SitesBLAST
Comparing PP_3732 FitnessBrowser__Putida:PP_3732 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)
7borA Structure of pseudomonas aeruginosa coa-bound odaa (see paper)
51% identity, 96% coverage: 2:238/248 of query aligns to 1:237/247 of 7borA
- active site: N63 (= N64), F68 (= F69), D77 (= D78), G81 (≠ F82), I105 (= I106), T108 (= T109), F128 (= F129), L133 (≠ V134), P135 (= P136), E136 (= E137), A222 (= A223), L232 (= L233)
- binding coenzyme a: D21 (= D22), K22 (= K23), A25 (= A26), S61 (≠ A62), I65 (≠ L66), V103 (≠ I104), F128 (= F129), L131 (= L132)
Sites not aligning to the query:
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
37% identity, 94% coverage: 4:237/248 of query aligns to 4:238/257 of 6slbAAA
- active site: Q64 (≠ N64), F69 (= F69), L80 (≠ V81), N84 (≠ M85), A108 (≠ I106), S111 (≠ T109), A130 (≠ P128), F131 (= F129), L136 (≠ V134), P138 (= P136), D139 (≠ E137), A224 (= A223), G234 (≠ L233)
- 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 (≠ H58), A62 (= A62), Q64 (≠ N64), D65 (= D65), L66 (= L66), Y76 (≠ L77), A108 (≠ I106), F131 (= F129), D139 (≠ E137)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
36% identity, 91% coverage: 4:228/248 of query aligns to 1:217/245 of 6slaAAA
- active site: Q61 (≠ N64), L68 (≠ V81), N72 (≠ M85), A96 (≠ I106), S99 (≠ T109), A118 (≠ P128), F119 (= F129), L124 (≠ V134), P126 (= P136), N127 (≠ E137), A212 (= A223)
- 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 (= L24), A59 (= A62), Q61 (≠ N64), D62 (= D65), L63 (= L66), L68 (≠ V81), Y71 (≠ L84), A94 (≠ I104), G95 (= G105), A96 (≠ I106), F119 (= F129), I122 (≠ L132), L124 (≠ V134), N127 (≠ E137)
Sites not aligning to the query:
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
32% identity, 94% coverage: 4:237/248 of query aligns to 7:238/255 of 3q0jC
- active site: A65 (≠ N64), M70 (≠ F69), T80 (≠ D78), F84 (= F82), G108 (≠ I106), E111 (≠ T109), P130 (= P128), E131 (≠ F129), V136 (= V134), P138 (= P136), G139 (≠ E137), L224 (≠ A223), F234 (≠ L233)
- binding acetoacetyl-coenzyme a: Q23 (≠ D22), A24 (≠ K23), L25 (= L24), A27 (= A26), A63 (= A62), G64 (= G63), A65 (≠ N64), D66 (= D65), I67 (≠ L66), K68 (≠ R67), M70 (≠ F69), F84 (= F82), G107 (= G105), G108 (≠ I106), E111 (≠ T109), P130 (= P128), E131 (≠ F129), P138 (= P136), G139 (≠ E137), M140 (≠ F138)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 94% coverage: 4:237/248 of query aligns to 7:238/255 of 3q0gC
- active site: A65 (≠ N64), M70 (≠ F69), T80 (≠ D78), F84 (= F82), G108 (≠ I106), E111 (≠ T109), P130 (= P128), E131 (≠ F129), V136 (= V134), P138 (= P136), G139 (≠ E137), L224 (≠ A223), F234 (≠ L233)
- binding coenzyme a: L25 (= L24), A63 (= A62), I67 (≠ L66), K68 (≠ R67), Y104 (≠ A102), P130 (= P128), E131 (≠ F129), L134 (= L132)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
32% identity, 94% coverage: 4:237/248 of query aligns to 6:237/256 of 3h81A
- active site: A64 (≠ N64), M69 (≠ F69), T79 (≠ D78), F83 (= F82), G107 (≠ I106), E110 (≠ T109), P129 (= P128), E130 (≠ F129), V135 (= V134), P137 (= P136), G138 (≠ E137), L223 (≠ A223), F233 (≠ L233)
- binding calcium ion: F233 (≠ L233)
Sites not aligning to the query:
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
32% identity, 94% coverage: 4:237/248 of query aligns to 6:233/250 of 3q0gD
- active site: A64 (≠ N64), M69 (vs. gap), T75 (≠ P74), F79 (= F82), G103 (≠ I106), E106 (≠ T109), P125 (= P128), E126 (≠ F129), V131 (= V134), P133 (= P136), G134 (≠ E137), L219 (≠ A223), F229 (≠ L233)
- binding Butyryl Coenzyme A: F225 (= F229)
Sites not aligning to the query:
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
33% identity, 71% coverage: 3:177/248 of query aligns to 4:181/259 of 5zaiC
- active site: A65 (≠ N64), F70 (= F69), S82 (≠ D78), R86 (≠ F82), G110 (≠ I106), E113 (≠ T109), P132 (= P128), E133 (≠ F129), I138 (≠ V134), P140 (= P136), G141 (≠ E137)
- binding coenzyme a: K24 (= K23), L25 (= L24), A63 (= A62), G64 (= G63), A65 (≠ N64), D66 (= D65), I67 (≠ L66), P132 (= P128), R166 (≠ L162)
Sites not aligning to the query:
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
29% identity, 95% coverage: 12:247/248 of query aligns to 17:245/254 of 2dubA
- active site: A67 (≠ N64), M72 (≠ F69), S82 (= S79), G105 (≠ I106), E108 (≠ T109), P127 (= P128), E128 (≠ F129), T133 (≠ V134), P135 (= P136), G136 (≠ E137), K221 (vs. gap), F231 (≠ L233)
- binding octanoyl-coenzyme a: K25 (≠ D22), A26 (≠ K23), L27 (= L24), A29 (= A26), A65 (= A62), A67 (≠ N64), D68 (= D65), I69 (≠ L66), K70 (≠ R67), G105 (≠ I106), E108 (≠ T109), P127 (= P128), E128 (≠ F129), G136 (≠ E137), A137 (≠ F138)
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
29% identity, 95% coverage: 12:247/248 of query aligns to 16:249/258 of 1ey3A
- active site: A66 (≠ N64), M71 (≠ F69), S81 (= S79), L85 (vs. gap), G109 (≠ I106), E112 (≠ T109), P131 (= P128), E132 (≠ F129), T137 (≠ V134), P139 (= P136), G140 (≠ E137), K225 (vs. gap), F235 (≠ L233)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ D22), L26 (= L24), A28 (= A26), A64 (= A62), G65 (= G63), A66 (≠ N64), D67 (= D65), I68 (≠ L66), L85 (vs. gap), W88 (≠ M85), G109 (≠ I106), P131 (= P128), L135 (= L132), G140 (≠ E137)
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
29% identity, 95% coverage: 12:247/248 of query aligns to 18:251/260 of 1dubA
- active site: A68 (≠ N64), M73 (≠ F69), S83 (= S79), L87 (vs. gap), G111 (≠ I106), E114 (≠ T109), P133 (= P128), E134 (≠ F129), T139 (≠ V134), P141 (= P136), G142 (≠ E137), K227 (vs. gap), F237 (≠ L233)
- binding acetoacetyl-coenzyme a: K26 (≠ D22), A27 (≠ K23), L28 (= L24), A30 (= A26), A66 (= A62), A68 (≠ N64), D69 (= D65), I70 (≠ L66), Y107 (≠ A102), G110 (= G105), G111 (≠ I106), E114 (≠ T109), P133 (= P128), E134 (≠ F129), L137 (= L132), G142 (≠ E137), F233 (= F229), F249 (≠ L245)
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
29% identity, 95% coverage: 12:247/248 of query aligns to 18:249/258 of 1mj3A
- active site: A68 (≠ N64), M73 (≠ F69), S83 (= S79), L85 (≠ V81), G109 (≠ I106), E112 (≠ T109), P131 (= P128), E132 (≠ F129), T137 (≠ V134), P139 (= P136), G140 (≠ E137), K225 (vs. gap), F235 (≠ L233)
- binding hexanoyl-coenzyme a: K26 (≠ D22), A27 (≠ K23), L28 (= L24), A30 (= A26), A66 (= A62), G67 (= G63), A68 (≠ N64), D69 (= D65), I70 (≠ L66), G109 (≠ I106), P131 (= P128), E132 (≠ F129), L135 (= L132), G140 (≠ E137)
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)
29% identity, 95% coverage: 12:247/248 of query aligns to 48:281/290 of P14604
- E144 (≠ T109) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (≠ F129) 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
3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium (see paper)
34% identity, 85% coverage: 15:225/248 of query aligns to 13:216/224 of 3p85A
- active site: L62 (≠ N64), L67 (≠ F69), P68 (≠ L70), G92 (≠ I106), E95 (≠ T109), T114 (≠ P128), H115 (≠ F129), L120 (≠ V134), P122 (= P136), T123 (≠ E137), W208 (vs. gap)
- binding calcium ion: D43 (= D45), D45 (≠ A47)
Sites not aligning to the query:
3rrvB Crystal structure of an enoyl-coa hydratase/isomerase from mycobacterium paratuberculosis (see paper)
29% identity, 95% coverage: 10:245/248 of query aligns to 13:250/254 of 3rrvB
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
28% identity, 95% coverage: 12:247/248 of query aligns to 18:251/260 of 2hw5C
- active site: A68 (≠ N64), M73 (≠ F69), S83 (= S79), L87 (vs. gap), G111 (≠ I106), E114 (≠ T109), P133 (= P128), E134 (≠ F129), T139 (≠ V134), P141 (= P136), G142 (≠ E137), K227 (vs. gap), F237 (≠ L233)
- binding crotonyl coenzyme a: K26 (≠ D22), A27 (≠ K23), L28 (= L24), A30 (= A26), K62 (≠ H58), I70 (≠ L66), F109 (≠ I104)
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
30% identity, 69% coverage: 8:177/248 of query aligns to 5:172/692 of 6iunB
Sites not aligning to the query:
- active site: 248, 407, 428, 440, 478
- binding nicotinamide-adenine-dinucleotide: 300, 301, 302, 321, 322, 365, 377, 378, 380, 384, 388, 405, 407
1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
29% identity, 80% coverage: 1:199/248 of query aligns to 1:206/269 of 1jxzB
- active site: C61 (≠ S61), F64 (≠ N64), I69 (≠ F69), A86 (vs. gap), Q90 (vs. gap), G113 (= G105), G114 (≠ I106), G117 (≠ T109), A136 (≠ P128), W137 (≠ F129), I142 (≠ V134), N144 (≠ P136), D145 (≠ E137)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ D22), H23 (≠ K23), R24 (≠ L24), A62 (= A62), F64 (≠ N64), Y65 (≠ D65), L66 (= L66), R67 (= R67), W89 (vs. gap), G113 (= G105), A136 (≠ P128), W137 (≠ F129), I142 (≠ V134), D145 (≠ E137), T146 (≠ F138)
- binding calcium ion: G49 (≠ D49), L202 (= L195), A203 (≠ Q196), A205 (≠ Y198)
Sites not aligning to the query:
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
32% identity, 86% coverage: 25:237/248 of query aligns to 27:242/261 of 5jbxB
- active site: A67 (≠ N64), R72 (≠ F69), L84 (= L77), R88 (≠ F82), G112 (≠ I106), E115 (≠ T109), T134 (≠ P128), E135 (≠ F129), I140 (≠ V134), P142 (= P136), G143 (≠ E137), A228 (= A223), L238 (= L233)
- binding coenzyme a: A28 (= A26), A65 (= A62), D68 (= D65), L69 (= L66), K70 (≠ R67), L110 (≠ I104), G111 (= G105), T134 (≠ P128), E135 (≠ F129), L138 (= L132), R168 (≠ L162)
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)
28% identity, 80% coverage: 1:199/248 of query aligns to 1:206/269 of A5JTM5
- R24 (≠ L24) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (≠ L34) mutation to T: Forms inclusion bodies.
- E43 (≠ G43) mutation to A: No effect on catalytic activity.
- D45 (= D45) mutation to A: No effect on catalytic activity.
- D46 (≠ P46) mutation to A: No effect on catalytic activity.
- G63 (= G63) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ N64) 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 (≠ D65) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (= R67) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (≠ D68) mutation to T: No effect on catalytic activity.
- H81 (≠ P80) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ V81) 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 (≠ F82) 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 (≠ R86) mutation to Q: No effect on catalytic activity.
- A112 (≠ I104) 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 (= G105) 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 (≠ I106) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G107) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D115) mutation to T: No effect on catalytic activity.
- D129 (≠ R121) mutation to T: No effect on catalytic activity.
- W137 (≠ F129) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (≠ E137) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (≠ R155) mutation to T: No effect on catalytic activity.
- E175 (≠ Q167) mutation to D: No effect on catalytic activity.
- W179 (= W171) 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.
Query Sequence
>PP_3732 FitnessBrowser__Putida:PP_3732
MNDLITRELDQGLLTLAFNRPDKLNALNTAMYQLLGDLLLAAGEDPAVDAIIITGGPHCF
SAGNDLRDFLDNPPSDLDSPVFRLMRVVMGLDKPLIAAVSGAAIGIGATLLLHCDQVLVS
RSTKLRMPFAPLGVCPEFGSSLLLPRVLGQARAARLLLTNALLDGEQMLAWGLANELHEN
GEQCLEAARTLARQLQGYPQAALRISKRLLKDSQRAELEATVARESQLFIECLRTEEARA
VLRGLIKD
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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