SitesBLAST
Comparing BPHYT_RS15070 FitnessBrowser__BFirm:BPHYT_RS15070 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)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
34% identity, 95% coverage: 13:449/459 of query aligns to 5:445/457 of 6c6gA
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 89% coverage: 47:454/459 of query aligns to 169:590/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A133), T258 (≠ G136), S281 (= S164), G302 (≠ T185), G303 (= G186), S305 (= S188), S472 (≠ L335), I532 (≠ G397), M539 (≠ L404)
Sites not aligning to the query:
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
29% identity, 89% coverage: 47:454/459 of query aligns to 169:590/607 of Q7XJJ7
- K205 (= K83) mutation to A: Loss of activity.
- SS 281:282 (= SS 164:165) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 185:188) binding substrate
- S305 (= S188) mutation to A: Loss of activity.
- R307 (= R190) mutation to A: Loss of activity.
- S360 (vs. gap) mutation to A: No effect.
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
32% identity, 95% coverage: 22:455/459 of query aligns to 41:490/507 of Q84DC4
- K100 (= K83) mutation to A: Abolishes activity on mandelamide.
- S180 (= S164) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S165) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G186) mutation to A: Increase in KM values for aromatic substrates, but not aliphatic substrates. Active against lactamide but not against mandelamide; when associated with H-207 and E-382.; mutation to V: Increase in KM values for aromatic substrates, but not aliphatic substrates.
- S204 (= S188) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I191) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with E-382. Active against lactamide but not against mandelamide; when associated with A-202 and E-382. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with S-316 and N-437.
- S316 (≠ N306) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-437.
- Q382 (≠ D348) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with H-207. Active against lactamide but not against mandelamide; when associated with A-202 and H-207.
- I437 (≠ L404) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with I-31. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-316.
Sites not aligning to the query:
- 31 T→I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
29% identity, 89% coverage: 47:454/459 of query aligns to 169:590/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A133), G302 (≠ T185), G303 (= G186), G304 (= G187), A305 (≠ S188), V442 (≠ I305), I475 (= I338), M539 (≠ L404)
Sites not aligning to the query:
8ey1D Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with n-(3-oxododecanoyl)-l-homoserine lactone
29% identity, 89% coverage: 47:454/459 of query aligns to 169:590/605 of 8ey1D
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 97% coverage: 11:456/459 of query aligns to 7:470/478 of 3h0mA
- active site: K72 (= K83), S147 (= S164), S148 (= S165), S166 (≠ T183), T168 (= T185), G169 (= G186), G170 (= G187), S171 (= S188), Q174 (≠ I191)
- binding glutamine: M122 (≠ L137), G123 (= G138), D167 (= D184), T168 (= T185), G169 (= G186), G170 (= G187), S171 (= S188), F199 (≠ L216), Y302 (vs. gap), R351 (= R337), D418 (≠ N400)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 97% coverage: 11:456/459 of query aligns to 7:470/478 of 3h0lA
- active site: K72 (= K83), S147 (= S164), S148 (= S165), S166 (≠ T183), T168 (= T185), G169 (= G186), G170 (= G187), S171 (= S188), Q174 (≠ I191)
- binding asparagine: G123 (= G138), S147 (= S164), G169 (= G186), G170 (= G187), S171 (= S188), Y302 (vs. gap), R351 (= R337), D418 (≠ N400)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 89% coverage: 47:453/459 of query aligns to 43:474/485 of 2f2aA
- active site: K79 (= K83), S154 (= S164), S155 (= S165), S173 (≠ T183), T175 (= T185), G176 (= G186), G177 (= G187), S178 (= S188), Q181 (≠ I191)
- binding glutamine: G130 (≠ S135), S154 (= S164), D174 (= D184), T175 (= T185), G176 (= G186), S178 (= S188), F206 (≠ L216), Y309 (vs. gap), Y310 (vs. gap), R358 (= R337), D425 (≠ N400)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 89% coverage: 47:453/459 of query aligns to 43:474/485 of 2dqnA
- active site: K79 (= K83), S154 (= S164), S155 (= S165), S173 (≠ T183), T175 (= T185), G176 (= G186), G177 (= G187), S178 (= S188), Q181 (≠ I191)
- binding asparagine: M129 (≠ F134), G130 (≠ S135), T175 (= T185), G176 (= G186), S178 (= S188), Y309 (vs. gap), Y310 (vs. gap), R358 (= R337), D425 (≠ N400)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
30% identity, 96% coverage: 13:452/459 of query aligns to 9:444/457 of 5h6sC