SitesBLAST
Comparing WP_089300343.1 NCBI__GCF_900188115.1:WP_089300343.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
44% identity, 100% coverage: 1:259/259 of query aligns to 4:257/257 of 6slbAAA
- active site: Q64 (= Q61), F69 (≠ L71), L80 (≠ G82), N84 (= N86), A108 (= A110), S111 (≠ A113), A130 (= A132), F131 (= F133), L136 (= L138), P138 (= P140), D139 (= D141), A224 (= A226), G234 (= G236)
- 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 (≠ T55), A62 (= A59), Q64 (= Q61), D65 (= D62), L66 (= L63), Y76 (≠ L78), A108 (= A110), F131 (= F133), D139 (= D141)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
44% identity, 100% coverage: 1:259/259 of query aligns to 1:245/245 of 6slaAAA
- active site: Q61 (= Q61), L68 (= L78), N72 (= N86), A96 (= A110), S99 (≠ A113), A118 (= A132), F119 (= F133), L124 (= L138), P126 (= P140), N127 (≠ D141), A212 (= A226), G222 (= G236)
- 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 (≠ Y21), A59 (= A59), Q61 (= Q61), D62 (= D62), L63 (= L63), L68 (= L78), Y71 (= Y85), A94 (= A108), G95 (= G109), A96 (= A110), F119 (= F133), I122 (≠ V136), L124 (= L138), N127 (≠ D141), F234 (= F248), K237 (= K251)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
38% identity, 95% coverage: 13:259/259 of query aligns to 17:259/259 of 5zaiC
- active site: A65 (≠ Q61), F70 (≠ H66), S82 (≠ G82), R86 (≠ N86), G110 (≠ A110), E113 (≠ A113), P132 (≠ A132), E133 (≠ F133), I138 (≠ L138), P140 (= P140), G141 (≠ D141), A226 (= A226), F236 (≠ G236)
- binding coenzyme a: K24 (≠ S20), L25 (≠ Y21), A63 (= A59), G64 (= G60), A65 (≠ Q61), D66 (= D62), I67 (≠ L63), P132 (≠ A132), R166 (≠ K166), F248 (= F248), K251 (= K251)
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
39% identity, 76% coverage: 8:203/259 of query aligns to 11:207/269 of 1nzyB
- active site: C61 (= C58), F64 (≠ Q61), I69 (vs. gap), A86 (≠ G82), H90 (≠ N86), G114 (≠ A110), G117 (≠ A113), A136 (= A132), W137 (≠ F133), I142 (≠ L138), N144 (≠ P140), D145 (= D141)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D19), H23 (≠ S20), R24 (≠ Y21), A62 (= A59), F64 (≠ Q61), Y65 (≠ D62), L66 (= L63), R67 (≠ K64), W89 (≠ Y85), G113 (= G109), G114 (≠ A110), A136 (= A132), W137 (≠ F133), D145 (= D141), T146 (≠ S142)
- binding calcium ion: G49 (= G46), L202 (= L198), A203 (= A199), A205 (≠ G201), T207 (= T203)
- binding phosphate ion: E57 (≠ G54), N108 (= N104), K188 (≠ D184), R192 (≠ T188)
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)
39% identity, 76% coverage: 8:203/259 of query aligns to 11:207/269 of 1jxzB
- active site: C61 (= C58), F64 (≠ Q61), I69 (vs. gap), A86 (≠ G82), Q90 (≠ N86), G113 (= G109), G114 (≠ A110), G117 (≠ A113), A136 (= A132), W137 (≠ F133), I142 (≠ L138), N144 (≠ P140), D145 (= D141)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D19), H23 (≠ S20), R24 (≠ Y21), A62 (= A59), F64 (≠ Q61), Y65 (≠ D62), L66 (= L63), R67 (≠ K64), W89 (≠ Y85), G113 (= G109), A136 (= A132), W137 (≠ F133), I142 (≠ L138), D145 (= D141), T146 (≠ S142)
- binding calcium ion: G49 (= G46), L202 (= L198), A203 (= A199), A205 (≠ G201), T207 (= T203)
Sites not aligning to the query:
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
35% identity, 96% coverage: 10:257/259 of query aligns to 14:255/255 of 3q0jC
- active site: A65 (≠ Q61), M70 (≠ H66), T80 (≠ G82), F84 (≠ N86), G108 (≠ A110), E111 (≠ A113), P130 (≠ A132), E131 (≠ F133), V136 (≠ L138), P138 (= P140), G139 (≠ D141), L224 (≠ A226), F234 (≠ G236)
- binding acetoacetyl-coenzyme a: Q23 (≠ D19), A24 (≠ S20), L25 (≠ Y21), A27 (= A23), A63 (= A59), G64 (= G60), A65 (≠ Q61), D66 (= D62), I67 (≠ L63), K68 (= K64), M70 (≠ H66), F84 (≠ N86), G107 (= G109), G108 (≠ A110), E111 (≠ A113), P130 (≠ A132), E131 (≠ F133), P138 (= P140), G139 (≠ D141), M140 (≠ S142)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 96% coverage: 10:257/259 of query aligns to 14:255/255 of 3q0gC
- active site: A65 (≠ Q61), M70 (≠ H66), T80 (≠ G82), F84 (≠ N86), G108 (≠ A110), E111 (≠ A113), P130 (≠ A132), E131 (≠ F133), V136 (≠ L138), P138 (= P140), G139 (≠ D141), L224 (≠ A226), F234 (≠ G236)
- binding coenzyme a: L25 (≠ Y21), A63 (= A59), I67 (≠ L63), K68 (= K64), Y104 (≠ P106), P130 (≠ A132), E131 (≠ F133), L134 (≠ V136)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
35% identity, 96% coverage: 10:257/259 of query aligns to 13:254/256 of 3h81A
- active site: A64 (≠ Q61), M69 (≠ H66), T79 (≠ G82), F83 (≠ N86), G107 (≠ A110), E110 (≠ A113), P129 (≠ A132), E130 (≠ F133), V135 (≠ L138), P137 (= P140), G138 (≠ D141), L223 (≠ A226), F233 (≠ G236)
- binding calcium ion: F233 (≠ G236), Q238 (≠ H241)
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)
38% identity, 76% coverage: 8:203/259 of query aligns to 11:207/269 of A5JTM5
- R24 (≠ Y21) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (≠ R31) mutation to T: Forms inclusion bodies.
- E43 (= E40) mutation to A: No effect on catalytic activity.
- D45 (= D42) mutation to A: No effect on catalytic activity.
- D46 (≠ Q43) mutation to A: No effect on catalytic activity.
- G63 (= G60) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ Q61) 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 (≠ D62) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (≠ K64) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (= E65) mutation to T: No effect on catalytic activity.
- H81 (≠ P77) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ L78) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (≠ Y85) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ N86) 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 (≠ T90) mutation to Q: No effect on catalytic activity.
- A112 (= A108) 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 (= G109) 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 (≠ A110) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G111) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D119) mutation to T: No effect on catalytic activity.
- D129 (≠ T125) mutation to T: No effect on catalytic activity.
- W137 (≠ F133) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D141) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (= E159) mutation to T: No effect on catalytic activity.
- E175 (= E171) mutation to D: No effect on catalytic activity.
- W179 (≠ I175) 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.
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
34% identity, 97% coverage: 10:259/259 of query aligns to 17:260/260 of 2hw5C
- active site: A68 (≠ Q61), M73 (≠ H66), S83 (≠ A76), L87 (≠ G82), G111 (≠ A110), E114 (≠ A113), P133 (≠ A132), E134 (≠ F133), T139 (≠ L138), P141 (= P140), G142 (≠ D141), K227 (≠ A226), F237 (≠ G236)
- binding crotonyl coenzyme a: K26 (≠ D19), A27 (≠ S20), L28 (≠ Y21), A30 (= A23), K62 (≠ T55), I70 (≠ L63), F109 (≠ A108)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
35% identity, 95% coverage: 10:256/259 of query aligns to 17:255/258 of 1mj3A
- active site: A68 (≠ Q61), M73 (≠ H66), S83 (≠ A76), L85 (= L78), G109 (≠ A110), E112 (≠ A113), P131 (≠ A132), E132 (≠ F133), T137 (≠ L138), P139 (= P140), G140 (≠ D141), K225 (≠ A226), F235 (≠ G236)
- binding hexanoyl-coenzyme a: K26 (≠ D19), A27 (≠ S20), L28 (≠ Y21), A30 (= A23), A66 (= A59), G67 (= G60), A68 (≠ Q61), D69 (= D62), I70 (≠ L63), G109 (≠ A110), P131 (≠ A132), E132 (≠ F133), L135 (≠ V136), G140 (≠ D141)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
35% identity, 96% coverage: 10:257/259 of query aligns to 13:250/250 of 3q0gD
- active site: A64 (≠ Q61), M69 (≠ H66), T75 (≠ A72), F79 (≠ L78), G103 (≠ A110), E106 (≠ A113), P125 (≠ A132), E126 (≠ F133), V131 (≠ L138), P133 (= P140), G134 (≠ D141), L219 (≠ A226), F229 (≠ G236)
- binding Butyryl Coenzyme A: F225 (≠ Q232), F241 (= F248)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
35% identity, 95% coverage: 10:256/259 of query aligns to 16:251/254 of 2dubA
- active site: A67 (≠ Q61), M72 (≠ H66), S82 (≠ E83), G105 (≠ A110), E108 (≠ A113), P127 (≠ A132), E128 (≠ F133), T133 (≠ L138), P135 (= P140), G136 (≠ D141), K221 (≠ A226), F231 (≠ G236)
- binding octanoyl-coenzyme a: K25 (≠ D19), A26 (≠ S20), L27 (≠ Y21), A29 (= A23), A65 (= A59), A67 (≠ Q61), D68 (= D62), I69 (≠ L63), K70 (= K64), G105 (≠ A110), E108 (≠ A113), P127 (≠ A132), E128 (≠ F133), G136 (≠ D141), A137 (≠ S142)
Q9P4U9 Enoyl-CoA hydratase AKT3-1; AF-toxin biosynthesis protein 3-1; EC 4.2.1.17 from Alternaria alternata (Alternaria rot fungus) (Torula alternata) (see paper)
34% identity, 97% coverage: 6:256/259 of query aligns to 21:268/296 of Q9P4U9
Sites not aligning to the query:
- 294:296 Peroxisomal targeting signal type 1
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
35% identity, 95% coverage: 10:256/259 of query aligns to 15:255/258 of 1ey3A
- active site: A66 (≠ Q61), M71 (≠ H66), S81 (≠ A76), L85 (≠ G82), G109 (≠ A110), E112 (≠ A113), P131 (≠ A132), E132 (≠ F133), T137 (≠ L138), P139 (= P140), G140 (≠ D141), K225 (≠ A226), F235 (≠ G236)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ D19), L26 (≠ Y21), A28 (= A23), A64 (= A59), G65 (= G60), A66 (≠ Q61), D67 (= D62), I68 (≠ L63), L85 (≠ G82), W88 (≠ Y85), G109 (≠ A110), P131 (≠ A132), L135 (≠ V136), G140 (≠ D141)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
35% identity, 95% coverage: 10:256/259 of query aligns to 17:257/260 of 1dubA
- active site: A68 (≠ Q61), M73 (≠ H66), S83 (≠ A76), L87 (≠ G82), G111 (≠ A110), E114 (≠ A113), P133 (≠ A132), E134 (≠ F133), T139 (≠ L138), P141 (= P140), G142 (≠ D141), K227 (≠ A226), F237 (≠ G236)
- binding acetoacetyl-coenzyme a: K26 (≠ D19), A27 (≠ S20), L28 (≠ Y21), A30 (= A23), A66 (= A59), A68 (≠ Q61), D69 (= D62), I70 (≠ L63), Y107 (≠ P106), G110 (= G109), G111 (≠ A110), E114 (≠ A113), P133 (≠ A132), E134 (≠ F133), L137 (≠ V136), G142 (≠ D141), F233 (≠ Q232), F249 (= F248)
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)
35% identity, 95% coverage: 10:256/259 of query aligns to 47:287/290 of P14604
- E144 (≠ A113) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ F133) 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
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
33% identity, 97% coverage: 3:253/259 of query aligns to 59:318/327 of Q62651
- D176 (≠ A113) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (≠ F133) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (= D141) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
5du6A Crystal structure of m. Tuberculosis echa6 bound to ligand gsk059a. (see paper)
38% identity, 100% coverage: 1:258/259 of query aligns to 2:241/242 of 5du6A
- active site: A61 (≠ Q61), P71 (= P75), I75 (≠ V81), A99 (= A110), Q102 (≠ A113), P121 (≠ A132), T122 (≠ F133), L127 (= L138), L129 (≠ P140), D130 (= D141), P209 (≠ G222), W219 (≠ L235)
- binding (5R,7R)-5-(4-ethylphenyl)-N-(4-fluorobenzyl)-7-methyl-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L74 (≠ T80), D82 (≠ A93), D130 (= D141), W132 (≠ G143), A207 (≠ T220), K212 (≠ E228), F215 (≠ A231)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
33% identity, 98% coverage: 6:259/259 of query aligns to 10:261/261 of 5jbxB
- active site: A67 (≠ Q61), R72 (≠ H66), L84 (≠ G82), R88 (≠ N86), G112 (≠ A110), E115 (≠ A113), T134 (≠ A132), E135 (≠ F133), I140 (≠ L138), P142 (= P140), G143 (≠ D141), A228 (= A226), L238 (≠ G236)
- binding coenzyme a: S24 (≠ D19), R25 (≠ S20), R26 (≠ Y21), A28 (= A23), A65 (= A59), D68 (= D62), L69 (= L63), K70 (= K64), L110 (≠ A108), G111 (= G109), T134 (≠ A132), E135 (≠ F133), L138 (≠ V136), R168 (≠ K166)
Query Sequence
>WP_089300343.1 NCBI__GCF_900188115.1:WP_089300343.1
MVTTADAEGVRTITLNRPDSYNALNVALKERLLAELRAAEADQQVGAIVLTGAGTAFCAG
QDLKEHVSLLLADDPAPLRTVGEHYNPIATAIASMPKPIIAAVNGPAAGAGAAFAYAADL
RIAATSSNFLMAFANVGLGPDSGASWTLQRLIGYGRALELMLLARKVPAEEALRIGLVSE
VVPDGEATNRAQQLAARLAAGPTVAYRKIKESLSGAAESTFGEALATEEAAQTELGRTAD
HREAVEAFVAKREPTFTGQ
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