SitesBLAST
Comparing RR42_RS12795 FitnessBrowser__Cup4G11:RR42_RS12795 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, 93% coverage: 14:350/362 of query aligns to 12:347/362 of 3bptA
- active site: G67 (= G69), P84 (≠ D86), R88 (≠ V90), G115 (= G117), G118 (= G120), E138 (= E140), D146 (= D148)
- binding (2r)-3-hydroxy-2-methylpropanoic acid: G66 (= G68), G67 (= G69), I69 (= I71), E90 (= E92), G114 (= G116), G115 (= G117), E138 (= E140), D146 (= D148), V147 (= V149)
- binding 3,5,7,3',4'-pentahydroxyflavone: F25 (≠ A27), L26 (= L28), A28 (= A30), G66 (= G68), G67 (= G69), I69 (= I71), P137 (= P139), I141 (= I143), L319 (≠ A322)
4hdtA Crystal structure of a carnitinyl-coa dehydratase from mycobacterium thermoresistibile (see paper)
43% identity, 93% coverage: 12:348/362 of query aligns to 7:328/340 of 4hdtA
- active site: G64 (= G69), I69 (≠ F74), W84 (≠ F89), Y88 (= Y93), G112 (= G117), G115 (= G120), E135 (= E140), P142 (= P147), D143 (= D148), R283 (= R299)
- binding zinc ion: H28 (≠ L33), E42 (≠ A47), E57 (≠ G62), E79 (≠ A84), H93 (≠ L98), H185 (≠ G190)
Sites not aligning to the query:
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)
37% identity, 93% coverage: 14:349/362 of query aligns to 16:354/378 of Q9LKJ1
- G70 (= G69) mutation to S: Loss of activity.
- E142 (= E140) mutation to A: Loss of activity.
- D150 (= D148) mutation to G: Reduced activity.
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
33% identity, 50% coverage: 9:189/362 of query aligns to 6:183/259 of 5zaiC
- active site: A65 (≠ G69), F70 (= F74), S82 (≠ F89), R86 (≠ Y93), G110 (= G117), E113 (≠ G120), P132 (= P139), E133 (= E140), I138 (≠ L145), P140 (= P147), G141 (≠ D148)
- binding coenzyme a: K24 (≠ A27), L25 (= L28), A63 (= A67), G64 (= G68), A65 (≠ G69), D66 (= D70), I67 (= I71), P132 (= P139), R166 (≠ M172)
Sites not aligning to the query:
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
34% identity, 53% coverage: 3:195/362 of query aligns to 4:190/260 of 2hw5C
- active site: A68 (≠ G69), M73 (≠ F74), S83 (≠ D86), L87 (≠ V90), G111 (= G117), E114 (≠ G120), P133 (= P139), E134 (= E140), T139 (≠ L145), P141 (= P147), G142 (≠ D148)
- binding crotonyl coenzyme a: K26 (≠ Q26), A27 (= A27), L28 (= L28), A30 (= A30), K62 (= K63), I70 (= I71), F109 (≠ M115)
Sites not aligning to the query:
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
33% identity, 53% coverage: 5:195/362 of query aligns to 6:188/258 of 1mj3A
- active site: A68 (≠ G69), M73 (≠ F74), S83 (≠ A94), L85 (= L95), G109 (= G117), E112 (≠ G120), P131 (= P139), E132 (= E140), T137 (≠ L145), P139 (= P147), G140 (≠ D148)
- binding hexanoyl-coenzyme a: K26 (≠ Q26), A27 (= A27), L28 (= L28), A30 (= A30), A66 (= A67), G67 (= G68), A68 (≠ G69), D69 (= D70), I70 (= I71), G109 (= G117), P131 (= P139), E132 (= E140), L135 (≠ I143), G140 (≠ D148)
Sites not aligning to the query:
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
33% identity, 53% coverage: 5:195/362 of query aligns to 5:184/254 of 2dubA
- active site: A67 (≠ G69), M72 (≠ F74), S82 (≠ A94), G105 (= G117), E108 (≠ G120), P127 (= P139), E128 (= E140), T133 (≠ L145), P135 (= P147), G136 (≠ D148)
- binding octanoyl-coenzyme a: K25 (≠ Q26), A26 (= A27), L27 (= L28), A29 (= A30), A65 (= A67), A67 (≠ G69), D68 (= D70), I69 (= I71), K70 (≠ R72), G105 (= G117), E108 (≠ G120), P127 (= P139), E128 (= E140), G136 (≠ D148), A137 (≠ V149)
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)
32% identity, 53% coverage: 5:195/362 of query aligns to 36:220/290 of P14604
- E144 (≠ G120) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E140) 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
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
32% identity, 53% coverage: 5:195/362 of query aligns to 6:190/260 of 1dubA
- active site: A68 (≠ G69), M73 (≠ F74), S83 (≠ A94), L87 (= L98), G111 (= G117), E114 (≠ G120), P133 (= P139), E134 (= E140), T139 (≠ L145), P141 (= P147), G142 (≠ D148)
- binding acetoacetyl-coenzyme a: K26 (≠ Q26), A27 (= A27), L28 (= L28), A30 (= A30), A66 (= A67), A68 (≠ G69), D69 (= D70), I70 (= I71), Y107 (≠ V113), G110 (= G116), G111 (= G117), E114 (≠ G120), P133 (= P139), E134 (= E140), L137 (≠ I143), G142 (≠ D148)
Sites not aligning to the query:
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
32% identity, 53% coverage: 5:195/362 of query aligns to 4:188/258 of 1ey3A
- active site: A66 (≠ G69), M71 (≠ F74), S81 (≠ A94), L85 (= L98), G109 (= G117), E112 (≠ G120), P131 (= P139), E132 (= E140), T137 (≠ L145), P139 (= P147), G140 (≠ D148)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ Q26), L26 (= L28), A28 (= A30), A64 (= A67), G65 (= G68), A66 (≠ G69), D67 (= D70), I68 (= I71), L85 (= L98), W88 (vs. gap), G109 (= G117), P131 (= P139), L135 (≠ I143), G140 (≠ D148)
Sites not aligning to the query:
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
32% identity, 48% coverage: 17:191/362 of query aligns to 14:183/255 of 3q0jC
- active site: A65 (≠ G69), M70 (≠ F74), T80 (≠ F89), F84 (≠ Y93), G108 (= G117), E111 (≠ G120), P130 (= P139), E131 (= E140), V136 (≠ L145), P138 (= P147), G139 (≠ D148)
- binding acetoacetyl-coenzyme a: Q23 (= Q26), A24 (= A27), L25 (= L28), A27 (= A30), A63 (= A67), G64 (= G68), A65 (≠ G69), D66 (= D70), I67 (= I71), K68 (≠ R72), M70 (≠ F74), F84 (≠ Y93), G107 (= G116), G108 (= G117), E111 (≠ G120), P130 (= P139), E131 (= E140), P138 (= P147), G139 (≠ D148), M140 (≠ V149)
Sites not aligning to the query:
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 48% coverage: 17:191/362 of query aligns to 14:183/255 of 3q0gC
- active site: A65 (≠ G69), M70 (≠ F74), T80 (≠ F89), F84 (≠ Y93), G108 (= G117), E111 (≠ G120), P130 (= P139), E131 (= E140), V136 (≠ L145), P138 (= P147), G139 (≠ D148)
- binding coenzyme a: L25 (= L28), A63 (= A67), I67 (= I71), K68 (≠ R72), Y104 (≠ V113), P130 (= P139), E131 (= E140), L134 (≠ I143)
Sites not aligning to the query:
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
32% identity, 48% coverage: 17:191/362 of query aligns to 13:182/256 of 3h81A
- active site: A64 (≠ G69), M69 (≠ F74), T79 (≠ F89), F83 (≠ Y93), G107 (= G117), E110 (≠ G120), P129 (= P139), E130 (= E140), V135 (≠ L145), P137 (= P147), G138 (≠ D148)
Sites not aligning to the query:
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
31% identity, 48% coverage: 17:191/362 of query aligns to 13:178/250 of 3q0gD
- active site: A64 (≠ G69), M69 (≠ F74), T75 (≠ F89), F79 (≠ Y93), G103 (= G117), E106 (≠ G120), P125 (= P139), E126 (= E140), V131 (≠ L145), P133 (= P147), G134 (≠ D148)
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)
34% identity, 50% coverage: 20:199/362 of query aligns to 21:201/266 of O53561
- K135 (= K135) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 135:142, 25% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (≠ N142) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
6z1pBI mS93 (see paper)
30% identity, 47% coverage: 15:184/362 of query aligns to 30:201/1413 of 6z1pBI
- active site: T85 (≠ G69), S134 (≠ G117), E157 (= E140), D165 (= D148)
- binding : Y41 (≠ Q26), K42 (≠ A27), Q43 (≠ L28), T45 (≠ A30), D47 (≠ S32), H49 (≠ E34), K83 (≠ A67), T85 (≠ G69), D86 (= D70), F87 (≠ I71), K88 (≠ R72), K92 (= K76), L130 (≠ V113), K152 (= K135)
Sites not aligning to the query:
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
32% identity, 42% coverage: 10:160/362 of query aligns to 3:144/692 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
1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
30% identity, 52% coverage: 9:196/362 of query aligns to 5:194/269 of 1jxzB
- active site: C61 (= C66), F64 (≠ G69), I69 (≠ F74), A86 (≠ E92), Q90 (≠ N96), G113 (= G116), G114 (= G117), G117 (= G120), A136 (≠ P139), W137 (≠ E140), I142 (≠ L145), N144 (≠ P147), D145 (= D148)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ Q26), H23 (≠ A27), R24 (≠ L28), A62 (= A67), F64 (≠ G69), Y65 (≠ D70), L66 (≠ I71), R67 (= R72), W89 (≠ L95), G113 (= G116), A136 (≠ P139), W137 (≠ E140), I142 (≠ L145), D145 (= D148), T146 (≠ V149)
- binding calcium ion: G49 (≠ A53)
Sites not aligning to the query:
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
30% identity, 52% coverage: 9:196/362 of query aligns to 5:194/269 of 1nzyB
- active site: C61 (= C66), F64 (≠ G69), I69 (≠ F74), A86 (≠ E92), H90 (≠ N96), G114 (= G117), G117 (= G120), A136 (≠ P139), W137 (≠ E140), I142 (≠ L145), N144 (≠ P147), D145 (= D148)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ Q26), H23 (≠ A27), R24 (≠ L28), A62 (= A67), F64 (≠ G69), Y65 (≠ D70), L66 (≠ I71), R67 (= R72), W89 (≠ L95), G113 (= G116), G114 (= G117), A136 (≠ P139), W137 (≠ E140), D145 (= D148), T146 (≠ V149)
- binding calcium ion: G49 (≠ A53)
- binding phosphate ion: E57 (≠ G62), N108 (≠ D111), K188 (≠ G190), R192 (≠ A194)
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)
30% identity, 52% coverage: 9:196/362 of query aligns to 5:194/269 of A5JTM5
- R24 (≠ L28) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (≠ A38) mutation to T: Forms inclusion bodies.
- E43 (≠ A47) mutation to A: No effect on catalytic activity.
- D45 (≠ A49) mutation to A: No effect on catalytic activity.
- D46 (≠ P50) mutation to A: No effect on catalytic activity.
- G63 (= G68) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ G69) 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 (≠ D70) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (= R72) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (≠ F73) mutation to T: No effect on catalytic activity.
- H81 (≠ Q87) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (= F88) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (≠ L95) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ N96) 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 (= H100) mutation to Q: No effect on catalytic activity.
- A112 (≠ M115) 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 (= G116) 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 (= G117) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G118) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (≠ R126) mutation to T: No effect on catalytic activity.
- D129 (≠ E132) mutation to T: No effect on catalytic activity.
- W137 (≠ E140) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D148) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (≠ Y165) mutation to T: No effect on catalytic activity.
- E175 (≠ D177) mutation to D: No effect on catalytic activity.
- W179 (≠ A181) 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.
Query Sequence
>RR42_RS12795 FitnessBrowser__Cup4G11:RR42_RS12795
MTDLVTSEIQGRIEGGIGYLTLNRPQALNALSLEMIRAITQALNAWAVAPEVAAVVIAGA
GGKAFCAGGDIRFFHKAALAGDPALDQFFVEEYALNHLIHTYAKPYIALMDGVVMGGGMG
ISQGARRRLVTERTKMAMPETNIGLFPDVGGGWFLSRTPGRLGEYLGLTGAMIHAADALY
AGLADAYLPGNAMAELVEVLRARQFADGDAVLACVDEATAAHRAACPPGESQLAKLQEEI
DGLFAGASVTGIVAAVSDAGSDWAAQTAAMLRTRSPLMLNVTLEQIRRARTMALNDELRM
ELDMMYHVFRHGDGVEGIRALAVDKDHAPKWQPARLDEVTRERVHAFFDSPWAHGEHPLA
AL
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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