SitesBLAST
Comparing AZOBR_RS26485 AZOBR_RS26485 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)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
46% identity, 98% coverage: 7:262/262 of query aligns to 6:259/259 of 5zaiC
- active site: A65 (≠ G67), F70 (≠ L72), S82 (≠ A85), R86 (≠ H89), G110 (= G113), E113 (= E116), P132 (= P135), E133 (= E136), I138 (≠ L141), P140 (= P143), G141 (= G144), A226 (= A229), F236 (≠ L239)
- binding coenzyme a: K24 (≠ T25), L25 (= L26), A63 (= A65), G64 (= G66), A65 (≠ G67), D66 (= D68), I67 (= I69), P132 (= P135), R166 (≠ Q169), F248 (= F251), K251 (= K254)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
43% identity, 97% coverage: 7:260/262 of query aligns to 6:255/255 of 3q0jC
- active site: A65 (≠ G67), M70 (≠ L72), T80 (≠ H89), F84 (= F95), G108 (= G113), E111 (= E116), P130 (= P135), E131 (= E136), V136 (≠ L141), P138 (= P143), G139 (= G144), L224 (≠ A229), F234 (≠ L239)
- binding acetoacetyl-coenzyme a: Q23 (≠ T24), A24 (≠ T25), L25 (= L26), A27 (= A28), A63 (= A65), G64 (= G66), A65 (≠ G67), D66 (= D68), I67 (= I69), K68 (≠ A70), M70 (≠ L72), F84 (= F95), G107 (= G112), G108 (= G113), E111 (= E116), P130 (= P135), E131 (= E136), P138 (= P143), G139 (= G144), M140 (≠ A145)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
43% identity, 97% coverage: 7:260/262 of query aligns to 6:255/255 of 3q0gC
- active site: A65 (≠ G67), M70 (≠ L72), T80 (≠ H89), F84 (= F95), G108 (= G113), E111 (= E116), P130 (= P135), E131 (= E136), V136 (≠ L141), P138 (= P143), G139 (= G144), L224 (≠ A229), F234 (≠ L239)
- binding coenzyme a: L25 (= L26), A63 (= A65), I67 (= I69), K68 (≠ A70), Y104 (≠ W109), P130 (= P135), E131 (= E136), L134 (= L139)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
43% identity, 97% coverage: 7:260/262 of query aligns to 5:254/256 of 3h81A
- active site: A64 (≠ G67), M69 (≠ L72), T79 (≠ H89), F83 (= F95), G107 (= G113), E110 (= E116), P129 (= P135), E130 (= E136), V135 (≠ L141), P137 (= P143), G138 (= G144), L223 (≠ A229), F233 (≠ L239)
- binding calcium ion: F233 (≠ L239), Q238 (≠ A244)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
43% identity, 97% coverage: 7:260/262 of query aligns to 5:250/250 of 3q0gD
- active site: A64 (≠ G67), M69 (≠ L72), T75 (≠ L78), F79 (= F84), G103 (= G113), E106 (= E116), P125 (= P135), E126 (= E136), V131 (≠ L141), P133 (= P143), G134 (= G144), L219 (≠ A229), F229 (≠ L239)
- binding Butyryl Coenzyme A: F225 (≠ I235), F241 (= F251)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
42% identity, 97% coverage: 7:259/262 of query aligns to 6:255/258 of 1mj3A
- active site: A68 (≠ G67), M73 (≠ L72), S83 (≠ Q76), L85 (= L78), G109 (= G113), E112 (= E116), P131 (= P135), E132 (= E136), T137 (≠ L141), P139 (= P143), G140 (= G144), K225 (≠ A229), F235 (≠ L239)
- binding hexanoyl-coenzyme a: K26 (≠ T24), A27 (≠ T25), L28 (= L26), A30 (= A28), A66 (= A65), G67 (= G66), A68 (≠ G67), D69 (= D68), I70 (= I69), G109 (= G113), P131 (= P135), E132 (= E136), L135 (= L139), G140 (= G144)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
42% identity, 97% coverage: 7:259/262 of query aligns to 5:251/254 of 2dubA
- active site: A67 (≠ G67), M72 (≠ L72), S82 (≠ L82), G105 (= G113), E108 (= E116), P127 (= P135), E128 (= E136), T133 (≠ L141), P135 (= P143), G136 (= G144), K221 (≠ A229), F231 (≠ L239)
- binding octanoyl-coenzyme a: K25 (≠ T24), A26 (≠ T25), L27 (= L26), A29 (= A28), A65 (= A65), A67 (≠ G67), D68 (= D68), I69 (= I69), K70 (≠ A70), G105 (= G113), E108 (= E116), P127 (= P135), E128 (= E136), G136 (= G144), A137 (= A145)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
42% identity, 97% coverage: 7:259/262 of query aligns to 6:257/260 of 1dubA
- active site: A68 (≠ G67), M73 (≠ L72), S83 (vs. gap), L87 (= L82), G111 (= G113), E114 (= E116), P133 (= P135), E134 (= E136), T139 (≠ L141), P141 (= P143), G142 (= G144), K227 (≠ A229), F237 (≠ L239)
- binding acetoacetyl-coenzyme a: K26 (≠ T24), A27 (≠ T25), L28 (= L26), A30 (= A28), A66 (= A65), A68 (≠ G67), D69 (= D68), I70 (= I69), Y107 (≠ W109), G110 (= G112), G111 (= G113), E114 (= E116), P133 (= P135), E134 (= E136), L137 (= L139), G142 (= G144), F233 (≠ I235), F249 (= F251)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
42% identity, 97% coverage: 7:259/262 of query aligns to 4:255/258 of 1ey3A
- active site: A66 (≠ G67), M71 (≠ L72), S81 (vs. gap), L85 (= L82), G109 (= G113), E112 (= E116), P131 (= P135), E132 (= E136), T137 (≠ L141), P139 (= P143), G140 (= G144), K225 (≠ A229), F235 (≠ L239)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ T24), L26 (= L26), A28 (= A28), A64 (= A65), G65 (= G66), A66 (≠ G67), D67 (= D68), I68 (= I69), L85 (= L82), W88 (≠ A85), G109 (= G113), P131 (= P135), L135 (= L139), G140 (= G144)
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)
42% identity, 97% coverage: 7:259/262 of query aligns to 36:287/290 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
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
40% identity, 96% coverage: 11:262/262 of query aligns to 13:260/260 of 2hw5C
- active site: A68 (≠ G67), M73 (≠ L72), S83 (≠ A85), L87 (≠ H89), G111 (= G113), E114 (= E116), P133 (= P135), E134 (= E136), T139 (≠ L141), P141 (= P143), G142 (= G144), K227 (≠ A229), F237 (≠ L239)
- binding crotonyl coenzyme a: K26 (≠ T24), A27 (≠ T25), L28 (= L26), A30 (= A28), K62 (≠ R61), I70 (= I69), F109 (≠ L111)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
39% identity, 95% coverage: 13:262/262 of query aligns to 13:261/261 of 5jbxB
- active site: A67 (= A70), R72 (= R75), L84 (≠ A85), R88 (≠ H89), G112 (= G113), E115 (= E116), T134 (≠ P135), E135 (= E136), I140 (≠ L141), P142 (= P143), G143 (= G144), A228 (= A229), L238 (= L239)
- binding coenzyme a: S24 (≠ T24), R25 (≠ T25), R26 (≠ L26), A28 (= A28), A65 (= A65), D68 (= D71), L69 (= L72), K70 (≠ D73), L110 (= L111), G111 (= G112), T134 (≠ P135), E135 (= E136), L138 (= L139), R168 (≠ Q169)
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)
36% identity, 93% coverage: 17:259/262 of query aligns to 23:265/270 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, 98% coverage: 7:262/262 of query aligns to 5:257/257 of 6slbAAA
- active site: Q64 (≠ G67), F69 (≠ L72), L80 (≠ A85), N84 (≠ H89), A108 (≠ G113), S111 (≠ E116), A130 (≠ P135), F131 (≠ E136), L136 (= L141), P138 (= P143), D139 (≠ G144), A224 (= A229), G234 (≠ L239)
- 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 (= R61), A62 (= A65), Q64 (≠ G67), D65 (= D68), L66 (≠ I69), Y76 (= Y81), A108 (≠ G113), F131 (≠ E136), D139 (≠ G144)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 98% coverage: 7:262/262 of query aligns to 2:245/245 of 6slaAAA
- active site: Q61 (≠ G67), L68 (≠ Y81), N72 (≠ H89), A96 (≠ G113), S99 (≠ E116), A118 (≠ P135), F119 (≠ E136), L124 (= L141), P126 (= P143), N127 (≠ G144), A212 (= A229), G222 (≠ L239)
- 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 (= L26), A59 (= A65), Q61 (≠ G67), D62 (= D68), L63 (≠ I69), L68 (≠ Y81), Y71 (≠ F84), A94 (≠ L111), G95 (= G112), A96 (≠ G113), F119 (≠ E136), I122 (≠ L139), L124 (= L141), N127 (≠ G144), F234 (= F251), K237 (= K254)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
34% identity, 97% coverage: 8:262/262 of query aligns to 11:266/266 of O53561
- K135 (= K131) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 131:138, 50% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ N138) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
36% identity, 96% coverage: 10:260/262 of query aligns to 27:261/267 of 4elwA
- active site: G83 (= G67), L91 (= L82), G115 (= G113), V118 (≠ E116), G138 (≠ E136), S143 (≠ L141), D145 (≠ P143), G146 (= G144), A232 (= A229), Y240 (≠ L239)
- binding nitrate ion: G114 (= G112), T137 (≠ P135), G138 (≠ E136), F144 (= F142), W166 (≠ V164)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
36% identity, 96% coverage: 10:260/262 of query aligns to 30:279/285 of 4i42A
- active site: G86 (= G67), R91 (= R75), Y97 (= Y81), H105 (= H89), L109 (vs. gap), G133 (= G113), V136 (≠ E116), G156 (≠ E136), S161 (≠ L141), D163 (≠ P143), G164 (= G144), A250 (= A229), Y258 (≠ L239)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ T25), R45 (≠ L26), S84 (≠ A65), G85 (= G66), G86 (= G67), D87 (= D68), Q88 (≠ L72), K89 (≠ D73), Y97 (= Y81), V108 (vs. gap), Y129 (≠ W109), G133 (= G113), T155 (≠ P135), S161 (≠ L141), T254 (≠ A233), F270 (= F251), K273 (= K254)
P0ABU0 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Escherichia coli (strain K12) (see 4 papers)
36% identity, 96% coverage: 10:260/262 of query aligns to 30:279/285 of P0ABU0
- R45 (≠ L26) binding in other chain
- SGGD---QK 84:89 (≠ AGGDIADLD 65:73) binding in other chain
- K89 (≠ D73) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- R91 (= R75) mutation to A: Loss of DHNA-CoA synthase activity.
- Y97 (= Y81) binding in other chain; mutation to F: Loss of DHNA-CoA synthase activity.
- YSIGG 129:133 (≠ WALGG 109:113) binding in other chain
- Q154 (≠ L134) mutation to A: Reduces the specific DHNA-CoA synthase activity by 15-fold, whereas its affinity for hydrogencarbonate is reduced by 36-fold.
- QTG 154:156 (≠ LPE 134:136) binding
- T155 (≠ P135) binding in other chain
- G156 (≠ E136) mutation to D: Loss of DHNA-CoA synthase activity.
- S161 (≠ L141) binding in other chain
- W184 (≠ V164) mutation to F: Reduces the specific DHNA-CoA synthase activity by 530-fold, whereas its affinity for hydrogencarbonate is reduced by 20-fold.
- Y258 (≠ L239) binding
- R267 (≠ C248) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- F270 (= F251) mutation to A: Strongly decreases affinity for substrate and DHNA-CoA synthase activity.
- K273 (= K254) binding ; mutation to A: Impairs protein folding.
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
36% identity, 96% coverage: 10:260/262 of query aligns to 26:275/281 of 3t88A
- active site: G82 (= G67), R87 (= R75), Y93 (= Y81), H101 (= H89), L105 (vs. gap), G129 (= G113), V132 (≠ E116), G152 (≠ E136), S157 (≠ L141), D159 (≠ P143), G160 (= G144), A246 (= A229), Y254 (≠ L239)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ T24), V40 (≠ T25), R41 (≠ L26), A43 (= A28), S80 (≠ A65), G81 (= G66), G82 (= G67), D83 (= D68), Q84 (≠ L72), K85 (≠ D73), Y93 (= Y81), V104 (vs. gap), L105 (vs. gap), Y125 (≠ W109), G129 (= G113), T151 (≠ P135), V155 (≠ L139), F158 (= F142), D159 (≠ P143), T250 (≠ A233), Y254 (≠ L239), F266 (= F251), K269 (= K254)
Query Sequence
>AZOBR_RS26485 AZOBR_RS26485 enoyl-CoA hydratase
MTDERPILTSRDGAVGLITINRPTTLNALDVPTLLELERALGELESDDGVHVIVVTGAGE
RAFVAGGDIADLDSRQGLAHYLDFAEVVHRVFRRFETCDKPTIAAVNGWALGGGTELVLS
LDIRIAADTAKFGLPEINLGLFPGAGGTQRILRQIPPCRARELVFTGDQFTAAEAVAWGL
VNRAVPKADLMAEAMATAQKIAAKSPLILKLTKRTLRHGAEMPLGASLAYEQAMIGLVLD
SQDAHEGCRAFLEKRKAAFTGQ
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