SitesBLAST
Comparing AZOBR_RS07775 AZOBR_RS07775 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)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
35% identity, 94% coverage: 17:268/268 of query aligns to 11:260/260 of 2hw5C
- active site: A68 (≠ H74), M73 (= M79), S83 (≠ E89), L87 (≠ V93), G111 (≠ A120), E114 (≠ Q123), P133 (= P142), E134 (≠ G143), T139 (≠ L148), P141 (≠ C150), G142 (≠ S151), K227 (≠ A235), F237 (≠ M245)
- binding crotonyl coenzyme a: K26 (≠ Q32), A27 (= A33), L28 (≠ R34), A30 (= A36), K62 (≠ P68), I70 (≠ L76), F109 (≠ T118)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
36% identity, 89% coverage: 23:261/268 of query aligns to 15:251/258 of 1ey3A
- active site: A66 (≠ H74), M71 (= M79), S81 (≠ E89), L85 (≠ V93), G109 (≠ A120), E112 (≠ Q123), P131 (= P142), E132 (≠ G143), T137 (≠ L148), P139 (vs. gap), G140 (≠ C150), K225 (≠ A235), F235 (≠ M245)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ Q32), L26 (≠ R34), A28 (= A36), A64 (= A72), G65 (= G73), A66 (≠ H74), D67 (= D75), I68 (≠ L76), L85 (≠ V93), W88 (≠ S96), G109 (≠ A120), P131 (= P142), L135 (≠ I146), G140 (≠ C150)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
36% identity, 89% coverage: 23:261/268 of query aligns to 17:253/260 of 1dubA
- active site: A68 (≠ H74), M73 (= M79), S83 (≠ E89), L87 (≠ V93), G111 (≠ A120), E114 (≠ Q123), P133 (= P142), E134 (≠ G143), T139 (≠ L148), P141 (vs. gap), G142 (≠ C150), K227 (≠ A235), F237 (≠ M245)
- binding acetoacetyl-coenzyme a: K26 (≠ Q32), A27 (= A33), L28 (≠ R34), A30 (= A36), A66 (= A72), A68 (≠ H74), D69 (= D75), I70 (≠ L76), Y107 (≠ I116), G110 (≠ A119), G111 (≠ A120), E114 (≠ Q123), P133 (= P142), E134 (≠ G143), L137 (≠ I146), G142 (≠ C150), F233 (≠ M241), F249 (= F257)
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)
36% identity, 89% coverage: 23:261/268 of query aligns to 47:283/290 of P14604
- E144 (≠ Q123) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ G143) 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
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
36% identity, 89% coverage: 23:261/268 of query aligns to 16:247/254 of 2dubA
- active site: A67 (≠ H74), M72 (= M79), S82 (≠ K97), G105 (≠ A120), E108 (≠ Q123), P127 (= P142), E128 (≠ G143), T133 (≠ L148), P135 (vs. gap), G136 (≠ C150), K221 (≠ A235), F231 (≠ M245)
- binding octanoyl-coenzyme a: K25 (≠ Q32), A26 (= A33), L27 (≠ R34), A29 (= A36), A65 (= A72), A67 (≠ H74), D68 (= D75), I69 (≠ L76), K70 (= K77), G105 (≠ A120), E108 (≠ Q123), P127 (= P142), E128 (≠ G143), G136 (≠ C150), A137 (≠ S151)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
36% identity, 89% coverage: 23:261/268 of query aligns to 17:251/258 of 1mj3A
- active site: A68 (≠ H74), M73 (= M79), S83 (≠ E89), L85 (= L91), G109 (≠ A120), E112 (≠ Q123), P131 (= P142), E132 (≠ G143), T137 (≠ L148), P139 (≠ C150), G140 (≠ S151), K225 (≠ A235), F235 (≠ M245)
- binding hexanoyl-coenzyme a: K26 (≠ Q32), A27 (= A33), L28 (≠ R34), A30 (= A36), A66 (= A72), G67 (= G73), A68 (≠ H74), D69 (= D75), I70 (≠ L76), G109 (≠ A120), P131 (= P142), E132 (≠ G143), L135 (≠ I146), G140 (≠ S151)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 95% coverage: 14:268/268 of query aligns to 4:257/257 of 6slbAAA
- active site: Q64 (≠ H74), F69 (≠ M79), L80 (≠ F92), N84 (≠ S96), A108 (= A120), S111 (≠ Q123), A130 (≠ P142), F131 (≠ G143), L136 (= L148), P138 (≠ C150), D139 (≠ S151), A224 (= A235), G234 (≠ M245)
- 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 (≠ P68), A62 (= A72), Q64 (≠ H74), D65 (= D75), L66 (= L76), Y76 (= Y88), A108 (= A120), F131 (≠ G143), D139 (≠ S151)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
36% identity, 94% coverage: 14:266/268 of query aligns to 6:250/250 of 3q0gD
- active site: A64 (≠ H74), M69 (= M79), T75 (≠ R85), F79 (= F92), G103 (≠ A120), E106 (≠ Q123), P125 (= P142), E126 (≠ G143), V131 (≠ L148), P133 (= P153), G134 (≠ M154), L219 (≠ A235), F229 (≠ M245)
- binding Butyryl Coenzyme A: F225 (≠ M241), F241 (= F257)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
35% identity, 94% coverage: 14:266/268 of query aligns to 7:255/255 of 3q0jC
- active site: A65 (≠ H74), M70 (= M79), T80 (≠ E89), F84 (= F92), G108 (≠ A120), E111 (≠ Q123), P130 (= P142), E131 (≠ G143), V136 (≠ L148), P138 (= P153), G139 (≠ M154), L224 (≠ A235), F234 (≠ M245)
- binding acetoacetyl-coenzyme a: Q23 (= Q32), A24 (= A33), L25 (≠ R34), A27 (= A36), A63 (= A72), G64 (= G73), A65 (≠ H74), D66 (= D75), I67 (≠ L76), K68 (= K77), M70 (= M79), F84 (= F92), G107 (≠ A119), G108 (≠ A120), E111 (≠ Q123), P130 (= P142), E131 (≠ G143), P138 (= P153), G139 (≠ M154), M140 (≠ V155)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 94% coverage: 14:266/268 of query aligns to 7:255/255 of 3q0gC
- active site: A65 (≠ H74), M70 (= M79), T80 (≠ E89), F84 (= F92), G108 (≠ A120), E111 (≠ Q123), P130 (= P142), E131 (≠ G143), V136 (≠ L148), P138 (= P153), G139 (≠ M154), L224 (≠ A235), F234 (≠ M245)
- binding coenzyme a: L25 (≠ R34), A63 (= A72), I67 (≠ L76), K68 (= K77), Y104 (≠ I116), P130 (= P142), E131 (≠ G143), L134 (≠ I146)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
35% identity, 94% coverage: 14:266/268 of query aligns to 6:254/256 of 3h81A
- active site: A64 (≠ H74), M69 (= M79), T79 (≠ E89), F83 (= F92), G107 (≠ A120), E110 (≠ Q123), P129 (= P142), E130 (≠ G143), V135 (≠ L148), P137 (= P153), G138 (≠ M154), L223 (≠ A235), F233 (≠ M245)
- binding calcium ion: F233 (≠ M245), Q238 (≠ A250)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
36% identity, 95% coverage: 14:268/268 of query aligns to 1:245/245 of 6slaAAA
- active site: Q61 (≠ H74), L68 (≠ F92), N72 (≠ S96), A96 (= A120), S99 (≠ Q123), A118 (≠ P142), F119 (≠ G143), L124 (= L148), P126 (≠ C150), N127 (≠ S151), A212 (= A235), G222 (≠ M245)
- 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 (≠ R34), A59 (= A72), Q61 (≠ H74), D62 (= D75), L63 (= L76), L68 (≠ F92), Y71 (≠ C95), A94 (≠ T118), G95 (≠ A119), A96 (= A120), F119 (≠ G143), I122 (= I146), L124 (= L148), N127 (≠ S151), F234 (= F257), K237 (= K260)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
32% identity, 91% coverage: 26:268/268 of query aligns to 17:259/259 of 5zaiC
- active site: A65 (≠ H74), F70 (≠ M79), S82 (≠ F92), R86 (≠ S96), G110 (≠ A120), E113 (≠ Q123), P132 (= P142), E133 (≠ G143), I138 (≠ L148), P140 (≠ C150), G141 (≠ S151), A226 (= A235), F236 (≠ M245)
- binding coenzyme a: K24 (≠ A33), L25 (≠ R34), A63 (= A72), G64 (= G73), A65 (≠ H74), D66 (= D75), I67 (≠ L76), P132 (= P142), R166 (≠ L175), F248 (= F257), K251 (= K260)
O69762 Hydroxycinnamoyl-CoA hydratase-lyase; HCHL; P-hydroxycinnamoyl CoA hydratase/lyase; Trans-feruloyl-CoA hydratase/vanillin synthase; EC 4.1.2.61 from Pseudomonas fluorescens (see 2 papers)
33% identity, 91% coverage: 18:261/268 of query aligns to 14:265/276 of O69762
- K29 (≠ A33) binding
- A68 (= A72) binding
- M70 (≠ H74) binding
- L72 (= L76) binding
- Y75 (≠ M79) binding
- G120 (≠ A120) binding
- S123 (≠ Q123) mutation to A: Reduced kcat compared to wild-type but not markerdly.
- S142 (≠ P142) binding
- E143 (≠ G143) mutation to A: Abolishes catalytic activity.
- W146 (≠ I146) binding
- G151 (≠ S151) binding
- Y239 (= Y236) binding ; mutation to F: Increased KM for feruloyl-CoA but retains a significant amount of catalytic activity with a kcat 10 times less than that of the wild-type.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
35% identity, 82% coverage: 18:237/268 of query aligns to 11:237/247 of 2vssB
- active site: M67 (≠ H74), Y72 (≠ M79), D77 (= D84), R89 (≠ V93), Q93 (≠ K97), G117 (≠ A120), S120 (≠ Q123), S139 (≠ P142), E140 (≠ G143), I145 (≠ L148), P147 (≠ C150), G148 (≠ S151), Y236 (= Y236)
- binding acetyl coenzyme *a: E25 (≠ Q32), K26 (≠ A33), R27 (= R34), A29 (= A36), A65 (= A72), M67 (≠ H74), D68 (= D75), W113 (≠ I116), F115 (≠ T118), G117 (≠ A120), S139 (≠ P142), E140 (≠ G143)
Sites not aligning to the query:
2vssD Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin (see paper)
35% identity, 82% coverage: 18:237/268 of query aligns to 12:238/246 of 2vssD
- active site: M68 (≠ H74), Y73 (≠ M79), D78 (= D84), R90 (≠ V93), Q94 (≠ K97), G118 (≠ A120), S121 (≠ Q123), S140 (≠ P142), E141 (≠ G143), I146 (≠ L148), P148 (≠ C150), G149 (≠ S151), Y237 (= Y236)
- binding acetyl coenzyme *a: E26 (≠ Q32), K27 (≠ A33), R28 (= R34), A30 (= A36), A66 (= A72), M68 (≠ H74), D69 (= D75), L70 (= L76), F74 (≠ R80), W114 (≠ I116), F116 (≠ T118), S140 (≠ P142)
- binding 4-hydroxy-3-methoxybenzaldehyde: M68 (≠ H74), Y73 (≠ M79), F74 (≠ R80), Q96 (≠ M99), E141 (≠ G143), G149 (≠ S151), N150 (≠ T152)
1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
34% identity, 79% coverage: 21:232/268 of query aligns to 11:227/269 of 1jxzB
- active site: C61 (= C71), F64 (≠ H74), I69 (≠ M79), A86 (vs. gap), Q90 (≠ S96), G113 (≠ A119), G114 (≠ A120), G117 (≠ Q123), A136 (≠ P142), W137 (≠ G143), I142 (≠ L148), N144 (≠ C150), D145 (≠ S151)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ Q32), H23 (≠ A33), R24 (= R34), A62 (= A72), F64 (≠ H74), Y65 (≠ D75), L66 (= L76), R67 (≠ K77), W89 (≠ C95), G113 (≠ A119), A136 (≠ P142), W137 (≠ G143), I142 (≠ L148), D145 (≠ S151), T146 (= T152)
- binding calcium ion: G49 (≠ R59), L202 (≠ I207), A203 (= A208), A205 (≠ K210), T207 (≠ P212), Q210 (≠ L215)
Sites not aligning to the query:
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
34% identity, 79% coverage: 21:232/268 of query aligns to 11:227/269 of 1nzyB
- active site: C61 (= C71), F64 (≠ H74), I69 (≠ M79), A86 (vs. gap), H90 (≠ S96), G114 (≠ A120), G117 (≠ Q123), A136 (≠ P142), W137 (≠ G143), I142 (≠ L148), N144 (≠ C150), D145 (≠ S151)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ Q32), H23 (≠ A33), R24 (= R34), A62 (= A72), F64 (≠ H74), Y65 (≠ D75), L66 (= L76), R67 (≠ K77), W89 (≠ C95), G113 (≠ A119), G114 (≠ A120), A136 (≠ P142), W137 (≠ G143), D145 (≠ S151), T146 (= T152)
- binding calcium ion: G49 (≠ R59), L202 (≠ I207), A203 (= A208), A205 (≠ K210), T207 (≠ P212), Q210 (≠ L215)
- binding phosphate ion: E57 (≠ G67), N108 (≠ H114), K188 (≠ A193), R192 (≠ D197)
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)
34% identity, 79% coverage: 21:232/268 of query aligns to 11:227/269 of A5JTM5
- R24 (= R34) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (≠ A44) mutation to T: Forms inclusion bodies.
- E43 (≠ H53) mutation to A: No effect on catalytic activity.
- D45 (= D55) mutation to A: No effect on catalytic activity.
- D46 (≠ S56) mutation to A: No effect on catalytic activity.
- G63 (= G73) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ H74) 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 (≠ D75) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (≠ K77) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (= E78) mutation to T: No effect on catalytic activity.
- H81 (≠ L91) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (= F92) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (≠ C95) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ S96) 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 (≠ L100) mutation to Q: No effect on catalytic activity.
- A112 (≠ T118) 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 (≠ A119) 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 (≠ A120) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G121) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D129) mutation to T: No effect on catalytic activity.
- D129 (= D135) mutation to T: No effect on catalytic activity.
- W137 (≠ G143) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (≠ S151) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (= E168) mutation to T: No effect on catalytic activity.
- E175 (= E180) mutation to D: No effect on catalytic activity.
- W179 (≠ I184) mutation to F: No effect on catalytic activity.
- H208 (≠ L213) mutation to Q: No effect on catalytic activity.
- R216 (≠ A221) mutation R->E,K,L: Yields insoluble protein.
Sites not aligning to the query:
- 232 mutation E->A,N,Q,R: Yields insoluble protein.; E→D: Reduced catalytic activity, increased substrate binding.
- 257 R→K: Retains catalytic activity and substrate CoA binding.; R→L: Significantly reduces catalytic activity and substrate CoA binding.
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
31% identity, 95% coverage: 10:263/268 of query aligns to 5:261/266 of O53561
- K135 (≠ R138) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 138:148, 18% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ L148) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
Query Sequence
>AZOBR_RS07775 AZOBR_RS07775 enoyl-CoA hydratase
MNDTPPLIGDDAPLVLREDRDGVATLTLNRPQARNALSVGLMGALQAELDTIHQDSTVRA
VVLAGAGPAFCAGHDLKEMRANPDRAAYESLFVQCSKLMLTVSRIRQPVIAKVHGIATAA
GCQLVATCDLAYCADTARFATPGVNIGLFCSTPMVALSRAVGRKAAMEMLLLGDLIGAEE
AVRIGLVNRAVPADRLDAVVTEAAGKIAAKSPLTLAIGKEAFYRQIELDVEEAYAYAARV
MTENMLARDAEEGIDAFLQKRPPVWCGQ
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