SitesBLAST
Comparing WP_011445547.1 NCBI__GCF_000013325.1:WP_011445547.1 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)
44% identity, 98% coverage: 6:260/260 of query aligns to 5:257/257 of 6slbAAA
- active site: Q64 (≠ A62), F69 (≠ R67), L80 (≠ T83), N84 (= N87), A108 (≠ V111), S111 (= S114), A130 (= A133), F131 (= F134), L136 (= L139), P138 (= P141), D139 (= D142), A224 (≠ L227), G234 (= G237)
- 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 (= R56), A62 (≠ S60), Q64 (≠ A62), D65 (= D63), L66 (= L64), Y76 (= Y79), A108 (≠ V111), F131 (= F134), D139 (= D142)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
42% identity, 98% coverage: 6:260/260 of query aligns to 2:245/245 of 6slaAAA
- active site: Q61 (≠ A62), L68 (≠ T83), N72 (= N87), A96 (≠ V111), S99 (= S114), A118 (= A133), F119 (= F134), L124 (= L139), P126 (= P141), N127 (≠ D142), A212 (≠ L227), G222 (= G237)
- 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 (= L25), A59 (≠ S60), Q61 (≠ A62), D62 (= D63), L63 (= L64), L68 (≠ T83), Y71 (= Y86), A94 (= A109), G95 (= G110), A96 (≠ V111), F119 (= F134), I122 (= I137), L124 (= L139), N127 (≠ D142), F234 (= F249), K237 (= K252)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
35% identity, 100% coverage: 1:260/260 of query aligns to 1:259/259 of 5zaiC
- active site: A65 (= A62), F70 (≠ R67), S82 (≠ T83), R86 (≠ N87), G110 (≠ V111), E113 (≠ S114), P132 (≠ A133), E133 (≠ F134), I138 (≠ L139), P140 (= P141), G141 (≠ D142), A226 (≠ L227), F236 (≠ G237)
- binding coenzyme a: K24 (≠ R24), L25 (= L25), A63 (≠ S60), G64 (= G61), A65 (= A62), D66 (= D63), I67 (≠ L64), P132 (≠ A133), R166 (≠ K167), F248 (= F249), K251 (= K252)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
35% identity, 99% coverage: 1:258/260 of query aligns to 1:255/255 of 3q0jC
- active site: A65 (= A62), M70 (≠ R67), T80 (= T83), F84 (≠ N87), G108 (≠ V111), E111 (≠ S114), P130 (≠ A133), E131 (≠ F134), V136 (≠ L139), P138 (= P141), G139 (≠ D142), L224 (= L227), F234 (≠ G237)
- binding acetoacetyl-coenzyme a: Q23 (≠ E23), A24 (≠ R24), L25 (= L25), A27 (= A27), A63 (≠ S60), G64 (= G61), A65 (= A62), D66 (= D63), I67 (≠ L64), K68 (≠ A65), M70 (≠ R67), F84 (≠ N87), G107 (= G110), G108 (≠ V111), E111 (≠ S114), P130 (≠ A133), E131 (≠ F134), P138 (= P141), G139 (≠ D142), M140 (≠ G143)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 99% coverage: 1:258/260 of query aligns to 1:255/255 of 3q0gC
- active site: A65 (= A62), M70 (≠ R67), T80 (= T83), F84 (≠ N87), G108 (≠ V111), E111 (≠ S114), P130 (≠ A133), E131 (≠ F134), V136 (≠ L139), P138 (= P141), G139 (≠ D142), L224 (= L227), F234 (≠ G237)
- binding coenzyme a: L25 (= L25), A63 (≠ S60), I67 (≠ L64), K68 (≠ A65), Y104 (≠ P107), P130 (≠ A133), E131 (≠ F134), L134 (≠ I137)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
34% identity, 99% coverage: 3:260/260 of query aligns to 2:256/256 of 3h81A
- active site: A64 (= A62), M69 (≠ R67), T79 (= T83), F83 (≠ N87), G107 (≠ V111), E110 (≠ S114), P129 (≠ A133), E130 (≠ F134), V135 (≠ L139), P137 (= P141), G138 (≠ D142), L223 (= L227), F233 (≠ G237)
- binding calcium ion: F233 (≠ G237), Q238 (≠ A242)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 98% coverage: 3:258/260 of query aligns to 2:250/250 of 3q0gD
- active site: A64 (= A62), M69 (≠ S71), T75 (= T83), F79 (≠ N87), G103 (≠ V111), E106 (≠ S114), P125 (≠ A133), E126 (≠ F134), V131 (≠ L139), P133 (= P141), G134 (≠ D142), L219 (= L227), F229 (≠ G237)
- binding Butyryl Coenzyme A: F225 (≠ Q233), F241 (= F249)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
31% identity, 98% coverage: 2:257/260 of query aligns to 2:255/258 of 1mj3A
- active site: A68 (= A62), M73 (≠ R67), S83 (≠ T80), L85 (= L82), G109 (≠ V111), E112 (≠ S114), P131 (≠ A133), E132 (≠ F134), T137 (≠ L139), P139 (= P141), G140 (≠ D142), K225 (≠ L227), F235 (≠ G237)
- binding hexanoyl-coenzyme a: K26 (≠ E23), A27 (≠ R24), L28 (= L25), A30 (= A27), A66 (≠ S60), G67 (= G61), A68 (= A62), D69 (= D63), I70 (≠ L64), G109 (≠ V111), P131 (≠ A133), E132 (≠ F134), L135 (≠ I137), G140 (≠ D142)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
31% identity, 98% coverage: 2:257/260 of query aligns to 1:251/254 of 2dubA
- active site: A67 (= A62), M72 (≠ R67), S82 (≠ G77), G105 (≠ V111), E108 (≠ S114), P127 (≠ A133), E128 (≠ F134), T133 (≠ L139), P135 (= P141), G136 (≠ D142), K221 (≠ L227), F231 (≠ G237)
- binding octanoyl-coenzyme a: K25 (≠ E23), A26 (≠ R24), L27 (= L25), A29 (= A27), A65 (≠ S60), A67 (= A62), D68 (= D63), I69 (≠ L64), K70 (≠ A65), G105 (≠ V111), E108 (≠ S114), P127 (≠ A133), E128 (≠ F134), G136 (≠ D142), A137 (≠ G143)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
31% identity, 98% coverage: 2:257/260 of query aligns to 2:257/260 of 2hw5C
- active site: A68 (= A62), M73 (≠ R67), S83 (≠ N87), L87 (= L91), G111 (≠ V111), E114 (≠ S114), P133 (≠ A133), E134 (≠ F134), T139 (≠ L139), P141 (= P141), G142 (≠ D142), K227 (≠ L227), F237 (≠ G237)
- binding crotonyl coenzyme a: K26 (≠ E23), A27 (≠ R24), L28 (= L25), A30 (= A27), K62 (≠ R56), I70 (≠ L64), F109 (≠ A109)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
30% identity, 98% coverage: 2:257/260 of query aligns to 2:257/260 of 1dubA
- active site: A68 (= A62), M73 (≠ R67), S83 (≠ N87), L87 (= L91), G111 (≠ V111), E114 (≠ S114), P133 (≠ A133), E134 (≠ F134), T139 (≠ L139), P141 (= P141), G142 (≠ D142), K227 (≠ L227), F237 (≠ G237)
- binding acetoacetyl-coenzyme a: K26 (≠ E23), A27 (≠ R24), L28 (= L25), A30 (= A27), A66 (≠ S60), A68 (= A62), D69 (= D63), I70 (≠ L64), Y107 (≠ P107), G110 (= G110), G111 (≠ V111), E114 (≠ S114), P133 (≠ A133), E134 (≠ F134), L137 (≠ I137), G142 (≠ D142), F233 (≠ Q233), F249 (= F249)
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)
30% identity, 98% coverage: 2:257/260 of query aligns to 32:287/290 of P14604
- E144 (≠ S114) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ F134) 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)
31% identity, 98% coverage: 3:257/260 of query aligns to 1:255/258 of 1ey3A
- active site: A66 (= A62), M71 (≠ R67), S81 (≠ N87), L85 (= L91), G109 (≠ V111), E112 (≠ S114), P131 (≠ A133), E132 (≠ F134), T137 (≠ L139), P139 (= P141), G140 (≠ D142), K225 (≠ L227), F235 (≠ G237)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ E23), L26 (= L25), A28 (= A27), A64 (≠ S60), G65 (= G61), A66 (= A62), D67 (= D63), I68 (≠ L64), L85 (= L91), W88 (vs. gap), G109 (≠ V111), P131 (≠ A133), L135 (≠ I137), G140 (≠ D142)
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
35% identity, 78% coverage: 3:204/260 of query aligns to 2:207/269 of 1nzyB
- active site: C61 (= C59), F64 (≠ A62), I69 (≠ R67), A86 (≠ T83), H90 (≠ N87), G114 (≠ V111), G117 (≠ S114), A136 (= A133), W137 (≠ F134), I142 (≠ L139), N144 (≠ P141), D145 (= D142)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ E23), H23 (≠ R24), R24 (≠ L25), A62 (≠ S60), F64 (≠ A62), Y65 (≠ D63), L66 (= L64), R67 (≠ A65), W89 (≠ Y86), G113 (= G110), G114 (≠ V111), A136 (= A133), W137 (≠ F134), D145 (= D142), T146 (≠ G143)
- binding calcium ion: G49 (≠ R47), L202 (= L199), A203 (= A200), A205 (≠ G202), T207 (= T204)
- binding phosphate ion: E57 (≠ G55), N108 (= N105), K188 (≠ D185), R192 (≠ M189)
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)
35% identity, 78% coverage: 3:204/260 of query aligns to 2:207/269 of 1jxzB
- active site: C61 (= C59), F64 (≠ A62), I69 (≠ R67), A86 (≠ T83), Q90 (≠ N87), G113 (= G110), G114 (≠ V111), G117 (≠ S114), A136 (= A133), W137 (≠ F134), I142 (≠ L139), N144 (≠ P141), D145 (= D142)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ E23), H23 (≠ R24), R24 (≠ L25), A62 (≠ S60), F64 (≠ A62), Y65 (≠ D63), L66 (= L64), R67 (≠ A65), W89 (≠ Y86), G113 (= G110), A136 (= A133), W137 (≠ F134), I142 (≠ L139), D145 (= D142), T146 (≠ G143)
- binding calcium ion: G49 (≠ R47), L202 (= L199), A203 (= A200), A205 (≠ G202), T207 (= T204)
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)
35% identity, 78% coverage: 3:204/260 of query aligns to 2:207/269 of A5JTM5
- R24 (≠ L25) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (= E35) mutation to T: Forms inclusion bodies.
- E43 (vs. gap) mutation to A: No effect on catalytic activity.
- D45 (≠ L43) mutation to A: No effect on catalytic activity.
- D46 (= D44) mutation to A: No effect on catalytic activity.
- G63 (= G61) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ A62) 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 (≠ D63) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (≠ A65) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (≠ A66) mutation to T: No effect on catalytic activity.
- H81 (≠ A78) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ Y79) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (≠ Y86) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ N87) 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 (≠ L91) mutation to Q: No effect on catalytic activity.
- A112 (= A109) 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 (= G110) 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 (≠ V111) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G112) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D120) mutation to T: No effect on catalytic activity.
- D129 (≠ R126) mutation to T: No effect on catalytic activity.
- W137 (≠ F134) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D142) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (= E160) mutation to T: No effect on catalytic activity.
- E175 (≠ K172) mutation to D: No effect on catalytic activity.
- W179 (= W176) 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.
3rrvB Crystal structure of an enoyl-coa hydratase/isomerase from mycobacterium paratuberculosis (see paper)
36% identity, 83% coverage: 17:233/260 of query aligns to 19:236/254 of 3rrvB
7borA Structure of pseudomonas aeruginosa coa-bound odaa (see paper)
34% identity, 96% coverage: 4:252/260 of query aligns to 2:247/247 of 7borA
- active site: N63 (≠ A62), F68 (≠ R67), D77 (≠ S71), G81 (= G75), I105 (≠ V111), T108 (≠ S114), F128 (= F134), L133 (= L139), P135 (= P141), E136 (≠ D142), A222 (≠ V228), L232 (vs. gap)
- binding coenzyme a: D21 (≠ E23), K22 (≠ R24), A25 (= A27), S61 (= S60), I65 (≠ L64), V103 (≠ A109), F128 (= F134), L131 (≠ I137), F244 (= F249), R247 (≠ K252)
Q8GYN9 1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal; DHNS; Enoyl-CoA hydratase/isomerase D; ECHID; Naphthoate synthase; EC 4.1.3.36 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 99% coverage: 2:258/260 of query aligns to 73:331/337 of Q8GYN9
Sites not aligning to the query:
- 20 H→V: Loss of peroxisomal targeting.
5du6A Crystal structure of m. Tuberculosis echa6 bound to ligand gsk059a. (see paper)
34% identity, 95% coverage: 14:259/260 of query aligns to 11:241/242 of 5du6A
- active site: A61 (= A62), P71 (≠ T83), I75 (≠ N87), A99 (≠ V111), Q102 (≠ S114), P121 (≠ A133), T122 (≠ F134), L127 (= L139), L129 (≠ P141), D130 (= D142), P209 (≠ L227), W219 (≠ G237)
- binding (5R,7R)-5-(4-ethylphenyl)-N-(4-fluorobenzyl)-7-methyl-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L74 (≠ Y86), D82 (≠ S94), D130 (= D142), W132 (≠ G144), A207 (= A225), K212 (≠ A230), F215 (≠ Q233)
Query Sequence
>WP_011445547.1 NCBI__GCF_000013325.1:WP_011445547.1
MDYETILVERVGDVLKITLNRPERLNACPPNMALELANAVNDLDGARAVLITGQGRAFCS
GADLAARGERSIAGGRGAYTALTQAYNPLMLALSRLPVPVVTAVNGPAAGVGCSIALAAD
FVVAARSAYFLQAFVNIGLVPDGGASWMLTRLVGKARATEMMMLGEKIGAEKAENWGLIY
KAVDDAALMDEAMALASRLAAGPTVALGTMRQNLAKALEVDYASALLVEAEGQWAAGDSA
DAAEGGKAFLEKRKAAFTGK
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