SitesBLAST
Comparing PfGW456L13_3427 Enoyl-CoA hydratase (EC 4.2.1.17) to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
40% identity, 95% coverage: 15:272/272 of query aligns to 4:259/259 of 5zaiC
- active site: A65 (= A77), F70 (vs. gap), S82 (≠ R92), R86 (≠ E96), G110 (= G122), E113 (= E125), P132 (= P144), E133 (= E145), I138 (≠ L150), P140 (= P152), G141 (= G153), A226 (≠ D239), F236 (≠ A249)
- binding coenzyme a: K24 (≠ Q35), L25 (≠ I36), A63 (= A75), G64 (= G76), A65 (= A77), D66 (= D78), I67 (= I79), P132 (= P144), R166 (= R178), F248 (= F261), K251 (≠ R264)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
41% identity, 92% coverage: 21:269/272 of query aligns to 13:257/260 of 2hw5C
- active site: A68 (= A77), M73 (≠ R82), S83 (≠ R94), L87 (≠ V98), G111 (= G122), E114 (= E125), P133 (= P144), E134 (= E145), T139 (≠ L150), P141 (= P152), G142 (= G153), K227 (≠ D239), F237 (≠ A249)
- binding crotonyl coenzyme a: K26 (≠ R34), A27 (≠ Q35), L28 (≠ I36), A30 (= A38), K62 (≠ R71), I70 (= I79), F109 (≠ M120)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
40% identity, 92% coverage: 21:269/272 of query aligns to 13:257/260 of 1dubA
- active site: A68 (= A77), M73 (≠ R82), S83 (≠ N97), L87 (≠ I101), G111 (= G122), E114 (= E125), P133 (= P144), E134 (= E145), T139 (≠ L150), P141 (= P152), G142 (= G153), K227 (≠ D239), F237 (≠ A249)
- binding acetoacetyl-coenzyme a: K26 (≠ R34), A27 (≠ Q35), L28 (≠ I36), A30 (= A38), A66 (= A75), A68 (= A77), D69 (= D78), I70 (= I79), Y107 (= Y118), G110 (= G121), G111 (= G122), E114 (= E125), P133 (= P144), E134 (= E145), L137 (= L148), G142 (= G153), F233 (= F245), F249 (= F261)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
41% identity, 92% coverage: 21:269/272 of query aligns to 12:251/254 of 2dubA
- active site: A67 (= A77), M72 (≠ L89), S82 (≠ R99), G105 (= G122), E108 (= E125), P127 (= P144), E128 (= E145), T133 (≠ L150), P135 (= P152), G136 (= G153), K221 (≠ D239), F231 (≠ A249)
- binding octanoyl-coenzyme a: K25 (≠ R34), A26 (≠ Q35), L27 (≠ I36), A29 (= A38), A65 (= A75), A67 (= A77), D68 (= D78), I69 (= I79), K70 (= K80), G105 (= G122), E108 (= E125), P127 (= P144), E128 (= E145), G136 (= G153), A137 (≠ G154)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
41% identity, 92% coverage: 21:269/272 of query aligns to 13:255/258 of 1mj3A
- active site: A68 (= A77), M73 (≠ L89), S83 (≠ R99), L85 (≠ I101), G109 (= G122), E112 (= E125), P131 (= P144), E132 (= E145), T137 (≠ L150), P139 (= P152), G140 (= G153), K225 (≠ D239), F235 (≠ A249)
- binding hexanoyl-coenzyme a: K26 (≠ R34), A27 (≠ Q35), L28 (≠ I36), A30 (= A38), A66 (= A75), G67 (= G76), A68 (= A77), D69 (= D78), I70 (= I79), G109 (= G122), P131 (= P144), E132 (= E145), L135 (= L148), G140 (= G153)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
40% identity, 92% coverage: 21:269/272 of query aligns to 11:255/258 of 1ey3A
- active site: A66 (= A77), M71 (≠ R82), S81 (≠ N97), L85 (≠ I101), G109 (= G122), E112 (= E125), P131 (= P144), E132 (= E145), T137 (≠ L150), P139 (= P152), G140 (= G153), K225 (≠ D239), F235 (≠ A249)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ R34), L26 (≠ I36), A28 (= A38), A64 (= A75), G65 (= G76), A66 (= A77), D67 (= D78), I68 (= I79), L85 (≠ I101), W88 (≠ L104), G109 (= G122), P131 (= P144), L135 (= L148), G140 (= G153)
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)
40% identity, 92% coverage: 21:269/272 of query aligns to 43:287/290 of P14604
- E144 (= E125) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E145) 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
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
39% identity, 94% coverage: 15:270/272 of query aligns to 3:250/250 of 3q0gD
- active site: A64 (= A77), M69 (≠ R82), T75 (≠ S88), F79 (≠ R92), G103 (= G122), E106 (= E125), P125 (= P144), E126 (= E145), V131 (≠ L150), P133 (= P152), G134 (= G153), L219 (≠ D239), F229 (≠ A249)
- binding Butyryl Coenzyme A: F225 (= F245), F241 (= F261)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
38% identity, 95% coverage: 12:270/272 of query aligns to 1:255/255 of 3q0jC
- active site: A65 (= A77), M70 (≠ R82), T80 (≠ R94), F84 (≠ V98), G108 (= G122), E111 (= E125), P130 (= P144), E131 (= E145), V136 (≠ L150), P138 (= P152), G139 (= G153), L224 (≠ D239), F234 (≠ A249)
- binding acetoacetyl-coenzyme a: Q23 (≠ R34), A24 (≠ Q35), L25 (≠ I36), A27 (= A38), A63 (= A75), G64 (= G76), A65 (= A77), D66 (= D78), I67 (= I79), K68 (= K80), M70 (≠ R82), F84 (≠ V98), G107 (= G121), G108 (= G122), E111 (= E125), P130 (= P144), E131 (= E145), P138 (= P152), G139 (= G153), M140 (≠ G154)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
38% identity, 95% coverage: 12:270/272 of query aligns to 1:255/255 of 3q0gC
- active site: A65 (= A77), M70 (≠ R82), T80 (≠ R94), F84 (≠ V98), G108 (= G122), E111 (= E125), P130 (= P144), E131 (= E145), V136 (≠ L150), P138 (= P152), G139 (= G153), L224 (≠ D239), F234 (≠ A249)
- binding coenzyme a: L25 (≠ I36), A63 (= A75), I67 (= I79), K68 (= K80), Y104 (= Y118), P130 (= P144), E131 (= E145), L134 (= L148)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
39% identity, 94% coverage: 15:270/272 of query aligns to 3:254/256 of 3h81A
- active site: A64 (= A77), M69 (≠ R82), T79 (≠ R94), F83 (≠ V98), G107 (= G122), E110 (= E125), P129 (= P144), E130 (= E145), V135 (≠ L150), P137 (= P152), G138 (= G153), L223 (≠ D239), F233 (≠ A249)
- binding calcium ion: F233 (≠ A249), Q238 (≠ A254)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
39% identity, 90% coverage: 27:271/272 of query aligns to 18:260/261 of 5jbxB
- active site: A67 (= A77), R72 (= R82), L84 (≠ M95), R88 (= R99), G112 (= G122), E115 (= E125), T134 (≠ P144), E135 (= E145), I140 (≠ L150), P142 (= P152), G143 (= G153), A228 (≠ D239), L238 (≠ A249)
- binding coenzyme a: S24 (≠ P33), R25 (= R34), R26 (≠ Q35), A28 (= A38), A65 (= A75), D68 (= D78), L69 (≠ I79), K70 (= K80), L110 (≠ M120), G111 (= G121), T134 (≠ P144), E135 (= E145), L138 (= L148), R168 (= R178)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 93% coverage: 20:271/272 of query aligns to 8:256/257 of 6slbAAA
- active site: Q64 (≠ A77), F69 (vs. gap), L80 (≠ V91), N84 (≠ M95), A108 (≠ G122), S111 (≠ E125), A130 (≠ P144), F131 (≠ E145), L136 (= L150), P138 (= P152), D139 (≠ G153), A224 (≠ D239), G234 (≠ A249)
- 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 (= R71), A62 (= A75), Q64 (≠ A77), D65 (= D78), L66 (≠ I79), Y76 (≠ S87), A108 (≠ G122), F131 (≠ E145), D139 (≠ G153)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 93% coverage: 20:271/272 of query aligns to 5:244/245 of 6slaAAA
- active site: Q61 (≠ A77), L68 (≠ Q93), N72 (= N97), A96 (≠ G122), S99 (≠ E125), A118 (≠ P144), F119 (≠ E145), L124 (= L150), P126 (= P152), N127 (≠ G153), A212 (≠ D239), G222 (≠ A249)
- 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 (≠ I36), A59 (= A75), Q61 (≠ A77), D62 (= D78), L63 (≠ I79), L68 (≠ Q93), Y71 (≠ E96), A94 (≠ M120), G95 (= G121), A96 (≠ G122), F119 (≠ E145), I122 (≠ L148), L124 (= L150), N127 (≠ G153), F234 (= F261), K237 (≠ R264)
Q13825 Methylglutaconyl-CoA hydratase, mitochondrial; 3-MG-CoA hydratase; AU-specific RNA-binding enoyl-CoA hydratase; AU-binding protein/enoyl-CoA hydratase; Itaconyl-CoA hydratase; EC 4.2.1.18; EC 4.2.1.56 from Homo sapiens (Human) (see 4 papers)
37% identity, 91% coverage: 26:272/272 of query aligns to 88:339/339 of Q13825
- K105 (≠ D41) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 (vs. 41:55, 13% identical) RNA-binding
- K109 (≠ Q45) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ Q49) mutation to Q: Abolishes RNA-binding; when associated with N-105 and E-109.
- A240 (≠ G176) to V: in MGCA1; decreased methylglutaconyl-CoA hydratase activity; dbSNP:rs769894315
Sites not aligning to the query:
- 1:67 modified: transit peptide, Mitochondrion
6p5uE Structure of an enoyl-coa hydratase/aldolase isolated from a lignin- degrading consortium (see paper)
34% identity, 80% coverage: 17:233/272 of query aligns to 8:227/246 of 6p5uE
- active site: M67 (≠ A77), Y72 (≠ R82), D77 (≠ E86), R89 (≠ Q93), A93 (≠ N97), G117 (= G122), T120 (≠ E125), E140 (= E145), I145 (≠ L150), P147 (= P152), A148 (≠ G153)
- binding coenzyme a: D25 (≠ R34), K26 (≠ Q35), R27 (≠ I36), A29 (= A38), A65 (= A75), M67 (≠ A77), D68 (= D78), L69 (≠ I79), W113 (≠ Y118), F115 (≠ M120), S139 (≠ P144), W143 (≠ L148)
Sites not aligning to the query:
7xwvA Feruloyl-coa hydratase/lyase complexed with vanillin and coenzyme a (see paper)
32% identity, 85% coverage: 15:244/272 of query aligns to 5:236/244 of 7xwvA
- binding coenzyme a: T24 (≠ R34), K25 (≠ Q35), R26 (≠ I36), A64 (= A75), G65 (= G76), M66 (≠ A77), D67 (= D78), L68 (≠ I79), W111 (≠ Y118), F113 (≠ M120), G114 (= G121), G115 (= G122), S137 (≠ P144)
- binding 4-hydroxy-3-methoxybenzaldehyde: M66 (≠ A77), Y71 (≠ R82), F72 (vs. gap), E138 (= E145), G146 (= G153), G147 (= G154)
7xwtB Crystal structure of feruoyl-coa hydratase/lyase complexed with coa from sphingomonas paucimobilis (see paper)
32% identity, 83% coverage: 15:240/272 of query aligns to 6:233/277 of 7xwtB
- binding acetyl coenzyme *a: T25 (≠ R34), K26 (≠ Q35), R27 (≠ I36), A29 (= A38), A65 (= A75), G66 (= G76), M67 (≠ A77), D68 (= D78), L69 (≠ I79), F73 (vs. gap), F114 (≠ M120), G116 (= G122), S138 (≠ P144), W142 (≠ L148)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
31% identity, 92% coverage: 19:269/272 of query aligns to 12:263/266 of O53561
- K135 (≠ V140) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 140:147, 25% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ G147) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
40% identity, 58% coverage: 25:183/272 of query aligns to 10:162/692 of 6iunB
Sites not aligning to the query:
- active site: 248, 407, 428, 440, 478
- binding nicotinamide-adenine-dinucleotide: 300, 301, 302, 321, 322, 365, 377, 378, 380, 384, 388, 405, 407
Query Sequence
>PfGW456L13_3427 Enoyl-CoA hydratase (EC 4.2.1.17)
MSTAQNQQPPVLINDAVRLERDAMVGWVVLTRPRQINAINDEIRQGVPQALALLQQDPDI
RVIVIRGEGDRGFCAGADIKERRGPESSLQVRQRMENVRWIETLDGITKPVIAAIHGYCM
GGGLELVLACDIRFAAPDAVFALPETGLGLIPGGGGTQRLSRVVAPGQALDMLLTGDRVG
AEQAQRIGLVSRLASDSANLVQEVRAFAQRIASKPPTASAFVKQAARAALEMDLKRGLDL
ELDLFALLAPTKDAREAAQAFSERREPRFTGE
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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