SitesBLAST
Comparing Ga0059261_2668 Ga0059261_2668 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)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
41% identity, 93% coverage: 16:254/256 of query aligns to 17:257/259 of 5zaiC
- active site: A65 (≠ S65), F70 (≠ L70), S82 (≠ R80), R86 (vs. gap), G110 (= G107), E113 (= E110), P132 (= P129), E133 (= E130), I138 (≠ W135), P140 (≠ G137), G141 (= G138), A226 (≠ E223), F236 (= F233)
- binding coenzyme a: K24 (= K23), L25 (= L24), A63 (= A63), G64 (= G64), A65 (≠ S65), D66 (= D66), I67 (= I67), P132 (= P129), R166 (≠ M163), F248 (= F245), K251 (= K248)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
40% identity, 95% coverage: 13:254/256 of query aligns to 16:252/254 of 2dubA
- active site: A67 (≠ S65), M72 (≠ L70), S82 (≠ D84), G105 (= G107), E108 (= E110), P127 (= P129), E128 (= E130), T133 (≠ W135), P135 (≠ G137), G136 (= G138), K221 (≠ E223), F231 (= F233)
- binding octanoyl-coenzyme a: K25 (≠ A22), A26 (≠ K23), L27 (= L24), A29 (= A26), A65 (= A63), A67 (≠ S65), D68 (= D66), I69 (= I67), K70 (≠ T68), G105 (= G107), E108 (= E110), P127 (= P129), E128 (= E130), G136 (= G138), A137 (≠ G139)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
41% identity, 95% coverage: 13:254/256 of query aligns to 17:256/258 of 1mj3A
- active site: A68 (≠ S65), M73 (≠ L70), S83 (≠ N81), L85 (≠ D83), G109 (= G107), E112 (= E110), P131 (= P129), E132 (= E130), T137 (≠ W135), P139 (≠ G137), G140 (= G138), K225 (≠ E223), F235 (= F233)
- binding hexanoyl-coenzyme a: K26 (≠ A22), A27 (≠ K23), L28 (= L24), A30 (= A26), A66 (= A63), G67 (= G64), A68 (≠ S65), D69 (= D66), I70 (= I67), G109 (= G107), P131 (= P129), E132 (= E130), L135 (= L133), G140 (= G138)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
40% identity, 95% coverage: 11:254/256 of query aligns to 15:258/260 of 2hw5C
- active site: A68 (≠ S65), M73 (≠ L70), S83 (≠ R80), L87 (vs. gap), G111 (= G107), E114 (= E110), P133 (= P129), E134 (= E130), T139 (≠ W135), P141 (≠ G137), G142 (= G138), K227 (≠ E223), F237 (= F233)
- binding crotonyl coenzyme a: K26 (≠ A22), A27 (≠ K23), L28 (= L24), A30 (= A26), K62 (= K59), I70 (= I67), F109 (≠ L105)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
39% identity, 95% coverage: 13:254/256 of query aligns to 15:256/258 of 1ey3A
- active site: A66 (≠ S65), M71 (≠ L70), S81 (vs. gap), L85 (≠ A74), G109 (= G107), E112 (= E110), P131 (= P129), E132 (= E130), T137 (≠ W135), P139 (≠ G137), G140 (= G138), K225 (≠ E223), F235 (= F233)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ A22), L26 (= L24), A28 (= A26), A64 (= A63), G65 (= G64), A66 (≠ S65), D67 (= D66), I68 (= I67), L85 (≠ A74), W88 (= W77), G109 (= G107), P131 (= P129), L135 (= L133), G140 (= G138)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
39% identity, 95% coverage: 13:254/256 of query aligns to 17:258/260 of 1dubA
- active site: A68 (≠ S65), M73 (≠ L70), S83 (vs. gap), L87 (≠ A74), G111 (= G107), E114 (= E110), P133 (= P129), E134 (= E130), T139 (≠ W135), P141 (≠ G137), G142 (= G138), K227 (≠ E223), F237 (= F233)
- binding acetoacetyl-coenzyme a: K26 (≠ A22), A27 (≠ K23), L28 (= L24), A30 (= A26), A66 (= A63), A68 (≠ S65), D69 (= D66), I70 (= I67), Y107 (= Y103), G110 (= G106), G111 (= G107), E114 (= E110), P133 (= P129), E134 (= E130), L137 (= L133), G142 (= G138), F233 (≠ Q229), F249 (= F245)
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)
39% identity, 95% coverage: 13:254/256 of query aligns to 47:288/290 of P14604
- E144 (= E110) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E130) 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
41% identity, 95% coverage: 11:253/256 of query aligns to 11:249/250 of 3q0gD
- active site: A64 (≠ S65), M69 (≠ L70), T75 (≠ P76), F79 (≠ R80), G103 (= G107), E106 (= E110), P125 (= P129), E126 (= E130), V131 (≠ W135), P133 (≠ G137), G134 (= G138), L219 (≠ E223), F229 (= F233)
- binding Butyryl Coenzyme A: F225 (≠ Q229), F241 (= F245)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
40% identity, 96% coverage: 11:256/256 of query aligns to 11:256/256 of 3h81A
- active site: A64 (≠ S65), M69 (≠ L70), T79 (≠ N81), F83 (≠ Y85), G107 (= G107), E110 (= E110), P129 (= P129), E130 (= E130), V135 (≠ W135), P137 (≠ G137), G138 (= G138), L223 (≠ E223), F233 (= F233)
- binding calcium ion: F233 (= F233), Q238 (≠ A238)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
40% identity, 99% coverage: 1:253/256 of query aligns to 1:254/255 of 3q0jC
- active site: A65 (≠ S65), M70 (≠ L70), T80 (≠ N81), F84 (≠ Y85), G108 (= G107), E111 (= E110), P130 (= P129), E131 (= E130), V136 (≠ W135), P138 (≠ G137), G139 (= G138), L224 (≠ E223), F234 (= F233)
- binding acetoacetyl-coenzyme a: Q23 (≠ A22), A24 (≠ K23), L25 (= L24), A27 (= A26), A63 (= A63), G64 (= G64), A65 (≠ S65), D66 (= D66), I67 (= I67), K68 (≠ T68), M70 (≠ L70), F84 (≠ Y85), G107 (= G106), G108 (= G107), E111 (= E110), P130 (= P129), E131 (= E130), P138 (≠ G137), G139 (= G138), M140 (≠ G139)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
40% identity, 99% coverage: 1:253/256 of query aligns to 1:254/255 of 3q0gC
- active site: A65 (≠ S65), M70 (≠ L70), T80 (≠ N81), F84 (≠ Y85), G108 (= G107), E111 (= E110), P130 (= P129), E131 (= E130), V136 (≠ W135), P138 (≠ G137), G139 (= G138), L224 (≠ E223), F234 (= F233)
- binding coenzyme a: L25 (= L24), A63 (= A63), I67 (= I67), K68 (≠ T68), Y104 (= Y103), P130 (= P129), E131 (= E130), L134 (= L133)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 96% coverage: 11:256/256 of query aligns to 11:257/257 of 6slbAAA
- active site: Q64 (≠ S65), F69 (≠ L70), L80 (≠ F79), N84 (≠ D83), A108 (≠ G107), S111 (≠ E110), A130 (≠ P129), F131 (≠ E130), L136 (≠ W135), P138 (≠ G137), D139 (≠ G138), A224 (≠ E223), G234 (≠ F233)
- 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 (≠ K59), A62 (= A63), Q64 (≠ S65), D65 (= D66), L66 (≠ I67), Y76 (≠ W77), A108 (≠ G107), F131 (≠ E130), D139 (≠ G138)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 96% coverage: 11:256/256 of query aligns to 8:245/245 of 6slaAAA
- active site: Q61 (≠ S65), L68 (≠ F79), N72 (≠ D83), A96 (≠ G107), S99 (≠ E110), A118 (≠ P129), F119 (≠ E130), L124 (≠ W135), P126 (≠ G137), N127 (≠ G138), A212 (≠ E223), G222 (≠ F233)
- 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 (= L24), A59 (= A63), Q61 (≠ S65), D62 (= D66), L63 (≠ I67), L68 (≠ F79), Y71 (≠ R82), A94 (≠ L105), G95 (= G106), A96 (≠ G107), F119 (≠ E130), I122 (≠ L133), L124 (≠ W135), N127 (≠ G138), F234 (= F245), K237 (= K248)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
35% identity, 99% coverage: 4:256/256 of query aligns to 9:266/266 of O53561
- K135 (≠ R125) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 125:132, 38% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (= K132) 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)
37% identity, 94% coverage: 17:256/256 of query aligns to 19:261/261 of 5jbxB
- active site: A67 (≠ S65), R72 (≠ L70), L84 (≠ R82), R88 (≠ C86), G112 (= G107), E115 (= E110), T134 (≠ P129), E135 (= E130), I140 (≠ W135), P142 (≠ G137), G143 (= G138), A228 (≠ E223), L238 (≠ F233)
- binding coenzyme a: S24 (≠ A22), R25 (≠ K23), R26 (≠ L24), A28 (= A26), A65 (= A63), D68 (= D66), L69 (≠ I67), K70 (≠ T68), L110 (= L105), G111 (= G106), T134 (≠ P129), E135 (= E130), L138 (= L133), R168 (≠ M163)
Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
32% identity, 96% coverage: 11:255/256 of query aligns to 32:280/285 of Q7CQ56
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
32% identity, 96% coverage: 11:255/256 of query aligns to 28:261/266 of 3h02A
- active site: G82 (≠ S65), H86 (≠ T69), L90 (≠ D83), G114 (= G107), V117 (≠ E110), G137 (≠ E130), S142 (≠ W135), D144 (≠ G137), G145 (= G138), A231 (≠ E225), Y239 (≠ F233)
- binding bicarbonate ion: G113 (= G106), Q135 (≠ A128), G137 (≠ E130), W165 (≠ L158)
3t88A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa (see paper)
32% identity, 96% coverage: 11:255/256 of query aligns to 28:276/281 of 3t88A
- active site: G82 (≠ S65), R87 (≠ L70), Y93 (≠ P76), H101 (≠ F79), L105 (≠ D83), G129 (= G107), V132 (≠ E110), G152 (≠ E130), S157 (≠ W135), D159 (≠ G137), G160 (= G138), A246 (≠ E225), Y254 (≠ F233)
- binding o-succinylbenzoyl-N-coenzyme A: Q39 (≠ A22), V40 (≠ K23), R41 (≠ L24), A43 (= A26), S80 (≠ A63), G81 (= G64), G82 (≠ S65), D83 (= D66), Q84 (≠ I67), K85 (≠ T68), Y93 (≠ P76), V104 (≠ R82), L105 (≠ D83), Y125 (= Y103), G129 (= G107), T151 (≠ P129), V155 (≠ L133), F158 (≠ I136), D159 (≠ G137), T250 (≠ Q229), Y254 (≠ F233), F266 (= F245), K269 (= K248)
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
32% identity, 96% coverage: 11:255/256 of query aligns to 29:262/267 of 4elwA
- active site: G83 (≠ S65), L91 (≠ D83), G115 (= G107), V118 (≠ E110), G138 (≠ E130), S143 (≠ W135), D145 (≠ G137), G146 (= G138), A232 (≠ E225), Y240 (≠ F233)
- binding nitrate ion: G114 (= G106), T137 (≠ P129), G138 (≠ E130), F144 (≠ I136), W166 (≠ L158)
4i42A E.Coli. 1,4-dihydroxy-2-naphthoyl coenzyme a synthase (ecmenb) in complex with 1-hydroxy-2-naphthoyl-coa (see paper)
32% identity, 96% coverage: 11:255/256 of query aligns to 32:280/285 of 4i42A
- active site: G86 (≠ S65), R91 (≠ L70), Y97 (≠ P76), H105 (≠ F79), L109 (≠ D83), G133 (= G107), V136 (≠ E110), G156 (≠ E130), S161 (≠ W135), D163 (≠ G137), G164 (= G138), A250 (≠ E225), Y258 (≠ F233)
- binding 1-hydroxy-2-naphthoyl-CoA: V44 (≠ K23), R45 (≠ L24), S84 (≠ A63), G85 (= G64), G86 (≠ S65), D87 (= D66), Q88 (≠ I67), K89 (≠ T68), Y97 (≠ P76), V108 (≠ R82), Y129 (= Y103), G133 (= G107), T155 (≠ P129), S161 (≠ W135), T254 (≠ Q229), F270 (= F245), K273 (= K248)
Query Sequence
>Ga0059261_2668 Ga0059261_2668 Enoyl-CoA hydratase/carnithine racemase
MTDDLLFTVADHVATITLNRPAKLNALTPEMAAALIASVSACNSSDAVRCVVITGAGEKA
FSAGSDITTLDGYATPWDFRNRDDYCDALRACRKPVVAAINGYALGGGLETAMAADIRIA
STNARFAAPEIKLGWIGGGGMAAGLTYSMGASNAALMLFTGDMIDAEKALAWGLVSEVVA
PDALLARAQEIARTIASRAPIAAETAKLNLRAAHTMPWDKAIEYERDLQAICFATDDAKE
GRAAFAEKRAPVFRRR
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