SitesBLAST
Comparing SMc01153 SMc01153 enoyl-CoA hydratase 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)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
68% identity, 100% coverage: 2:257/257 of query aligns to 1:256/256 of 3h81A
- active site: A64 (= A65), M69 (= M70), T79 (≠ L80), F83 (≠ L84), G107 (= G108), E110 (= E111), P129 (= P130), E130 (= E131), V135 (= V136), P137 (= P138), G138 (= G139), L223 (≠ R224), F233 (= F234)
- binding calcium ion: F233 (= F234), Q238 (= Q239)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
68% identity, 99% coverage: 1:254/257 of query aligns to 1:254/255 of 3q0jC
- active site: A65 (= A65), M70 (= M70), T80 (≠ L80), F84 (≠ L84), G108 (= G108), E111 (= E111), P130 (= P130), E131 (= E131), V136 (= V136), P138 (= P138), G139 (= G139), L224 (≠ R224), F234 (= F234)
- binding acetoacetyl-coenzyme a: Q23 (= Q23), A24 (= A24), L25 (= L25), A27 (= A27), A63 (= A63), G64 (= G64), A65 (= A65), D66 (= D66), I67 (= I67), K68 (= K68), M70 (= M70), F84 (≠ L84), G107 (= G107), G108 (= G108), E111 (= E111), P130 (= P130), E131 (= E131), P138 (= P138), G139 (= G139), M140 (= M140)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
68% identity, 99% coverage: 1:254/257 of query aligns to 1:254/255 of 3q0gC
- active site: A65 (= A65), M70 (= M70), T80 (≠ L80), F84 (≠ L84), G108 (= G108), E111 (= E111), P130 (= P130), E131 (= E131), V136 (= V136), P138 (= P138), G139 (= G139), L224 (≠ R224), F234 (= F234)
- binding coenzyme a: L25 (= L25), A63 (= A63), I67 (= I67), K68 (= K68), Y104 (≠ F104), P130 (= P130), E131 (= E131), L134 (= L134)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
67% identity, 98% coverage: 2:254/257 of query aligns to 1:249/250 of 3q0gD
- active site: A64 (= A65), M69 (= M70), T75 (≠ L80), F79 (≠ L84), G103 (= G108), E106 (= E111), P125 (= P130), E126 (= E131), V131 (= V136), P133 (= P138), G134 (= G139), L219 (≠ R224), F229 (= F234)
- binding Butyryl Coenzyme A: F225 (= F230), F241 (= F246)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
58% identity, 100% coverage: 2:257/257 of query aligns to 2:260/260 of 2hw5C
- active site: A68 (= A65), M73 (= M70), S83 (≠ L80), L87 (= L84), G111 (= G108), E114 (= E111), P133 (= P130), E134 (= E131), T139 (≠ V136), P141 (= P138), G142 (= G139), K227 (≠ R224), F237 (= F234)
- binding crotonyl coenzyme a: K26 (≠ Q23), A27 (= A24), L28 (= L25), A30 (= A27), K62 (= K59), I70 (= I67), F109 (≠ L106)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
58% identity, 99% coverage: 2:255/257 of query aligns to 2:258/260 of 1dubA
- active site: A68 (= A65), M73 (= M70), S83 (≠ L80), L87 (= L84), G111 (= G108), E114 (= E111), P133 (= P130), E134 (= E131), T139 (≠ V136), P141 (= P138), G142 (= G139), K227 (≠ R224), F237 (= F234)
- binding acetoacetyl-coenzyme a: K26 (≠ Q23), A27 (= A24), L28 (= L25), A30 (= A27), A66 (= A63), A68 (= A65), D69 (= D66), I70 (= I67), Y107 (≠ F104), G110 (= G107), G111 (= G108), E114 (= E111), P133 (= P130), E134 (= E131), L137 (= L134), G142 (= G139), F233 (= F230), F249 (= F246)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
58% identity, 98% coverage: 3:255/257 of query aligns to 1:256/258 of 1ey3A
- active site: A66 (= A65), M71 (= M70), S81 (≠ L80), L85 (= L84), G109 (= G108), E112 (= E111), P131 (= P130), E132 (= E131), T137 (≠ V136), P139 (= P138), G140 (= G139), K225 (≠ R224), F235 (= F234)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ Q23), L26 (= L25), A28 (= A27), A64 (= A63), G65 (= G64), A66 (= A65), D67 (= D66), I68 (= I67), L85 (= L84), W88 (= W87), G109 (= G108), P131 (= P130), L135 (= L134), G140 (= G139)
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)
58% identity, 99% coverage: 2:255/257 of query aligns to 32:288/290 of P14604
- E144 (= E111) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E131) 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)
58% identity, 99% coverage: 2:255/257 of query aligns to 2:256/258 of 1mj3A
- active site: A68 (= A65), M73 (= M70), S83 (≠ L80), L85 (= L84), G109 (= G108), E112 (= E111), P131 (= P130), E132 (= E131), T137 (≠ V136), P139 (= P138), G140 (= G139), K225 (≠ R224), F235 (= F234)
- binding hexanoyl-coenzyme a: K26 (≠ Q23), A27 (= A24), L28 (= L25), A30 (= A27), A66 (= A63), G67 (= G64), A68 (= A65), D69 (= D66), I70 (= I67), G109 (= G108), P131 (= P130), E132 (= E131), L135 (= L134), G140 (= G139)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
57% identity, 99% coverage: 2:255/257 of query aligns to 1:252/254 of 2dubA
- active site: A67 (= A65), M72 (= M70), S82 (≠ G85), G105 (= G108), E108 (= E111), P127 (= P130), E128 (= E131), T133 (≠ V136), P135 (= P138), G136 (= G139), K221 (≠ R224), F231 (= F234)
- binding octanoyl-coenzyme a: K25 (≠ Q23), A26 (= A24), L27 (= L25), A29 (= A27), A65 (= A63), A67 (= A65), D68 (= D66), I69 (= I67), K70 (= K68), G105 (= G108), E108 (= E111), P127 (= P130), E128 (= E131), G136 (= G139), A137 (≠ M140)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
43% identity, 100% coverage: 1:257/257 of query aligns to 1:259/259 of 5zaiC
- active site: A65 (= A65), F70 (≠ M70), S82 (≠ D82), R86 (≠ G86), G110 (= G108), E113 (= E111), P132 (= P130), E133 (= E131), I138 (≠ V136), P140 (= P138), G141 (= G139), A226 (≠ R224), F236 (= F234)
- binding coenzyme a: K24 (≠ A24), L25 (= L25), A63 (= A63), G64 (= G64), A65 (= A65), D66 (= D66), I67 (= I67), P132 (= P130), R166 (≠ M164), F248 (= F246), K251 (= K249)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
38% identity, 97% coverage: 8:257/257 of query aligns to 9:261/261 of 5jbxB
- active site: A67 (= A65), R72 (≠ M70), L84 (= L80), R88 (≠ L84), G112 (= G108), E115 (= E111), T134 (≠ P130), E135 (= E131), I140 (≠ V136), P142 (= P138), G143 (= G139), A228 (≠ R224), L238 (≠ F234)
- binding coenzyme a: S24 (≠ Q23), R25 (≠ A24), R26 (≠ L25), A28 (= A27), A65 (= A63), D68 (= D66), L69 (≠ I67), K70 (= K68), L110 (= L106), G111 (= G107), T134 (≠ P130), E135 (= E131), L138 (= L134), R168 (≠ M164)
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)
35% identity, 93% coverage: 16:255/257 of query aligns to 23:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 98% coverage: 6:257/257 of query aligns to 5:257/257 of 6slbAAA
- active site: Q64 (≠ A65), F69 (≠ M70), L80 (= L80), N84 (≠ L84), A108 (≠ G108), S111 (≠ E111), A130 (≠ P130), F131 (≠ E131), L136 (≠ V136), P138 (= P138), D139 (≠ G139), A224 (≠ R224), G234 (≠ F234)
- 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 (≠ F75), A108 (≠ G108), F131 (≠ E131), D139 (≠ G139)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 98% coverage: 6:257/257 of query aligns to 2:245/245 of 6slaAAA
- active site: Q61 (≠ A65), L68 (= L80), N72 (≠ L84), A96 (≠ G108), S99 (≠ E111), A118 (≠ P130), F119 (≠ E131), L124 (≠ V136), P126 (= P138), N127 (≠ G139), A212 (≠ R224), G222 (≠ F234)
- 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 (= L80), Y71 (≠ F83), A94 (≠ L106), G95 (= G107), A96 (≠ G108), F119 (≠ E131), I122 (≠ L134), L124 (≠ V136), N127 (≠ G139), F234 (= F246), K237 (= K249)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
35% identity, 98% coverage: 7:257/257 of query aligns to 11:266/266 of O53561
- K135 (= K126) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 126:133, 50% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ T133) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
3omeC Crystal structure of a probable enoyl-coa hydratase from mycobacterium smegmatis (see paper)
40% identity, 79% coverage: 14:217/257 of query aligns to 14:217/247 of 3omeC
- active site: H65 (≠ A65), E70 (= E69), A82 (= A81), L86 (vs. gap), G110 (= G108), L113 (≠ E111), V133 (≠ E131), I138 (≠ V136), G139 (= G141), E142 (≠ Q144)
- binding zinc ion: E81 (≠ L80), E142 (≠ Q144)
Sites not aligning to the query:
3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
41% identity, 76% coverage: 4:198/257 of query aligns to 1:178/224 of 3p85A
- active site: L62 (≠ A65), L67 (= L80), P68 (≠ A81), G92 (= G108), E95 (= E111), T114 (≠ P130), H115 (≠ E131), L120 (≠ V136), P122 (= P138), T123 (≠ G139)
- binding calcium ion: D43 (= D46), D45 (≠ A48)
Sites not aligning to the query:
Q08426 Peroxisomal bifunctional enzyme; PBE; PBFE; L-bifunctional protein; LBP; Multifunctional enzyme 1; MFE1; EC 4.2.1.17; EC 5.3.3.8; EC 1.1.1.35 from Homo sapiens (Human) (see 5 papers)
33% identity, 87% coverage: 14:237/257 of query aligns to 11:231/723 of Q08426
- V40 (≠ D44) to G: in dbSNP:rs1062551
- I41 (≠ A45) to R: in dbSNP:rs1062552
- T75 (≠ V76) to I: in dbSNP:rs1062553
- K165 (≠ R172) modified: N6-acetyllysine; alternate; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-171; Q-346 and Q-584.
- K171 (≠ R178) modified: N6-acetyllysine; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-346 and Q-584.
Sites not aligning to the query:
- 3 E → K: in FRTS3; the mutant is mistargeted to mitochondria; results in impaired mitochondrial oxidative phosphorylation and defects in the transport of fluids across the epithelium of renal proximal tubular cells; dbSNP:rs398124646
- 274 A → T: in dbSNP:rs2302819
- 325 A → G: in dbSNP:rs1062555
- 346 modified: N6-acetyllysine; K→Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-584.
- 584 modified: N6-acetyllysine; alternate; K→Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-346.
- 598 K → T: in dbSNP:rs1042437
- 606 T → P: in dbSNP:rs1042438
3t3wF Crystal structure of probable enoyl-coa hydratase from mycobacterium thermoresistibile (see paper)
37% identity, 81% coverage: 9:217/257 of query aligns to 9:218/248 of 3t3wF
- active site: H65 (≠ A65), D71 (≠ E69), S83 (≠ A81), L87 (vs. gap), G111 (= G108), L114 (≠ E111), V134 (≠ E131), I139 (≠ V136), G140 (= G141), E143 (≠ Q144)
- binding zinc ion: E82 (≠ L80), E143 (≠ Q144)
Sites not aligning to the query:
Query Sequence
>SMc01153 SMc01153 enoyl-CoA hydratase
MSYETLLVETQGRVGLITLNRPQALNALNAVLMRELDAALKAFDADRAVGAIVLAGSEKA
FAAGADIKEMQGLDFVDGYLADFLGGWEHVANARKPMIAAVSGFALGGGCELAMMCDFII
ASETAKFGQPEITLGVIPGMGGSQRLTRAVGKAKAMDLILTGRMMDAAEAERSGLVSRVV
APDRLLEEALGAAEKIASFSLPAAMMAKEAVNRSLELTLAEGLRFERRLFQSLFATEDQK
EGMAAFVAKRKAEFKHR
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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