SitesBLAST
Comparing 3608349 FitnessBrowser__Dino:3608349 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)
4hdtA Crystal structure of a carnitinyl-coa dehydratase from mycobacterium thermoresistibile (see paper)
42% identity, 99% coverage: 3:346/348 of query aligns to 3:340/340 of 4hdtA
- active site: G64 (= G64), I69 (≠ M69), W84 (= W85), Y88 (= Y89), G112 (= G113), G115 (= G116), E135 (= E136), P142 (= P143), D143 (= D144), R283 (= R284)
- binding zinc ion: H28 (≠ Y28), E42 (≠ A42), E57 (= E57), E79 (≠ Y80), H93 (≠ R94), H185 (≠ Q186), E340 (= E346)
3bptA Crystal structure of human beta-hydroxyisobutyryl-coa hydrolase in complex with quercetin
36% identity, 96% coverage: 10:343/348 of query aligns to 13:355/362 of 3bptA
- active site: G67 (= G64), P84 (≠ R82), R88 (= R86), G115 (= G113), G118 (= G116), E138 (= E136), D146 (= D144)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: G66 (= G63), G67 (= G64), I69 (= I66), E90 (= E88), G114 (= G112), G115 (= G113), E138 (= E136), D146 (= D144), V147 (= V145)
- binding 3,5,7,3',4'-pentahydroxyflavone: F25 (≠ A22), L26 (= L23), A28 (= A25), G66 (= G63), G67 (= G64), I69 (= I66), P137 (= P135), I141 (= I139), L319 (≠ V307)
Q9LKJ1 3-hydroxyisobutyryl-CoA hydrolase 1; CoA-thioester hydrolase CHY1; EC 3.1.2.-; EC 3.1.2.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
35% identity, 89% coverage: 15:324/348 of query aligns to 22:344/378 of Q9LKJ1
- G70 (= G64) mutation to S: Loss of activity.
- E142 (= E136) mutation to A: Loss of activity.
- D150 (= D144) mutation to G: Reduced activity.
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
36% identity, 51% coverage: 9:185/348 of query aligns to 13:178/254 of 2dubA
- active site: A67 (≠ G64), M72 (= M69), S82 (≠ R90), G105 (= G113), E108 (≠ G116), P127 (= P135), E128 (= E136), T133 (≠ L141), P135 (= P143), G136 (≠ D144)
- binding octanoyl-coenzyme a: K25 (≠ R21), A26 (= A22), L27 (= L23), A29 (= A25), A65 (= A62), A67 (≠ G64), D68 (= D65), I69 (= I66), K70 (≠ V67), G105 (= G113), E108 (≠ G116), P127 (= P135), E128 (= E136), G136 (≠ D144), A137 (≠ V145)
Sites not aligning to the query:
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
37% identity, 51% coverage: 9:185/348 of query aligns to 14:182/258 of 1mj3A
- active site: A68 (≠ G64), M73 (= M69), S83 (= S79), L85 (≠ R82), G109 (= G113), E112 (≠ G116), P131 (= P135), E132 (= E136), T137 (≠ L141), P139 (= P143), G140 (≠ D144)
- binding hexanoyl-coenzyme a: K26 (≠ R21), A27 (= A22), L28 (= L23), A30 (= A25), A66 (= A62), G67 (= G63), A68 (≠ G64), D69 (= D65), I70 (= I66), G109 (= G113), P131 (= P135), E132 (= E136), L135 (≠ I139), G140 (≠ D144)
Sites not aligning to the query:
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
36% identity, 51% coverage: 9:185/348 of query aligns to 14:184/260 of 2hw5C
- active site: A68 (≠ G64), M73 (= M69), S83 (= S79), L87 (≠ R82), G111 (= G113), E114 (≠ G116), P133 (= P135), E134 (= E136), T139 (≠ L141), P141 (= P143), G142 (≠ D144)
- binding crotonyl coenzyme a: K26 (≠ R21), A27 (= A22), L28 (= L23), A30 (= A25), K62 (= K58), I70 (= I66), F109 (≠ M111)
Sites not aligning to the query:
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
31% identity, 59% coverage: 4:209/348 of query aligns to 6:203/255 of 3q0jC
- active site: A65 (≠ G64), M70 (= M69), T80 (≠ W85), F84 (≠ Y89), G108 (= G113), E111 (≠ G116), P130 (= P135), E131 (= E136), V136 (≠ L141), P138 (= P143), G139 (≠ D144)
- binding acetoacetyl-coenzyme a: Q23 (≠ R21), A24 (= A22), L25 (= L23), A27 (= A25), A63 (= A62), G64 (= G63), A65 (≠ G64), D66 (= D65), I67 (= I66), K68 (≠ V67), M70 (= M69), F84 (≠ Y89), G107 (= G112), G108 (= G113), E111 (≠ G116), P130 (= P135), E131 (= E136), P138 (= P143), G139 (≠ D144), M140 (≠ V145)
Sites not aligning to the query:
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
31% identity, 59% coverage: 4:209/348 of query aligns to 6:203/255 of 3q0gC
- active site: A65 (≠ G64), M70 (= M69), T80 (≠ W85), F84 (≠ Y89), G108 (= G113), E111 (≠ G116), P130 (= P135), E131 (= E136), V136 (≠ L141), P138 (= P143), G139 (≠ D144)
- binding coenzyme a: L25 (= L23), A63 (= A62), I67 (= I66), K68 (≠ V67), Y104 (≠ F109), P130 (= P135), E131 (= E136), L134 (≠ I139)
Sites not aligning to the query:
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
31% identity, 59% coverage: 4:209/348 of query aligns to 5:202/256 of 3h81A
- active site: A64 (≠ G64), M69 (= M69), T79 (≠ W85), F83 (≠ Y89), G107 (= G113), E110 (≠ G116), P129 (= P135), E130 (= E136), V135 (≠ L141), P137 (= P143), G138 (≠ D144)
Sites not aligning to the query:
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
36% identity, 51% coverage: 9:185/348 of query aligns to 14:184/260 of 1dubA
- active site: A68 (≠ G64), M73 (= M69), S83 (= S79), L87 (≠ F84), G111 (= G113), E114 (≠ G116), P133 (= P135), E134 (= E136), T139 (≠ L141), P141 (= P143), G142 (≠ D144)
- binding acetoacetyl-coenzyme a: K26 (≠ R21), A27 (= A22), L28 (= L23), A30 (= A25), A66 (= A62), A68 (≠ G64), D69 (= D65), I70 (= I66), Y107 (≠ F109), G110 (= G112), G111 (= G113), E114 (≠ G116), P133 (= P135), E134 (= E136), L137 (≠ I139), G142 (≠ D144)
Sites not aligning to the query:
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, 51% coverage: 9:185/348 of query aligns to 44:214/290 of P14604
- E144 (≠ G116) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E136) 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
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
36% identity, 51% coverage: 9:185/348 of query aligns to 12:182/258 of 1ey3A
- active site: A66 (≠ G64), M71 (= M69), S81 (= S79), L85 (≠ F84), G109 (= G113), E112 (≠ G116), P131 (= P135), E132 (= E136), T137 (≠ L141), P139 (= P143), G140 (≠ D144)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ R21), L26 (= L23), A28 (= A25), A64 (= A62), G65 (= G63), A66 (≠ G64), D67 (= D65), I68 (= I66), L85 (≠ F84), W88 (≠ D87), G109 (= G113), P131 (= P135), L135 (≠ I139), G140 (≠ D144)
Sites not aligning to the query:
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
31% identity, 56% coverage: 4:198/348 of query aligns to 6:196/259 of 5zaiC
- active site: A65 (≠ G64), F70 (≠ M69), S82 (≠ W85), R86 (≠ Y89), G110 (= G113), E113 (≠ G116), P132 (= P135), E133 (= E136), I138 (≠ L141), P140 (= P143), G141 (≠ D144)
- binding coenzyme a: K24 (≠ A22), L25 (= L23), A63 (= A62), G64 (= G63), A65 (≠ G64), D66 (= D65), I67 (= I66), P132 (= P135), R166 (= R168)
Sites not aligning to the query:
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
30% identity, 59% coverage: 4:209/348 of query aligns to 5:198/250 of 3q0gD
- active site: A64 (≠ G64), M69 (= M69), T75 (≠ W85), F79 (≠ Y89), G103 (= G113), E106 (≠ G116), P125 (= P135), E126 (= E136), V131 (≠ L141), P133 (= P143), G134 (≠ D144)
Sites not aligning to the query:
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 49% coverage: 15:185/348 of query aligns to 16:181/257 of 6slbAAA
- active site: Q64 (≠ G64), F69 (≠ M69), L80 (≠ G81), N84 (≠ Y89), A108 (≠ G113), S111 (≠ G116), A130 (≠ P135), F131 (≠ E136), L136 (= L141), P138 (= P143), D139 (= D144)
- 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 (≠ K58), A62 (= A62), Q64 (≠ G64), D65 (= D65), L66 (≠ I66), Y76 (= Y78), A108 (≠ G113), F131 (≠ E136), D139 (= D144)
Sites not aligning to the query:
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
31% identity, 49% coverage: 15:185/348 of query aligns to 13:169/245 of 6slaAAA
- active site: Q61 (≠ G64), L68 (≠ G81), N72 (≠ Y89), A96 (≠ G113), S99 (≠ G116), A118 (≠ P135), F119 (≠ E136), L124 (= L141), P126 (= P143), N127 (≠ D144)
- 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 (= L23), A59 (= A62), Q61 (≠ G64), D62 (= D65), L63 (≠ I66), L68 (≠ G81), Y71 (≠ F84), A94 (≠ M111), G95 (= G112), A96 (≠ G113), F119 (≠ E136), I122 (= I139), L124 (= L141), N127 (≠ D144)
Sites not aligning to the query:
3rrvB Crystal structure of an enoyl-coa hydratase/isomerase from mycobacterium paratuberculosis (see paper)
30% identity, 52% coverage: 2:182/348 of query aligns to 6:184/254 of 3rrvB
Sites not aligning to the query:
A5JTM5 4-chlorobenzoyl coenzyme A dehalogenase; 4-CBA-CoA dehalogenase; 4-CBCoA dehalogenase; 4-chlorobenzoyl-CoA dehalogenase; EC 3.8.1.7 from Pseudomonas sp. (strain CBS-3) (see 7 papers)
28% identity, 53% coverage: 4:189/348 of query aligns to 5:191/269 of A5JTM5
- R24 (≠ L23) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (≠ A33) mutation to T: Forms inclusion bodies.
- E43 (≠ A42) mutation to A: No effect on catalytic activity.
- D45 (= D44) mutation to A: No effect on catalytic activity.
- D46 (≠ P45) mutation to A: No effect on catalytic activity.
- G63 (= G63) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ G64) mutation to A: 30-fold reduction in catalytic activity, substrate benzoyl group binding is unaffected.; mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to P: Severely reduces catalytic activity. Arylated intermediate does not accumulate.
- Y65 (≠ D65) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (≠ V67) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (= E68) mutation to T: No effect on catalytic activity.
- H81 (≠ D77) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ Y78) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (= W85) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ Y89) active site, Proton acceptor; mutation to Q: Complete loss of catalytic activity (PubMed:8718880, PubMed:9063883). Significantly reduced activity (PubMed:11695894). Substrate binding is not significantly affected. Reduced arylated intermediate formation.
- H94 (≠ A93) mutation to Q: No effect on catalytic activity.
- A112 (≠ M111) mutation to G: Yields insoluble protein.; mutation to S: Protein precipitates upon purification.; mutation to V: Catalytic activity is almost as efficient as wild type.
- G113 (= G112) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding. Arylated intermediate does not accumulate.; mutation G->N,S: Strongly reduced catalytic activity. Arylated intermediate does not accumulate.; mutation to V: Protein precipitates upon purification.
- G114 (= G113) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G114) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (≠ S122) mutation to T: No effect on catalytic activity.
- D129 (≠ E128) mutation to T: No effect on catalytic activity.
- W137 (≠ E136) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D144) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (≠ Y161) mutation to T: No effect on catalytic activity.
- E175 (≠ D173) mutation to D: No effect on catalytic activity.
- W179 (≠ T177) mutation to F: No effect on catalytic activity.
Sites not aligning to the query:
- 208 H→Q: No effect on catalytic activity.
- 216 mutation R->E,K,L: Yields insoluble protein.
- 232 mutation E->A,N,Q,R: Yields insoluble protein.; E→D: Reduced catalytic activity, increased substrate binding.
- 257 R→K: Retains catalytic activity and substrate CoA binding.; R→L: Significantly reduces catalytic activity and substrate CoA binding.
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
33% identity, 41% coverage: 15:156/348 of query aligns to 13:144/692 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
7borA Structure of pseudomonas aeruginosa coa-bound odaa (see paper)
31% identity, 43% coverage: 6:156/348 of query aligns to 4:148/247 of 7borA
- active site: N63 (≠ G64), F68 (≠ M69), D77 (≠ Y78), G81 (≠ R82), I105 (≠ G113), T108 (≠ G116), F128 (≠ E136), L133 (= L141), P135 (= P143), E136 (≠ D144)
- binding coenzyme a: D21 (≠ R21), K22 (≠ A22), A25 (= A25), S61 (≠ A62), I65 (= I66), V103 (≠ M111), F128 (≠ E136), L131 (≠ I139)
Sites not aligning to the query:
Query Sequence
>3608349 FitnessBrowser__Dino:3608349
MSDIAIRIDGRAGRITLNRPRALNALTYEMCLAIDAALRAWAEDPEVALVLIEGAGEKAF
SAGGDIVEMYETGTRGDYSYGRRFWRDEYRMNARIAGYPKPVVSFLQGFTMGGGVGVGCH
GSHRIVGETSQIAMPECGIGLIPDVGGTYLLARAPGRLGEYYGMTGARMGPGDAVLTGFA
SHYLPQADWDAAKAALVETGTVTEMEAACPAPPEARIAPFCAEIDADFNYVFGVEVEAAL
DTRDTEFSRNALLGLRRGAPLSTASALHLIRMARGYADLREALRHEYRWTWRAAEHGDFI
EGIRAQVIDKDRTPRWQHAKLGNVTPEDVRAMVATLGPDELTFEGETP
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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