SitesBLAST
Comparing HSERO_RS12745 HSERO_RS12745 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)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
38% identity, 99% coverage: 4:260/260 of query aligns to 3:259/259 of 5zaiC
- active site: A65 (= A66), F70 (= F71), S82 (≠ A83), R86 (≠ G87), G110 (= G111), E113 (= E114), P132 (= P133), E133 (= E134), I138 (≠ L139), P140 (= P141), G141 (≠ C142), A226 (≠ Q227), F236 (= F237)
- binding coenzyme a: K24 (≠ A25), L25 (vs. gap), A63 (= A64), G64 (= G65), A65 (= A66), D66 (= D67), I67 (≠ L68), P132 (= P133), R166 (= R167), F248 (= F249), K251 (= K252)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
39% identity, 90% coverage: 26:260/260 of query aligns to 27:261/261 of 5jbxB
- active site: A67 (= A66), R72 (≠ F71), L84 (≠ G87), R88 (vs. gap), G112 (= G111), E115 (= E114), T134 (≠ P133), E135 (= E134), I140 (≠ L139), P142 (= P141), G143 (≠ C142), A228 (≠ Q227), L238 (≠ F237)
- binding coenzyme a: A28 (≠ T27), A65 (= A64), D68 (= D67), L69 (= L68), K70 (= K69), L110 (≠ M109), G111 (= G110), T134 (≠ P133), E135 (= E134), L138 (≠ V137), R168 (= R167)
Sites not aligning to the query:
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
37% identity, 99% coverage: 3:260/260 of query aligns to 1:256/256 of 3h81A
- active site: A64 (= A66), M69 (≠ F71), T79 (≠ A83), F83 (≠ G87), G107 (= G111), E110 (= E114), P129 (= P133), E130 (= E134), V135 (≠ L139), P137 (= P141), G138 (≠ C142), L223 (≠ Q227), F233 (= F237)
- binding calcium ion: F233 (= F237), Q238 (= Q242)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
37% identity, 98% coverage: 3:257/260 of query aligns to 2:254/255 of 3q0jC
- active site: A65 (= A66), M70 (≠ F71), T80 (≠ A83), F84 (≠ G87), G108 (= G111), E111 (= E114), P130 (= P133), E131 (= E134), V136 (≠ L139), P138 (= P141), G139 (≠ C142), L224 (≠ Q227), F234 (= F237)
- binding acetoacetyl-coenzyme a: Q23 (≠ P24), A24 (= A25), L25 (vs. gap), A27 (≠ T27), A63 (= A64), G64 (= G65), A65 (= A66), D66 (= D67), I67 (≠ L68), K68 (= K69), M70 (≠ F71), F84 (≠ G87), G107 (= G110), G108 (= G111), E111 (= E114), P130 (= P133), E131 (= E134), P138 (= P141), G139 (≠ C142), M140 (≠ A143)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
37% identity, 98% coverage: 3:257/260 of query aligns to 2:254/255 of 3q0gC
- active site: A65 (= A66), M70 (≠ F71), T80 (≠ A83), F84 (≠ G87), G108 (= G111), E111 (= E114), P130 (= P133), E131 (= E134), V136 (≠ L139), P138 (= P141), G139 (≠ C142), L224 (≠ Q227), F234 (= F237)
- binding coenzyme a: L25 (vs. gap), A63 (= A64), I67 (≠ L68), K68 (= K69), Y104 (= Y107), P130 (= P133), E131 (= E134), L134 (≠ V137)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
37% identity, 98% coverage: 3:257/260 of query aligns to 1:249/250 of 3q0gD
- active site: A64 (= A66), M69 (≠ L70), T75 (≠ K76), F79 (≠ G87), G103 (= G111), E106 (= E114), P125 (= P133), E126 (= E134), V131 (≠ L139), P133 (= P141), G134 (≠ C142), L219 (≠ Q227), F229 (= F237)
- binding Butyryl Coenzyme A: F225 (= F233), F241 (= F249)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
35% identity, 96% coverage: 11:260/260 of query aligns to 13:260/260 of 2hw5C
- active site: A68 (= A66), M73 (≠ F71), S83 (≠ A83), L87 (≠ G87), G111 (= G111), E114 (= E114), P133 (= P133), E134 (= E134), T139 (≠ L139), P141 (= P141), G142 (≠ C142), K227 (≠ Q227), F237 (= F237)
- binding crotonyl coenzyme a: K26 (≠ P24), A27 (= A25), L28 (vs. gap), A30 (≠ T27), K62 (= K60), I70 (≠ L68), F109 (≠ M109)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
35% identity, 96% coverage: 11:260/260 of query aligns to 13:258/258 of 1mj3A
- active site: A68 (= A66), M73 (= M82), S83 (≠ E91), L85 (= L93), G109 (= G111), E112 (= E114), P131 (= P133), E132 (= E134), T137 (≠ L139), P139 (= P141), G140 (≠ C142), K225 (≠ Q227), F235 (= F237)
- binding hexanoyl-coenzyme a: K26 (≠ P24), A27 (= A25), L28 (vs. gap), A30 (≠ T27), A66 (= A64), G67 (= G65), A68 (= A66), D69 (= D67), I70 (≠ L68), G109 (= G111), P131 (= P133), E132 (= E134), L135 (≠ V137), G140 (≠ C142)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
34% identity, 96% coverage: 11:260/260 of query aligns to 13:260/260 of 1dubA
- active site: A68 (= A66), M73 (≠ F71), S83 (≠ A83), L87 (≠ G87), G111 (= G111), E114 (= E114), P133 (= P133), E134 (= E134), T139 (≠ L139), P141 (= P141), G142 (≠ C142), K227 (≠ Q227), F237 (= F237)
- binding acetoacetyl-coenzyme a: K26 (≠ P24), A27 (= A25), L28 (vs. gap), A30 (≠ T27), A66 (= A64), A68 (= A66), D69 (= D67), I70 (≠ L68), Y107 (= Y107), G110 (= G110), G111 (= G111), E114 (= E114), P133 (= P133), E134 (= E134), L137 (≠ V137), G142 (≠ C142), F233 (= F233), F249 (= F249)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
34% identity, 96% coverage: 11:260/260 of query aligns to 11:258/258 of 1ey3A
- active site: A66 (= A66), M71 (≠ F71), S81 (≠ A83), L85 (≠ G87), G109 (= G111), E112 (= E114), P131 (= P133), E132 (= E134), T137 (≠ L139), P139 (= P141), G140 (≠ C142), K225 (≠ Q227), F235 (= F237)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ P24), L26 (vs. gap), A28 (≠ T27), A64 (= A64), G65 (= G65), A66 (= A66), D67 (= D67), I68 (≠ L68), L85 (≠ G87), W88 (≠ F90), G109 (= G111), P131 (= P133), L135 (≠ V137), G140 (≠ C142)
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)
34% identity, 96% coverage: 11:260/260 of query aligns to 43:290/290 of P14604
- E144 (= E114) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E134) 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)
35% identity, 96% coverage: 11:260/260 of query aligns to 12:254/254 of 2dubA
- active site: A67 (= A66), M72 (= M82), S82 (vs. gap), G105 (= G111), E108 (= E114), P127 (= P133), E128 (= E134), T133 (≠ L139), P135 (= P141), G136 (≠ C142), K221 (≠ Q227), F231 (= F237)
- binding octanoyl-coenzyme a: K25 (≠ P24), A26 (= A25), L27 (vs. gap), A29 (≠ T27), A65 (= A64), A67 (= A66), D68 (= D67), I69 (≠ L68), K70 (= K69), G105 (= G111), E108 (= E114), P127 (= P133), E128 (= E134), G136 (≠ C142), A137 (= A143)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
36% identity, 97% coverage: 10:260/260 of query aligns to 8:257/257 of 6slbAAA
- active site: Q64 (≠ A66), F69 (= F71), L80 (≠ A83), N84 (≠ G87), A108 (≠ G111), S111 (≠ E114), A130 (≠ P133), F131 (≠ E134), L136 (= L139), P138 (= P141), D139 (≠ C142), A224 (≠ Q227), G234 (≠ F237)
- 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 (≠ K60), A62 (= A64), Q64 (≠ A66), D65 (= D67), L66 (= L68), Y76 (≠ A79), A108 (≠ G111), F131 (≠ E134), D139 (≠ C142)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 97% coverage: 10:260/260 of query aligns to 5:245/245 of 6slaAAA
- active site: Q61 (≠ A66), L68 (≠ A83), N72 (≠ G87), A96 (≠ G111), S99 (≠ E114), A118 (≠ P133), F119 (≠ E134), L124 (= L139), P126 (= P141), N127 (≠ C142), A212 (≠ Q227), G222 (≠ F237)
- 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 (vs. gap), A59 (= A64), Q61 (≠ A66), D62 (= D67), L63 (= L68), L68 (≠ A83), Y71 (≠ F86), A94 (≠ M109), G95 (= G110), A96 (≠ G111), F119 (≠ E134), I122 (≠ V137), L124 (= L139), N127 (≠ C142), F234 (= F249), K237 (= K252)
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)
31% identity, 99% coverage: 1:257/260 of query aligns to 1:281/723 of Q08426
- E3 (≠ T3) to 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
- V40 (≠ N44) to G: in dbSNP:rs1062551
- I41 (≠ A45) to R: in dbSNP:rs1062552
- T75 (≠ R85) to I: in dbSNP:rs1062553
- K165 (≠ R175) 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 (≠ E181) 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.
- A274 (vs. gap) to T: in dbSNP:rs2302819
Sites not aligning to the query:
- 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
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
36% identity, 77% coverage: 6:206/260 of query aligns to 7:206/707 of 6yswA
- active site: A66 (= A66), I71 (≠ F71), A84 (= A83), Q88 (≠ G87), G112 (= G111), E115 (= E114), P136 (= P133), E137 (= E134), G145 (≠ C142)
- binding coenzyme a: E23 (≠ A25), M25 (≠ T27), A66 (= A66), D67 (= D67), I68 (≠ L68), P136 (= P133), E137 (= E134), L140 (≠ V137)
Sites not aligning to the query:
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)
33% identity, 95% coverage: 12:258/260 of query aligns to 18:266/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
30% identity, 97% coverage: 9:260/260 of query aligns to 12:266/266 of O53561
- K135 (≠ Q129) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 129:136, 25% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ A136) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
Q13825 Methylglutaconyl-CoA hydratase, mitochondrial; 3-MG-CoA hydratase; AU-specific RNA-binding enoyl-CoA hydratase; AU-binding protein/enoyl-CoA hydratase; Itaconyl-CoA hydratase; EC 4.2.1.18; EC 4.2.1.56 from Homo sapiens (Human) (see 4 papers)
33% identity, 90% coverage: 26:260/260 of query aligns to 101:339/339 of Q13825
- K105 (≠ R30) mutation to N: Abolishes RNA-binding; when associated with E-109 and Q-113.
- 105:119 (vs. 30:44, 20% identical) RNA-binding
- K109 (≠ A34) mutation to E: Abolishes RNA-binding; when associated with N-105 and Q-113.
- K113 (≠ R38) mutation to Q: Abolishes RNA-binding; when associated with N-105 and E-109.
- A240 (≠ G165) to V: in MGCA1; decreased methylglutaconyl-CoA hydratase activity; dbSNP:rs769894315
Sites not aligning to the query:
- 1:67 modified: transit peptide, Mitochondrion
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
38% identity, 71% coverage: 15:198/260 of query aligns to 10:187/692 of 6iunB
Sites not aligning to the query:
- active site: 248, 407, 428, 440, 478
- binding nicotinamide-adenine-dinucleotide: 300, 301, 302, 321, 322, 365, 377, 378, 380, 384, 388, 405, 407
Query Sequence
>HSERO_RS12745 HSERO_RS12745 enoyl-CoA hydratase
MTTYTNLKLEKTGHTAVLTLSNPPANTWTRAALADLTRLVKELNADRDIYTLVVTGEGEK
FFSAGADLKLFADGDKAMAREMARRFGEAFETLSAFRGVSIAAINGYAMGGGLECALACD
IRIAEEQAQMALPEAAVGLLPCAGGTQNLPWLVGEGWAKRMILCGERVNAETALRIGLVE
EVVPRGQARERALALAQQAEKQSPSSVAASKQLIQGARHNPLGTILQTERELFVDLFDTQ
DQREGVQAFLEKRSPQWKNQ
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