SitesBLAST
Comparing AO356_30360 FitnessBrowser__pseudo5_N2C3_1:AO356_30360 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
32% identity, 90% coverage: 10:230/245 of query aligns to 6:224/259 of 5zaiC
- active site: A65 (≠ V70), F70 (vs. gap), S82 (≠ R83), R86 (= R87), G110 (= G117), E113 (≠ M120), P132 (= P139), E133 (= E140), I138 (= I145), P140 (≠ T147), G141 (vs. gap)
- binding coenzyme a: K24 (= K28), L25 (≠ A29), A63 (= A68), G64 (= G69), A65 (≠ V70), D66 (= D71), I67 (= I72), P132 (= P139), R166 (≠ A172)
Sites not aligning to the query:
3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
34% identity, 96% coverage: 10:245/245 of query aligns to 5:234/250 of 3q0gD
- active site: A64 (≠ V70), M69 (≠ Q75), T75 (= T81), F79 (≠ A93), G103 (= G117), E106 (≠ M120), P125 (= P139), E126 (= E140), V131 (≠ I145), P133 (≠ A146), G134 (≠ T147), L219 (vs. gap), F229 (≠ L240)
- binding Butyryl Coenzyme A: F225 (≠ R236)
Sites not aligning to the query:
3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
33% identity, 96% coverage: 10:245/245 of query aligns to 6:239/255 of 3q0jC
- active site: A65 (≠ V70), M70 (≠ Q75), T80 (= T81), F84 (≠ A93), G108 (= G117), E111 (≠ M120), P130 (= P139), E131 (= E140), V136 (≠ I145), P138 (≠ A146), G139 (≠ T147), L224 (vs. gap), F234 (≠ L240)
- binding acetoacetyl-coenzyme a: Q23 (≠ A27), A24 (≠ K28), L25 (≠ A29), A27 (= A31), A63 (= A68), G64 (= G69), A65 (≠ V70), D66 (= D71), I67 (= I72), K68 (≠ R73), M70 (≠ Q75), F84 (≠ A93), G107 (= G116), G108 (= G117), E111 (≠ M120), P130 (= P139), E131 (= E140), P138 (≠ A146), G139 (≠ T147), M140 (≠ F148)
3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
33% identity, 96% coverage: 10:245/245 of query aligns to 6:239/255 of 3q0gC
- active site: A65 (≠ V70), M70 (≠ Q75), T80 (= T81), F84 (≠ A93), G108 (= G117), E111 (≠ M120), P130 (= P139), E131 (= E140), V136 (≠ I145), P138 (≠ A146), G139 (≠ T147), L224 (vs. gap), F234 (≠ L240)
- binding coenzyme a: L25 (≠ A29), A63 (= A68), I67 (= I72), K68 (≠ R73), Y104 (≠ T113), P130 (= P139), E131 (= E140), L134 (= L143)
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
33% identity, 96% coverage: 10:245/245 of query aligns to 5:238/256 of 3h81A
- active site: A64 (≠ V70), M69 (≠ Q75), T79 (= T81), F83 (≠ A93), G107 (= G117), E110 (≠ M120), P129 (= P139), E130 (= E140), V135 (≠ I145), P137 (≠ A146), G138 (≠ T147), L223 (vs. gap), F233 (≠ L240)
- binding calcium ion: F233 (≠ L240), Q238 (= Q245)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 89% coverage: 13:230/245 of query aligns to 8:222/257 of 6slbAAA
- active site: Q64 (≠ V70), F69 (≠ D78), L80 (≠ S89), N84 (≠ A93), A108 (≠ G117), S111 (≠ M120), A130 (≠ P139), F131 (≠ E140), L136 (≠ I145), P138 (≠ T147), D139 (≠ F148)
- 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 (= R64), A62 (= A68), Q64 (≠ V70), D65 (= D71), L66 (≠ I72), Y76 (≠ R85), A108 (≠ G117), F131 (≠ E140), D139 (≠ F148)
Sites not aligning to the query:
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
33% identity, 89% coverage: 13:230/245 of query aligns to 5:210/245 of 6slaAAA
- active site: Q61 (≠ V70), L68 (≠ A82), N72 (≠ E86), A96 (≠ G117), S99 (≠ M120), A118 (≠ P139), F119 (≠ E140), L124 (≠ I145), P126 (≠ T147), N127 (≠ F148)
- 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 (≠ A29), A59 (= A68), Q61 (≠ V70), D62 (= D71), L63 (≠ I72), L68 (≠ A82), Y71 (≠ R85), A94 (≠ T115), G95 (= G116), A96 (≠ G117), F119 (≠ E140), I122 (≠ L143), L124 (≠ I145), N127 (≠ F148)
Sites not aligning to the query:
2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
33% identity, 71% coverage: 14:187/245 of query aligns to 12:176/254 of 2dubA
- active site: A67 (≠ V70), M72 (≠ Q75), S82 (≠ A94), G105 (= G117), E108 (≠ M120), P127 (= P139), E128 (= E140), T133 (vs. gap), P135 (≠ A146), G136 (≠ T147)
- binding octanoyl-coenzyme a: K25 (≠ A27), A26 (≠ K28), L27 (≠ A29), A29 (= A31), A65 (= A68), A67 (≠ V70), D68 (= D71), I69 (= I72), K70 (≠ R73), G105 (= G117), E108 (≠ M120), P127 (= P139), E128 (= E140), G136 (≠ T147), A137 (≠ F148)
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)
32% identity, 76% coverage: 21:206/245 of query aligns to 16:204/269 of 1jxzB
- active site: C61 (= C67), F64 (≠ V70), I69 (≠ Q75), A86 (≠ L92), Q90 (= Q96), G113 (= G116), G114 (= G117), G117 (≠ M120), A136 (≠ S137), W137 (≠ L138), I142 (≠ L143), N144 (≠ I145), D145 (≠ A146)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ A27), H23 (≠ K28), R24 (≠ A29), A62 (= A68), F64 (≠ V70), Y65 (≠ D71), L66 (≠ I72), R67 (= R73), W89 (≠ L95), G113 (= G116), A136 (≠ S137), W137 (≠ L138), I142 (≠ L143), D145 (≠ A146), T146 (= T147)
- binding calcium ion: G49 (≠ N54), L202 (= L204), A203 (≠ G205)
Sites not aligning to the query:
1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
33% identity, 71% coverage: 14:187/245 of query aligns to 11:180/258 of 1ey3A
- active site: A66 (≠ V70), M71 (≠ Q75), S81 (= S89), L85 (≠ A93), G109 (= G117), E112 (≠ M120), P131 (= P139), E132 (= E140), T137 (vs. gap), P139 (≠ A146), G140 (≠ T147)
- binding 4-(n,n-dimethylamino)cinnamoyl-coa: K24 (≠ A27), L26 (≠ A29), A28 (= A31), A64 (= A68), G65 (= G69), A66 (≠ V70), D67 (= D71), I68 (= I72), L85 (≠ A93), W88 (≠ Q96), G109 (= G117), P131 (= P139), L135 (= L143), G140 (≠ T147)
Sites not aligning to the query:
1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
33% identity, 71% coverage: 14:187/245 of query aligns to 13:182/260 of 1dubA
- active site: A68 (≠ V70), M73 (≠ Q75), S83 (= S89), L87 (≠ A93), G111 (= G117), E114 (≠ M120), P133 (= P139), E134 (= E140), T139 (vs. gap), P141 (≠ A146), G142 (≠ T147)
- binding acetoacetyl-coenzyme a: K26 (≠ A27), A27 (≠ K28), L28 (≠ A29), A30 (= A31), A66 (= A68), A68 (≠ V70), D69 (= D71), I70 (= I72), Y107 (≠ T113), G110 (= G116), G111 (= G117), E114 (≠ M120), P133 (= P139), E134 (= E140), L137 (= L143), G142 (≠ T147)
Sites not aligning to the query:
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, 71% coverage: 14:187/245 of query aligns to 43:212/290 of P14604
- E144 (≠ M120) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
- E164 (= E140) 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
1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
33% identity, 71% coverage: 14:187/245 of query aligns to 13:180/258 of 1mj3A
- active site: A68 (≠ V70), M73 (≠ Q75), S83 (≠ A93), L85 (= L95), G109 (= G117), E112 (≠ M120), P131 (= P139), E132 (= E140), T137 (vs. gap), P139 (≠ A146), G140 (≠ T147)
- binding hexanoyl-coenzyme a: K26 (≠ A27), A27 (≠ K28), L28 (≠ A29), A30 (= A31), A66 (= A68), G67 (= G69), A68 (≠ V70), D69 (= D71), I70 (= I72), G109 (= G117), P131 (= P139), E132 (= E140), L135 (= L143), G140 (≠ T147)
Sites not aligning to the query:
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
31% identity, 76% coverage: 21:206/245 of query aligns to 16:204/269 of 1nzyB
- active site: C61 (= C67), F64 (≠ V70), I69 (≠ Q75), A86 (vs. gap), H90 (≠ A93), G114 (= G117), G117 (≠ M120), A136 (≠ S137), W137 (≠ L138), I142 (≠ L143), N144 (≠ I145), D145 (≠ A146)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ A27), H23 (≠ K28), R24 (≠ A29), A62 (= A68), F64 (≠ V70), Y65 (≠ D71), L66 (≠ I72), R67 (= R73), W89 (≠ L92), G113 (= G116), G114 (= G117), A136 (≠ S137), W137 (≠ L138), D145 (≠ A146), T146 (= T147)
- binding calcium ion: G49 (≠ N54), L202 (= L204), A203 (≠ G205)
- binding phosphate ion: E57 (= E63), N108 (= N111), K188 (≠ R190), R192 (≠ H194)
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)
29% identity, 81% coverage: 11:209/245 of query aligns to 61:268/327 of Q62651
- D176 (≠ M120) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (= E140) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (≠ F148) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
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, 76% coverage: 21:206/245 of query aligns to 16:204/269 of A5JTM5
- R24 (≠ A29) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (≠ R39) mutation to T: Forms inclusion bodies.
- E43 (≠ T48) mutation to A: No effect on catalytic activity.
- D45 (= D50) mutation to A: No effect on catalytic activity.
- D46 (≠ P51) mutation to A: No effect on catalytic activity.
- G63 (= G69) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ V70) 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 (≠ D71) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (= R73) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (= E74) mutation to T: No effect on catalytic activity.
- H81 (≠ R87) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ R88) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (≠ L92) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ A93) 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 (≠ D97) mutation to Q: No effect on catalytic activity.
- A112 (≠ T115) 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 (= G116) 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 (= G117) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G118) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D126) mutation to T: No effect on catalytic activity.
- D129 (= D132) mutation to T: No effect on catalytic activity.
- W137 (≠ L138) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (≠ A146) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (≠ D165) mutation to T: No effect on catalytic activity.
- E175 (= E177) mutation to D: No effect on catalytic activity.
- W179 (≠ R181) 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.
Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 from Staphylococcus aureus (strain COL) (see paper)
31% identity, 73% coverage: 9:187/245 of query aligns to 14:192/273 of Q5HH38
- R34 (≠ A29) binding in other chain
- SGGDQ 73:77 (≠ AGVDI 68:72) binding in other chain
- S149 (≠ L143) binding in other chain
2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
27% identity, 88% coverage: 14:229/245 of query aligns to 13:224/260 of 2hw5C
- active site: A68 (≠ V70), M73 (≠ Q75), S83 (= S89), L87 (≠ A93), G111 (= G117), E114 (≠ M120), P133 (= P139), E134 (= E140), T139 (vs. gap), P141 (≠ A146), G142 (≠ T147)
- binding crotonyl coenzyme a: K26 (≠ A27), A27 (≠ K28), L28 (≠ A29), A30 (= A31), K62 (≠ R64), I70 (= I72), F109 (≠ T115)
Sites not aligning to the query:
3omeC Crystal structure of a probable enoyl-coa hydratase from mycobacterium smegmatis (see paper)
29% identity, 85% coverage: 16:223/245 of query aligns to 12:215/247 of 3omeC
- active site: H65 (≠ V70), E70 (≠ Q75), A82 (≠ R87), L86 (≠ A91), G110 (= G117), L113 (≠ M120), V133 (≠ E140), I138 (= I145), G139 (≠ A146), E142 (≠ S149)
- binding zinc ion: E81 (= E86), E142 (≠ S149)
Sites not aligning to the query:
Q9P4U9 Enoyl-CoA hydratase AKT3-1; AF-toxin biosynthesis protein 3-1; EC 4.2.1.17 from Alternaria alternata (Alternaria rot fungus) (Torula alternata) (see paper)
33% identity, 68% coverage: 21:186/245 of query aligns to 28:191/296 of Q9P4U9
Sites not aligning to the query:
- 294:296 Peroxisomal targeting signal type 1
Query Sequence
>AO356_30360 FitnessBrowser__pseudo5_N2C3_1:AO356_30360
MSVDELASELTVERHESLLWITLNRAAKANAMTVDMMERMTAALQAATDDPQINAVMLTG
SGERVFCAGVDIREQPADGDTARQRERRSLALAALQDAVMDCPKPVVTVLNGTATGGGAM
LALLADACVAVDTAKLSLPEIDLGIATFSGANILEVIGGRALALDLIQSGRAMKATEALA
RGLVREVALRDELHLKASALGQALGAKNPRTFAENKRWLNRSLRAALLQARDEHARHRAL
AQAEQ
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