SitesBLAST
Comparing WP_084235836.1 NCBI__GCF_001592305.1:WP_084235836.1 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)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
42% identity, 97% coverage: 8:267/268 of query aligns to 3:256/257 of 6slbAAA
- active site: Q64 (≠ A69), F69 (= F74), L80 (≠ K84), N84 (= N97), A108 (= A121), S111 (= S124), A130 (= A143), F131 (= F144), L136 (= L149), P138 (= P151), D139 (= D152), A224 (≠ D235), G234 (= G245)
- 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 (= R63), A62 (= A67), Q64 (≠ A69), D65 (= D70), L66 (= L71), Y76 (≠ P80), A108 (= A121), F131 (= F144), D139 (= D152)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
41% identity, 93% coverage: 18:267/268 of query aligns to 10:244/245 of 6slaAAA
- active site: Q61 (≠ A69), L68 (≠ F76), N72 (= N97), A96 (= A121), S99 (= S124), A118 (= A143), F119 (= F144), L124 (= L149), P126 (= P151), N127 (≠ D152), A212 (≠ D235), G222 (= G245)
- 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 (= L29), A59 (= A67), Q61 (≠ A69), D62 (= D70), L63 (= L71), L68 (≠ F76), Y71 (≠ F96), A94 (= A119), G95 (= G120), A96 (= A121), F119 (= F144), I122 (= I147), L124 (= L149), N127 (≠ D152), F234 (= F257), K237 (= K260)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
34% identity, 97% coverage: 9:268/268 of query aligns to 5:259/259 of 5zaiC
- active site: A65 (= A69), F70 (= F74), S82 (≠ A86), R86 (≠ P90), G110 (≠ A121), E113 (≠ S124), P132 (≠ A143), E133 (≠ F144), I138 (≠ L149), P140 (= P151), G141 (≠ D152), A226 (≠ D235), F236 (≠ G245)
- binding coenzyme a: K24 (≠ A28), L25 (= L29), A63 (= A67), G64 (= G68), A65 (= A69), D66 (= D70), I67 (≠ L71), P132 (≠ A143), R166 (≠ K177), F248 (= F257), K251 (= K260)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
36% identity, 96% coverage: 9:265/268 of query aligns to 5:254/255 of 3q0jC
- active site: A65 (= A69), M70 (≠ F74), T80 (≠ H93), F84 (≠ N97), G108 (≠ A121), E111 (≠ S124), P130 (≠ A143), E131 (≠ F144), V136 (≠ L149), P138 (= P151), G139 (≠ D152), L224 (≠ D235), F234 (≠ G245)
- binding acetoacetyl-coenzyme a: Q23 (≠ E27), A24 (= A28), L25 (= L29), A27 (≠ S31), A63 (= A67), G64 (= G68), A65 (= A69), D66 (= D70), I67 (≠ L71), K68 (≠ A72), M70 (≠ F74), F84 (≠ N97), G107 (= G120), G108 (≠ A121), E111 (≠ S124), P130 (≠ A143), E131 (≠ F144), P138 (= P151), G139 (≠ D152), M140 (≠ A153)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
36% identity, 96% coverage: 9:265/268 of query aligns to 5:254/255 of 3q0gC
- active site: A65 (= A69), M70 (≠ F74), T80 (≠ H93), F84 (≠ N97), G108 (≠ A121), E111 (≠ S124), P130 (≠ A143), E131 (≠ F144), V136 (≠ L149), P138 (= P151), G139 (≠ D152), L224 (≠ D235), F234 (≠ G245)
- binding coenzyme a: L25 (= L29), A63 (= A67), I67 (≠ L71), K68 (≠ A72), Y104 (≠ V117), P130 (≠ A143), E131 (≠ F144), L134 (≠ I147)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
36% identity, 96% coverage: 9:265/268 of query aligns to 4:253/256 of 3h81A
- active site: A64 (= A69), M69 (≠ F74), T79 (≠ H93), F83 (≠ N97), G107 (≠ A121), E110 (≠ S124), P129 (≠ A143), E130 (≠ F144), V135 (≠ L149), P137 (= P151), G138 (≠ D152), L223 (≠ D235), F233 (≠ G245)
- binding calcium ion: F233 (≠ G245), Q238 (≠ Y250)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
36% identity, 96% coverage: 9:265/268 of query aligns to 4:249/250 of 3q0gD
- active site: A64 (= A69), M69 (≠ F74), T75 (≠ H93), F79 (≠ N97), G103 (≠ A121), E106 (≠ S124), P125 (≠ A143), E126 (≠ F144), V131 (≠ L149), P133 (= P151), G134 (≠ D152), L219 (≠ D235), F229 (≠ G245)
- binding Butyryl Coenzyme A: F225 (≠ Q241), F241 (= F257)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
35% identity, 94% coverage: 14:266/268 of query aligns to 12:252/254 of 2dubA
- active site: A67 (= A69), M72 (≠ F74), S82 (≠ K84), G105 (≠ A121), E108 (≠ S124), P127 (≠ A143), E128 (≠ F144), T133 (≠ L149), P135 (= P151), G136 (≠ D152), K221 (≠ D235), F231 (≠ G245)
- binding octanoyl-coenzyme a: K25 (≠ E27), A26 (= A28), L27 (= L29), A29 (≠ S31), A65 (= A67), A67 (= A69), D68 (= D70), I69 (≠ L71), K70 (≠ A72), G105 (≠ A121), E108 (≠ S124), P127 (≠ A143), E128 (≠ F144), G136 (≠ D152), A137 (= A153)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
35% identity, 95% coverage: 14:268/268 of query aligns to 13:260/260 of 2hw5C
- active site: A68 (= A69), M73 (≠ F74), S83 (≠ H93), L87 (≠ N97), G111 (≠ A121), E114 (≠ S124), P133 (≠ A143), E134 (≠ F144), T139 (≠ L149), P141 (= P151), G142 (≠ D152), K227 (≠ D235), F237 (≠ G245)
- binding crotonyl coenzyme a: K26 (≠ E27), A27 (= A28), L28 (= L29), A30 (≠ S31), K62 (≠ R63), I70 (≠ L71), F109 (≠ A119)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
35% identity, 94% coverage: 14:266/268 of query aligns to 11:256/258 of 1ey3A
- active site: A66 (= A69), M71 (≠ F74), S81 (≠ H93), L85 (≠ N97), G109 (≠ A121), E112 (≠ S124), P131 (≠ A143), E132 (≠ F144), T137 (≠ L149), P139 (= P151), G140 (≠ D152), K225 (≠ D235), F235 (≠ G245)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E27), L26 (= L29), A28 (≠ S31), A64 (= A67), G65 (= G68), A66 (= A69), D67 (= D70), I68 (≠ L71), L85 (≠ N97), W88 (≠ A100), G109 (≠ A121), P131 (≠ A143), L135 (≠ I147), G140 (≠ D152)
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, 98% coverage: 5:266/268 of query aligns to 28:288/290 of P14604
- E144 (≠ S124) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ F144) 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)
35% identity, 94% coverage: 14:266/268 of query aligns to 13:258/260 of 1dubA
- active site: A68 (= A69), M73 (≠ F74), S83 (≠ H93), L87 (≠ N97), G111 (≠ A121), E114 (≠ S124), P133 (≠ A143), E134 (≠ F144), T139 (≠ L149), P141 (= P151), G142 (≠ D152), K227 (≠ D235), F237 (≠ G245)
- binding acetoacetyl-coenzyme a: K26 (≠ E27), A27 (= A28), L28 (= L29), A30 (≠ S31), A66 (= A67), A68 (= A69), D69 (= D70), I70 (≠ L71), Y107 (≠ V117), G110 (= G120), G111 (≠ A121), E114 (≠ S124), P133 (≠ A143), E134 (≠ F144), L137 (≠ I147), G142 (≠ D152), F233 (≠ Q241), F249 (= F257)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
35% identity, 94% coverage: 14:266/268 of query aligns to 13:256/258 of 1mj3A
- active site: A68 (= A69), M73 (≠ F74), S83 (≠ G89), L85 (≠ V91), G109 (≠ A121), E112 (≠ S124), P131 (≠ A143), E132 (≠ F144), T137 (≠ L149), P139 (= P151), G140 (≠ D152), K225 (≠ D235), F235 (≠ G245)
- binding hexanoyl-coenzyme a: K26 (≠ E27), A27 (= A28), L28 (= L29), A30 (≠ S31), A66 (= A67), G67 (= G68), A68 (= A69), D69 (= D70), I70 (≠ L71), G109 (≠ A121), P131 (≠ A143), E132 (≠ F144), L135 (≠ I147), G140 (≠ D152)
O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
32% identity, 97% coverage: 6:266/268 of query aligns to 6:264/266 of O53561
- K135 (≠ S139) modified: N6-succinyllysine; mutation to E: Nearly wild-type levels of succinylation in vitro, reduces specific activity 8-fold.
- 135:142 (vs. 139:146, 25% identical) mutation to EFGISEAE: Very low levels of succinylation in vitro, reduces specific activity 15-fold.
- K142 (= K146) modified: N6-succinyllysine; mutation to E: About 50% succinylation in vitro, reduces specific activity 7-fold.
3rrvB Crystal structure of an enoyl-coa hydratase/isomerase from mycobacterium paratuberculosis (see paper)
36% identity, 88% coverage: 16:250/268 of query aligns to 14:243/254 of 3rrvB
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
32% identity, 94% coverage: 15:267/268 of query aligns to 12:260/261 of 5jbxB
- active site: A67 (= A69), R72 (≠ D81), L84 (≠ H93), R88 (≠ N97), G112 (≠ A121), E115 (≠ S124), T134 (≠ A143), E135 (≠ F144), I140 (≠ L149), P142 (= P151), G143 (≠ D152), A228 (≠ D235), L238 (≠ G245)
- binding coenzyme a: S24 (≠ E27), R25 (≠ A28), R26 (≠ L29), A28 (≠ S31), A65 (= A67), D68 (= D70), L69 (= L71), K70 (≠ A72), L110 (≠ A119), G111 (= G120), T134 (≠ A143), E135 (≠ F144), L138 (≠ I147), R168 (≠ K177)
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)
34% identity, 75% coverage: 18:219/268 of query aligns to 13:214/269 of A5JTM5
- R24 (≠ L29) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (≠ D39) mutation to T: Forms inclusion bodies.
- E43 (= E48) mutation to A: No effect on catalytic activity.
- D45 (≠ N50) mutation to A: No effect on catalytic activity.
- D46 (≠ P51) mutation to A: No effect on catalytic activity.
- G63 (= G68) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ A69) 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 (≠ A72) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (= E73) mutation to T: No effect on catalytic activity.
- H81 (≠ P88) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ G89) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (≠ F96) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ N97) 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 (≠ R101) mutation to Q: No effect on catalytic activity.
- A112 (= A119) 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 (= G120) 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 (≠ A121) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G122) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D130) mutation to T: No effect on catalytic activity.
- D129 (≠ P136) mutation to T: No effect on catalytic activity.
- W137 (≠ F144) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D152) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (≠ A170) mutation to T: No effect on catalytic activity.
- E175 (≠ Q182) mutation to D: No effect on catalytic activity.
- W179 (= W186) mutation to F: No effect on catalytic activity.
- H208 (≠ K213) mutation to Q: No effect on catalytic activity.
Sites not aligning to the query:
- 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.
1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
34% identity, 75% coverage: 18:219/268 of query aligns to 13:214/269 of 1jxzB
- active site: C61 (= C66), F64 (≠ A69), I69 (≠ F74), A86 (≠ H93), Q90 (≠ N97), G113 (= G120), G114 (≠ A121), G117 (≠ S124), A136 (= A143), W137 (≠ F144), I142 (≠ L149), N144 (≠ P151), D145 (= D152)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ E27), H23 (≠ A28), R24 (≠ L29), A62 (= A67), F64 (≠ A69), Y65 (≠ D70), L66 (= L71), R67 (≠ A72), W89 (≠ F96), G113 (= G120), A136 (= A143), W137 (≠ F144), I142 (≠ L149), D145 (= D152), T146 (≠ A153)
- binding calcium ion: G49 (≠ R54), L202 (= L207), A203 (= A208), A205 (≠ M210), T207 (= T212), Q210 (≠ L215)
Sites not aligning to the query:
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
34% identity, 75% coverage: 18:219/268 of query aligns to 13:214/269 of 1nzyB
- active site: C61 (= C66), F64 (≠ A69), I69 (≠ F74), A86 (≠ H93), H90 (≠ N97), G114 (≠ A121), G117 (≠ S124), A136 (= A143), W137 (≠ F144), I142 (≠ L149), N144 (≠ P151), D145 (= D152)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ E27), H23 (≠ A28), R24 (≠ L29), A62 (= A67), F64 (≠ A69), Y65 (≠ D70), L66 (= L71), R67 (≠ A72), W89 (≠ F96), G113 (= G120), G114 (≠ A121), A136 (= A143), W137 (≠ F144), D145 (= D152), T146 (≠ A153)
- binding calcium ion: G49 (≠ R54), L202 (= L207), A203 (= A208), A205 (≠ M210), T207 (= T212), Q210 (≠ L215)
- binding phosphate ion: E57 (≠ G62), N108 (= N115), K188 (≠ Q193), R192 (≠ L197)
Sites not aligning to the query:
5du6A Crystal structure of m. Tuberculosis echa6 bound to ligand gsk059a. (see paper)
33% identity, 93% coverage: 18:267/268 of query aligns to 11:241/242 of 5du6A
- active site: A61 (= A69), P71 (≠ G79), I75 (≠ V83), A99 (= A121), Q102 (≠ S124), P121 (≠ A143), T122 (≠ F144), L127 (= L149), L129 (≠ P151), D130 (= D152), P209 (≠ D235), W219 (≠ G245)
- binding (5R,7R)-5-(4-ethylphenyl)-N-(4-fluorobenzyl)-7-methyl-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L74 (= L82), D82 (≠ N97), D130 (= D152), W132 (≠ G154), A207 (≠ Q233), K212 (≠ R238), F215 (≠ Q241)
Query Sequence
>WP_084235836.1 NCBI__GCF_001592305.1:WP_084235836.1
MNAPAAGGTVLYLERGTVALITLNRPEALNSFTRQMHHDLWAALDRAEANPLVRALVLTG
AGRGFCAGADLAEFDFEPGPDLVKRADPGPVIHQAFNPTARRIQSLRMPVIAAVNGVAAG
AGASLAMTCDIAIAAPGASFIQAFSKIGLIPDAGGSWFLVERLGLARAMALAMTGDKLPA
AQAKEWGMIWDVQDDPLAAALALAEKLAVMPTKALVSTRTLLRDAGTRTLNQQLDVERDT
QSALGATHDYIEGVMAFRQKRAPQFKGE
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