SitesBLAST
Comparing 3609989 Dshi_3370 Enoyl-CoA hydratase/isomerase (RefSeq) 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)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
59% identity, 99% coverage: 1:255/258 of query aligns to 1:254/255 of 3q0jC
- active site: A65 (= A65), M70 (= M70), T80 (≠ S80), F84 (= F84), G108 (= G109), E111 (= E112), P130 (= P131), E131 (= E132), V136 (= V137), P138 (≠ A139), G139 (= G140), L224 (= L225), F234 (= F235)
- binding acetoacetyl-coenzyme a: Q23 (≠ D23), A24 (= A24), L25 (= L25), A27 (= A27), A63 (= A63), G64 (= G64), A65 (= A65), D66 (= D66), I67 (= I67), K68 (= K68), M70 (= M70), F84 (= F84), G107 (= G108), G108 (= G109), E111 (= E112), P130 (= P131), E131 (= E132), P138 (≠ A139), G139 (= G140), M140 (≠ I141)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
59% identity, 99% coverage: 1:255/258 of query aligns to 1:254/255 of 3q0gC
- active site: A65 (= A65), M70 (= M70), T80 (≠ S80), F84 (= F84), G108 (= G109), E111 (= E112), P130 (= P131), E131 (= E132), V136 (= V137), P138 (≠ A139), G139 (= G140), L224 (= L225), F234 (= F235)
- binding coenzyme a: L25 (= L25), A63 (= A63), I67 (= I67), K68 (= K68), Y104 (= Y105), P130 (= P131), E131 (= E132), L134 (= L135)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
59% identity, 98% coverage: 3:255/258 of query aligns to 2:253/256 of 3h81A
- active site: A64 (= A65), M69 (= M70), T79 (≠ S80), F83 (= F84), G107 (= G109), E110 (= E112), P129 (= P131), E130 (= E132), V135 (= V137), P137 (≠ A139), G138 (= G140), L223 (= L225), F233 (= F235)
- binding calcium ion: F233 (= F235), Q238 (= Q240)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
59% identity, 98% coverage: 3:255/258 of query aligns to 2:249/250 of 3q0gD
- active site: A64 (= A65), M69 (= M70), T75 (≠ S80), F79 (= F84), G103 (= G109), E106 (= E112), P125 (= P131), E126 (= E132), V131 (= V137), P133 (≠ A139), G134 (= G140), L219 (= L225), F229 (= F235)
- binding Butyryl Coenzyme A: F225 (= F231), F241 (= F247)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
55% identity, 95% coverage: 14:257/258 of query aligns to 17:259/260 of 1dubA
- active site: A68 (= A65), M73 (= M70), S83 (= S80), L87 (≠ G85), G111 (= G109), E114 (= E112), P133 (= P131), E134 (= E132), T139 (≠ V137), P141 (≠ A139), G142 (= G140), K227 (≠ L225), F237 (= F235)
- binding acetoacetyl-coenzyme a: K26 (≠ D23), A27 (= A24), L28 (= L25), A30 (= A27), A66 (= A63), A68 (= A65), D69 (= D66), I70 (= I67), Y107 (= Y105), G110 (= G108), G111 (= G109), E114 (= E112), P133 (= P131), E134 (= E132), L137 (= L135), G142 (= G140), F233 (= F231), F249 (= F247)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
55% identity, 95% coverage: 14:257/258 of query aligns to 15:257/258 of 1ey3A
- active site: A66 (= A65), M71 (= M70), S81 (= S80), L85 (≠ G85), G109 (= G109), E112 (= E112), P131 (= P131), E132 (= E132), T137 (≠ V137), P139 (≠ A139), G140 (= G140), K225 (≠ L225), F235 (= F235)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ D23), L26 (= L25), A28 (= A27), A64 (= A63), G65 (= G64), A66 (= A65), D67 (= D66), I68 (= I67), L85 (≠ G85), W88 (≠ V88), G109 (= G109), P131 (= P131), L135 (= L135), G140 (= G140)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
55% identity, 95% coverage: 14:257/258 of query aligns to 17:257/258 of 1mj3A
- active site: A68 (= A65), M73 (= M70), S83 (= S80), L85 (≠ D82), G109 (= G109), E112 (= E112), P131 (= P131), E132 (= E132), T137 (≠ V137), P139 (≠ A139), G140 (= G140), K225 (≠ L225), F235 (= F235)
- binding hexanoyl-coenzyme a: K26 (≠ D23), A27 (= A24), L28 (= L25), A30 (= A27), A66 (= A63), G67 (= G64), A68 (= A65), D69 (= D66), I70 (= I67), G109 (= G109), P131 (= P131), E132 (= E132), L135 (= L135), G140 (= G140)
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)
55% identity, 95% coverage: 14:257/258 of query aligns to 47:289/290 of P14604
- E144 (= E112) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E132) 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
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
55% identity, 95% coverage: 14:257/258 of query aligns to 16:253/254 of 2dubA
- active site: A67 (= A65), M72 (= M70), S82 (= S80), G105 (= G109), E108 (= E112), P127 (= P131), E128 (= E132), T133 (≠ V137), P135 (≠ A139), G136 (= G140), K221 (≠ L225), F231 (= F235)
- binding octanoyl-coenzyme a: K25 (≠ D23), A26 (= A24), L27 (= L25), A29 (= A27), A65 (= A63), A67 (= A65), D68 (= D66), I69 (= I67), K70 (= K68), G105 (= G109), E108 (= E112), P127 (= P131), E128 (= E132), G136 (= G140), A137 (≠ I141)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
53% identity, 96% coverage: 12:258/258 of query aligns to 15:260/260 of 2hw5C
- active site: A68 (= A65), M73 (= M70), S83 (= S80), L87 (≠ G85), G111 (= G109), E114 (= E112), P133 (= P131), E134 (= E132), T139 (≠ V137), P141 (≠ A139), G142 (= G140), K227 (≠ L225), F237 (= F235)
- binding crotonyl coenzyme a: K26 (≠ D23), A27 (= A24), L28 (= L25), A30 (= A27), K62 (= K59), I70 (= I67), F109 (≠ L107)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
47% identity, 100% coverage: 1:258/258 of query aligns to 1:259/259 of 5zaiC
- active site: A65 (= A65), F70 (≠ M70), S82 (≠ D82), R86 (≠ P86), G110 (= G109), E113 (= E112), P132 (= P131), E133 (= E132), I138 (≠ V137), P140 (≠ A139), G141 (= G140), A226 (≠ L225), F236 (= F235)
- binding coenzyme a: K24 (≠ A24), L25 (= L25), A63 (= A63), G64 (= G64), A65 (= A65), D66 (= D66), I67 (= I67), P132 (= P131), R166 (≠ F165), F248 (= F247), K251 (= K250)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 98% coverage: 6:258/258 of query aligns to 2:245/245 of 6slaAAA
- active site: Q61 (≠ A65), L68 (≠ E72), N72 (≠ V76), A96 (≠ G109), S99 (≠ E112), A118 (≠ P131), F119 (≠ E132), L124 (≠ V137), P126 (≠ A139), N127 (≠ G140), A212 (≠ L225), G222 (≠ F235)
- 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 (= L25), A59 (= A63), Q61 (≠ A65), D62 (= D66), L63 (≠ I67), L68 (≠ E72), Y71 (≠ F75), A94 (≠ L107), G95 (= G108), A96 (≠ G109), F119 (≠ E132), I122 (≠ L135), L124 (≠ V137), N127 (≠ G140), F234 (= F247), K237 (= K250)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
36% identity, 98% coverage: 6:258/258 of query aligns to 5:257/257 of 6slbAAA
- active site: Q64 (≠ A65), F69 (≠ M70), L80 (≠ S81), N84 (≠ G85), A108 (≠ G109), S111 (≠ E112), A130 (≠ P131), F131 (≠ E132), L136 (≠ V137), P138 (≠ A139), D139 (≠ G140), A224 (≠ L225), G234 (≠ F235)
- 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 (≠ A65), D65 (= D66), L66 (≠ I67), Y76 (≠ E77), A108 (≠ G109), F131 (≠ E132), D139 (≠ G140)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
35% identity, 90% coverage: 26:258/258 of query aligns to 27:261/261 of 5jbxB
- active site: A67 (= A65), R72 (vs. gap), L84 (vs. gap), R88 (vs. gap), G112 (= G109), E115 (= E112), T134 (≠ P131), E135 (= E132), I140 (≠ V137), P142 (≠ A139), G143 (= G140), A228 (≠ L225), L238 (≠ F235)
- binding coenzyme a: A28 (= A27), A65 (= A63), D68 (= D66), L69 (≠ I67), K70 (= K68), L110 (= L107), G111 (= G108), T134 (≠ P131), E135 (= E132), L138 (= L135), R168 (≠ F165)
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)
34% identity, 98% coverage: 7:258/258 of query aligns to 11:266/266 of O53561
- K135 (= K127) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 127:134, 50% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ N134) 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)
34% identity, 95% coverage: 13:256/258 of query aligns to 20:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
4i52A Scmenb im complex with 1-hydroxy-2-naphthoyl-coa (see paper)
34% identity, 98% coverage: 3:255/258 of query aligns to 9:268/275 of 4i52A
- active site: G77 (≠ A65), R82 (≠ M70), Y87 (≠ F75), R95 (vs. gap), L99 (vs. gap), G123 (= G109), V126 (≠ E112), G146 (≠ E132), S151 (≠ V137), D153 (≠ A139), G154 (= G140), A240 (≠ L225), Y248 (≠ A233)
- binding 1-hydroxy-2-naphthoyl-CoA: H29 (≠ D23), K30 (≠ A24), R31 (≠ L25), A33 (= A27), S75 (≠ A63), G76 (= G64), G77 (≠ A65), D78 (= D66), Q79 (≠ I67), L96 (vs. gap), V98 (vs. gap), Y119 (= Y105), I121 (≠ L107), G123 (= G109), T145 (≠ P131), V149 (≠ L135), S151 (≠ V137), F152 (≠ V138)
4i4zA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with salicylyl-coa (see paper)
34% identity, 98% coverage: 3:255/258 of query aligns to 9:268/275 of 4i4zA
- active site: G77 (≠ A65), R82 (≠ M70), Y87 (≠ F75), R95 (vs. gap), L99 (vs. gap), G123 (= G109), V126 (≠ E112), G146 (≠ E132), S151 (≠ V137), D153 (≠ A139), G154 (= G140), A240 (≠ L225), Y248 (≠ A233)
- binding Salicylyl CoA: H29 (≠ D23), K30 (≠ A24), R31 (≠ L25), S75 (≠ A63), G76 (= G64), G77 (≠ A65), D78 (= D66), Q79 (≠ I67), Y87 (≠ F75), V98 (vs. gap), G123 (= G109), T145 (≠ P131), V149 (≠ L135), S151 (≠ V137), F260 (= F247), K263 (= K250)
- binding bicarbonate ion: G122 (= G108), Q144 (= Q130), T145 (≠ P131), G146 (≠ E132), W174 (≠ H160)
3h02A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
34% identity, 95% coverage: 12:255/258 of query aligns to 28:259/266 of 3h02A
- active site: G82 (≠ A65), H86 (≠ E69), L90 (≠ K73), G114 (= G109), V117 (≠ E112), G137 (≠ E132), S142 (≠ V137), D144 (≠ A139), G145 (= G140), A231 (≠ L224), Y239 (≠ F235)
- binding bicarbonate ion: G113 (= G108), Q135 (= Q130), G137 (≠ E132), W165 (≠ H160)
4elwA Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate (see paper)
33% identity, 95% coverage: 12:255/258 of query aligns to 29:260/267 of 4elwA
- active site: G83 (≠ A65), L91 (≠ K73), G115 (= G109), V118 (≠ E112), G138 (≠ E132), S143 (≠ V137), D145 (≠ A139), G146 (= G140), A232 (≠ L224), Y240 (≠ F235)
- binding nitrate ion: G114 (= G108), T137 (≠ P131), G138 (≠ E132), F144 (≠ V138), W166 (≠ H160)
Query Sequence
>3609989 Dshi_3370 Enoyl-CoA hydratase/isomerase (RefSeq)
MAYNTLIVEIEDHVALIRLNRPDALNALNTELLGELAKALRSAEENEKVRCIILTGSEKA
FAAGADIKEMSEKTFVEVFSSDLFGPEVERLLNCRKPIIAAVSGYALGGGCEIAMMCDFI
IASETAKFGQPEINLGVVAGIGGTQRLTRFVGKSKAMDMHLTGRFMDAEEAERSGLVSRV
VPTKKLMEEAMGAAQKIAEKSVLTSMAVKEAVNRSYETTLREGLLFERRLFHAMFATEDQ
TEGMGAFLEKREPQFRDK
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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