SitesBLAST
Comparing AO353_03780 AO353_03780 enoyl-CoA hydratase 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)
7borA Structure of pseudomonas aeruginosa coa-bound odaa (see paper)
67% identity, 98% coverage: 5:248/249 of query aligns to 4:247/247 of 7borA
- active site: N63 (= N64), F68 (= F69), D77 (≠ T78), G81 (≠ F82), I105 (= I106), T108 (= T109), F128 (= F129), L133 (= L134), P135 (= P136), E136 (= E137), A222 (≠ E223), L232 (= L233)
- binding coenzyme a: D21 (= D22), K22 (= K23), K23 (= K24), A25 (= A26), S61 (≠ A62), N63 (= N64), D64 (= D65), I65 (= I66), P101 (≠ A102), V103 (= V104), P127 (= P128), F128 (= F129), L131 (= L132), F244 (= F245), M245 (≠ I246), R247 (= R248)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 85% coverage: 5:215/249 of query aligns to 5:202/257 of 6slbAAA
- active site: Q64 (≠ N64), F69 (= F69), L80 (≠ V81), N84 (≠ M85), A108 (≠ I106), S111 (≠ T109), A130 (≠ P128), F131 (= F129), L136 (= L134), P138 (= P136), D139 (≠ E137)
- 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: L24 (≠ K24), A26 (= A26), R58 (≠ E58), A62 (= A62), G63 (= G63), Q64 (≠ N64), D65 (= D65), L66 (≠ I66), Y76 (≠ L77), H79 (≠ P80), Y83 (≠ F84), V104 (≠ A102), A106 (≠ V104), G107 (= G105), A108 (≠ I106), A130 (≠ P128), F131 (= F129), I134 (≠ L132), D139 (≠ E137)
Sites not aligning to the query:
3q0jA Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
31% identity, 98% coverage: 5:248/249 of query aligns to 6:249/255 of 3q0jA
- active site: A65 (≠ N64), M70 (≠ F69), T80 (= T78), F84 (= F82), G108 (≠ I106), E111 (≠ T109), P130 (= P128), E131 (≠ F129), V136 (≠ L134), P138 (= P136), G139 (≠ E137), L224 (≠ E223), F234 (≠ L233)
- binding acetoacetyl-coenzyme a: F246 (= F245), K249 (≠ R248)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
31% identity, 98% coverage: 5:248/249 of query aligns to 6:249/255 of 3q0gC
- active site: A65 (≠ N64), M70 (≠ F69), T80 (= T78), F84 (= F82), G108 (≠ I106), E111 (≠ T109), P130 (= P128), E131 (≠ F129), V136 (≠ L134), P138 (= P136), G139 (≠ E137), L224 (≠ E223), F234 (≠ L233)
- binding coenzyme a: A24 (≠ K23), L25 (≠ K24), A27 (= A26), A63 (= A62), A65 (≠ N64), D66 (= D65), I67 (= I66), K68 (≠ A67), Y104 (≠ A102), P130 (= P128), E131 (≠ F129), L134 (= L132)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
31% identity, 98% coverage: 5:248/249 of query aligns to 5:248/256 of 3h81A
- active site: A64 (≠ N64), M69 (≠ F69), T79 (= T78), F83 (= F82), G107 (≠ I106), E110 (≠ T109), P129 (= P128), E130 (≠ F129), V135 (≠ L134), P137 (= P136), G138 (≠ E137), L223 (≠ E223), F233 (≠ L233)
- binding calcium ion: R171 (≠ A170), S172 (≠ W171), F233 (≠ L233), Q238 (≠ A238)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
31% identity, 98% coverage: 5:248/249 of query aligns to 5:244/250 of 3q0gD
- active site: A64 (≠ N64), M69 (≠ F69), T75 (= T78), F79 (= F82), G103 (≠ I106), E106 (≠ T109), P125 (= P128), E126 (≠ F129), V131 (≠ L134), P133 (= P136), G134 (≠ E137), L219 (≠ E223), F229 (≠ L233)
- binding Butyryl Coenzyme A: F225 (= F229), F241 (= F245), K244 (≠ R248)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
35% identity, 70% coverage: 5:179/249 of query aligns to 6:183/259 of 5zaiC
- active site: A65 (≠ N64), F70 (= F69), S82 (≠ T78), R86 (≠ F82), G110 (≠ I106), E113 (≠ T109), P132 (= P128), E133 (≠ F129), I138 (≠ L134), P140 (= P136), G141 (≠ E137)
- binding coenzyme a: D23 (= D22), K24 (= K23), L25 (≠ K24), A27 (= A26), A63 (= A62), G64 (= G63), A65 (≠ N64), D66 (= D65), I67 (= I66), L108 (≠ V104), G109 (= G105), P132 (= P128), E133 (≠ F129), R166 (≠ G162)
Sites not aligning to the query:
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 85% coverage: 5:215/249 of query aligns to 2:190/245 of 6slaAAA
- active site: Q61 (≠ N64), L68 (≠ S75), N72 (≠ S79), A96 (≠ I106), S99 (≠ T109), A118 (≠ P128), F119 (= F129), L124 (= L134), P126 (= P136), N127 (≠ E137)
- 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: K20 (= K23), L21 (≠ K24), A23 (= A26), R55 (≠ E58), A59 (= A62), G60 (= G63), Q61 (≠ N64), D62 (= D65), L63 (= L70), L68 (≠ S75), Y71 (≠ T78), V92 (≠ A102), A94 (≠ V104), G95 (= G105), A96 (≠ I106), A118 (≠ P128), F119 (= F129), I122 (≠ L132), L124 (= L134), N127 (≠ E137)
Sites not aligning to the query:
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
28% identity, 80% coverage: 10:207/249 of query aligns to 63:275/327 of Q62651
- D176 (≠ T109) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (≠ F129) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (≠ E137) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
29% identity, 94% coverage: 16:248/249 of query aligns to 20:252/260 of 1dubA
- active site: A68 (≠ N64), M73 (≠ F69), S83 (= S79), L87 (vs. gap), G111 (≠ I106), E114 (≠ T109), P133 (= P128), E134 (≠ F129), T139 (≠ L134), P141 (= P136), G142 (≠ E137), K227 (≠ E223), F237 (≠ L233)
- binding acetoacetyl-coenzyme a: K26 (≠ D22), A27 (≠ K23), L28 (≠ K24), A30 (= A26), K62 (≠ E58), A66 (= A62), G67 (= G63), A68 (≠ N64), D69 (= D65), I70 (= I66), K71 (≠ A67), M73 (≠ F69), Y107 (≠ A102), L109 (≠ V104), G110 (= G105), G111 (≠ I106), E114 (≠ T109), P133 (= P128), E134 (≠ F129), L137 (= L132), G142 (≠ E137), F233 (= F229), F249 (= F245), K252 (≠ R248)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
29% identity, 94% coverage: 16:248/249 of query aligns to 18:250/258 of 1ey3A
- active site: A66 (≠ N64), M71 (≠ F69), S81 (= S79), L85 (vs. gap), G109 (≠ I106), E112 (≠ T109), P131 (= P128), E132 (≠ F129), T137 (≠ L134), P139 (= P136), G140 (≠ E137), K225 (≠ E223), F235 (≠ L233)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ D22), A25 (≠ K23), L26 (≠ K24), A28 (= A26), A64 (= A62), G65 (= G63), A66 (≠ N64), D67 (= D65), I68 (= I66), K69 (≠ A67), L85 (vs. gap), W88 (≠ M85), Y105 (≠ A102), L107 (≠ V104), G108 (= G105), G109 (≠ I106), P131 (= P128), E132 (≠ F129), L135 (= L132), G140 (≠ E137), A141 (≠ F138), R165 (≠ G162), F231 (= F229), F247 (= F245), K250 (≠ R248)
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)
29% identity, 94% coverage: 16:248/249 of query aligns to 50:282/290 of P14604
- E144 (≠ T109) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ F129) 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
28% identity, 94% coverage: 16:248/249 of query aligns to 20:252/260 of 2hw5C
- active site: A68 (≠ N64), M73 (≠ F69), S83 (= S79), L87 (vs. gap), G111 (≠ I106), E114 (≠ T109), P133 (= P128), E134 (≠ F129), T139 (≠ L134), P141 (= P136), G142 (≠ E137), K227 (≠ E223), F237 (≠ L233)
- binding crotonyl coenzyme a: K26 (≠ D22), A27 (≠ K23), L28 (≠ K24), A30 (= A26), K62 (≠ E58), A66 (= A62), A68 (≠ N64), D69 (= D65), I70 (= I66), K71 (≠ A67), Y107 (≠ A102), F109 (≠ V104)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
28% identity, 94% coverage: 16:248/249 of query aligns to 20:250/258 of 1mj3A
- active site: A68 (≠ N64), M73 (≠ F69), S83 (= S79), L85 (≠ V81), G109 (≠ I106), E112 (≠ T109), P131 (= P128), E132 (≠ F129), T137 (≠ L134), P139 (= P136), G140 (≠ E137), K225 (≠ E223), F235 (≠ L233)
- binding hexanoyl-coenzyme a: K26 (≠ D22), A27 (≠ K23), L28 (≠ K24), A30 (= A26), K62 (≠ E58), A66 (= A62), G67 (= G63), A68 (≠ N64), D69 (= D65), I70 (= I66), K71 (≠ A67), M73 (≠ F69), W88 (≠ F84), Y105 (≠ A102), L107 (≠ V104), G108 (= G105), G109 (≠ I106), E112 (≠ T109), P131 (= P128), E132 (≠ F129), L135 (= L132), G140 (≠ E137), A141 (≠ F138), F231 (= F229), F247 (= F245), K250 (≠ R248)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
29% identity, 94% coverage: 16:248/249 of query aligns to 19:246/254 of 2dubA
- active site: A67 (≠ N64), M72 (≠ F69), S82 (= S79), G105 (≠ I106), E108 (≠ T109), P127 (= P128), E128 (≠ F129), T133 (≠ L134), P135 (= P136), G136 (≠ E137), K221 (≠ E223), F231 (≠ L233)
- binding octanoyl-coenzyme a: K25 (≠ D22), A26 (≠ K23), L27 (≠ K24), A29 (= A26), K61 (≠ E58), A65 (= A62), G66 (= G63), A67 (≠ N64), D68 (= D65), I69 (= I66), K70 (≠ A67), Y101 (≠ A102), G104 (= G105), G105 (≠ I106), E108 (≠ T109), P127 (= P128), E128 (≠ F129), L131 (= L132), P135 (= P136), G136 (≠ E137), A137 (≠ F138)
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)
31% identity, 79% coverage: 13:208/249 of query aligns to 21:218/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
Q9Y232 Chromodomain Y-like protein; CDY-like; Crotonyl-CoA hydratase; EC 4.2.1.- from Homo sapiens (Human) (see 5 papers)
24% identity, 98% coverage: 5:248/249 of query aligns to 344:593/598 of Q9Y232
- S521 (≠ T175) mutation to A: Abolishes CoA-binding and ability to inhibit histone crotonylation.
Sites not aligning to the query:
- 2 T → A: in dbSNP:rs3812179
- 9 S → P: in dbSNP:rs3812178
- 48 V → A: in dbSNP:rs13196069
- 60 A → G: in dbSNP:rs28360500
- 61:309 Interaction with EZH2
- 135 modified: N6,N6,N6-trimethyllysine; by EHMT2; alternate; modified: N6,N6-dimethyllysine; by EHMT2; alternate; modified: N6-methyllysine; by EHMT2; alternate
- 205 S→A: No impact on recruitment to DNA double strand breaks.
Q9WTK2 Chromodomain Y-like protein; CDY-like; Crotonyl-CoA hydratase; Putative histone acetyltransferase Cdyl; EC 4.2.1.-; EC 2.3.1.48 from Mus musculus (Mouse) (see paper)
24% identity, 98% coverage: 5:248/249 of query aligns to 339:588/593 of Q9WTK2