SitesBLAST
Comparing RR42_RS28550 RR42_RS28550 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)
39% identity, 99% coverage: 2:254/256 of query aligns to 6:257/259 of 5zaiC
- active site: A65 (= A61), F70 (= F66), S82 (≠ A78), R86 (≠ G82), G110 (= G106), E113 (= E109), P132 (= P128), E133 (= E129), I138 (≠ L134), P140 (= P136), G141 (≠ C137), A226 (= A223), F236 (= F233)
- binding coenzyme a: K24 (≠ A20), L25 (vs. gap), A63 (= A59), G64 (= G60), A65 (= A61), D66 (= D62), I67 (≠ L63), P132 (= P128), R166 (= R162), F248 (= F245), K251 (= K248)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
40% identity, 91% coverage: 21:254/256 of query aligns to 27:259/261 of 5jbxB
- active site: A67 (= A61), R72 (≠ F66), L84 (≠ A78), R88 (≠ G82), G112 (= G106), E115 (= E109), T134 (≠ P128), E135 (= E129), I140 (≠ L134), P142 (= P136), G143 (≠ C137), A228 (= A223), L238 (≠ F233)
- binding coenzyme a: A28 (= A22), A65 (= A59), D68 (= D62), L69 (= L63), K70 (≠ N64), L110 (≠ M104), G111 (= G105), T134 (≠ P128), E135 (= E129), L138 (≠ V132), R168 (= R162)
Sites not aligning to the query:
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
38% identity, 97% coverage: 7:255/256 of query aligns to 10:255/256 of 3h81A
- active site: A64 (= A61), M69 (≠ F66), T79 (≠ A78), F83 (≠ G82), G107 (= G106), E110 (= E109), P129 (= P128), E130 (= E129), V135 (≠ L134), P137 (= P136), G138 (≠ C137), L223 (≠ A223), F233 (= F233)
- binding calcium ion: F233 (= F233), Q238 (= Q238)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
38% identity, 96% coverage: 7:253/256 of query aligns to 11:254/255 of 3q0jC
- active site: A65 (= A61), M70 (≠ F66), T80 (≠ A78), F84 (≠ G82), G108 (= G106), E111 (= E109), P130 (= P128), E131 (= E129), V136 (≠ L134), P138 (= P136), G139 (≠ C137), L224 (≠ A223), F234 (= F233)
- binding acetoacetyl-coenzyme a: Q23 (≠ P19), A24 (= A20), L25 (vs. gap), A27 (= A22), A63 (= A59), G64 (= G60), A65 (= A61), D66 (= D62), I67 (≠ L63), K68 (≠ N64), M70 (≠ F66), F84 (≠ G82), G107 (= G105), G108 (= G106), E111 (= E109), P130 (= P128), E131 (= E129), P138 (= P136), G139 (≠ C137), M140 (≠ G138)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
38% identity, 96% coverage: 7:253/256 of query aligns to 11:254/255 of 3q0gC
- active site: A65 (= A61), M70 (≠ F66), T80 (≠ A78), F84 (≠ G82), G108 (= G106), E111 (= E109), P130 (= P128), E131 (= E129), V136 (≠ L134), P138 (= P136), G139 (≠ C137), L224 (≠ A223), F234 (= F233)
- binding coenzyme a: L25 (vs. gap), A63 (= A59), I67 (≠ L63), K68 (≠ N64), Y104 (= Y102), P130 (= P128), E131 (= E129), L134 (≠ V132)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
34% identity, 97% coverage: 7:255/256 of query aligns to 14:259/260 of 1dubA
- active site: A68 (= A61), M73 (≠ F66), S83 (≠ A78), L87 (≠ G82), G111 (= G106), E114 (= E109), P133 (= P128), E134 (= E129), T139 (≠ L134), P141 (= P136), G142 (≠ C137), K227 (≠ A223), F237 (= F233)
- binding acetoacetyl-coenzyme a: K26 (≠ P19), A27 (= A20), L28 (vs. gap), A30 (= A22), A66 (= A59), A68 (= A61), D69 (= D62), I70 (≠ L63), Y107 (= Y102), G110 (= G105), G111 (= G106), E114 (= E109), P133 (= P128), E134 (= E129), L137 (≠ V132), G142 (≠ C137), F233 (= F229), F249 (= F245)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
34% identity, 97% coverage: 7:255/256 of query aligns to 12:257/258 of 1ey3A
- active site: A66 (= A61), M71 (≠ F66), S81 (≠ A78), L85 (≠ G82), G109 (= G106), E112 (= E109), P131 (= P128), E132 (= E129), T137 (≠ L134), P139 (= P136), G140 (≠ C137), K225 (≠ A223), F235 (= F233)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ P19), L26 (vs. gap), A28 (= A22), A64 (= A59), G65 (= G60), A66 (= A61), D67 (= D62), I68 (≠ L63), L85 (≠ G82), W88 (≠ F85), G109 (= G106), P131 (= P128), L135 (≠ V132), G140 (≠ C137)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
38% identity, 96% coverage: 7:253/256 of query aligns to 10:249/250 of 3q0gD
- active site: A64 (= A61), M69 (vs. gap), T75 (≠ R71), F79 (≠ G82), G103 (= G106), E106 (= E109), P125 (= P128), E126 (= E129), V131 (≠ L134), P133 (= P136), G134 (≠ C137), L219 (≠ A223), F229 (= F233)
- binding Butyryl Coenzyme A: F225 (= F229), F241 (= 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)
34% identity, 97% coverage: 7:255/256 of query aligns to 44:289/290 of P14604
- E144 (= E109) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E129) 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
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
33% identity, 97% coverage: 7:255/256 of query aligns to 14:259/260 of 2hw5C
- active site: A68 (= A61), M73 (≠ F66), S83 (≠ A78), L87 (≠ G82), G111 (= G106), E114 (= E109), P133 (= P128), E134 (= E129), T139 (≠ L134), P141 (= P136), G142 (≠ C137), K227 (≠ A223), F237 (= F233)
- binding crotonyl coenzyme a: K26 (≠ P19), A27 (= A20), L28 (vs. gap), A30 (= A22), K62 (≠ R55), I70 (≠ L63), F109 (≠ M104)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
34% identity, 97% coverage: 7:255/256 of query aligns to 13:253/254 of 2dubA
- active site: A67 (= A61), M72 (≠ H73), S82 (≠ A83), G105 (= G106), E108 (= E109), P127 (= P128), E128 (= E129), T133 (≠ L134), P135 (= P136), G136 (≠ C137), K221 (≠ A223), F231 (= F233)
- binding octanoyl-coenzyme a: K25 (≠ P19), A26 (= A20), L27 (vs. gap), A29 (= A22), A65 (= A59), A67 (= A61), D68 (= D62), I69 (≠ L63), K70 (≠ R71), G105 (= G106), E108 (= E109), P127 (= P128), E128 (= E129), G136 (≠ C137), A137 (≠ G138)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
33% identity, 97% coverage: 7:255/256 of query aligns to 14:257/258 of 1mj3A
- active site: A68 (= A61), M73 (≠ L76), S83 (≠ E86), L85 (= L88), G109 (= G106), E112 (= E109), P131 (= P128), E132 (= E129), T137 (≠ L134), P139 (= P136), G140 (≠ C137), K225 (≠ A223), F235 (= F233)
- binding hexanoyl-coenzyme a: K26 (≠ P19), A27 (= A20), L28 (vs. gap), A30 (= A22), A66 (= A59), G67 (= G60), A68 (= A61), D69 (= D62), I70 (≠ L63), G109 (= G106), P131 (= P128), E132 (= E129), L135 (≠ V132), G140 (≠ C137)
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)
38% identity, 73% coverage: 10:196/256 of query aligns to 11:190/723 of Q08426
- V40 (≠ N39) to G: in dbSNP:rs1062551
- I41 (≠ A40) to R: in dbSNP:rs1062552
- T75 (≠ R80) to I: in dbSNP:rs1062553
- K165 (≠ R170) 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 (≠ E176) 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
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
36% identity, 95% coverage: 13:254/256 of query aligns to 16:255/257 of 6slbAAA
- active site: Q64 (≠ A61), F69 (= F66), L80 (≠ A74), N84 (≠ G82), A108 (≠ G106), S111 (≠ E109), A130 (≠ P128), F131 (≠ E129), L136 (= L134), P138 (= P136), D139 (≠ C137), A224 (= A223), 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 (= R55), A62 (= A59), Q64 (≠ A61), D65 (= D62), L66 (= L63), Y76 (vs. gap), A108 (≠ G106), F131 (≠ E129), D139 (≠ C137)
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
37% identity, 72% coverage: 9:193/256 of query aligns to 12:201/707 of 6yswA
- active site: A66 (= A61), I71 (≠ F66), A84 (≠ Q79), Q88 (≠ A83), G112 (= G106), E115 (= E109), P136 (= P128), E137 (= E129), G145 (≠ C137)
- binding coenzyme a: E23 (vs. gap), M25 (≠ A20), A66 (= A61), D67 (= D62), I68 (≠ L63), P136 (= P128), E137 (= E129), L140 (≠ V132)
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)
32% identity, 96% coverage: 9:254/256 of query aligns to 20:266/270 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)
31% identity, 97% coverage: 8:255/256 of query aligns to 16:265/266 of O53561
- K135 (≠ Q124) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 124:131, 25% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ G131) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 95% coverage: 13:254/256 of query aligns to 13:243/245 of 6slaAAA
- active site: Q61 (≠ A61), L68 (≠ A74), N72 (≠ G82), A96 (≠ G106), S99 (≠ E109), A118 (≠ P128), F119 (≠ E129), L124 (= L134), P126 (= P136), N127 (≠ C137), A212 (= A223), 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 (vs. gap), A59 (= A59), Q61 (≠ A61), D62 (= D62), L63 (= L63), L68 (≠ A74), Y71 (≠ F81), A94 (≠ M104), G95 (= G105), A96 (≠ G106), F119 (≠ E129), I122 (≠ V132), L124 (= L134), N127 (≠ C137), F234 (= F245), K237 (= K248)
Q9P4U9 Enoyl-CoA hydratase AKT3-1; AF-toxin biosynthesis protein 3-1; EC 4.2.1.17 from Alternaria alternata (Alternaria rot fungus) (Torula alternata) (see paper)
33% identity, 98% coverage: 7:256/256 of query aligns to 23:271/296 of Q9P4U9
Sites not aligning to the query:
- 294:296 Peroxisomal targeting signal type 1
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
36% identity, 74% coverage: 4:192/256 of query aligns to 5:186/692 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
>RR42_RS28550 RR42_RS28550 enoyl-CoA hydratase
MIEHVIDGHIARLTLKRPPANAFNAEGLAQLQQLVATLNADTRVRAIVITGDGSRFFSAG
ADLNGFADGDRAHARLMAQRFGAAFEALQNARPLVIAAINGYAMGGGLECALACDVRIAE
EQAQMALPEAGVGLLPCGCGTQTLPWLVGEGWAKRMILANERIDAATALRIGLVEEMVPT
GQALDAALRLAERASNVSPRAAAYSKQLVHLARQGVPRGPALALERERFVDLFDGEDQRE
GVNAFLQKRAPQWRNA
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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