SitesBLAST
Comparing 15515 b1393 enoyl-CoA hydratase-isomerase (NCBI) 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)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
48% identity, 96% coverage: 8:253/255 of query aligns to 13:258/260 of 1dubA
- active site: A68 (= A63), M73 (= M68), S83 (≠ N78), L87 (≠ P82), G111 (≠ A106), E114 (= E109), P133 (= P128), E134 (= E129), T139 (≠ I134), P141 (= P136), G142 (= G137), K227 (≠ A222), F237 (≠ A232)
- binding acetoacetyl-coenzyme a: K26 (≠ A21), A27 (= A22), L28 (≠ R23), A30 (= A25), A66 (= A61), A68 (= A63), D69 (= D64), I70 (≠ L65), Y107 (= Y102), G110 (= G105), G111 (≠ A106), E114 (= E109), P133 (= P128), E134 (= E129), L137 (= L132), G142 (= G137), F233 (= F228), F249 (= F244)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
48% identity, 96% coverage: 8:253/255 of query aligns to 11:256/258 of 1ey3A
- active site: A66 (= A63), M71 (= M68), S81 (≠ N78), L85 (≠ P82), G109 (≠ A106), E112 (= E109), P131 (= P128), E132 (= E129), T137 (≠ I134), P139 (= P136), G140 (= G137), K225 (≠ A222), F235 (≠ A232)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ A21), L26 (≠ R23), A28 (= A25), A64 (= A61), G65 (= G62), A66 (= A63), D67 (= D64), I68 (≠ L65), L85 (≠ P82), W88 (= W85), G109 (≠ A106), P131 (= P128), L135 (= L132), G140 (= G137)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
49% identity, 96% coverage: 8:253/255 of query aligns to 13:256/258 of 1mj3A
- active site: A68 (= A63), M73 (= M68), S83 (≠ P82), L85 (= L84), G109 (≠ A106), E112 (= E109), P131 (= P128), E132 (= E129), T137 (≠ I134), P139 (= P136), G140 (= G137), K225 (≠ A222), F235 (≠ A232)
- binding hexanoyl-coenzyme a: K26 (≠ A21), A27 (= A22), L28 (≠ R23), A30 (= A25), A66 (= A61), G67 (= G62), A68 (= A63), D69 (= D64), I70 (≠ L65), G109 (≠ A106), P131 (= P128), E132 (= E129), L135 (= L132), G140 (= G137)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
49% identity, 96% coverage: 8:253/255 of query aligns to 12:252/254 of 2dubA
- active site: A67 (= A63), M72 (= M68), S82 (≠ P82), G105 (≠ A106), E108 (= E109), P127 (= P128), E128 (= E129), T133 (≠ I134), P135 (= P136), G136 (= G137), K221 (≠ A222), F231 (≠ A232)
- binding octanoyl-coenzyme a: K25 (≠ A21), A26 (= A22), L27 (≠ R23), A29 (= A25), A65 (= A61), A67 (= A63), D68 (= D64), I69 (≠ L65), K70 (≠ N66), G105 (≠ A106), E108 (= E109), P127 (= P128), E128 (= E129), G136 (= G137), A137 (= A138)
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)
48% identity, 96% coverage: 8:253/255 of query aligns to 43:288/290 of P14604
- E144 (= E109) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E129) 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
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
46% identity, 99% coverage: 4:255/255 of query aligns to 5:256/256 of 3h81A
- active site: A64 (= A63), M69 (= M68), T79 (≠ N78), F83 (≠ P82), G107 (≠ A106), E110 (= E109), P129 (= P128), E130 (= E129), V135 (≠ I134), P137 (= P136), G138 (= G137), L223 (≠ A222), F233 (≠ A232)
- binding calcium ion: F233 (≠ A232), Q238 (≠ R237)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
46% identity, 98% coverage: 4:252/255 of query aligns to 6:254/255 of 3q0jC
- active site: A65 (= A63), M70 (= M68), T80 (≠ N78), F84 (≠ P82), G108 (≠ A106), E111 (= E109), P130 (= P128), E131 (= E129), V136 (≠ I134), P138 (= P136), G139 (= G137), L224 (≠ A222), F234 (≠ A232)
- binding acetoacetyl-coenzyme a: Q23 (≠ A21), A24 (= A22), L25 (≠ R23), A27 (= A25), A63 (= A61), G64 (= G62), A65 (= A63), D66 (= D64), I67 (≠ L65), K68 (≠ N66), M70 (= M68), F84 (≠ P82), G107 (= G105), G108 (≠ A106), E111 (= E109), P130 (= P128), E131 (= E129), P138 (= P136), G139 (= G137), M140 (≠ A138)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
46% identity, 98% coverage: 4:252/255 of query aligns to 6:254/255 of 3q0gC
- active site: A65 (= A63), M70 (= M68), T80 (≠ N78), F84 (≠ P82), G108 (≠ A106), E111 (= E109), P130 (= P128), E131 (= E129), V136 (≠ I134), P138 (= P136), G139 (= G137), L224 (≠ A222), F234 (≠ A232)
- binding coenzyme a: L25 (≠ R23), A63 (= A61), I67 (≠ L65), K68 (≠ N66), Y104 (= Y102), P130 (= P128), E131 (= E129), L134 (= L132)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
46% identity, 96% coverage: 8:253/255 of query aligns to 13:258/260 of 2hw5C
- active site: A68 (= A63), M73 (= M68), S83 (≠ N78), L87 (≠ P82), G111 (≠ A106), E114 (= E109), P133 (= P128), E134 (= E129), T139 (≠ I134), P141 (= P136), G142 (= G137), K227 (≠ A222), F237 (≠ A232)
- binding crotonyl coenzyme a: K26 (≠ A21), A27 (= A22), L28 (≠ R23), A30 (= A25), K62 (≠ R57), I70 (≠ L65), F109 (≠ L104)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
46% identity, 98% coverage: 4:252/255 of query aligns to 5:249/250 of 3q0gD
- active site: A64 (= A63), M69 (= M68), T75 (≠ A74), F79 (≠ N78), G103 (≠ A106), E106 (= E109), P125 (= P128), E126 (= E129), V131 (≠ I134), P133 (= P136), G134 (= G137), L219 (≠ A222), F229 (≠ A232)
- binding Butyryl Coenzyme A: F225 (= F228), F241 (= F244)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
41% identity, 98% coverage: 6:255/255 of query aligns to 8:259/259 of 5zaiC
- active site: A65 (= A63), F70 (≠ M68), S82 (≠ T80), R86 (vs. gap), G110 (≠ A106), E113 (= E109), P132 (= P128), E133 (= E129), I138 (= I134), P140 (= P136), G141 (= G137), A226 (= A222), F236 (≠ A232)
- binding coenzyme a: K24 (≠ A22), L25 (≠ R23), A63 (= A61), G64 (= G62), A65 (= A63), D66 (= D64), I67 (≠ L65), P132 (= P128), R166 (≠ S162), F248 (= F244), K251 (= K247)
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)
40% identity, 95% coverage: 11:253/255 of query aligns to 20:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
33% identity, 99% coverage: 3:255/255 of query aligns to 9:266/266 of O53561
- K135 (≠ R124) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 124:131, 38% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ T131) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
38% identity, 100% coverage: 1:255/255 of query aligns to 4:261/261 of 5jbxB
- active site: A67 (= A63), R72 (vs. gap), L84 (= L77), R88 (= R81), G112 (≠ A106), E115 (= E109), T134 (≠ P128), E135 (= E129), I140 (= I134), P142 (= P136), G143 (= G137), A228 (= A222), L238 (≠ A232)
- binding coenzyme a: S24 (≠ A21), R25 (≠ A22), R26 (= R23), A28 (= A25), A65 (= A61), D68 (= D64), L69 (= L65), K70 (≠ N66), L110 (= L104), G111 (= G105), T134 (≠ P128), E135 (= E129), L138 (= L132), R168 (≠ S162)
3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
38% identity, 87% coverage: 4:224/255 of query aligns to 3:210/224 of 3p85A
- active site: L62 (≠ A63), L67 (≠ M68), P68 (= P82), G92 (≠ A106), E95 (= E109), T114 (≠ P128), H115 (≠ E129), L120 (≠ I134), P122 (= P136), T123 (≠ G137), W208 (≠ A222)
- binding calcium ion: D43 (= D44), D45 (≠ S46)
Sites not aligning to the query:
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 99% coverage: 4:255/255 of query aligns to 5:257/257 of 6slbAAA
- active site: Q64 (≠ A63), F69 (≠ M68), L80 (= L88), N84 (= N92), A108 (= A106), S111 (≠ E109), A130 (≠ P128), F131 (≠ E129), L136 (≠ I134), P138 (= P136), D139 (≠ G137), A224 (= A222), G234 (≠ A232)
- 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 (= R57), A62 (= A61), Q64 (≠ A63), D65 (= D64), L66 (= L65), Y76 (≠ L84), A108 (= A106), F131 (≠ E129), D139 (≠ G137)
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)
36% identity, 95% coverage: 12:254/255 of query aligns to 89:338/339 of Q13825
- K105 (≠ N28) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 (vs. 28:42, 20% identical) RNA-binding
- K109 (≠ M32) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ N36) mutation to Q: Abolishes RNA-binding; when associated with N-105 and E-109.
- A240 (≠ G160) to V: in MGCA1; decreased methylglutaconyl-CoA hydratase activity; dbSNP:rs769894315
Sites not aligning to the query:
- 1:67 modified: transit peptide, Mitochondrion
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
36% identity, 99% coverage: 4:255/255 of query aligns to 2:245/245 of 6slaAAA
- active site: Q61 (≠ A63), L68 (= L77), N72 (≠ R81), A96 (= A106), S99 (≠ E109), A118 (≠ P128), F119 (≠ E129), L124 (≠ I134), P126 (= P136), N127 (≠ G137), A212 (= A222), G222 (≠ A232)
- 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 (≠ R23), A59 (= A61), Q61 (≠ A63), D62 (= D64), L63 (= L65), L68 (= L77), Y71 (≠ T80), A94 (≠ L104), G95 (= G105), A96 (= A106), F119 (≠ E129), I122 (≠ L132), L124 (≠ I134), N127 (≠ G137), F234 (= F244), K237 (= K247)
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
30% identity, 96% coverage: 5:248/255 of query aligns to 59:317/327 of Q62651
- D176 (≠ E109) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (= E129) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (≠ G137) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
5ducA Crystal structure of m. Tuberculosis echa6 bound to ligand gsk951a (see paper)
34% identity, 98% coverage: 6:254/255 of query aligns to 5:243/244 of 5ducA
- active site: A61 (= A63), D66 (≠ M68), P73 (≠ N78), I77 (≠ P82), A101 (= A106), Q104 (≠ E109), P123 (= P128), T124 (≠ E129), L129 (≠ I134), L131 (≠ P136), D132 (≠ G137), P211 (≠ A222), W221 (≠ A232)
- binding (5R,7S)-N-(1,3-benzodioxol-5-ylmethyl)-5-(4-ethylphenyl)-7-(trifluoromethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L76 (≠ R81), H80 (≠ W85), D84 (≠ Q89), Q104 (≠ E109), D132 (≠ G137), W134 (≠ G139), F217 (= F228)
Query Sequence
>15515 b1393 enoyl-CoA hydratase-isomerase (NCBI)
MSELIVSRQQRVLLLTLNRPAARNALNNALLMQLVNELEAAATDTSISVCVITGNARFFA
AGADLNEMAEKDLAATLNDTRPQLWARLQAFNKPLIAAVNGYALGAGCELALLCDVVVAG
ENARFGLPEITLGIMPGAGGTQRLIRSVGKSLASKMVLSGESITAQQAQQAGLVSDVFPS
DLTLEYALQLASKMARHSPLALQAAKQALRQSQEVALQAGLAQERQLFTLLAATEDRHEG
ISAFLQKRTPDFKGR
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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