SitesBLAST
Comparing WP_013090628.1 NCBI__GCF_000092885.1:WP_013090628.1 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)
46% identity, 94% coverage: 16:263/263 of query aligns to 13:257/257 of 6slbAAA
- active site: Q64 (= Q66), F69 (≠ L71), L80 (≠ I85), N84 (= N90), A108 (= A114), S111 (≠ N117), A130 (= A136), F131 (= F137), L136 (= L142), P138 (= P144), D139 (= D145), A224 (≠ D230), G234 (= G240)
- 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 (= R60), A62 (= A64), Q64 (= Q66), D65 (= D67), L66 (= L68), Y76 (≠ L81), A108 (= A114), F131 (= F137), D139 (= D145)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
43% identity, 94% coverage: 16:263/263 of query aligns to 10:245/245 of 6slaAAA
- active site: Q61 (= Q66), L68 (≠ F73), N72 (= N90), A96 (= A114), S99 (≠ N117), A118 (= A136), F119 (= F137), L124 (= L142), P126 (= P144), N127 (≠ D145), A212 (≠ D230), G222 (= G240)
- 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 (= L27), A59 (= A64), Q61 (= Q66), D62 (= D67), L63 (= L68), L68 (≠ F73), Y71 (≠ F89), A94 (= A112), G95 (= G113), A96 (= A114), F119 (= F137), I122 (= I140), L124 (= L142), N127 (≠ D145), F234 (= F252), K237 (≠ Q255)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
34% identity, 100% coverage: 1:263/263 of query aligns to 1:259/259 of 5zaiC
- active site: A65 (≠ Q66), F70 (≠ L71), S82 (≠ G82), R86 (≠ D86), G110 (≠ A114), E113 (≠ N117), P132 (≠ A136), E133 (≠ F137), I138 (≠ L142), P140 (= P144), G141 (≠ D145), A226 (≠ D230), F236 (≠ G240)
- binding coenzyme a: K24 (= K26), L25 (= L27), A63 (= A64), G64 (= G65), A65 (≠ Q66), D66 (= D67), I67 (≠ L68), P132 (≠ A136), R166 (≠ K170), F248 (= F252), K251 (≠ Q255)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
34% identity, 99% coverage: 1:260/263 of query aligns to 1:254/255 of 3q0jC
- active site: A65 (≠ Q66), M70 (≠ L68), T80 (≠ M78), F84 (≠ N90), G108 (≠ A114), E111 (≠ N117), P130 (≠ A136), E131 (≠ F137), V136 (≠ L142), P138 (= P144), G139 (≠ D145), L224 (≠ D230), F234 (≠ G240)
- binding acetoacetyl-coenzyme a: Q23 (≠ D25), A24 (≠ K26), L25 (= L27), A27 (≠ S29), A63 (= A64), G64 (= G65), A65 (≠ Q66), D66 (= D67), I67 (vs. gap), K68 (vs. gap), M70 (≠ L68), F84 (≠ N90), G107 (= G113), G108 (≠ A114), E111 (≠ N117), P130 (≠ A136), E131 (≠ F137), P138 (= P144), G139 (≠ D145), M140 (≠ S146)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
34% identity, 99% coverage: 1:260/263 of query aligns to 1:254/255 of 3q0gC
- active site: A65 (≠ Q66), M70 (≠ L68), T80 (≠ M78), F84 (≠ N90), G108 (≠ A114), E111 (≠ N117), P130 (≠ A136), E131 (≠ F137), V136 (≠ L142), P138 (= P144), G139 (≠ D145), L224 (≠ D230), F234 (≠ G240)
- binding coenzyme a: L25 (= L27), A63 (= A64), I67 (vs. gap), K68 (vs. gap), Y104 (≠ T110), P130 (≠ A136), E131 (≠ F137), L134 (≠ I140)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
34% identity, 100% coverage: 2:263/263 of query aligns to 1:256/256 of 3h81A
- active site: A64 (≠ Q66), M69 (≠ L68), T79 (≠ M78), F83 (≠ N90), G107 (≠ A114), E110 (≠ N117), P129 (≠ A136), E130 (≠ F137), V135 (≠ L142), P137 (= P144), G138 (≠ D145), L223 (≠ D230), F233 (≠ G240)
- binding calcium ion: F233 (≠ G240), Q238 (≠ Y245)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
33% identity, 95% coverage: 12:261/263 of query aligns to 11:256/258 of 1ey3A
- active site: A66 (≠ Q66), M71 (≠ L71), S81 (≠ L81), L85 (≠ I85), G109 (≠ A114), E112 (≠ N117), P131 (≠ A136), E132 (≠ F137), T137 (≠ L142), P139 (= P144), G140 (≠ D145), K225 (≠ D230), F235 (≠ G240)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ D25), L26 (= L27), A28 (≠ S29), A64 (= A64), G65 (= G65), A66 (≠ Q66), D67 (= D67), I68 (≠ L68), L85 (≠ I85), W88 (≠ Y88), G109 (≠ A114), P131 (≠ A136), L135 (≠ I140), G140 (≠ D145)
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)
33% identity, 95% coverage: 12:261/263 of query aligns to 43:288/290 of P14604
- E144 (≠ N117) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ F137) 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)
33% identity, 95% coverage: 12:261/263 of query aligns to 13:258/260 of 1dubA
- active site: A68 (≠ Q66), M73 (≠ L71), S83 (≠ L81), L87 (≠ I85), G111 (≠ A114), E114 (≠ N117), P133 (≠ A136), E134 (≠ F137), T139 (≠ L142), P141 (= P144), G142 (≠ D145), K227 (≠ D230), F237 (≠ G240)
- binding acetoacetyl-coenzyme a: K26 (≠ D25), A27 (≠ K26), L28 (= L27), A30 (≠ S29), A66 (= A64), A68 (≠ Q66), D69 (= D67), I70 (≠ L68), Y107 (≠ T110), G110 (= G113), G111 (≠ A114), E114 (≠ N117), P133 (≠ A136), E134 (≠ F137), L137 (≠ I140), G142 (≠ D145), F233 (≠ Q236), F249 (= F252)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
33% identity, 95% coverage: 12:261/263 of query aligns to 13:258/260 of 2hw5C
- active site: A68 (≠ Q66), M73 (= M78), S83 (≠ F89), L87 (≠ I93), G111 (≠ A114), E114 (≠ N117), P133 (≠ A136), E134 (≠ F137), T139 (≠ L142), P141 (= P144), G142 (≠ D145), K227 (≠ D230), F237 (≠ G240)
- binding crotonyl coenzyme a: K26 (≠ D25), A27 (≠ K26), L28 (= L27), A30 (≠ S29), K62 (≠ R60), I70 (≠ L68), F109 (≠ A112)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
33% identity, 95% coverage: 12:261/263 of query aligns to 12:252/254 of 2dubA
- active site: A67 (≠ Q66), M72 (≠ L71), S82 (≠ A83), G105 (≠ A114), E108 (≠ N117), P127 (≠ A136), E128 (≠ F137), T133 (≠ L142), P135 (= P144), G136 (≠ D145), K221 (≠ D230), F231 (≠ G240)
- binding octanoyl-coenzyme a: K25 (≠ D25), A26 (≠ K26), L27 (= L27), A29 (≠ S29), A65 (= A64), A67 (≠ Q66), D68 (= D67), I69 (≠ L68), K70 (≠ A69), G105 (≠ A114), E108 (≠ N117), P127 (≠ A136), E128 (≠ F137), G136 (≠ D145), A137 (≠ S146)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
33% identity, 95% coverage: 12:261/263 of query aligns to 13:256/258 of 1mj3A
- active site: A68 (≠ Q66), M73 (≠ L71), S83 (≠ A83), L85 (≠ I85), G109 (≠ A114), E112 (≠ N117), P131 (≠ A136), E132 (≠ F137), T137 (≠ L142), P139 (= P144), G140 (≠ D145), K225 (≠ D230), F235 (≠ G240)
- binding hexanoyl-coenzyme a: K26 (≠ D25), A27 (≠ K26), L28 (= L27), A30 (≠ S29), A66 (= A64), G67 (= G65), A68 (≠ Q66), D69 (= D67), I70 (≠ L68), G109 (≠ A114), P131 (≠ A136), E132 (≠ F137), L135 (≠ I140), G140 (≠ D145)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 98% coverage: 2:260/263 of query aligns to 1:249/250 of 3q0gD
- active site: A64 (≠ Q66), M69 (≠ L71), T75 (≠ M78), F79 (≠ N90), G103 (≠ A114), E106 (≠ N117), P125 (≠ A136), E126 (≠ F137), V131 (≠ L142), P133 (= P144), G134 (≠ D145), L219 (≠ D230), F229 (≠ G240)
- binding Butyryl Coenzyme A: F225 (≠ Q236), F241 (= F252)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
35% identity, 97% coverage: 10:263/263 of query aligns to 9:261/261 of 5jbxB
- active site: A67 (≠ Q66), R72 (≠ L71), L84 (≠ F89), R88 (≠ I93), G112 (≠ A114), E115 (≠ N117), T134 (≠ A136), E135 (≠ F137), I140 (≠ L142), P142 (= P144), G143 (≠ D145), A228 (≠ D230), L238 (≠ G240)
- binding coenzyme a: S24 (≠ D25), R25 (≠ K26), R26 (≠ L27), A28 (≠ S29), A65 (= A64), D68 (= D67), L69 (= L68), K70 (≠ A69), L110 (≠ A112), G111 (= G113), T134 (≠ A136), E135 (≠ F137), L138 (≠ I140), R168 (≠ K170)
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
32% identity, 87% coverage: 3:232/263 of query aligns to 2:232/269 of 1nzyB
- active site: C61 (= C63), F64 (≠ Q66), I69 (≠ L71), A86 (≠ D86), H90 (≠ N90), G114 (≠ A114), G117 (≠ N117), A136 (= A136), W137 (≠ F137), I142 (≠ L142), N144 (≠ P144), D145 (= D145), E230 (≠ D230)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D25), H23 (≠ K26), R24 (≠ L27), A62 (= A64), F64 (≠ Q66), Y65 (≠ D67), L66 (= L68), R67 (≠ A69), W89 (≠ F89), G113 (= G113), G114 (≠ A114), A136 (= A136), W137 (≠ F137), D145 (= D145), T146 (≠ S146)
- binding calcium ion: G49 (vs. gap), L202 (= L202), A203 (= A203), A205 (≠ Q205), T207 (= T207), Q210 (≠ I210)
- binding phosphate ion: E57 (≠ G59), N108 (= N108), K188 (≠ D188), R192 (≠ A192)
Sites not aligning to the query:
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: 2:256/263 of query aligns to 53:317/327 of Q62651
- D176 (≠ N117) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (≠ F137) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (= D145) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
32% identity, 87% coverage: 3:232/263 of query aligns to 2:232/269 of 1jxzB
- active site: C61 (= C63), F64 (≠ Q66), I69 (≠ L71), A86 (≠ D86), Q90 (≠ N90), G113 (= G113), G114 (≠ A114), G117 (≠ N117), A136 (= A136), W137 (≠ F137), I142 (≠ L142), N144 (≠ P144), D145 (= D145), E230 (≠ D230)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D25), H23 (≠ K26), R24 (≠ L27), A62 (= A64), F64 (≠ Q66), Y65 (≠ D67), L66 (= L68), R67 (≠ A69), W89 (≠ F89), G113 (= G113), A136 (= A136), W137 (≠ F137), I142 (≠ L142), D145 (= D145), T146 (≠ S146)
- binding calcium ion: G49 (vs. gap), L202 (= L202), A203 (= A203), A205 (≠ Q205), T207 (= T207), Q210 (≠ I210)
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)
31% identity, 87% coverage: 3:232/263 of query aligns to 2:232/269 of A5JTM5
- R24 (≠ L27) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (= E37) mutation to T: Forms inclusion bodies.
- E43 (= E46) mutation to A: No effect on catalytic activity.
- D45 (≠ S48) mutation to A: No effect on catalytic activity.
- D46 (≠ G49) mutation to A: No effect on catalytic activity.
- G63 (= G65) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ Q66) 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 (≠ D67) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (≠ A69) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (≠ D70) mutation to T: No effect on catalytic activity.
- H81 (≠ L81) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ G82) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (≠ F89) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ N90) 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 (≠ R94) mutation to Q: No effect on catalytic activity.
- A112 (= A112) 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 (= G113) 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 (≠ A114) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G115) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D123) mutation to T: No effect on catalytic activity.
- D129 (≠ R129) mutation to T: No effect on catalytic activity.
- W137 (≠ F137) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D145) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (≠ G163) mutation to T: No effect on catalytic activity.
- E175 (≠ K175) mutation to D: No effect on catalytic activity.
- W179 (= W179) mutation to F: No effect on catalytic activity.
- H208 (≠ R208) mutation to Q: No effect on catalytic activity.
- R216 (≠ A216) mutation R->E,K,L: Yields insoluble protein.
- E232 (= E232) mutation E->A,N,Q,R: Yields insoluble protein.; mutation to D: Reduced catalytic activity, increased substrate binding.
Sites not aligning to the query:
- 257 R→K: Retains catalytic activity and substrate CoA binding.; R→L: Significantly reduces catalytic activity and substrate CoA binding.
1ef9A The crystal structure of methylmalonyl coa decarboxylase complexed with 2s-carboxypropyl coa (see paper)
27% identity, 100% coverage: 1:263/263 of query aligns to 1:261/261 of 1ef9A
- active site: H66 (≠ Q66), L71 (= L71), D82 (= D86), R86 (≠ N90), G110 (≠ A114), E113 (≠ N117), P133 (≠ F137), V138 (≠ L142), Y140 (≠ P144), N141 (≠ D145), E228 (= E232), Y238 (≠ G240)
- binding 2-carboxypropyl-coenzyme a: A64 (= A64), H66 (≠ Q66), D67 (= D67), I68 (≠ L68), H69 (≠ A69), W108 (≠ A112), G110 (≠ A114), T132 (≠ A136), P133 (≠ F137), K253 (≠ Q255)
P52045 Methylmalonyl-CoA decarboxylase; MMCD; Transcarboxylase; EC 4.1.1.- from Escherichia coli (strain K12) (see paper)
27% identity, 100% coverage: 1:263/263 of query aligns to 1:261/261 of P52045
- G110 (≠ A114) binding substrate
- T132 (≠ A136) binding substrate
- K253 (≠ Q255) binding substrate
Query Sequence
>WP_013090628.1 NCBI__GCF_000092885.1:WP_013090628.1
MSYEAIRLDIDSSSHVATITLSRPDKLNSFTRAMHQELGAALDQVEKSGARALVFTGAGR
GFCAGQDLADLDFTPGGMTDLGAVIDEYFNPLIRRLQALPFPVIAAVNGTAAGAGANLAF
ACDLVLAARSASFIQAFVKIGLVPDSGGTWFLPQRVGMARALGLAITGDKLSADKAESWG
LIWQVLDDAELAPAAAKLAAQLAQQPTRAIAAIKQAMRAGTTHTLDRQLDLERDLQRELG
ASHDYAEGVQAFIEQRAPRFEGR
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