SitesBLAST
Comparing PfGW456L13_2433 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2433 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)
47% identity, 100% coverage: 2:263/263 of query aligns to 1:257/257 of 6slbAAA
- active site: Q64 (= Q65), F69 (≠ R70), L80 (≠ E86), N84 (= N90), A108 (= A114), S111 (≠ N117), A130 (= A136), F131 (= F137), L136 (= L142), P138 (= P144), D139 (= D145), A224 (≠ E230), 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 (= R59), A62 (= A63), Q64 (= Q65), D65 (= D66), L66 (= L67), Y76 (≠ L81), A108 (= A114), F131 (= F137), D139 (= D145)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
45% identity, 98% coverage: 6:263/263 of query aligns to 2:245/245 of 6slaAAA
- active site: Q61 (= Q65), L68 (≠ V72), N72 (= N90), A96 (= A114), S99 (≠ N117), A118 (= A136), F119 (= F137), L124 (= L142), P126 (= P144), N127 (≠ D145), A212 (≠ E230), 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 (= L25), A59 (= A63), Q61 (= Q65), D62 (= D66), L63 (= L67), L68 (≠ V72), Y71 (= Y89), A94 (= A112), G95 (= G113), A96 (= A114), F119 (= F137), I122 (= I140), L124 (= L142), N127 (≠ D145), F234 (= F252), K237 (= K255)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
35% identity, 100% coverage: 1:263/263 of query aligns to 1:259/259 of 5zaiC
- active site: A65 (≠ Q65), F70 (≠ R70), S82 (≠ E86), R86 (≠ N90), G110 (≠ A114), E113 (≠ N117), P132 (≠ A136), E133 (≠ F137), I138 (≠ L142), P140 (= P144), G141 (≠ D145), A226 (≠ E230), F236 (≠ G240)
- binding coenzyme a: K24 (≠ Q24), L25 (= L25), A63 (= A63), G64 (= G64), A65 (≠ Q65), D66 (= D66), I67 (≠ L67), P132 (≠ A136), R166 (= R170), F248 (= F252), K251 (= K255)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
32% identity, 99% coverage: 1:260/263 of query aligns to 1:254/255 of 3q0jC
- active site: A65 (≠ Q65), M70 (≠ V78), T80 (≠ E86), F84 (≠ N90), G108 (≠ A114), E111 (≠ N117), P130 (≠ A136), E131 (≠ F137), V136 (≠ L142), P138 (= P144), G139 (≠ D145), L224 (≠ E230), F234 (≠ G240)
- binding acetoacetyl-coenzyme a: Q23 (≠ D23), A24 (≠ Q24), L25 (= L25), A27 (≠ S27), A63 (= A63), G64 (= G64), A65 (≠ Q65), D66 (= D66), I67 (≠ L67), K68 (≠ S68), M70 (≠ V78), 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
32% identity, 99% coverage: 1:260/263 of query aligns to 1:254/255 of 3q0gC
- active site: A65 (≠ Q65), M70 (≠ V78), T80 (≠ E86), F84 (≠ N90), G108 (≠ A114), E111 (≠ N117), P130 (≠ A136), E131 (≠ F137), V136 (≠ L142), P138 (= P144), G139 (≠ D145), L224 (≠ E230), F234 (≠ G240)
- binding coenzyme a: L25 (= L25), A63 (= A63), I67 (≠ L67), K68 (≠ S68), Y104 (≠ V110), P130 (≠ A136), E131 (≠ F137), L134 (≠ I140)
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
35% identity, 99% coverage: 2:261/263 of query aligns to 2:258/260 of 2hw5C
- active site: A68 (≠ Q65), M73 (vs. gap), S83 (≠ E83), L87 (≠ Y89), G111 (≠ A114), E114 (≠ N117), P133 (≠ A136), E134 (≠ F137), T139 (≠ L142), P141 (= P144), G142 (≠ D145), K227 (≠ E230), F237 (≠ G240)
- binding crotonyl coenzyme a: K26 (≠ D23), A27 (≠ Q24), L28 (= L25), A30 (≠ S27), K62 (≠ R59), I70 (≠ L67), F109 (≠ A112)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
32% identity, 100% coverage: 2:263/263 of query aligns to 1:256/256 of 3h81A
- active site: A64 (≠ Q65), M69 (≠ V78), T79 (≠ E86), F83 (≠ N90), G107 (≠ A114), E110 (≠ N117), P129 (≠ A136), E130 (≠ F137), V135 (≠ L142), P137 (= P144), G138 (≠ D145), L223 (≠ E230), F233 (≠ G240)
- binding calcium ion: F233 (≠ G240), Q238 (≠ Y245)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
33% identity, 99% coverage: 2:261/263 of query aligns to 2:256/258 of 1mj3A
- active site: A68 (≠ Q65), M73 (≠ R70), S83 (≠ N90), L85 (= L92), G109 (≠ A114), E112 (≠ N117), P131 (≠ A136), E132 (≠ F137), T137 (≠ L142), P139 (= P144), G140 (≠ D145), K225 (≠ E230), F235 (≠ G240)
- binding hexanoyl-coenzyme a: K26 (≠ D23), A27 (≠ Q24), L28 (= L25), A30 (≠ S27), A66 (= A63), G67 (= G64), A68 (≠ Q65), D69 (= D66), I70 (≠ L67), 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
31% identity, 98% coverage: 2:260/263 of query aligns to 1:249/250 of 3q0gD
- active site: A64 (≠ Q65), M69 (≠ R70), T75 (≠ E86), F79 (≠ N90), G103 (≠ A114), E106 (≠ N117), P125 (≠ A136), E126 (≠ F137), V131 (≠ L142), P133 (= P144), G134 (≠ D145), L219 (≠ E230), F229 (≠ G240)
- binding Butyryl Coenzyme A: F225 (≠ Q236), F241 (= F252)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
33% identity, 99% coverage: 2:261/263 of query aligns to 1:252/254 of 2dubA
- active site: A67 (≠ Q65), M72 (≠ R70), S82 (≠ N90), G105 (≠ A114), E108 (≠ N117), P127 (≠ A136), E128 (≠ F137), T133 (≠ L142), P135 (= P144), G136 (≠ D145), K221 (≠ E230), F231 (≠ G240)
- binding octanoyl-coenzyme a: K25 (≠ D23), A26 (≠ Q24), L27 (= L25), A29 (≠ S27), A65 (= A63), A67 (≠ Q65), D68 (= D66), I69 (≠ L67), K70 (≠ S68), G105 (≠ A114), E108 (≠ N117), P127 (≠ A136), E128 (≠ F137), G136 (≠ D145), A137 (≠ S146)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
34% identity, 99% coverage: 2:261/263 of query aligns to 2:258/260 of 1dubA
- active site: A68 (≠ Q65), M73 (≠ R70), S83 (≠ E83), L87 (≠ Y89), G111 (≠ A114), E114 (≠ N117), P133 (≠ A136), E134 (≠ F137), T139 (≠ L142), P141 (= P144), G142 (≠ D145), K227 (≠ E230), F237 (≠ G240)
- binding acetoacetyl-coenzyme a: K26 (≠ D23), A27 (≠ Q24), L28 (= L25), A30 (≠ S27), A66 (= A63), A68 (≠ Q65), D69 (= D66), I70 (≠ L67), Y107 (≠ V110), G110 (= G113), G111 (≠ A114), E114 (≠ N117), P133 (≠ A136), E134 (≠ F137), L137 (≠ I140), G142 (≠ D145), F233 (≠ Q236), F249 (= F252)
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, 99% coverage: 2:261/263 of query aligns to 32:288/290 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
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
34% identity, 95% coverage: 12:261/263 of query aligns to 13:256/258 of 1ey3A
- active site: A66 (≠ Q65), M71 (≠ R70), S81 (≠ E83), L85 (≠ Y89), G109 (≠ A114), E112 (≠ N117), P131 (≠ A136), E132 (≠ F137), T137 (≠ L142), P139 (= P144), G140 (≠ D145), K225 (≠ E230), F235 (≠ G240)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ D23), L26 (= L25), A28 (≠ S27), A64 (= A63), G65 (= G64), A66 (≠ Q65), D67 (= D66), I68 (≠ L67), L85 (≠ Y89), W88 (≠ L92), G109 (≠ A114), P131 (≠ A136), L135 (≠ I140), G140 (≠ D145)
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
33% identity, 87% coverage: 3:232/263 of query aligns to 2:232/269 of 1nzyB
- active site: C61 (= C62), F64 (≠ Q65), I69 (≠ R70), A86 (≠ E86), H90 (≠ N90), G114 (≠ A114), G117 (≠ N117), A136 (= A136), W137 (≠ F137), I142 (≠ L142), N144 (≠ P144), D145 (= D145), E230 (= E230)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D23), H23 (≠ Q24), R24 (≠ L25), A62 (= A63), F64 (≠ Q65), Y65 (≠ D66), L66 (= L67), R67 (≠ S68), W89 (≠ Y89), G113 (= G113), G114 (≠ A114), A136 (= A136), W137 (≠ F137), D145 (= D145), T146 (≠ S146)
- binding calcium ion: G49 (≠ R50), L202 (= L202), A203 (= A203), A205 (≠ Q205), T207 (= T207), Q210 (≠ L210)
- binding phosphate ion: E57 (≠ G58), N108 (= N108), K188 (≠ D188), R192 (= R192)
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)
33% identity, 87% coverage: 3:232/263 of query aligns to 2:232/269 of 1jxzB
- active site: C61 (= C62), F64 (≠ Q65), I69 (≠ R70), A86 (≠ E86), Q90 (≠ N90), G113 (= G113), G114 (≠ A114), G117 (≠ N117), A136 (= A136), W137 (≠ F137), I142 (≠ L142), N144 (≠ P144), D145 (= D145), E230 (= E230)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D23), H23 (≠ Q24), R24 (≠ L25), A62 (= A63), F64 (≠ Q65), Y65 (≠ D66), L66 (= L67), R67 (≠ S68), W89 (≠ Y89), G113 (= G113), A136 (= A136), W137 (≠ F137), I142 (≠ L142), D145 (= D145), T146 (≠ S146)
- binding calcium ion: G49 (≠ R50), L202 (= L202), A203 (= A203), A205 (≠ Q205), T207 (= T207), Q210 (≠ L210)
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)
33% identity, 87% coverage: 3:232/263 of query aligns to 2:232/269 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 (≠ R44) mutation to A: No effect on catalytic activity.
- D45 (≠ N46) mutation to A: No effect on catalytic activity.
- D46 (≠ P47) mutation to A: No effect on catalytic activity.
- G63 (= G64) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ Q65) 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 (≠ S68) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (≠ D69) 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 (≠ Y89) 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 (≠ A163) mutation to T: No effect on catalytic activity.
- E175 (≠ Q175) mutation to D: No effect on catalytic activity.
- W179 (= W179) mutation to F: No effect on catalytic activity.
- H208 (≠ Y208) mutation to Q: No effect on catalytic activity.
- R216 (≠ S216) 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.
2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa (see paper)
30% identity, 98% coverage: 3:260/263 of query aligns to 7:253/260 of 2uzfA
- active site: G70 (≠ Q65), R80 (≠ G75), L84 (≠ P79), G108 (≠ A114), V111 (≠ N117), T130 (≠ A136), G131 (≠ F137), S136 (≠ L142), D138 (≠ P144), A139 (≠ D145), A225 (≠ E232), Y233 (≠ G240)
- binding acetoacetyl-coenzyme a: V28 (≠ Q24), R29 (≠ L25), S68 (≠ A63), G69 (= G64), G70 (≠ Q65), D71 (= D66), Y104 (≠ V110), G108 (≠ A114)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
32% identity, 95% coverage: 14:263/263 of query aligns to 15:261/261 of 5jbxB
- active site: A67 (≠ Q65), R72 (= R70), L84 (≠ Y89), R88 (≠ I93), G112 (≠ A114), E115 (≠ N117), T134 (≠ A136), E135 (≠ F137), I140 (≠ L142), P142 (= P144), G143 (≠ D145), A228 (≠ E230), L238 (≠ G240)
- binding coenzyme a: S24 (≠ D23), R25 (≠ Q24), R26 (≠ L25), A28 (≠ S27), A65 (= A63), D68 (= D66), L69 (= L67), K70 (≠ S68), L110 (≠ A112), G111 (= G113), T134 (≠ A136), E135 (≠ F137), L138 (≠ I140), R168 (= R170)
4i52A Scmenb im complex with 1-hydroxy-2-naphthoyl-coa (see paper)
31% identity, 98% coverage: 2:260/263 of query aligns to 8:268/275 of 4i52A
- active site: G77 (≠ Q65), R82 (= R70), Y87 (≠ A77), R95 (≠ I85), L99 (≠ Y89), G123 (≠ A114), V126 (≠ N117), G146 (≠ F137), S151 (≠ L142), D153 (≠ P144), G154 (≠ D145), A240 (≠ E232), Y248 (≠ G240)
- binding 1-hydroxy-2-naphthoyl-CoA: H29 (≠ D23), K30 (≠ Q24), R31 (≠ L25), A33 (≠ S27), S75 (≠ A63), G76 (= G64), G77 (≠ Q65), D78 (= D66), Q79 (≠ L67), L96 (≠ E86), V98 (≠ F88), Y119 (≠ V110), I121 (≠ A112), G123 (≠ A114), T145 (≠ A136), V149 (≠ I140), S151 (≠ L142), F152 (≠ I143)
4i4zA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with salicylyl-coa (see paper)
31% identity, 98% coverage: 2:260/263 of query aligns to 8:268/275 of 4i4zA
- active site: G77 (≠ Q65), R82 (= R70), Y87 (≠ A77), R95 (≠ I85), L99 (≠ Y89), G123 (≠ A114), V126 (≠ N117), G146 (≠ F137), S151 (≠ L142), D153 (≠ P144), G154 (≠ D145), A240 (≠ E232), Y248 (≠ G240)
- binding Salicylyl CoA: H29 (≠ D23), K30 (≠ Q24), R31 (≠ L25), S75 (≠ A63), G76 (= G64), G77 (≠ Q65), D78 (= D66), Q79 (≠ L67), Y87 (≠ A77), V98 (≠ F88), G123 (≠ A114), T145 (≠ A136), V149 (≠ I140), S151 (≠ L142), F260 (= F252), K263 (= K255)
- binding bicarbonate ion: G122 (= G113), Q144 (= Q135), T145 (≠ A136), G146 (≠ F137), W174 (≠ A165)
Query Sequence
>PfGW456L13_2433 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_2433
MNFEHILFSIEAGVALLSLNRPDQLNSFNTQMHGEVKEALKQVRQNPDVRVLLLTGEGRG
FCAGQDLSDRNVAPGSAVPDLGESIEKFYNPLIRQLRDLPMPVICAVNGVAAGAGANIPL
ACDLVLAARSASFIQAFCKIGLIPDSGGTWTLPRLVGMARAKALALLGNRLSAEQAEQWG
LIYQCVEDAELRDEALKLARHLATQPTYGLALIKRSLNASMSNSFDEQLELEKDLQRLAG
RSEDYREGVGAFMEKRTPSFKGR
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