SitesBLAST
Comparing RR42_RS18255 RR42_RS18255 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)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
48% identity, 97% coverage: 9:256/256 of query aligns to 13:257/257 of 6slbAAA
- active site: Q64 (= Q59), F69 (≠ L64), L80 (= L74), N84 (= N83), A108 (= A107), S111 (≠ N110), A130 (= A129), F131 (= F130), L136 (= L135), P138 (= P137), D139 (= D138), A224 (≠ D223), G234 (= G233)
- 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 (= R53), A62 (= A57), Q64 (= Q59), D65 (= D60), L66 (= L61), Y76 (≠ A70), A108 (= A107), F131 (= F130), D139 (= D138)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
46% identity, 97% coverage: 9:256/256 of query aligns to 10:245/245 of 6slaAAA
- active site: Q61 (= Q59), L68 (≠ F66), N72 (= N83), A96 (= A107), S99 (≠ N110), A118 (= A129), F119 (= F130), L124 (= L135), P126 (= P137), N127 (≠ D138), A212 (≠ D223), G222 (= G233)
- 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 (= L20), A59 (= A57), Q61 (= Q59), D62 (= D60), L63 (= L61), L68 (≠ F66), Y71 (≠ F82), A94 (= A105), G95 (= G106), A96 (= A107), F119 (= F130), I122 (= I133), L124 (= L135), N127 (≠ D138), F234 (= F245), K237 (= K248)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
35% identity, 98% coverage: 6:256/256 of query aligns to 11:259/259 of 5zaiC
- active site: A65 (≠ Q59), F70 (≠ L64), S82 (≠ N83), R86 (vs. gap), G110 (≠ A107), E113 (≠ N110), P132 (≠ A129), E133 (≠ F130), I138 (≠ L135), P140 (= P137), G141 (≠ D138), A226 (≠ D223), F236 (≠ G233)
- binding coenzyme a: K24 (= K19), L25 (= L20), A63 (= A57), G64 (= G58), A65 (≠ Q59), D66 (= D60), I67 (≠ L61), P132 (≠ A129), R166 (≠ K163), F248 (= F245), K251 (= K248)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
35% identity, 100% coverage: 1:256/256 of query aligns to 5:256/256 of 3h81A
- active site: A64 (≠ Q59), M69 (vs. gap), T79 (≠ M71), F83 (≠ I78), G107 (≠ A107), E110 (≠ N110), P129 (≠ A129), E130 (≠ F130), V135 (≠ L135), P137 (= P137), G138 (≠ D138), L223 (≠ D223), F233 (≠ G233)
- binding calcium ion: F233 (≠ G233), Q238 (≠ Y238)
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)
34% identity, 97% coverage: 6:253/256 of query aligns to 44:287/290 of P14604
- E144 (≠ N110) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ F130) 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
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
34% identity, 97% coverage: 6:253/256 of query aligns to 14:257/260 of 1dubA
- active site: A68 (≠ Q59), M73 (≠ L64), S83 (≠ L74), L87 (≠ I78), G111 (≠ A107), E114 (≠ N110), P133 (≠ A129), E134 (≠ F130), T139 (≠ L135), P141 (= P137), G142 (≠ D138), K227 (≠ D223), F237 (≠ G233)
- binding acetoacetyl-coenzyme a: K26 (≠ D18), A27 (≠ K19), L28 (= L20), A30 (≠ S22), A66 (= A57), A68 (≠ Q59), D69 (= D60), I70 (≠ L61), Y107 (≠ T103), G110 (= G106), G111 (≠ A107), E114 (≠ N110), P133 (≠ A129), E134 (≠ F130), L137 (≠ I133), G142 (≠ D138), F233 (≠ Q229), F249 (= F245)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
34% identity, 97% coverage: 6:253/256 of query aligns to 12:255/258 of 1ey3A
- active site: A66 (≠ Q59), M71 (≠ L64), S81 (≠ L74), L85 (≠ I78), G109 (≠ A107), E112 (≠ N110), P131 (≠ A129), E132 (≠ F130), T137 (≠ L135), P139 (= P137), G140 (≠ D138), K225 (≠ D223), F235 (≠ G233)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ D18), L26 (= L20), A28 (≠ S22), A64 (= A57), G65 (= G58), A66 (≠ Q59), D67 (= D60), I68 (≠ L61), L85 (≠ I78), W88 (= W81), G109 (≠ A107), P131 (≠ A129), L135 (≠ I133), G140 (≠ D138)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
34% identity, 97% coverage: 6:253/256 of query aligns to 14:257/260 of 2hw5C
- active site: A68 (≠ Q59), M73 (= M71), S83 (≠ F82), L87 (≠ I86), G111 (≠ A107), E114 (≠ N110), P133 (≠ A129), E134 (≠ F130), T139 (≠ L135), P141 (= P137), G142 (≠ D138), K227 (≠ D223), F237 (≠ G233)
- binding crotonyl coenzyme a: K26 (≠ D18), A27 (≠ K19), L28 (= L20), A30 (≠ S22), K62 (≠ R53), I70 (≠ L61), F109 (≠ A105)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
35% identity, 99% coverage: 1:254/256 of query aligns to 6:255/255 of 3q0jC
- active site: A65 (≠ Q59), M70 (vs. gap), T80 (≠ M71), F84 (≠ I78), G108 (≠ A107), E111 (≠ N110), P130 (≠ A129), E131 (≠ F130), V136 (≠ L135), P138 (= P137), G139 (≠ D138), L224 (≠ D223), F234 (≠ G233)
- binding acetoacetyl-coenzyme a: Q23 (≠ D18), A24 (≠ K19), L25 (= L20), A27 (≠ S22), A63 (= A57), G64 (= G58), A65 (≠ Q59), D66 (= D60), I67 (≠ L61), K68 (vs. gap), M70 (vs. gap), F84 (≠ I78), G107 (= G106), G108 (≠ A107), E111 (≠ N110), P130 (≠ A129), E131 (≠ F130), P138 (= P137), G139 (≠ D138), M140 (≠ S139)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 99% coverage: 1:254/256 of query aligns to 6:255/255 of 3q0gC
- active site: A65 (≠ Q59), M70 (vs. gap), T80 (≠ M71), F84 (≠ I78), G108 (≠ A107), E111 (≠ N110), P130 (≠ A129), E131 (≠ F130), V136 (≠ L135), P138 (= P137), G139 (≠ D138), L224 (≠ D223), F234 (≠ G233)
- binding coenzyme a: L25 (= L20), A63 (= A57), I67 (≠ L61), K68 (vs. gap), Y104 (≠ T103), P130 (≠ A129), E131 (≠ F130), L134 (≠ I133)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
34% identity, 97% coverage: 6:253/256 of query aligns to 14:255/258 of 1mj3A
- active site: A68 (≠ Q59), M73 (≠ L64), S83 (≠ E76), L85 (≠ I78), G109 (≠ A107), E112 (≠ N110), P131 (≠ A129), E132 (≠ F130), T137 (≠ L135), P139 (= P137), G140 (≠ D138), K225 (≠ D223), F235 (≠ G233)
- binding hexanoyl-coenzyme a: K26 (≠ D18), A27 (≠ K19), L28 (= L20), A30 (≠ S22), A66 (= A57), G67 (= G58), A68 (≠ Q59), D69 (= D60), I70 (≠ L61), G109 (≠ A107), P131 (≠ A129), E132 (≠ F130), L135 (≠ I133), G140 (≠ D138)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 99% coverage: 1:254/256 of query aligns to 5:250/250 of 3q0gD
- active site: A64 (≠ Q59), M69 (≠ L64), T75 (≠ M71), F79 (≠ I78), G103 (≠ A107), E106 (≠ N110), P125 (≠ A129), E126 (≠ F130), V131 (≠ L135), P133 (= P137), G134 (≠ D138), L219 (≠ D223), F229 (≠ G233)
- binding Butyryl Coenzyme A: F225 (≠ Q229), F241 (= F245)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
34% identity, 97% coverage: 6:253/256 of query aligns to 13:251/254 of 2dubA
- active site: A67 (≠ Q59), M72 (≠ L64), S82 (≠ D79), G105 (≠ A107), E108 (≠ N110), P127 (≠ A129), E128 (≠ F130), T133 (≠ L135), P135 (= P137), G136 (≠ D138), K221 (≠ D223), F231 (≠ G233)
- binding octanoyl-coenzyme a: K25 (≠ D18), A26 (≠ K19), L27 (= L20), A29 (≠ S22), A65 (= A57), A67 (≠ Q59), D68 (= D60), I69 (≠ L61), K70 (≠ A62), G105 (≠ A107), E108 (≠ N110), P127 (≠ A129), E128 (≠ F130), G136 (≠ D138), A137 (≠ S139)
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
31% identity, 95% coverage: 9:252/256 of query aligns to 13:260/269 of 1nzyB
- active site: C61 (= C56), F64 (≠ Q59), I69 (≠ L64), A86 (≠ D79), H90 (≠ N83), G114 (≠ A107), G117 (≠ N110), A136 (= A129), W137 (≠ F130), I142 (≠ L135), N144 (≠ P137), D145 (= D138), E230 (≠ D223)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D18), H23 (≠ K19), R24 (≠ L20), A62 (= A57), F64 (≠ Q59), Y65 (≠ D60), L66 (= L61), R67 (≠ A62), W89 (≠ F82), G113 (= G106), G114 (≠ A107), A136 (= A129), W137 (≠ F130), D145 (= D138), T146 (≠ S139), F252 (= F245), R257 (= R249)
- binding calcium ion: G49 (vs. gap), L202 (= L195), A203 (= A196), A205 (≠ Q198), T207 (= T200), Q210 (≠ L203)
- binding phosphate ion: E57 (≠ G52), N108 (= N101), K188 (≠ D181), R192 (≠ P185)
1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
31% identity, 95% coverage: 9:252/256 of query aligns to 13:260/269 of 1jxzB
- active site: C61 (= C56), F64 (≠ Q59), I69 (≠ L64), A86 (≠ D79), Q90 (≠ N83), G113 (= G106), G114 (≠ A107), G117 (≠ N110), A136 (= A129), W137 (≠ F130), I142 (≠ L135), N144 (≠ P137), D145 (= D138), E230 (≠ D223)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D18), H23 (≠ K19), R24 (≠ L20), A62 (= A57), F64 (≠ Q59), Y65 (≠ D60), L66 (= L61), R67 (≠ A62), W89 (≠ F82), G113 (= G106), A136 (= A129), W137 (≠ F130), I142 (≠ L135), D145 (= D138), T146 (≠ S139), F252 (= F245), R257 (= R249)
- binding calcium ion: G49 (vs. gap), L202 (= L195), A203 (= A196), A205 (≠ Q198), T207 (= T200), Q210 (≠ L203)
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)
31% identity, 95% coverage: 9:252/256 of query aligns to 13:260/269 of A5JTM5
- R24 (≠ L20) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (≠ V30) mutation to T: Forms inclusion bodies.
- E43 (= E39) mutation to A: No effect on catalytic activity.
- D45 (≠ G41) mutation to A: No effect on catalytic activity.
- D46 (≠ G42) mutation to A: No effect on catalytic activity.
- G63 (= G58) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ Q59) 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 (≠ D60) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (≠ A62) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (≠ D63) mutation to T: No effect on catalytic activity.
- H81 (≠ L74) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ G75) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (≠ F82) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ N83) 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 (≠ R87) mutation to Q: No effect on catalytic activity.
- A112 (= A105) 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 (= G106) 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 (≠ A107) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G108) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D116) mutation to T: No effect on catalytic activity.
- D129 (≠ R122) mutation to T: No effect on catalytic activity.
- W137 (≠ F130) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D138) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (≠ G156) mutation to T: No effect on catalytic activity.
- E175 (= E168) mutation to D: No effect on catalytic activity.
- W179 (= W172) mutation to F: No effect on catalytic activity.
- H208 (≠ R201) mutation to Q: No effect on catalytic activity.
- R216 (≠ A209) mutation R->E,K,L: Yields insoluble protein.
- E232 (= E225) mutation E->A,N,Q,R: Yields insoluble protein.; mutation to D: Reduced catalytic activity, increased substrate binding.
- R257 (= R249) mutation to K: Retains catalytic activity and substrate CoA binding.; mutation to L: Significantly reduces catalytic activity and substrate CoA binding.
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
34% identity, 98% coverage: 6:256/256 of query aligns to 12:261/261 of 5jbxB
- active site: A67 (≠ Q59), R72 (≠ L64), L84 (≠ I78), R88 (≠ N83), G112 (≠ A107), E115 (≠ N110), T134 (≠ A129), E135 (≠ F130), I140 (≠ L135), P142 (= P137), G143 (≠ D138), A228 (≠ D223), L238 (≠ G233)
- binding coenzyme a: S24 (≠ D18), R25 (≠ K19), R26 (≠ L20), A28 (≠ S22), A65 (= A57), D68 (= D60), L69 (= L61), K70 (≠ A62), L110 (≠ A105), G111 (= G106), T134 (≠ A129), E135 (≠ F130), L138 (≠ I133), R168 (≠ K163)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
33% identity, 100% coverage: 2:256/256 of query aligns to 11:266/266 of O53561
- K135 (≠ S125) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 125:132, 25% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (= K132) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
7borA Structure of pseudomonas aeruginosa coa-bound odaa (see paper)
33% identity, 93% coverage: 11:248/256 of query aligns to 14:247/247 of 7borA
- active site: N63 (≠ Q59), F68 (≠ L64), D77 (= D73), G81 (≠ N83), I105 (≠ A107), T108 (≠ N110), F128 (= F130), L133 (= L135), P135 (= P137), E136 (≠ D138), A222 (≠ D223), L232 (≠ G233)
- binding coenzyme a: D21 (= D18), K22 (= K19), A25 (≠ S22), S61 (≠ A57), I65 (≠ L61), V103 (≠ A105), F128 (= F130), L131 (≠ I133), F244 (= F245), R247 (≠ K248)
3rrvB Crystal structure of an enoyl-coa hydratase/isomerase from mycobacterium paratuberculosis (see paper)
32% identity, 95% coverage: 7:248/256 of query aligns to 14:253/254 of 3rrvB
Query Sequence
>RR42_RS18255 RR42_RS18255 enoyl-CoA hydratase
MLLAWHGQVAVITLNRPDKLNSFTREMHAVLQQALDHVEAGGARALLLTGAGRGFCAGQD
LADLDFTPGAMTDLGELIDVWFNRLIRRLQKLPLPVIAAVNGTAAGAGANLALACDMVLA
ARSASFIQAFVKIGLVPDSGGTWLLPKRIGMARAMGLAMTGDKLSADEAEKWGLIWEAMD
DPLLPEQALALATHLAAQPTRALAAIKQAMYAGASQGLDAQLDLERDLQRELGASPDYAE
GVNAFLEKRAPRFTGR
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