SitesBLAST
Comparing CCNA_01891 CCNA_01891 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)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
36% identity, 88% coverage: 32:273/275 of query aligns to 17:258/260 of 1dubA
- active site: A68 (= A82), M73 (vs. gap), S83 (≠ A94), L87 (≠ F98), G111 (≠ A129), E114 (≠ G132), P133 (= P151), E134 (= E152), T139 (≠ L157), P141 (vs. gap), G142 (vs. gap), K227 (≠ R242), F237 (≠ S252)
- binding acetoacetyl-coenzyme a: K26 (≠ P41), A27 (vs. gap), L28 (≠ V42), A30 (≠ S44), A66 (= A80), A68 (= A82), D69 (= D83), I70 (≠ L84), Y107 (≠ A125), G110 (= G128), G111 (≠ A129), E114 (≠ G132), P133 (= P151), E134 (= E152), L137 (≠ V155), G142 (vs. gap), F233 (≠ T248), F249 (= F264)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
36% identity, 88% coverage: 32:273/275 of query aligns to 15:256/258 of 1ey3A
- active site: A66 (= A82), M71 (vs. gap), S81 (≠ A94), L85 (≠ F98), G109 (≠ A129), E112 (≠ G132), P131 (= P151), E132 (= E152), T137 (≠ L157), P139 (vs. gap), G140 (vs. gap), K225 (≠ R242), F235 (≠ S252)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ P41), L26 (≠ V42), A28 (≠ S44), A64 (= A80), G65 (= G81), A66 (= A82), D67 (= D83), I68 (≠ L84), L85 (≠ F98), W88 (= W109), G109 (≠ A129), P131 (= P151), L135 (≠ V155), G140 (vs. gap)
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)
36% identity, 88% coverage: 32:273/275 of query aligns to 47:288/290 of P14604
- E144 (≠ G132) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E152) 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
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
36% identity, 88% coverage: 32:273/275 of query aligns to 17:256/258 of 1mj3A
- active site: A68 (= A82), M73 (vs. gap), S83 (≠ A94), L85 (≠ T96), G109 (≠ A129), E112 (≠ G132), P131 (= P151), E132 (= E152), T137 (≠ L157), P139 (vs. gap), G140 (vs. gap), K225 (≠ R242), F235 (≠ S252)
- binding hexanoyl-coenzyme a: K26 (≠ P41), A27 (vs. gap), L28 (≠ V42), A30 (≠ S44), A66 (= A80), G67 (= G81), A68 (= A82), D69 (= D83), I70 (≠ L84), G109 (≠ A129), P131 (= P151), E132 (= E152), L135 (≠ V155), G140 (vs. gap)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
34% identity, 88% coverage: 35:275/275 of query aligns to 17:259/259 of 5zaiC
- active site: A65 (= A82), F70 (vs. gap), S82 (≠ Q101), R86 (= R105), G110 (≠ A129), E113 (≠ G132), P132 (= P151), E133 (= E152), I138 (≠ L157), P140 (vs. gap), G141 (vs. gap), A226 (≠ R242), F236 (≠ S252)
- binding coenzyme a: K24 (≠ P41), L25 (≠ V42), A63 (= A80), G64 (= G81), A65 (= A82), D66 (= D83), I67 (≠ L84), P132 (= P151), R166 (= R182), F248 (= F264), K251 (= K267)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
36% identity, 88% coverage: 32:273/275 of query aligns to 16:252/254 of 2dubA
- active site: A67 (= A82), M72 (vs. gap), S82 (≠ A94), G105 (≠ A129), E108 (≠ G132), P127 (= P151), E128 (= E152), T133 (≠ L157), P135 (vs. gap), G136 (vs. gap), K221 (≠ R242), F231 (≠ S252)
- binding octanoyl-coenzyme a: K25 (≠ P41), A26 (vs. gap), L27 (≠ V42), A29 (≠ S44), A65 (= A80), A67 (= A82), D68 (= D83), I69 (≠ L84), K70 (= K85), G105 (≠ A129), E108 (≠ G132), P127 (= P151), E128 (= E152), G136 (vs. gap), A137 (= A158)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
36% identity, 88% coverage: 32:273/275 of query aligns to 17:258/260 of 2hw5C
- active site: A68 (= A82), M73 (vs. gap), S83 (≠ A94), L87 (≠ A99), G111 (≠ A129), E114 (≠ G132), P133 (= P151), E134 (= E152), T139 (≠ L157), P141 (vs. gap), G142 (vs. gap), K227 (≠ R242), F237 (≠ S252)
- binding crotonyl coenzyme a: K26 (≠ P41), A27 (≠ V42), L28 (≠ N43), A30 (= A45), K62 (= K76), I70 (≠ L84), F109 (≠ L127)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
33% identity, 91% coverage: 26:275/275 of query aligns to 7:256/256 of 3h81A
- active site: A64 (= A82), M69 (≠ R87), T79 (≠ A99), F83 (≠ M103), G107 (≠ A129), E110 (≠ G132), P129 (= P151), E130 (= E152), V135 (≠ L157), P137 (vs. gap), G138 (vs. gap), L223 (≠ R242), F233 (≠ S252)
- binding calcium ion: F233 (≠ S252), Q238 (≠ A257)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
33% identity, 90% coverage: 26:272/275 of query aligns to 8:254/255 of 3q0jC
- active site: A65 (= A82), M70 (≠ R87), T80 (≠ A99), F84 (≠ M103), G108 (≠ A129), E111 (≠ G132), P130 (= P151), E131 (= E152), V136 (≠ L157), P138 (vs. gap), G139 (vs. gap), L224 (≠ R242), F234 (≠ S252)
- binding acetoacetyl-coenzyme a: Q23 (vs. gap), A24 (≠ P41), L25 (≠ V42), A27 (≠ S44), A63 (= A80), G64 (= G81), A65 (= A82), D66 (= D83), I67 (≠ L84), K68 (= K85), M70 (≠ R87), F84 (≠ M103), G107 (= G128), G108 (≠ A129), E111 (≠ G132), P130 (= P151), E131 (= E152), P138 (vs. gap), G139 (vs. gap), M140 (≠ A158)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 90% coverage: 26:272/275 of query aligns to 8:254/255 of 3q0gC
- active site: A65 (= A82), M70 (≠ R87), T80 (≠ A99), F84 (≠ M103), G108 (≠ A129), E111 (≠ G132), P130 (= P151), E131 (= E152), V136 (≠ L157), P138 (vs. gap), G139 (vs. gap), L224 (≠ R242), F234 (≠ S252)
- binding coenzyme a: L25 (≠ V42), A63 (= A80), I67 (≠ L84), K68 (= K85), Y104 (≠ A125), P130 (= P151), E131 (= E152), L134 (≠ V155)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 90% coverage: 26:272/275 of query aligns to 7:249/250 of 3q0gD
- active site: A64 (= A82), M69 (≠ R87), T75 (≠ A94), F79 (= F98), G103 (≠ A129), E106 (≠ G132), P125 (= P151), E126 (= E152), V131 (≠ L157), P133 (vs. gap), G134 (vs. gap), L219 (≠ R242), F229 (≠ S252)
- binding Butyryl Coenzyme A: F225 (≠ T248), F241 (= F264)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
36% identity, 85% coverage: 43:275/275 of query aligns to 27:261/261 of 5jbxB
- active site: A67 (= A82), R72 (= R87), L84 (vs. gap), R88 (≠ Q101), G112 (≠ A129), E115 (≠ G132), T134 (≠ P151), E135 (= E152), I140 (≠ L157), P142 (vs. gap), G143 (vs. gap), A228 (≠ R242), L238 (≠ S252)
- binding coenzyme a: A28 (≠ S44), A65 (= A80), D68 (= D83), L69 (= L84), K70 (= K85), L110 (= L127), G111 (= G128), T134 (≠ P151), E135 (= E152), L138 (≠ V155), R168 (= R182)
Sites not aligning to the query:
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
33% identity, 91% coverage: 26:275/275 of query aligns to 12:266/266 of O53561
- K135 (≠ V147) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 147:154, 38% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ D154) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
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)
32% identity, 91% coverage: 23:273/275 of query aligns to 12:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
34% identity, 91% coverage: 27:275/275 of query aligns to 8:257/257 of 6slbAAA
- active site: Q64 (≠ A82), F69 (≠ P88), L80 (≠ A99), N84 (vs. gap), A108 (= A129), S111 (≠ G132), A130 (≠ P151), F131 (≠ E152), L136 (= L157), P138 (vs. gap), D139 (vs. gap), A224 (≠ R242), G234 (≠ S252)
- 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 (≠ K76), A62 (= A80), Q64 (≠ A82), D65 (= D83), L66 (= L84), Y76 (≠ G95), A108 (= A129), F131 (≠ E152), D139 (vs. gap)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 91% coverage: 27:275/275 of query aligns to 5:245/245 of 6slaAAA
- active site: Q61 (≠ A82), L68 (≠ Q101), N72 (≠ R105), A96 (= A129), S99 (≠ G132), A118 (≠ P151), F119 (≠ E152), L124 (= L157), P126 (vs. gap), N127 (vs. gap), A212 (≠ R242), G222 (≠ S252)
- 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 (≠ V42), A59 (= A80), Q61 (≠ A82), D62 (= D83), L63 (= L84), L68 (≠ Q101), Y71 (≠ A104), A94 (≠ L127), G95 (= G128), A96 (= A129), F119 (≠ E152), I122 (≠ V155), L124 (= L157), N127 (vs. gap), F234 (= F264), K237 (= K267)
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
29% identity, 79% coverage: 52:268/275 of query aligns to 87:317/327 of Q62651
- D176 (≠ G132) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (= E152) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (vs. gap) 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)
33% identity, 88% coverage: 32:274/275 of query aligns to 11:243/244 of 5ducA
- active site: A61 (= A82), D66 (≠ T96), P73 (≠ M103), I77 (vs. gap), A101 (= A129), Q104 (≠ G132), P123 (= P151), T124 (≠ E152), L129 (= L157), L131 (vs. gap), D132 (vs. gap), P211 (≠ R242), W221 (≠ S252)
- 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 (vs. gap), H80 (≠ S108), D84 (≠ V112), Q104 (≠ G132), D132 (vs. gap), W134 (≠ G159), F217 (≠ T248)
5du4A Crystal structure of m. Tuberculosis echa6 bound to ligand gsk366a (see paper)
33% identity, 88% coverage: 32:274/275 of query aligns to 11:243/244 of 5du4A
- active site: A61 (= A82), D66 (≠ T96), P73 (≠ M103), I77 (vs. gap), A101 (= A129), Q104 (≠ G132), P123 (= P151), T124 (≠ E152), L129 (= L157), L131 (vs. gap), D132 (vs. gap), P211 (≠ R242), W221 (≠ S252)
- binding (5R,7S)-5-(4-ethylphenyl)-N-(4-methoxybenzyl)-7-(trifluoromethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L76 (vs. gap), I77 (vs. gap), H80 (≠ S108), D84 (≠ V112), Q104 (≠ G132), D132 (vs. gap), W134 (≠ G159)
5dtwA Crystal structure of m. Tuberculosis echa6 bound to c20-coa (see paper)
33% identity, 88% coverage: 32:274/275 of query aligns to 11:243/244 of 5dtwA
- active site: A61 (= A82), D66 (≠ T96), P73 (≠ M103), I77 (vs. gap), A101 (= A129), Q104 (≠ G132), P123 (= P151), T124 (≠ E152), L129 (= L157), L131 (vs. gap), D132 (vs. gap), P211 (≠ R242), W221 (≠ S252)
- binding Arachinoyl-CoA: R18 (≠ N39), E20 (≠ P41), R21 (≠ V42), R21 (≠ V42), R22 (vs. gap), A24 (≠ S44), A59 (= A80), A61 (= A82), D62 (= D83), L63 (= L84), H80 (≠ S108), D84 (≠ V112), G100 (= G128), A101 (= A129), Y127 (≠ V155), W134 (≠ G159)
Query Sequence
>CCNA_01891 CCNA_01891 enoyl-CoA hydratase/carnithine racemase
MSGYQVQEAVHDRRLGKEQMMSCLKIEVEDFVATVTLANPPVNSASVDMMLELTAAFDAF
NESPDVRAVLLTAEGKTFCAGADLKNRPGPDAPAGTAFARQRMAREMSWSMVECSKPVVV
AVNGAALGAGLGIVASCDIIVASERAVFGLPEIDVGLAGGAKHAVRFIPHSLARRMVLTG
WRVPAEELYRRGLIEAALPHEEFLDYARGIAKEIASKSPVAVAAAKDSLNVIDNLSLRDG
YRYEQGNTYKLSKSEDAKEAVRAFIEKRPPVFQGR
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