SitesBLAST
Comparing Ga0059261_2840 Ga0059261_2840 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)
42% identity, 96% coverage: 7:259/263 of query aligns to 8:254/257 of 6slbAAA
- active site: Q64 (≠ A64), F69 (= F70), L80 (≠ Q83), N84 (≠ A87), A108 (≠ G111), S111 (≠ A114), A130 (= A133), F131 (≠ N134), L136 (= L139), P138 (≠ A141), D139 (≠ E143), A224 (= A229), G234 (= G239)
- 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 (= A62), Q64 (≠ A64), D65 (= D65), L66 (= L66), Y76 (≠ E77), A108 (≠ G111), F131 (≠ N134), D139 (≠ E143)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
40% identity, 96% coverage: 7:259/263 of query aligns to 5:242/245 of 6slaAAA
- active site: Q61 (≠ A64), L68 (≠ V71), N72 (≠ A87), A96 (≠ G111), S99 (≠ A114), A118 (= A133), F119 (≠ N134), L124 (= L139), P126 (≠ A141), N127 (≠ G142), A212 (= A229), G222 (= G239)
- 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 (≠ M24), A59 (= A62), Q61 (≠ A64), D62 (= D65), L63 (= L66), L68 (≠ V71), Y71 (≠ L86), A94 (= A109), G95 (= G110), A96 (≠ G111), F119 (≠ N134), I122 (≠ L137), L124 (= L139), N127 (≠ G142), F234 (= F251), K237 (= K254)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
37% identity, 96% coverage: 8:259/263 of query aligns to 9:256/259 of 5zaiC
- active site: A65 (= A64), F70 (= F70), S82 (≠ Q83), R86 (≠ A87), G110 (= G111), E113 (≠ A114), P132 (≠ A133), E133 (≠ N134), I138 (≠ L139), P140 (≠ A141), G141 (= G142), A226 (= A229), F236 (≠ G239)
- binding coenzyme a: K24 (≠ R23), L25 (≠ M24), A63 (= A62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (≠ L66), P132 (≠ A133), R166 (≠ K168), F248 (= F251), K251 (= K254)
Q9P4U9 Enoyl-CoA hydratase AKT3-1; AF-toxin biosynthesis protein 3-1; EC 4.2.1.17 from Alternaria alternata (Alternaria rot fungus) (Torula alternata) (see paper)
37% identity, 98% coverage: 2:259/263 of query aligns to 13:268/296 of Q9P4U9
Sites not aligning to the query:
- 294:296 Peroxisomal targeting signal type 1
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, 95% coverage: 13:262/263 of query aligns to 21:268/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
37% identity, 95% coverage: 10:260/263 of query aligns to 10:250/250 of 3q0gD
- active site: A64 (= A64), M69 (≠ D69), T75 (≠ P76), F79 (≠ L80), G103 (= G111), E106 (≠ A114), P125 (≠ A133), E126 (≠ N134), V131 (≠ L139), P133 (≠ A141), G134 (= G142), L219 (≠ A229), F229 (≠ G239)
- binding Butyryl Coenzyme A: F225 (≠ Q235), F241 (= F251)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
37% identity, 95% coverage: 11:259/263 of query aligns to 16:263/266 of O53561
- K135 (≠ H129) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 129:136, 38% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ R136) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
36% identity, 96% coverage: 10:261/263 of query aligns to 10:255/256 of 3h81A
- active site: A64 (= A64), M69 (≠ S73), T79 (≠ Q83), F83 (≠ A87), G107 (= G111), E110 (≠ A114), P129 (≠ A133), E130 (≠ N134), V135 (≠ L139), P137 (≠ A141), G138 (= G142), L223 (≠ A229), F233 (≠ G239)
- binding calcium ion: F233 (≠ G239), Q238 (≠ F244)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
34% identity, 96% coverage: 8:260/263 of query aligns to 9:255/255 of 3q0jC
- active site: A65 (= A64), M70 (vs. gap), T80 (vs. gap), F84 (≠ V71), G108 (= G111), E111 (≠ A114), P130 (≠ A133), E131 (≠ N134), V136 (≠ L139), P138 (≠ A141), G139 (= G142), L224 (≠ A229), F234 (≠ G239)
- binding acetoacetyl-coenzyme a: Q23 (≠ A22), A24 (≠ R23), L25 (≠ M24), A27 (= A26), A63 (= A62), G64 (= G63), A65 (= A64), D66 (= D65), I67 (≠ L66), K68 (= K67), M70 (vs. gap), F84 (≠ V71), G107 (= G110), G108 (= G111), E111 (≠ A114), P130 (≠ A133), E131 (≠ N134), P138 (≠ A141), G139 (= G142), M140 (≠ E143)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
34% identity, 96% coverage: 8:260/263 of query aligns to 9:255/255 of 3q0gC
- active site: A65 (= A64), M70 (vs. gap), T80 (vs. gap), F84 (≠ V71), G108 (= G111), E111 (≠ A114), P130 (≠ A133), E131 (≠ N134), V136 (≠ L139), P138 (≠ A141), G139 (= G142), L224 (≠ A229), F234 (≠ G239)
- binding coenzyme a: L25 (≠ M24), A63 (= A62), I67 (≠ L66), K68 (= K67), Y104 (≠ A107), P130 (≠ A133), E131 (≠ N134), L134 (= L137)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
35% identity, 98% coverage: 1:259/263 of query aligns to 4:258/261 of 5jbxB
- active site: A67 (= A64), R72 (≠ D69), L84 (≠ A81), R88 (= R85), G112 (= G111), E115 (≠ A114), T134 (≠ A133), E135 (≠ N134), I140 (≠ L139), P142 (≠ A141), G143 (= G142), A228 (= A229), L238 (≠ G239)
- binding coenzyme a: S24 (≠ A22), R25 (= R23), R26 (≠ M24), A28 (= A26), A65 (= A62), D68 (= D65), L69 (= L66), K70 (= K67), L110 (≠ A109), G111 (= G110), T134 (≠ A133), E135 (≠ N134), L138 (= L137), R168 (≠ K168)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
32% identity, 92% coverage: 18:259/263 of query aligns to 20:255/258 of 1ey3A
- active site: A66 (= A64), M71 (≠ V71), S81 (≠ A81), L85 (≠ A87), G109 (= G111), E112 (≠ A114), P131 (≠ A133), E132 (≠ N134), T137 (≠ L139), P139 (≠ A141), G140 (= G142), K225 (≠ A229), F235 (≠ G239)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ A22), L26 (≠ M24), A28 (= A26), A64 (= A62), G65 (= G63), A66 (= A64), D67 (= D65), I68 (≠ L66), L85 (≠ A87), W88 (≠ M90), G109 (= G111), P131 (≠ A133), L135 (= L137), G140 (= G142)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
32% identity, 92% coverage: 18:259/263 of query aligns to 22:257/260 of 1dubA
- active site: A68 (= A64), M73 (≠ V71), S83 (≠ A81), L87 (≠ A87), G111 (= G111), E114 (≠ A114), P133 (≠ A133), E134 (≠ N134), T139 (≠ L139), P141 (≠ A141), G142 (= G142), K227 (≠ A229), F237 (≠ G239)
- binding acetoacetyl-coenzyme a: K26 (≠ A22), A27 (≠ R23), L28 (≠ M24), A30 (= A26), A66 (= A62), A68 (= A64), D69 (= D65), I70 (≠ L66), Y107 (≠ A107), G110 (= G110), G111 (= G111), E114 (≠ A114), P133 (≠ A133), E134 (≠ N134), L137 (= L137), G142 (= G142), F233 (≠ Q235), F249 (= F251)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
31% identity, 92% coverage: 18:259/263 of query aligns to 22:257/260 of 2hw5C
- active site: A68 (= A64), M73 (≠ V71), S83 (≠ A81), L87 (≠ A87), G111 (= G111), E114 (≠ A114), P133 (≠ A133), E134 (≠ N134), T139 (≠ L139), P141 (≠ A141), G142 (= G142), K227 (≠ A229), F237 (≠ G239)
- binding crotonyl coenzyme a: K26 (≠ A22), A27 (≠ R23), L28 (≠ M24), A30 (= A26), K62 (≠ R58), I70 (≠ L66), F109 (≠ A109)
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)
32% identity, 92% coverage: 18:259/263 of query aligns to 52:287/290 of P14604
- E144 (≠ A114) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ N134) 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)
32% identity, 92% coverage: 18:259/263 of query aligns to 21:251/254 of 2dubA
- active site: A67 (= A64), M72 (≠ V71), S82 (≠ A81), G105 (= G111), E108 (≠ A114), P127 (≠ A133), E128 (≠ N134), T133 (≠ L139), P135 (≠ A141), G136 (= G142), K221 (≠ A229), F231 (≠ G239)
- binding octanoyl-coenzyme a: K25 (≠ A22), A26 (≠ R23), L27 (≠ M24), A29 (= A26), A65 (= A62), A67 (= A64), D68 (= D65), I69 (≠ L66), K70 (= K67), G105 (= G111), E108 (≠ A114), P127 (≠ A133), E128 (≠ N134), G136 (= G142), A137 (≠ E143)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
32% identity, 92% coverage: 18:259/263 of query aligns to 22:255/258 of 1mj3A
- active site: A68 (= A64), M73 (≠ V71), S83 (≠ A81), L85 (≠ Q83), G109 (= G111), E112 (≠ A114), P131 (≠ A133), E132 (≠ N134), T137 (≠ L139), P139 (≠ A141), G140 (= G142), K225 (≠ A229), F235 (≠ G239)
- binding hexanoyl-coenzyme a: K26 (≠ A22), A27 (≠ R23), L28 (≠ M24), A30 (= A26), A66 (= A62), G67 (= G63), A68 (= A64), D69 (= D65), I70 (≠ L66), G109 (= G111), P131 (≠ A133), E132 (≠ N134), L135 (= L137), G140 (= G142)
4i52A Scmenb im complex with 1-hydroxy-2-naphthoyl-coa (see paper)
32% identity, 95% coverage: 11:261/263 of query aligns to 18:270/275 of 4i52A
- active site: G77 (≠ A64), R82 (vs. gap), Y87 (≠ F70), R95 (≠ E77), L99 (≠ A81), G123 (= G111), V126 (≠ A114), G146 (≠ N134), S151 (≠ L139), D153 (≠ A141), G154 (= G142), A240 (≠ E231), Y248 (≠ G239)
- binding 1-hydroxy-2-naphthoyl-CoA: H29 (≠ A22), K30 (≠ R23), R31 (≠ M24), A33 (= A26), S75 (≠ A62), G76 (= G63), G77 (≠ A64), D78 (= D65), Q79 (≠ L66), L96 (≠ E78), V98 (≠ L80), Y119 (≠ A107), I121 (≠ A109), G123 (= G111), T145 (≠ A133), V149 (≠ L137), S151 (≠ L139), F152 (≠ S140)
4i4zA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with salicylyl-coa (see paper)
32% identity, 95% coverage: 11:261/263 of query aligns to 18:270/275 of 4i4zA
- active site: G77 (≠ A64), R82 (vs. gap), Y87 (≠ F70), R95 (≠ E77), L99 (≠ A81), G123 (= G111), V126 (≠ A114), G146 (≠ N134), S151 (≠ L139), D153 (≠ A141), G154 (= G142), A240 (≠ E231), Y248 (≠ G239)
- binding Salicylyl CoA: H29 (≠ A22), K30 (≠ R23), R31 (≠ M24), S75 (≠ A62), G76 (= G63), G77 (≠ A64), D78 (= D65), Q79 (≠ L66), Y87 (≠ F70), V98 (≠ L80), G123 (= G111), T145 (≠ A133), V149 (≠ L137), S151 (≠ L139), F260 (= F251), K263 (= K254)
- binding bicarbonate ion: G122 (= G110), Q144 (≠ I132), T145 (≠ A133), G146 (≠ N134), W174 (≠ M163)
4izdA Crystal structure of dmdd e121a in complex with mmpa-coa (see paper)
32% identity, 78% coverage: 2:206/263 of query aligns to 9:210/253 of 4izdA
- active site: L70 (≠ A64), H75 (≠ D69), C89 (≠ Q83), H93 (≠ A87), G117 (= G111), A120 (= A114), E140 (≠ N134), G148 (= G142)
- binding 3-methylmercaptopropionate-CoA (MMPA-CoA): D29 (≠ A22), K30 (≠ R23), R31 (≠ M24), A33 (= A26), A68 (= A62), L70 (≠ A64), D71 (= D65), L72 (= L66)
Sites not aligning to the query:
Query Sequence
>Ga0059261_2840 Ga0059261_2840 Enoyl-CoA hydratase/carnithine racemase
MNELQIDRHDGGIVIATINRPARMNAIDRNLIASFEALFDRLDADREARVLILTGAGRAF
CAGADLKSDFVESAGPEESLASQLRLARLMERIANLRQPVIAAVNGAAAGGGFAFTLAAD
IRIAGRSAHFSIANARLGLSAGECGISWLLPRLIGLSRAFELMLTGRKFDAEEAERIGYV
VRTVADDVLLDTALETARLIAANAPFGVAMTKDVVRRNLETASMQAAIALEARTQLLCGG
SGDFREAVSAFLEKRPPDFTRSG
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