SitesBLAST
Comparing RR42_RS36495 FitnessBrowser__Cup4G11:RR42_RS36495 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, 95% coverage: 10:256/259 of query aligns to 11:255/257 of 6slbAAA
- active site: Q64 (≠ G63), F69 (≠ M68), L80 (≠ Q79), N84 (≠ H85), A108 (= A109), S111 (= S112), A130 (≠ P131), F131 (= F132), L136 (= L137), P138 (= P139), D139 (= D140), A224 (≠ E225), G234 (≠ F235)
- 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 (≠ S57), A62 (≠ S61), Q64 (≠ G63), D65 (= D64), L66 (≠ I65), Y76 (≠ E75), A108 (= A109), F131 (= F132), D139 (= D140)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
38% identity, 95% coverage: 10:256/259 of query aligns to 8:243/245 of 6slaAAA
- active site: Q61 (≠ G63), L68 (= L81), N72 (≠ H85), A96 (= A109), S99 (= S112), A118 (≠ P131), F119 (= F132), L124 (= L137), P126 (= P139), N127 (≠ D140), A212 (≠ E225), G222 (≠ F235)
- 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 (≠ K23), A59 (≠ S61), Q61 (≠ G63), D62 (= D64), L63 (≠ I65), L68 (= L81), Y71 (≠ I84), A94 (≠ Y107), G95 (= G108), A96 (= A109), F119 (= F132), I122 (≠ L135), L124 (= L137), N127 (≠ D140), F234 (= F247), K237 (= K250)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
33% identity, 99% coverage: 1:256/259 of query aligns to 3:257/259 of 5zaiC
- active site: A65 (≠ G63), F70 (≠ M68), S82 (vs. gap), R86 (= R78), G110 (≠ A109), E113 (≠ S112), P132 (= P131), E133 (≠ F132), I138 (≠ L137), P140 (= P139), G141 (≠ D140), A226 (≠ E225), F236 (= F235)
- binding coenzyme a: K24 (≠ R22), L25 (≠ K23), A63 (≠ S61), G64 (= G62), A65 (≠ G63), D66 (= D64), I67 (= I65), P132 (= P131), R166 (≠ E165), F248 (= F247), K251 (= K250)
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
33% identity, 93% coverage: 16:256/259 of query aligns to 19:259/261 of 5jbxB
- active site: A67 (≠ G63), R72 (≠ Q69), L84 (= L81), R88 (≠ H85), G112 (≠ A109), E115 (≠ S112), T134 (≠ P131), E135 (≠ F132), I140 (≠ L137), P142 (= P139), G143 (≠ D140), A228 (≠ E225), L238 (≠ F235)
- binding coenzyme a: S24 (≠ K21), R25 (= R22), R26 (≠ K23), A28 (= A25), A65 (≠ S61), D68 (= D64), L69 (≠ I65), K70 (≠ S66), L110 (≠ Y107), G111 (= G108), T134 (≠ P131), E135 (≠ F132), L138 (= L135), R168 (≠ E165)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
31% identity, 95% coverage: 12:256/259 of query aligns to 17:256/258 of 1mj3A
- active site: A68 (≠ G63), M73 (= M68), S83 (≠ A82), L85 (≠ I84), G109 (≠ A109), E112 (≠ S112), P131 (= P131), E132 (≠ F132), T137 (≠ L137), P139 (= P139), G140 (≠ D140), K225 (≠ E225), F235 (= F235)
- binding hexanoyl-coenzyme a: K26 (= K21), A27 (≠ R22), L28 (≠ K23), A30 (= A25), A66 (≠ S61), G67 (= G62), A68 (≠ G63), D69 (= D64), I70 (= I65), G109 (≠ A109), P131 (= P131), E132 (≠ F132), L135 (= L135), G140 (≠ D140)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
31% identity, 95% coverage: 12:256/259 of query aligns to 15:256/258 of 1ey3A
- active site: A66 (≠ G63), M71 (= M68), S81 (≠ R78), L85 (≠ I84), G109 (≠ A109), E112 (≠ S112), P131 (= P131), E132 (≠ F132), T137 (≠ L137), P139 (= P139), G140 (≠ D140), K225 (≠ E225), F235 (= F235)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (= K21), L26 (≠ K23), A28 (= A25), A64 (≠ S61), G65 (= G62), A66 (≠ G63), D67 (= D64), I68 (= I65), L85 (≠ I84), W88 (= W87), G109 (≠ A109), P131 (= P131), L135 (= L135), G140 (≠ D140)
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
31% identity, 95% coverage: 12:256/259 of query aligns to 16:252/254 of 2dubA
- active site: A67 (≠ G63), M72 (= M68), S82 (≠ P86), G105 (≠ A109), E108 (≠ S112), P127 (= P131), E128 (≠ F132), T133 (≠ L137), P135 (= P139), G136 (≠ D140), K221 (≠ E225), F231 (= F235)
- binding octanoyl-coenzyme a: K25 (= K21), A26 (≠ R22), L27 (≠ K23), A29 (= A25), A65 (≠ S61), A67 (≠ G63), D68 (= D64), I69 (= I65), K70 (≠ S66), G105 (≠ A109), E108 (≠ S112), P127 (= P131), E128 (≠ F132), G136 (≠ D140), A137 (≠ C141)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
31% identity, 95% coverage: 12:256/259 of query aligns to 17:258/260 of 1dubA
- active site: A68 (≠ G63), M73 (= M68), S83 (≠ R78), L87 (≠ I84), G111 (≠ A109), E114 (≠ S112), P133 (= P131), E134 (≠ F132), T139 (≠ L137), P141 (= P139), G142 (≠ D140), K227 (≠ E225), F237 (= F235)
- binding acetoacetyl-coenzyme a: K26 (= K21), A27 (≠ R22), L28 (≠ K23), A30 (= A25), A66 (≠ S61), A68 (≠ G63), D69 (= D64), I70 (= I65), Y107 (≠ A105), G110 (= G108), G111 (≠ A109), E114 (≠ S112), P133 (= P131), E134 (≠ F132), L137 (= L135), G142 (≠ D140), F233 (≠ Q231), F249 (= F247)
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)
31% identity, 95% coverage: 12:256/259 of query aligns to 47:288/290 of P14604
- E144 (≠ S112) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ F132) 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
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
32% identity, 95% coverage: 12:256/259 of query aligns to 17:258/260 of 2hw5C
- active site: A68 (≠ G63), M73 (= M68), S83 (≠ Q79), L87 (≠ A83), G111 (≠ A109), E114 (≠ S112), P133 (= P131), E134 (≠ F132), T139 (≠ L137), P141 (= P139), G142 (≠ D140), K227 (≠ E225), F237 (= F235)
- binding crotonyl coenzyme a: K26 (= K21), A27 (≠ R22), L28 (≠ K23), A30 (= A25), K62 (≠ S57), I70 (= I65), F109 (≠ Y107)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
33% identity, 98% coverage: 2:255/259 of query aligns to 3:253/256 of 3h81A
- active site: A64 (≠ G63), M69 (= M68), T79 (≠ R78), F83 (≠ A82), G107 (≠ A109), E110 (≠ S112), P129 (= P131), E130 (≠ F132), V135 (≠ L137), P137 (= P139), G138 (≠ D140), L223 (≠ E225), F233 (= F235)
- binding calcium ion: F233 (= F235), Q238 (≠ R240)
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
33% identity, 98% coverage: 2:255/259 of query aligns to 4:254/255 of 3q0jC
- active site: A65 (≠ G63), M70 (= M68), T80 (≠ R78), F84 (≠ A82), G108 (≠ A109), E111 (≠ S112), P130 (= P131), E131 (≠ F132), V136 (≠ L137), P138 (= P139), G139 (≠ D140), L224 (≠ E225), F234 (= F235)
- binding acetoacetyl-coenzyme a: Q23 (≠ K21), A24 (≠ R22), L25 (≠ K23), A27 (= A25), A63 (≠ S61), G64 (= G62), A65 (≠ G63), D66 (= D64), I67 (= I65), K68 (≠ S66), M70 (= M68), F84 (≠ A82), G107 (= G108), G108 (≠ A109), E111 (≠ S112), P130 (= P131), E131 (≠ F132), P138 (= P139), G139 (≠ D140), M140 (≠ C141)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 98% coverage: 2:255/259 of query aligns to 4:254/255 of 3q0gC
- active site: A65 (≠ G63), M70 (= M68), T80 (≠ R78), F84 (≠ A82), G108 (≠ A109), E111 (≠ S112), P130 (= P131), E131 (≠ F132), V136 (≠ L137), P138 (= P139), G139 (≠ D140), L224 (≠ E225), F234 (= F235)
- binding coenzyme a: L25 (≠ K23), A63 (≠ S61), I67 (= I65), K68 (≠ S66), Y104 (≠ A105), P130 (= P131), E131 (≠ F132), L134 (= L135)
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 98% coverage: 2:255/259 of query aligns to 3:249/250 of 3q0gD
- active site: A64 (≠ G63), M69 (= M68), T75 (≠ Q69), F79 (≠ S73), G103 (≠ A109), E106 (≠ S112), P125 (= P131), E126 (≠ F132), V131 (≠ L137), P133 (= P139), G134 (≠ D140), L219 (≠ E225), F229 (= F235)
- binding Butyryl Coenzyme A: F225 (≠ Q231), F241 (= F247)
1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
28% identity, 96% coverage: 2:249/259 of query aligns to 3:254/269 of 1jxzB
- active site: C61 (= C60), F64 (≠ G63), I69 (vs. gap), A86 (= A83), Q90 (≠ E89), G113 (= G108), G114 (≠ A109), G117 (≠ S112), A136 (≠ P131), W137 (≠ F132), I142 (≠ L137), N144 (≠ P139), D145 (= D140), E230 (= E225)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ K21), H23 (≠ R22), R24 (≠ K23), A62 (≠ S61), F64 (≠ G63), Y65 (≠ D64), L66 (≠ I65), R67 (≠ S66), W89 (≠ L88), G113 (= G108), A136 (≠ P131), W137 (≠ F132), I142 (≠ L137), D145 (= D140), T146 (≠ C141), F252 (= F247)
- binding calcium ion: G49 (≠ R48), L202 (≠ F197), A203 (≠ T198), A205 (= A200), T207 (≠ P202), Q210 (≠ V205)
Sites not aligning to the query:
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
27% identity, 96% coverage: 2:249/259 of query aligns to 3:254/269 of 1nzyB
- active site: C61 (= C60), F64 (≠ G63), I69 (vs. gap), A86 (= A83), H90 (= H85), G114 (≠ A109), G117 (≠ S112), A136 (≠ P131), W137 (≠ F132), I142 (≠ L137), N144 (≠ P139), D145 (= D140), E230 (= E225)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ K21), H23 (≠ R22), R24 (≠ K23), A62 (≠ S61), F64 (≠ G63), Y65 (≠ D64), L66 (≠ I65), R67 (≠ S66), W89 (vs. gap), G113 (= G108), G114 (≠ A109), A136 (≠ P131), W137 (≠ F132), D145 (= D140), T146 (≠ C141), F252 (= F247)
- binding calcium ion: G49 (≠ R48), L202 (≠ F197), A203 (≠ T198), A205 (= A200), T207 (≠ P202), Q210 (≠ V205)
- binding phosphate ion: E57 (≠ G56), N108 (≠ D103), K188 (≠ P183), R192 (≠ Q187)
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)
27% identity, 96% coverage: 2:249/259 of query aligns to 3:254/269 of A5JTM5
- R24 (≠ K23) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (= E33) mutation to T: Forms inclusion bodies.
- E43 (≠ R42) mutation to A: No effect on catalytic activity.
- D45 (= D44) mutation to A: No effect on catalytic activity.
- D46 (≠ T45) mutation to A: No effect on catalytic activity.
- G63 (= G62) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ G63) 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 (≠ D64) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (≠ S66) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (≠ S67) mutation to T: No effect on catalytic activity.
- H81 (≠ R78) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ Q79) 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 (= H85) 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 (≠ E89) mutation to Q: No effect on catalytic activity.
- A112 (≠ Y107) 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 (= G108) 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 (≠ A109) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G110) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D118) mutation to T: No effect on catalytic activity.
- D129 (≠ P124) mutation to T: No effect on catalytic activity.
- W137 (≠ F132) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D140) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (≠ T158) mutation to T: No effect on catalytic activity.
- E175 (≠ A170) mutation to D: No effect on catalytic activity.
- W179 (≠ Q174) mutation to F: No effect on catalytic activity.
- H208 (≠ V203) mutation to Q: No effect on catalytic activity.
- R216 (≠ A211) mutation R->E,K,L: Yields insoluble protein.
- E232 (= E227) 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.
4i52A Scmenb im complex with 1-hydroxy-2-naphthoyl-coa (see paper)
31% identity, 99% coverage: 2:257/259 of query aligns to 10:273/275 of 4i52A
- active site: G77 (= G63), R82 (≠ M68), Y87 (≠ I72), R95 (= R80), L99 (≠ I84), G123 (≠ A109), V126 (≠ S112), G146 (≠ F132), S151 (≠ L137), D153 (≠ P139), G154 (≠ D140), A240 (≠ E227), Y248 (≠ F235)
- binding 1-hydroxy-2-naphthoyl-CoA: H29 (≠ K21), K30 (≠ R22), R31 (≠ K23), A33 (= A25), S75 (= S61), G76 (= G62), G77 (= G63), D78 (= D64), Q79 (≠ I65), L96 (= L81), V98 (≠ A83), Y119 (≠ A105), I121 (≠ Y107), G123 (≠ A109), T145 (≠ P131), V149 (≠ L135), S151 (≠ L137), F152 (≠ V138)
4i4zA Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with salicylyl-coa (see paper)
31% identity, 99% coverage: 2:257/259 of query aligns to 10:273/275 of 4i4zA
- active site: G77 (= G63), R82 (≠ M68), Y87 (≠ I72), R95 (= R80), L99 (≠ I84), G123 (≠ A109), V126 (≠ S112), G146 (≠ F132), S151 (≠ L137), D153 (≠ P139), G154 (≠ D140), A240 (≠ E227), Y248 (≠ F235)
- binding Salicylyl CoA: H29 (≠ K21), K30 (≠ R22), R31 (≠ K23), S75 (= S61), G76 (= G62), G77 (= G63), D78 (= D64), Q79 (≠ I65), Y87 (≠ I72), V98 (≠ A83), G123 (≠ A109), T145 (≠ P131), V149 (≠ L135), S151 (≠ L137), F260 (= F247), K263 (= K250)
- binding bicarbonate ion: G122 (= G108), Q144 (≠ L130), T145 (≠ P131), G146 (≠ F132), W174 (≠ M160)
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
30% identity, 98% coverage: 2:255/259 of query aligns to 13:266/273 of Q5HH38
- R34 (≠ K23) binding in other chain
- SGGDQ 73:77 (≠ SGGDI 61:65) binding in other chain
- S149 (vs. gap) binding in other chain
Query Sequence
>RR42_RS36495 FitnessBrowser__Cup4G11:RR42_RS36495
METIRYAVADGVATLTLDFPKRKNALNGTMRREIGEVVHQLRQDTSVRALILTGAGSDFC
SGGDISSMQGEISAEQGRQRLAAIHPWLEDLIHLDRPVIAAVDGAAYGAGFSLALVADII
LATPRARFGLPFLRLGLVPDCGVFYTLPRMIGLQRAKTLMFSMRELSAAAALEQGIVMEI
VPPEALQARALALASAFTEASPVAVALTKKALNASLNQDLHSMLEMEADGQGIAFATAYR
QEAATRFLEKQPPRYRWPD
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