SitesBLAST
Comparing WP_011780796.1 NCBI__GCF_000015305.1:WP_011780796.1 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)
39% identity, 94% coverage: 11:258/264 of query aligns to 10:254/257 of 6slbAAA
- active site: Q64 (≠ G65), F69 (= F70), L80 (≠ V80), N84 (≠ H88), A108 (= A112), S111 (= S115), A130 (= A134), F131 (≠ Y135), L136 (= L140), P138 (= P142), D139 (= D143), A224 (≠ E228), G234 (≠ A238)
- 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 (= R59), A62 (= A63), Q64 (≠ G65), D65 (= D66), L66 (= L67), Y76 (≠ R76), A108 (= A112), F131 (≠ Y135), D139 (= D143)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
38% identity, 94% coverage: 11:258/264 of query aligns to 7:242/245 of 6slaAAA
- active site: Q61 (≠ G65), L68 (≠ V80), N72 (≠ H88), A96 (= A112), S99 (= S115), A118 (= A134), F119 (≠ Y135), L124 (= L140), P126 (= P142), N127 (≠ D143), A212 (≠ E228), G222 (≠ A238)
- 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 (≠ A26), A59 (= A63), Q61 (≠ G65), D62 (= D66), L63 (= L67), L68 (≠ V80), Y71 (≠ L87), A94 (= A110), G95 (= G111), A96 (= A112), F119 (≠ Y135), I122 (≠ V138), L124 (= L140), N127 (≠ D143), F234 (= F250), K237 (= K253)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
30% identity, 97% coverage: 3:258/264 of query aligns to 2:256/259 of 5zaiC
- active site: A65 (≠ G65), F70 (= F70), S82 (≠ K81), R86 (≠ D85), G110 (≠ A112), E113 (≠ S115), P132 (≠ A134), E133 (≠ Y135), I138 (≠ L140), P140 (= P142), G141 (≠ D143), A226 (≠ E228), F236 (≠ A238)
- binding coenzyme a: K24 (≠ A25), L25 (≠ A26), A63 (= A63), G64 (= G64), A65 (≠ G65), D66 (= D66), I67 (≠ L67), P132 (≠ A134), R166 (≠ T168), F248 (= F250), K251 (= K253)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
34% identity, 97% coverage: 4:258/264 of query aligns to 3:254/255 of 3q0jC
- active site: A65 (≠ G65), M70 (≠ F70), T80 (≠ A84), F84 (≠ H88), G108 (≠ A112), E111 (≠ S115), P130 (≠ A134), E131 (≠ Y135), V136 (≠ L140), P138 (= P142), G139 (≠ D143), L224 (≠ E228), F234 (≠ A238)
- binding acetoacetyl-coenzyme a: Q23 (≠ D24), A24 (= A25), L25 (≠ A26), A27 (≠ G28), A63 (= A63), G64 (= G64), A65 (≠ G65), D66 (= D66), I67 (≠ L67), K68 (= K68), M70 (≠ F70), F84 (≠ H88), G107 (= G111), G108 (≠ A112), E111 (≠ S115), P130 (≠ A134), E131 (≠ Y135), P138 (= P142), G139 (≠ D143), M140 (≠ G144)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
34% identity, 97% coverage: 4:258/264 of query aligns to 3:254/255 of 3q0gC
- active site: A65 (≠ G65), M70 (≠ F70), T80 (≠ A84), F84 (≠ H88), G108 (≠ A112), E111 (≠ S115), P130 (≠ A134), E131 (≠ Y135), V136 (≠ L140), P138 (= P142), G139 (≠ D143), L224 (≠ E228), F234 (≠ A238)
- binding coenzyme a: L25 (≠ A26), A63 (= A63), I67 (≠ L67), K68 (= K68), Y104 (≠ T108), P130 (≠ A134), E131 (≠ Y135), L134 (≠ V138)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
34% identity, 97% coverage: 4:258/264 of query aligns to 2:253/256 of 3h81A
- active site: A64 (≠ G65), M69 (≠ F70), T79 (≠ A84), F83 (≠ H88), G107 (≠ A112), E110 (≠ S115), P129 (≠ A134), E130 (≠ Y135), V135 (≠ L140), P137 (= P142), G138 (≠ D143), L223 (≠ E228), F233 (≠ A238)
- binding calcium ion: F233 (≠ A238), Q238 (≠ G243)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
34% identity, 97% coverage: 4:258/264 of query aligns to 2:249/250 of 3q0gD
- active site: A64 (≠ G65), M69 (vs. gap), T75 (≠ A84), F79 (≠ H88), G103 (≠ A112), E106 (≠ S115), P125 (≠ A134), E126 (≠ Y135), V131 (≠ L140), P133 (= P142), G134 (≠ D143), L219 (≠ E228), F229 (≠ A238)
- binding Butyryl Coenzyme A: F225 (≠ I234), F241 (= F250)
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)
32% identity, 85% coverage: 4:228/264 of query aligns to 2:226/269 of A5JTM5
- R24 (≠ A26) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (= E36) mutation to T: Forms inclusion bodies.
- E43 (≠ D45) mutation to A: No effect on catalytic activity.
- D45 (≠ A47) mutation to A: No effect on catalytic activity.
- D46 (vs. gap) mutation to A: No effect on catalytic activity.
- G63 (= G64) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ G65) 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 (≠ D66) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (≠ K68) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (≠ D69) mutation to T: No effect on catalytic activity.
- H81 (≠ D86) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ L87) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (vs. gap) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (= H88) 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 (≠ S92) mutation to Q: No effect on catalytic activity.
- A112 (= A110) 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 (= G111) 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 (≠ A112) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G113) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D121) mutation to T: No effect on catalytic activity.
- D129 (≠ E127) mutation to T: No effect on catalytic activity.
- W137 (≠ Y135) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D143) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (≠ Q161) mutation to T: No effect on catalytic activity.
- E175 (= E173) mutation to D: No effect on catalytic activity.
- W179 (= W177) mutation to F: No effect on catalytic activity.
- H208 (≠ G210) mutation to Q: No effect on catalytic activity.
- R216 (≠ T218) mutation R->E,K,L: Yields insoluble protein.
Sites not aligning to the query:
- 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.
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
31% identity, 85% coverage: 4:228/264 of query aligns to 2:226/269 of 1nzyB
- active site: C61 (= C62), F64 (≠ G65), I69 (≠ F70), A86 (vs. gap), H90 (= H88), G114 (≠ A112), G117 (≠ S115), A136 (= A134), W137 (≠ Y135), I142 (≠ L140), N144 (≠ P142), D145 (= D143)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D24), H23 (≠ A25), R24 (≠ A26), A62 (= A63), F64 (≠ G65), Y65 (≠ D66), L66 (= L67), R67 (≠ K68), W89 (vs. gap), G113 (= G111), G114 (≠ A112), A136 (= A134), W137 (≠ Y135), D145 (= D143), T146 (≠ G144)
- binding calcium ion: G49 (≠ K50), L202 (≠ S204), A203 (= A205), A205 (≠ S207), T207 (≠ G209), Q210 (≠ K212)
- binding phosphate ion: E57 (≠ G58), N108 (= N106), K188 (≠ D186), R192 (≠ Q190)
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)
31% identity, 85% coverage: 4:228/264 of query aligns to 2:226/269 of 1jxzB
- active site: C61 (= C62), F64 (≠ G65), I69 (≠ F70), A86 (vs. gap), Q90 (≠ H88), G113 (= G111), G114 (≠ A112), G117 (≠ S115), A136 (= A134), W137 (≠ Y135), I142 (≠ L140), N144 (≠ P142), D145 (= D143)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D24), H23 (≠ A25), R24 (≠ A26), A62 (= A63), F64 (≠ G65), Y65 (≠ D66), L66 (= L67), R67 (≠ K68), W89 (vs. gap), G113 (= G111), A136 (= A134), W137 (≠ Y135), I142 (≠ L140), D145 (= D143), T146 (≠ G144)
- binding calcium ion: G49 (≠ K50), L202 (≠ S204), A203 (= A205), A205 (≠ S207), T207 (≠ G209), Q210 (≠ K212)
Sites not aligning to the query:
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
33% identity, 98% coverage: 1:258/264 of query aligns to 4:253/260 of 2uzfA
- active site: G70 (= G65), R80 (≠ S75), L84 (≠ D85), G108 (≠ A112), V111 (≠ S115), T130 (≠ A134), G131 (≠ Y135), S136 (≠ L140), D138 (≠ P142), A139 (≠ D143), A225 (≠ E228), Y233 (≠ A236)
- binding acetoacetyl-coenzyme a: V28 (≠ A25), R29 (≠ A26), S68 (≠ A63), G69 (= G64), G70 (= G65), D71 (= D66), Y104 (≠ T108), G108 (≠ A112)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
31% identity, 98% coverage: 1:258/264 of query aligns to 4:258/261 of 5jbxB
- active site: A67 (≠ G65), R72 (≠ F70), L84 (≠ A84), R88 (≠ H88), G112 (≠ A112), E115 (≠ S115), T134 (≠ A134), E135 (≠ Y135), I140 (≠ L140), P142 (= P142), G143 (≠ D143), A228 (≠ E228), L238 (≠ A238)
- binding coenzyme a: S24 (≠ D24), R25 (≠ A25), R26 (≠ A26), A28 (≠ G28), A65 (= A63), D68 (= D66), L69 (= L67), K70 (= K68), L110 (≠ A110), G111 (= G111), T134 (≠ A134), E135 (≠ Y135), L138 (≠ V138), R168 (≠ T168)
4jvtA Crystal structure of tfu_1878, a putative enoyl-coa hydratase fromthermobifida fusca yx in complex with coa
37% identity, 85% coverage: 7:230/264 of query aligns to 15:243/257 of 4jvtA
- active site: I72 (≠ G65), F77 (= F70), I97 (= I91), Q101 (≠ A95), A125 (= A112), Q128 (≠ S115), K147 (≠ A134), E148 (≠ Y135), D156 (= D143), R241 (≠ E228)
- binding acetyl coenzyme *a: H32 (≠ D24), R33 (≠ A25), R34 (≠ A26), A36 (≠ G28), S70 (≠ A63), G71 (= G64), I72 (≠ G65), I123 (≠ A110), G124 (= G111)
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
32% identity, 98% coverage: 1:258/264 of query aligns to 9:266/273 of Q5HH38
- R34 (≠ A26) binding in other chain
- SGGDQ 73:77 (≠ AGGDL 63:67) binding in other chain
- S149 (≠ L140) binding in other chain
4omrA Crystal structure of tfu_1878, a putative enoyl-coa hydratase from thermobifida fusca yx in complex with acetoacetyl-coa
36% identity, 85% coverage: 7:230/264 of query aligns to 13:244/255 of 4omrA
- active site: I70 (≠ G65), F75 (= F70), I98 (= I91), Q102 (≠ A95), A126 (= A112), Q129 (≠ S115), K148 (≠ A134), E149 (≠ Y135), D157 (= D143), R242 (≠ E228)
- binding acetoacetyl-coenzyme a: H30 (≠ D24), R31 (≠ A25), R32 (≠ A26), A34 (≠ G28), S68 (≠ A63), I70 (≠ G65), D71 (= D66), L72 (= L67), I124 (≠ A110), G125 (= G111), A126 (= A112), K148 (≠ A134), E149 (≠ Y135)
4i52A Scmenb im complex with 1-hydroxy-2-naphthoyl-coa (see paper)
33% identity, 97% coverage: 3:258/264 of query aligns to 8:268/275 of 4i52A
- active site: G77 (= G65), R82 (≠ P74), Y87 (≠ H79), R95 (≠ D85), L99 (vs. gap), G123 (≠ A112), V126 (≠ S115), G146 (≠ Y135), S151 (≠ L140), D153 (≠ P142), G154 (≠ D143), A240 (≠ E230), Y248 (≠ A238)
- binding 1-hydroxy-2-naphthoyl-CoA: H29 (≠ D24), K30 (≠ A25), R31 (≠ A26), A33 (≠ G28), S75 (≠ A63), G76 (= G64), G77 (= G65), D78 (= D66), Q79 (≠ A71), L96 (vs. gap), V98 (vs. gap), Y119 (≠ T108), I121 (≠ A110), G123 (≠ A112), T145 (≠ A134), V149 (= V138), S151 (≠ L140), F152 (≠ S141)
4i4zA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with salicylyl-coa (see paper)
33% identity, 97% coverage: 3:258/264 of query aligns to 8:268/275 of 4i4zA
- active site: G77 (= G65), R82 (≠ P74), Y87 (≠ H79), R95 (≠ D85), L99 (vs. gap), G123 (≠ A112), V126 (≠ S115), G146 (≠ Y135), S151 (≠ L140), D153 (≠ P142), G154 (≠ D143), A240 (≠ E230), Y248 (≠ A238)
- binding Salicylyl CoA: H29 (≠ D24), K30 (≠ A25), R31 (≠ A26), S75 (≠ A63), G76 (= G64), G77 (= G65), D78 (= D66), Q79 (≠ A71), Y87 (≠ H79), V98 (vs. gap), G123 (≠ A112), T145 (≠ A134), V149 (= V138), S151 (≠ L140), F260 (= F250), K263 (= K253)
- binding bicarbonate ion: G122 (= G111), Q144 (≠ M133), T145 (≠ A134), G146 (≠ Y135), W174 (≠ M163)
4emlA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with bicarbonate (see paper)
33% identity, 97% coverage: 3:258/264 of query aligns to 8:254/261 of 4emlA
- active site: G77 (= G65), R81 (≠ D69), L85 (≠ A73), G109 (≠ A112), V112 (≠ S115), G132 (≠ Y135), S137 (≠ L140), D139 (≠ P142), G140 (≠ D143), A226 (≠ E230), Y234 (≠ A238)
- binding bicarbonate ion: G108 (= G111), Q130 (≠ M133), G132 (≠ Y135), W160 (≠ M163)
- binding chloride ion: D184 (= D187), R185 (= R188), E187 (≠ Q190), E188 (≠ A191)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
30% identity, 97% coverage: 4:258/264 of query aligns to 2:251/254 of 2dubA
- active site: A67 (≠ G65), M72 (≠ F70), S82 (≠ R89), G105 (≠ A112), E108 (≠ S115), P127 (≠ A134), E128 (≠ Y135), T133 (≠ L140), P135 (= P142), G136 (≠ D143), K221 (≠ E228), F231 (≠ A238)
- binding octanoyl-coenzyme a: K25 (≠ D24), A26 (= A25), L27 (≠ A26), A29 (≠ G28), A65 (= A63), A67 (≠ G65), D68 (= D66), I69 (≠ L67), K70 (= K68), G105 (≠ A112), E108 (≠ S115), P127 (≠ A134), E128 (≠ Y135), G136 (≠ D143), A137 (≠ G144)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
30% identity, 97% coverage: 4:258/264 of query aligns to 3:255/258 of 1mj3A
- active site: A68 (≠ G65), M73 (≠ F70), S83 (≠ R89), L85 (≠ I91), G109 (≠ A112), E112 (≠ S115), P131 (≠ A134), E132 (≠ Y135), T137 (≠ L140), P139 (= P142), G140 (≠ D143), K225 (≠ E228), F235 (≠ A238)
- binding hexanoyl-coenzyme a: K26 (≠ D24), A27 (= A25), L28 (≠ A26), A30 (≠ G28), A66 (= A63), G67 (= G64), A68 (≠ G65), D69 (= D66), I70 (≠ L67), G109 (≠ A112), P131 (≠ A134), E132 (≠ Y135), L135 (≠ V138), G140 (≠ D143)
Query Sequence
>WP_011780796.1 NCBI__GCF_000015305.1:WP_011780796.1
MTEYQTITFEQAGVVARITLNRPDAANGMNGTMTRELADAAARCDTAATKVVVITGAGRF
FCAGGDLKDFASAPSRGRHVKGVADDLHRAISTFARMDAVVITAVNGTAAGAGFSLAVSG
DLVLAAESASFTMAYTRVGLSPDGSASYHLPRLIGIAKTKQLMLTNRTLSAQEALQWGLV
GEVVADDRLQARADELAEQMAETSAGSNGGVKALLSDTFANGLEQQMELEGRLIAARAES
ADGREGVDAFLAKRRPKFGAQSAG
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