SitesBLAST
Comparing Ga0059261_3683 FitnessBrowser__Korea:Ga0059261_3683 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)
3bptA Crystal structure of human beta-hydroxyisobutyryl-coa hydrolase in complex with quercetin
40% identity, 99% coverage: 3:343/345 of query aligns to 6:355/362 of 3bptA
- active site: G67 (= G64), P84 (≠ R81), R88 (= R85), G115 (= G112), G118 (= G115), E138 (= E135), D146 (= D143)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: G66 (= G63), G67 (= G64), I69 (= I66), E90 (= E87), G114 (= G111), G115 (= G112), E138 (= E135), D146 (= D143), V147 (= V144)
- binding 3,5,7,3',4'-pentahydroxyflavone: F25 (≠ A22), L26 (≠ I23), A28 (= A25), G66 (= G63), G67 (= G64), I69 (= I66), P137 (= P134), I141 (= I138), L319 (≠ I308)
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)
38% identity, 97% coverage: 2:334/345 of query aligns to 9:353/378 of Q9LKJ1
- G70 (= G64) mutation to S: Loss of activity.
- E142 (= E135) mutation to A: Loss of activity.
- D150 (= D143) mutation to G: Reduced activity.
4hdtA Crystal structure of a carnitinyl-coa dehydratase from mycobacterium thermoresistibile (see paper)
39% identity, 99% coverage: 3:344/345 of query aligns to 3:338/340 of 4hdtA
- active site: G64 (= G64), I69 (= I69), W84 (≠ F84), Y88 (= Y88), G112 (= G112), G115 (= G115), E135 (= E135), P142 (= P142), D143 (= D143), R283 (= R285)
- binding zinc ion: H28 (≠ T28), E42 (≠ R42), E57 (≠ G57), E79 (≠ A79), H93 (≠ A93), H185 (≠ S185)
Sites not aligning to the query:
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
27% identity, 54% coverage: 9:195/345 of query aligns to 11:194/259 of 5zaiC
- active site: A65 (≠ G64), F70 (≠ I69), S82 (≠ F84), R86 (≠ Y88), G110 (= G112), E113 (≠ G115), P132 (= P134), E133 (= E135), I138 (≠ L140), P140 (= P142), G141 (≠ D143)
- binding coenzyme a: K24 (≠ A22), L25 (≠ I23), A63 (= A62), G64 (= G63), A65 (≠ G64), D66 (= D65), I67 (= I66), P132 (= P134), R166 (= R167)
Sites not aligning to the query:
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
28% identity, 68% coverage: 4:238/345 of query aligns to 6:224/255 of 3q0jC
- active site: A65 (≠ G64), M70 (≠ I69), T80 (≠ A79), F84 (= F84), G108 (= G112), E111 (≠ G115), P130 (= P134), E131 (= E135), V136 (≠ L140), P138 (= P142), G139 (≠ D143), L224 (= L238)
- binding acetoacetyl-coenzyme a: Q23 (≠ K21), A24 (= A22), L25 (≠ I23), A27 (= A25), A63 (= A62), G64 (= G63), A65 (≠ G64), D66 (= D65), I67 (= I66), K68 (≠ R67), M70 (≠ I69), F84 (= F84), G107 (= G111), G108 (= G112), E111 (≠ G115), P130 (= P134), E131 (= E135), P138 (= P142), G139 (≠ D143), M140 (≠ V144)
Sites not aligning to the query:
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
28% identity, 68% coverage: 4:238/345 of query aligns to 6:224/255 of 3q0gC
- active site: A65 (≠ G64), M70 (≠ I69), T80 (≠ A79), F84 (= F84), G108 (= G112), E111 (≠ G115), P130 (= P134), E131 (= E135), V136 (≠ L140), P138 (= P142), G139 (≠ D143), L224 (= L238)
- binding coenzyme a: L25 (≠ I23), A63 (= A62), I67 (= I66), K68 (≠ R67), Y104 (≠ I108), P130 (= P134), E131 (= E135), L134 (≠ I138)
Sites not aligning to the query:
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
28% identity, 68% coverage: 4:238/345 of query aligns to 5:223/256 of 3h81A
- active site: A64 (≠ G64), M69 (≠ I69), T79 (≠ A79), F83 (= F84), G107 (= G112), E110 (≠ G115), P129 (= P134), E130 (= E135), V135 (≠ L140), P137 (= P142), G138 (≠ D143), L223 (= L238)
Sites not aligning to the query:
6z1pBI mS93 (see paper)
29% identity, 52% coverage: 1:179/345 of query aligns to 21:201/1413 of 6z1pBI
- active site: T85 (≠ G64), S134 (≠ G112), E157 (= E135), D165 (= D143)
- binding : Y41 (≠ K21), K42 (≠ A22), Q43 (≠ I23), T45 (≠ A25), D47 (≠ N27), H49 (≠ G29), K83 (≠ A62), T85 (≠ G64), D86 (= D65), F87 (≠ I66), K88 (≠ R67), K92 (≠ E71), L130 (≠ I108), K152 (= K130)
Sites not aligning to the query:
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
28% identity, 68% coverage: 4:238/345 of query aligns to 5:219/250 of 3q0gD
- active site: A64 (≠ G64), M69 (= M68), T75 (≠ A74), F79 (= F84), G103 (= G112), E106 (≠ G115), P125 (= P134), E126 (= E135), V131 (≠ L140), P133 (= P142), G134 (≠ D143), L219 (= L238)
Sites not aligning to the query:
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
30% identity, 51% coverage: 12:188/345 of query aligns to 16:182/254 of 2dubA
- active site: A67 (≠ G64), M72 (≠ I69), S82 (≠ Y88), G105 (= G112), E108 (≠ G115), P127 (= P134), E128 (= E135), T133 (≠ L140), P135 (= P142), G136 (≠ D143)
- binding octanoyl-coenzyme a: K25 (= K21), A26 (= A22), L27 (≠ I23), A29 (= A25), A65 (= A62), A67 (≠ G64), D68 (= D65), I69 (= I66), K70 (≠ R67), G105 (= G112), E108 (≠ G115), P127 (= P134), E128 (= E135), G136 (≠ D143), A137 (≠ V144)
Sites not aligning to the query:
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
30% identity, 51% coverage: 12:188/345 of query aligns to 17:186/258 of 1mj3A
- active site: A68 (≠ G64), M73 (≠ I69), S83 (≠ Y88), L85 (≠ M90), G109 (= G112), E112 (≠ G115), P131 (= P134), E132 (= E135), T137 (≠ L140), P139 (= P142), G140 (≠ D143)
- binding hexanoyl-coenzyme a: K26 (= K21), A27 (= A22), L28 (≠ I23), A30 (= A25), A66 (= A62), G67 (= G63), A68 (≠ G64), D69 (= D65), I70 (= I66), G109 (= G112), P131 (= P134), E132 (= E135), L135 (≠ I138), G140 (≠ D143)
Sites not aligning to the query:
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
31% identity, 51% coverage: 12:188/345 of query aligns to 17:188/260 of 2hw5C
- active site: A68 (≠ G64), M73 (≠ I69), S83 (≠ A79), L87 (≠ F84), G111 (= G112), E114 (≠ G115), P133 (= P134), E134 (= E135), T139 (≠ L140), P141 (= P142), G142 (≠ D143)
- binding crotonyl coenzyme a: K26 (= K21), A27 (= A22), L28 (≠ I23), A30 (= A25), K62 (≠ R58), I70 (= I66), F109 (≠ M110)
Sites not aligning to the query:
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
29% identity, 51% coverage: 12:188/345 of query aligns to 15:186/258 of 1ey3A
- active site: A66 (≠ G64), M71 (≠ I69), S81 (≠ A79), L85 (≠ F83), G109 (= G112), E112 (≠ G115), P131 (= P134), E132 (= E135), T137 (≠ L140), P139 (= P142), G140 (≠ D143)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K21), L26 (≠ I23), A28 (= A25), A64 (= A62), G65 (= G63), A66 (≠ G64), D67 (= D65), I68 (= I66), L85 (≠ F83), W88 (≠ V86), G109 (= G112), P131 (= P134), L135 (≠ I138), G140 (≠ D143)
Sites not aligning to the query:
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
29% identity, 51% coverage: 12:188/345 of query aligns to 17:188/260 of 1dubA
- active site: A68 (≠ G64), M73 (≠ I69), S83 (≠ A79), L87 (≠ F83), G111 (= G112), E114 (≠ G115), P133 (= P134), E134 (= E135), T139 (≠ L140), P141 (= P142), G142 (≠ D143)
- binding acetoacetyl-coenzyme a: K26 (= K21), A27 (= A22), L28 (≠ I23), A30 (= A25), A66 (= A62), A68 (≠ G64), D69 (= D65), I70 (= I66), Y107 (≠ I108), G110 (= G111), G111 (= G112), E114 (≠ G115), P133 (= P134), E134 (= E135), L137 (≠ I138), G142 (≠ D143)
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)
29% identity, 51% coverage: 12:188/345 of query aligns to 47:218/290 of P14604
- E144 (≠ G115) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E135) 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
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, 51% coverage: 15:191/345 of query aligns to 14:181/723 of Q08426
- V40 (≠ R42) to G: in dbSNP:rs1062551
- I41 (≠ D43) to R: in dbSNP:rs1062552
- T75 (≠ V86) to I: in dbSNP:rs1062553
- K165 (≠ A175) 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 (≠ H181) 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
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)
31% identity, 50% coverage: 8:180/345 of query aligns to 9:183/269 of A5JTM5
- R24 (≠ I23) 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 (≠ R42) mutation to A: No effect on catalytic activity.
- D45 (= D44) mutation to A: No effect on catalytic activity.
- D46 (≠ T45) 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 (= R67) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (≠ M68) mutation to T: No effect on catalytic activity.
- H81 (≠ F83) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (= F84) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (≠ E87) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ Y88) 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 (= H92) mutation to Q: No effect on catalytic activity.
- A112 (≠ M110) 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 (= G111) 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 (= G112) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G113) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (≠ K121) mutation to T: No effect on catalytic activity.
- D129 (≠ E127) mutation to T: No effect on catalytic activity.
- W137 (≠ E135) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D143) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (≠ Y160) mutation to T: No effect on catalytic activity.
- E175 (= E172) mutation to D: No effect on catalytic activity.
- W179 (≠ L176) 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.
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
31% identity, 50% coverage: 8:180/345 of query aligns to 9:183/269 of 1nzyB
- active site: C61 (= C61), F64 (≠ G64), I69 (= I69), A86 (vs. gap), H90 (≠ Y88), G114 (= G112), G117 (= G115), A136 (≠ P134), W137 (≠ E135), I142 (≠ L140), N144 (≠ P142), D145 (= D143)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ K21), H23 (≠ A22), R24 (≠ I23), A62 (= A62), F64 (≠ G64), Y65 (≠ D65), L66 (≠ I66), R67 (= R67), W89 (vs. gap), G113 (= G111), G114 (= G112), A136 (≠ P134), W137 (≠ E135), D145 (= D143), T146 (≠ V144)
- binding calcium ion: G49 (≠ E48)
- binding phosphate ion: E57 (= E56), N108 (≠ D106)
Sites not aligning to the query:
1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
31% identity, 50% coverage: 8:180/345 of query aligns to 9:183/269 of 1jxzB
- active site: C61 (= C61), F64 (≠ G64), I69 (= I69), A86 (vs. gap), Q90 (≠ Y88), G113 (= G111), G114 (= G112), G117 (= G115), A136 (≠ P134), W137 (≠ E135), I142 (≠ L140), N144 (≠ P142), D145 (= D143)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ K21), H23 (≠ A22), R24 (≠ I23), A62 (= A62), F64 (≠ G64), Y65 (≠ D65), L66 (≠ I66), R67 (= R67), W89 (vs. gap), G113 (= G111), A136 (≠ P134), W137 (≠ E135), I142 (≠ L140), D145 (= D143), T146 (≠ V144)
- binding calcium ion: G49 (≠ E48)
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)
29% identity, 60% coverage: 3:209/345 of query aligns to 9:220/266 of O53561
- K135 (= K130) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 130:137, 25% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ G137) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
Query Sequence
>Ga0059261_3683 FitnessBrowser__Korea:Ga0059261_3683
MSDVLISVEGQVGRIRLNRPKAIHALNTGMCAAILDALISWRDDTAVEVVMIDHAEGRGF
CAGGDIRMIAESGAGDGSAARDFFRVEYRMNHALFTYAKPVVAFMDGITMGGGVGISQPA
KYRVATENTKLAMPETGIGLFPDVGGGWYLSRLAGRTGQYLALTGHRLDGAECLALGLAS
HYLHSEALEDAKARIIADPQAIDAVLDALSSPAPDARILAHRGAIDRLFASDRLEDVLAA
LEADGGEWAAQQLATLRTKSPQTMKVSLKLLLDGKTMPTFEDEMRQEFAVGSHVVQRHDF
IEGVRALIIDKDNAPKWNPANVEEVSDHLIDQIFAPLSADQQWEP
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