SitesBLAST
Comparing BPHYT_RS35465 FitnessBrowser__BFirm:BPHYT_RS35465 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)
6slbAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
35% identity, 89% coverage: 31:282/283 of query aligns to 11:256/257 of 6slbAAA
- active site: Q64 (≠ G84), F69 (≠ I89), L80 (≠ T105), N84 (≠ G109), A108 (= A133), S111 (≠ I136), A130 (≠ L155), F131 (= F156), L136 (= L161), P138 (≠ C164), D139 (= D165), A224 (≠ E250), G234 (≠ M260)
- 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 (≠ D78), A62 (≠ S82), Q64 (≠ G84), D65 (= D85), L66 (≠ V86), Y76 (≠ L101), A108 (= A133), F131 (= F156), D139 (= D165)
6slaAAA Enoyl-CoA hydratase/carnithine racemase (see paper)
34% identity, 89% coverage: 31:282/283 of query aligns to 8:244/245 of 6slaAAA
- active site: Q61 (≠ G84), L68 (≠ T105), N72 (≠ G109), A96 (= A133), S99 (≠ I136), A118 (≠ L155), F119 (= F156), L124 (= L161), P126 (≠ C164), N127 (≠ D165), A212 (≠ E250), G222 (≠ M260)
- 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 (≠ K44), A59 (≠ S82), Q61 (≠ G84), D62 (= D85), L63 (≠ V86), L68 (≠ T105), Y71 (≠ T108), A94 (= A131), G95 (= G132), A96 (= A133), F119 (= F156), I122 (≠ V159), L124 (= L161), N127 (≠ D165), F234 (= F272), K237 (= K275)
1jxzB Structure of the h90q mutant of 4-chlorobenzoyl-coenzyme a dehalogenase complexed with 4-hydroxybenzoyl-coenzyme a (product) (see paper)
32% identity, 83% coverage: 20:254/283 of query aligns to 2:234/269 of 1jxzB
- active site: C61 (= C81), F64 (≠ G84), I69 (= I89), A86 (≠ L101), Q90 (≠ T105), G113 (= G132), G114 (≠ A133), G117 (≠ I136), A136 (≠ L155), W137 (≠ F156), I142 (≠ L161), N144 (≠ C164), D145 (= D165), E230 (= E250)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ E42), H23 (≠ R43), R24 (≠ K44), A62 (≠ S82), F64 (≠ G84), Y65 (≠ D85), L66 (≠ V86), R67 (≠ H87), W89 (≠ F104), G113 (= G132), A136 (≠ L155), W137 (≠ F156), I142 (≠ L161), D145 (= D165), T146 (≠ M166)
- binding calcium ion: G49 (≠ K69), L202 (= L222), A203 (≠ V223), A205 (≠ G225), T207 (= T227), Q210 (≠ H230)
Sites not aligning to the query:
1nzyB 4-chlorobenzoyl coenzyme a dehalogenase from pseudomonas sp. Strain cbs-3 (see paper)
32% identity, 83% coverage: 20:254/283 of query aligns to 2:234/269 of 1nzyB
- active site: C61 (= C81), F64 (≠ G84), I69 (= I89), A86 (≠ L101), H90 (≠ T105), G114 (≠ A133), G117 (≠ I136), A136 (≠ L155), W137 (≠ F156), I142 (≠ L161), N144 (≠ C164), D145 (= D165), E230 (= E250)
- binding 4-hydroxybenzoyl coenzyme a: R22 (≠ E42), H23 (≠ R43), R24 (≠ K44), A62 (≠ S82), F64 (≠ G84), Y65 (≠ D85), L66 (≠ V86), R67 (≠ H87), W89 (≠ F104), G113 (= G132), G114 (≠ A133), A136 (≠ L155), W137 (≠ F156), D145 (= D165), T146 (≠ M166)
- binding calcium ion: G49 (≠ K69), L202 (= L222), A203 (≠ V223), A205 (≠ G225), T207 (= T227), Q210 (≠ H230)
- binding phosphate ion: E57 (≠ G77), N108 (≠ D127), K188 (≠ P208), R192 (≠ L212)
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)
32% identity, 83% coverage: 20:254/283 of query aligns to 2:234/269 of A5JTM5
- R24 (≠ K44) binding in other chain; mutation R->K,L: Does not strongly affect catalytic activity, but reduces substrate CoA binding.
- E34 (= E54) mutation to T: Forms inclusion bodies.
- E43 (≠ T63) mutation to A: No effect on catalytic activity.
- D45 (≠ A65) mutation to A: No effect on catalytic activity.
- D46 (≠ T66) mutation to A: No effect on catalytic activity.
- G63 (= G83) mutation G->A,I,P: Yields insoluble protein.
- F64 (≠ G84) 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 (≠ D85) mutation to D: Catalytic activity is almost as efficient as wild type.
- R67 (≠ H87) mutation to K: Reduces substrate CoA binding.; mutation to L: Forms inclusion bodies.
- E68 (≠ D88) mutation to T: No effect on catalytic activity.
- H81 (≠ L96) mutation to Q: Loss of catalytic activity, substrate benzoyl group binding is not affected.
- F82 (≠ P97) mutation to L: Retains catalytic activity, but substrate benzoyl group binding is decreased.
- W89 (≠ F104) mutation to F: Retains catalytic activity, but substrate benzoyl group binding is decreased.; mutation to Y: Reduced activity and substrate benzoyl group binding.
- H90 (≠ T105) 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 (≠ G109) mutation to Q: No effect on catalytic activity.
- A112 (= A131) 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 (= G132) 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 (≠ A133) mutation to A: Strongly reduced catalytic activity and substrate benzoyl group binding.; mutation to P: Unstable.
- G115 (= G134) mutation G->L,N,S,V: Yields insoluble protein.
- D123 (= D142) mutation to T: No effect on catalytic activity.
- D129 (≠ A148) mutation to T: No effect on catalytic activity.
- W137 (≠ F156) mutation to F: Low catalytic activity, but KM unaffected (PubMed:8718880). Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
- D145 (= D165) active site, Nucleophile; mutation to A: Complete loss of catalytic activity, but not substrate binding.
- E163 (= E183) mutation to T: No effect on catalytic activity.
- E175 (= E195) mutation to D: No effect on catalytic activity.
- W179 (= W199) mutation to F: No effect on catalytic activity.
- H208 (≠ F228) mutation to Q: No effect on catalytic activity.
- R216 (≠ M236) mutation R->E,K,L: Yields insoluble protein.
- E232 (= E252) 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.
5zaiC Crystal structure of 3-hydroxypropionyl-coa dehydratase from metallosphaera sedula (see paper)
27% identity, 87% coverage: 36:282/283 of query aligns to 17:258/259 of 5zaiC
- active site: A65 (≠ G84), F70 (≠ L93), S82 (≠ T105), R86 (≠ G109), G110 (≠ A133), E113 (≠ I136), P132 (≠ L155), E133 (≠ F156), I138 (≠ L161), P140 (≠ C164), G141 (≠ D165), A226 (≠ E250), F236 (≠ M260)
- binding coenzyme a: K24 (≠ R43), L25 (≠ K44), A63 (≠ S82), G64 (= G83), A65 (≠ G84), D66 (= D85), I67 (= I90), P132 (≠ L155), R166 (≠ S190), F248 (= F272), K251 (= K275)
Q62651 Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; EC 5.3.3.- from Rattus norvegicus (Rat) (see paper)
30% identity, 86% coverage: 33:275/283 of query aligns to 66:316/327 of Q62651
- D176 (≠ I136) mutation D->A,D: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- E196 (≠ F156) mutation E->D,Q: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
- D204 (= D165) mutation D->A,N: Strongly decreases dienoyl-CoA and trienoyl-CoA isomerase activity.
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)
29% identity, 89% coverage: 30:281/283 of query aligns to 22:269/296 of Q9P4U9
Sites not aligning to the query:
- 294:296 Peroxisomal targeting signal type 1
Q4WF54 Mevalonyl-coenzyme A hydratase sidH; Siderophore biosynthesis protein H; EC 4.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
29% identity, 87% coverage: 36:280/283 of query aligns to 24:265/270 of Q4WF54
Sites not aligning to the query:
- 268:270 PTS1-type peroxisomal targeting signal
5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
29% identity, 87% coverage: 37:282/283 of query aligns to 19:260/261 of 5jbxB
- active site: A67 (≠ G84), R72 (≠ I89), L84 (= L102), R88 (= R106), G112 (≠ A133), E115 (≠ I136), T134 (≠ L155), E135 (≠ F156), I140 (≠ L161), P142 (≠ G163), G143 (≠ C164), A228 (≠ E250), L238 (≠ M260)
- binding coenzyme a: S24 (≠ E42), R25 (= R43), R26 (≠ K44), A28 (≠ P46), A65 (≠ S82), D68 (= D85), L69 (≠ V86), K70 (≠ H87), L110 (≠ A131), G111 (= G132), T134 (≠ L155), E135 (≠ F156), L138 (≠ V159), R168 (≠ S190)
3omeC Crystal structure of a probable enoyl-coa hydratase from mycobacterium smegmatis (see paper)
30% identity, 76% coverage: 24:239/283 of query aligns to 5:213/247 of 3omeC
- active site: H65 (= H87), E70 (≠ P92), A82 (≠ T105), L86 (≠ G109), G110 (≠ A133), L113 (≠ I136), V133 (≠ F156), I138 (≠ L161), G139 (≠ A162), E142 (≠ D165)
- binding zinc ion: E81 (vs. gap), E142 (≠ D165)
Sites not aligning to the query:
5du6A Crystal structure of m. Tuberculosis echa6 bound to ligand gsk059a. (see paper)
29% identity, 91% coverage: 25:282/283 of query aligns to 3:241/242 of 5du6A
- active site: A61 (≠ G84), P71 (= P99), I75 (≠ L103), A99 (= A133), Q102 (≠ I136), P121 (≠ L155), T122 (≠ F156), L127 (= L161), L129 (≠ C164), D130 (= D165), P209 (≠ E250), W219 (≠ M260)
- binding (5R,7R)-5-(4-ethylphenyl)-N-(4-fluorobenzyl)-7-methyl-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L74 (= L102), D82 (≠ R116), D130 (= D165), W132 (≠ G167), A207 (= A248), K212 (≠ A253), F215 (≠ Q256)
5du8A Crystal structure of m. Tuberculosis echa6 bound to gsk572a (see paper)
29% identity, 91% coverage: 25:282/283 of query aligns to 3:233/234 of 5du8A
- active site: A61 (≠ G84), P63 (= P99), I67 (≠ L103), A91 (= A133), Q94 (≠ I136), P113 (≠ L155), T114 (≠ F156), L119 (= L161), L121 (≠ C164), D122 (= D165), P201 (≠ E250), W211 (≠ M260)
- binding (5R,7S)-5-(4-ethylphenyl)-N-[(5-fluoropyridin-2-yl)methyl]-7-(trifluoromethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L66 (= L102), I67 (≠ L103), H70 (≠ V112), Q94 (≠ I136), D122 (= D165), W124 (≠ G167), F207 (≠ Q256)
5ducA Crystal structure of m. Tuberculosis echa6 bound to ligand gsk951a (see paper)
30% identity, 91% coverage: 25:282/283 of query aligns to 3:243/244 of 5ducA
- active site: A61 (≠ G84), D66 (= D88), P73 (= P99), I77 (≠ L103), A101 (= A133), Q104 (≠ I136), P123 (≠ L155), T124 (≠ F156), L129 (= L161), L131 (≠ C164), D132 (= D165), P211 (≠ E250), W221 (≠ M260)
- binding (5R,7S)-N-(1,3-benzodioxol-5-ylmethyl)-5-(4-ethylphenyl)-7-(trifluoromethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L76 (= L102), H80 (≠ V112), D84 (≠ R116), Q104 (≠ I136), D132 (= D165), W134 (≠ G167), F217 (≠ Q256)
5du4A Crystal structure of m. Tuberculosis echa6 bound to ligand gsk366a (see paper)
30% identity, 91% coverage: 25:282/283 of query aligns to 3:243/244 of 5du4A
- active site: A61 (≠ G84), D66 (= D88), P73 (= P99), I77 (≠ L103), A101 (= A133), Q104 (≠ I136), P123 (≠ L155), T124 (≠ F156), L129 (= L161), L131 (≠ C164), D132 (= D165), P211 (≠ E250), W221 (≠ M260)
- binding (5R,7S)-5-(4-ethylphenyl)-N-(4-methoxybenzyl)-7-(trifluoromethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxamide: L76 (= L102), I77 (≠ L103), H80 (≠ V112), D84 (≠ R116), Q104 (≠ I136), D132 (= D165), W134 (≠ G167)
5dtwA Crystal structure of m. Tuberculosis echa6 bound to c20-coa (see paper)
30% identity, 91% coverage: 25:282/283 of query aligns to 3:243/244 of 5dtwA
- active site: A61 (≠ G84), D66 (= D88), P73 (= P99), I77 (≠ L103), A101 (= A133), Q104 (≠ I136), P123 (≠ L155), T124 (≠ F156), L129 (= L161), L131 (≠ C164), D132 (= D165), P211 (≠ E250), W221 (≠ M260)
- binding Arachinoyl-CoA: R18 (= R40), E20 (= E42), R21 (= R43), R21 (= R43), R22 (≠ K44), A24 (≠ P46), A59 (≠ S82), A61 (≠ G84), D62 (= D85), L63 (≠ V86), H80 (≠ V112), D84 (≠ R116), G100 (= G132), A101 (= A133), Y127 (≠ V159), W134 (≠ G167)
5dufA Crystal structure of m. Tuberculosis echa6 bound to ligand gsk729a (see paper)
30% identity, 91% coverage: 25:282/283 of query aligns to 4:244/245 of 5dufA
- active site: A62 (≠ G84), D67 (= D88), P74 (= P99), I78 (≠ L103), A102 (= A133), Q105 (≠ I136), P124 (≠ L155), T125 (≠ F156), L130 (= L161), L132 (≠ C164), D133 (= D165), P212 (≠ E250), W222 (≠ M260)
- binding (5R,7S)-5-(4-ethylphenyl)-7-(trifluoromethyl)-4,5,6,7-tetrahydropyrazolo[1,5-a]pyrimidine-3-carboxylic acid: L77 (= L102), I78 (≠ L103), H81 (≠ V112), D85 (≠ R116), Q105 (≠ I136), D133 (= D165), W135 (≠ G167)
7borA Structure of pseudomonas aeruginosa coa-bound odaa (see paper)
33% identity, 57% coverage: 35:195/283 of query aligns to 14:166/247 of 7borA
- active site: N63 (≠ G84), F68 (≠ I89), D77 (= D95), G81 (= G109), I105 (≠ A133), T108 (≠ I136), F128 (= F156), L133 (= L161), P135 (≠ C164), E136 (≠ D165)
- binding coenzyme a: D21 (≠ E42), K22 (≠ R43), A25 (≠ P46), S61 (= S82), I65 (≠ V86), V103 (≠ A131), F128 (= F156), L131 (≠ V159)
Sites not aligning to the query:
3t3wF Crystal structure of probable enoyl-coa hydratase from mycobacterium thermoresistibile (see paper)
29% identity, 76% coverage: 24:239/283 of query aligns to 5:214/248 of 3t3wF
- active site: H65 (= H87), D71 (= D95), S83 (≠ T105), L87 (≠ G109), G111 (≠ A133), L114 (≠ I136), V134 (≠ F156), I139 (≠ L161), G140 (≠ A162), E143 (≠ D165)
- binding zinc ion: E82 (vs. gap), E143 (≠ D165)
Sites not aligning to the query:
3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
27% identity, 88% coverage: 32:280/283 of query aligns to 12:253/256 of 3h81A
- active site: A64 (≠ G84), M69 (= M98), T79 (= T108), F83 (≠ V112), G107 (≠ A133), E110 (≠ I136), P129 (≠ L155), E130 (≠ F156), V135 (vs. gap), P137 (≠ A162), G138 (= G163), L223 (≠ E250), F233 (≠ M260)
- binding calcium ion: F233 (≠ M260), Q238 (≠ F265)
Query Sequence
>BPHYT_RS35465 FitnessBrowser__BFirm:BPHYT_RS35465
MTRSNADGLLAGNRLTLAGYEARHFGWSVADKVATITLNRPERKNPLTFESYAELRDLFR
QLTYATDVKAVVIHGAGDNFCSGGDVHDIIAPLIDLPMPELLLFTRMTGDLVKAMRHCPQ
PVIAAVDGVCAGAGAILAMSSDMRLGTARSKLAFLFSRVGLAGCDMGACTILPRIIGQGR
AAELLFTGRSASGEEGHAWGFYNRLCEPAALLEEAHKLAADLVAGPTFAHGITKKMLHQE
WSMSIDEAIESEAQAQAICMSTRDFERAYSAFAAKSRPVFEGD
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