S81 (≠ N80), L85 (vs. gap), G109 (≠ A110), E112 (≠ G113), P131 (≠ A132), E132 (≠ F133), T137 (≠ L138), P139 (= P140), G140 (≠ D141), K225 (≠ S226), F235 (≠ G236)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ D23), L26 (= L25), A28 (= A27), A64 (≠ S62), G65 (= G63), A66 (= A64), D67 (= D65), I68 (≠ V67), L85 (vs. gap), W88 (≠ Y85), G109 (≠ A110), P131 (≠ A132), L135 (≠ I136), G140 (≠ D141)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
31% identity, 94% coverage: 14:257/259 of query aligns to 17:258/260 of 1dubA
- active site: A68 (= A64), M73 (= M70), S83 (≠ N80), L87 (vs. gap), G111 (≠ A110), E114 (≠ G113), P133 (≠ A132), E134 (≠ F133), T139 (≠ L138), P141 (= P140), G142 (≠ D141), K227 (≠ S226), F237 (≠ G236)
- binding acetoacetyl-coenzyme a: K26 (≠ D23), A27 (≠ R24), L28 (= L25), A30 (= A27), A66 (≠ S62), A68 (= A64), D69 (= D65), I70 (≠ V67), Y107 (≠ P106), G110 (= G109), G111 (≠ A110), E114 (≠ G113), P133 (≠ A132), E134 (≠ F133), L137 (≠ I136), G142 (≠ D141), F233 (≠ Q232), F249 (= F248)
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)
31% identity, 94% coverage: 14:257/259 of query aligns to 47:288/290 of P14604
- E144 (≠ G113) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ F133) 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
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
31% identity, 94% coverage: 14:257/259 of query aligns to 17:256/258 of 1mj3A
- active site: A68 (= A64), M73 (= M70), S83 (≠ N80), L85 (≠ E82), G109 (≠ A110), E112 (≠ G113), P131 (≠ A132), E132 (≠ F133), T137 (≠ L138), P139 (= P140), G140 (≠ D141), K225 (≠ S226), F235 (≠ G236)
- binding hexanoyl-coenzyme a: K26 (≠ D23), A27 (≠ R24), L28 (= L25), A30 (= A27), A66 (≠ S62), G67 (= G63), A68 (= A64), D69 (= D65), I70 (≠ V67), G109 (≠ A110), P131 (≠ A132), E132 (≠ F133), L135 (≠ I136), G140 (≠ D141)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
31% identity, 94% coverage: 14:257/259 of query aligns to 16:252/254 of 2dubA
- active site: A67 (= A64), M72 (= M70), S82 (≠ N80), G105 (≠ A110), E108 (≠ G113), P127 (≠ A132), E128 (≠ F133), T133 (≠ L138), P135 (= P140), G136 (≠ D141), K221 (≠ S226), F231 (≠ G236)
- binding octanoyl-coenzyme a: K25 (≠ D23), A26 (≠ R24), L27 (= L25), A29 (= A27), A65 (≠ S62), A67 (= A64), D68 (= D65), I69 (≠ V67), K70 (≠ G68), G105 (≠ A110), E108 (≠ G113), P127 (≠ A132), E128 (≠ F133), G136 (≠ D141), A137 (≠ C142)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
31% identity, 99% coverage: 1:256/259 of query aligns to 1:254/255 of 3q0jC
- active site: A65 (= A64), M70 (≠ R69), T80 (≠ E82), F84 (≠ N86), G108 (≠ A110), E111 (≠ G113), P130 (≠ A132), E131 (≠ F133), V136 (≠ L138), P138 (= P140), G139 (≠ D141), L224 (≠ S226), F234 (≠ G236)
- binding acetoacetyl-coenzyme a: Q23 (≠ D23), A24 (≠ R24), L25 (= L25), A27 (= A27), A63 (≠ S62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (≠ L66), K68 (≠ V67), M70 (≠ R69), F84 (≠ N86), G107 (= G109), G108 (≠ A110), E111 (≠ G113), P130 (≠ A132), E131 (≠ F133), P138 (= P140), G139 (≠ D141), M140 (≠ C142)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
31% identity, 99% coverage: 1:256/259 of query aligns to 1:254/255 of 3q0gC
- active site: A65 (= A64), M70 (≠ R69), T80 (≠ E82), F84 (≠ N86), G108 (≠ A110), E111 (≠ G113), P130 (≠ A132), E131 (≠ F133), V136 (≠ L138), P138 (= P140), G139 (≠ D141), L224 (≠ S226), F234 (≠ G236)
- binding coenzyme a: L25 (= L25), A63 (≠ S62), I67 (≠ L66), K68 (≠ V67), Y104 (≠ P106), P130 (≠ A132), E131 (≠ F133), L134 (≠ I136)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
31% identity, 100% coverage: 2:259/259 of query aligns to 1:256/256 of 3h81A
- active site: A64 (= A64), M69 (≠ R69), T79 (≠ E82), F83 (≠ N86), G107 (≠ A110), E110 (≠ G113), P129 (≠ A132), E130 (≠ F133), V135 (≠ L138), P137 (= P140), G138 (≠ D141), L223 (≠ S226), F233 (≠ G236)
- binding calcium ion: F233 (≠ G236), Q238 (≠ F241)
5ducA Crystal structure of m. Tuberculosis echa6 bound to ligand gsk951a (see paper)
33% identity, 95% coverage: 12:258/259 of query aligns to 9:243/244 of 5ducA
- active site: A61 (= A64), D66 (= D71), P73 (≠ A78), I77 (vs. gap), A101 (= A110), Q104 (≠ G113), P123 (≠ A132), T124 (≠ F133), L129 (= L138), L131 (≠ P140), D132 (= D141), P211 (≠ S226), W221 (≠ G236)
- binding (5R,7S)-N-(1,3-benzodioxol-5-ylmethyl)-5-(4-ethylphenyl)-7-(trifluoromethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L76 (= L81), H80 (= H84), D84 (≠ S93), Q104 (≠ G113), D132 (= D141), W134 (≠ G143), F217 (≠ Q232)
5du4A Crystal structure of m. Tuberculosis echa6 bound to ligand gsk366a (see paper)
33% identity, 95% coverage: 12:258/259 of query aligns to 9:243/244 of 5du4A
- active site: A61 (= A64), D66 (= D71), P73 (≠ A78), I77 (vs. gap), A101 (= A110), Q104 (≠ G113), P123 (≠ A132), T124 (≠ F133), L129 (= L138), L131 (≠ P140), D132 (= D141), P211 (≠ S226), W221 (≠ G236)
- binding (5R,7S)-5-(4-ethylphenyl)-N-(4-methoxybenzyl)-7-(trifluoromethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L76 (= L81), I77 (vs. gap), H80 (= H84), D84 (≠ S93), Q104 (≠ G113), D132 (= D141), W134 (≠ G143)
5dtwA Crystal structure of m. Tuberculosis echa6 bound to c20-coa (see paper)
33% identity, 95% coverage: 12:258/259 of query aligns to 9:243/244 of 5dtwA
- active site: A61 (= A64), D66 (= D71), P73 (≠ A78), I77 (vs. gap), A101 (= A110), Q104 (≠ G113), P123 (≠ A132), T124 (≠ F133), L129 (= L138), L131 (≠ P140), D132 (= D141), P211 (≠ S226), W221 (≠ G236)
- binding Arachinoyl-CoA: R18 (= R21), E20 (≠ D23), R21 (= R24), R21 (= R24), R22 (≠ L25), A24 (= A27), A59 (≠ S62), A61 (= A64), D62 (= D65), L63 (= L66), H80 (= H84), D84 (≠ S93), G100 (= G109), A101 (= A110), Y127 (≠ I136), W134 (≠ G143)
5dufA Crystal structure of m. Tuberculosis echa6 bound to ligand gsk729a (see paper)
33% identity, 95% coverage: 12:258/259 of query aligns to 10:244/245 of 5dufA
- active site: A62 (= A64), D67 (= D71), P74 (≠ A78), I78 (vs. gap), A102 (= A110), Q105 (≠ G113), P124 (≠ A132), T125 (≠ F133), L130 (= L138), L132 (≠ P140), D133 (= D141), P212 (≠ S226), W222 (≠ G236)
- binding (5R,7S)-5-(4-ethylphenyl)-7-(trifluoromethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxylic acid: L77 (= L81), I78 (vs. gap), H81 (= H84), D85 (≠ S93), Q105 (≠ G113), D133 (= D141), W135 (≠ G143)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
30% identity, 98% coverage: 2:256/259 of query aligns to 1:249/250 of 3q0gD
- active site: A64 (= A64), M69 (≠ R69), T75 (≠ E82), F79 (≠ N86), G103 (≠ A110), E106 (≠ G113), P125 (≠ A132), E126 (≠ F133), V131 (≠ L138), P133 (= P140), G134 (≠ D141), L219 (≠ S226), F229 (≠ G236)
- binding Butyryl Coenzyme A: F225 (≠ Q232), F241 (= F248)
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, 95% coverage: 4:249/259 of query aligns to 3:253/269 of A5JTM5
- R24 (≠ L25) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (≠ L35) mutation to T: Forms inclusion bodies.
- E43 (≠ V44) mutation to A: No effect on catalytic activity.
- D45 (= D45) mutation to A: No effect on catalytic activity.
- D46 (≠ E46) mutation to A: No effect on catalytic activity.
- G63 (= G63) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ A64) 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 (≠ D71) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (≠ G72) mutation to T: No effect on catalytic activity.
- H81 (≠ N80) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ L81) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (≠ Y85) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ N86) 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 (≠ E90) mutation to Q: No effect on catalytic activity.
- A112 (= A108) 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 (= G109) 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 (≠ A110) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G111) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D119) mutation to T: No effect on catalytic activity.
- D129 (≠ K125) mutation to T: No effect on catalytic activity.
- W137 (≠ F133) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D141) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (= E159) mutation to T: No effect on catalytic activity.
- E175 (≠ D171) mutation to D: No effect on catalytic activity.
- W179 (≠ A175) mutation to F: No effect on catalytic activity.
- H208 (≠ V204) mutation to Q: No effect on catalytic activity.
- R216 (≠ Q212) mutation R->E,K,L: Yields insoluble protein.
- E232 (= E228) 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.
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
30% identity, 95% coverage: 4:249/259 of query aligns to 3:253/269 of 1nzyB
- active site: C61 (= C61), F64 (≠ A64), I69 (≠ K73), A86 (vs. gap), H90 (≠ N86), G114 (≠ A110), G117 (= G113), A136 (= A132), W137 (≠ F133), I142 (≠ L138), N144 (≠ P140), D145 (= D141), E230 (≠ S226)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D23), H23 (≠ R24), R24 (≠ L25), A62 (≠ S62), F64 (≠ A64), Y65 (≠ D65), L66 (= L66), R67 (≠ D71), W89 (≠ Y85), G113 (= G109), G114 (≠ A110), A136 (= A132), W137 (≠ F133), D145 (= D141), T146 (≠ C142), F252 (= F248)
- binding calcium ion: G49 (≠ R49), L202 (= L198), A203 (= A199), A205 (≠ K201), T207 (= T203), Q210 (≠ L206)
- binding phosphate ion: E57 (≠ G57), N108 (= N104), K188 (≠ D184), R192 (≠ L188)
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, 95% coverage: 4:249/259 of query aligns to 3:253/269 of 1jxzB
- active site: C61 (= C61), F64 (≠ A64), I69 (≠ K73), A86 (vs. gap), Q90 (≠ N86), G113 (= G109), G114 (≠ A110), G117 (= G113), A136 (= A132), W137 (≠ F133), I142 (≠ L138), N144 (≠ P140), D145 (= D141), E230 (≠ S226)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D23), H23 (≠ R24), R24 (≠ L25), A62 (≠ S62), F64 (≠ A64), Y65 (≠ D65), L66 (= L66), R67 (≠ D71), W89 (≠ Y85), G113 (= G109), A136 (= A132), W137 (≠ F133), I142 (≠ L138), D145 (= D141), T146 (≠ C142), F252 (= F248)
- binding calcium ion: G49 (≠ R49), L202 (= L198), A203 (= A199), A205 (≠ K201), T207 (= T203), Q210 (≠ L206)
Sites not aligning to the query:
Query Sequence
>Ga0059261_3986 Ga0059261_3986 Enoyl-CoA hydratase/carnithine racemase
MSQETVLYDLTDGVATLRLNRPDRLNAVTGEMLDLIRASLLRAVDEGARAVLLTGEGRAF
CSGADLVGRMDGKPIDPADNLEFHYNPLAETLSKLPIPVVTAVNGPAAGAGVGIALAGDI
VVMAKSAYLLLAFSNIGLVPDCGATWLVAKSAGRAKALEMALLGEKVSADDAKDAGLVAR
VAEDDALLATAGGIAAKLAAKPTVALGLIRAQVKAALNSTLSETLSIEAQNQRAAGKTED
FREGVTAFLAKRAPEFRGR
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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