SitesBLAST
Comparing GFF3276 FitnessBrowser__Phaeo:GFF3276 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)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 88% coverage: 50:439/442 of query aligns to 175:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A129), T258 (≠ G132), S281 (= S155), G302 (≠ T176), G303 (= G177), S305 (= S179), S472 (≠ R327), I532 (≠ Y384), M539 (= M391)
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)
30% identity, 88% coverage: 50:439/442 of query aligns to 175:589/607 of Q7XJJ7
- K205 (= K80) mutation to A: Loss of activity.
- SS 281:282 (= SS 155:156) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 176:179) binding substrate
- S305 (= S179) mutation to A: Loss of activity.
- R307 (= R181) mutation to A: Loss of activity.
- S360 (≠ N234) mutation to A: No effect.
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
30% identity, 88% coverage: 50:439/442 of query aligns to 175:589/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A129), G302 (≠ T176), G303 (= G177), G304 (= G178), A305 (≠ S179), V442 (≠ A298), I475 (≠ S330), M539 (= M391)
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
30% identity, 88% coverage: 50:439/442 of query aligns to 175:589/605 of 8ey1D
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
30% identity, 97% coverage: 10:439/442 of query aligns to 9:477/487 of 1m21A
- active site: K81 (= K80), S160 (= S155), S161 (= S156), T179 (≠ S174), T181 (= T176), D182 (≠ G177), G183 (= G178), S184 (= S179), C187 (≠ I182)
- binding : A129 (= A129), N130 (vs. gap), F131 (vs. gap), C158 (≠ G153), G159 (= G154), S160 (= S155), S184 (= S179), C187 (≠ I182), I212 (≠ L207), R318 (vs. gap), L321 (≠ V289), L365 (≠ I324), F426 (≠ Y385)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 98% coverage: 7:438/442 of query aligns to 6:473/485 of 2f2aA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (= S174), T175 (= T176), G176 (= G177), G177 (= G178), S178 (= S179), Q181 (≠ I182)
- binding glutamine: G130 (≠ S131), S154 (= S155), D174 (= D175), T175 (= T176), G176 (= G177), S178 (= S179), F206 (≠ L207), Y309 (≠ S297), Y310 (≠ A298), R358 (vs. gap), D425 (≠ A392)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 98% coverage: 7:438/442 of query aligns to 6:473/485 of 2dqnA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (= S174), T175 (= T176), G176 (= G177), G177 (= G178), S178 (= S179), Q181 (≠ I182)
- binding asparagine: M129 (≠ F130), G130 (≠ S131), T175 (= T176), G176 (= G177), S178 (= S179), Y309 (≠ S297), Y310 (≠ A298), R358 (vs. gap), D425 (≠ A392)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 98% coverage: 7:441/442 of query aligns to 5:469/478 of 3h0mA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (= S174), T168 (= T176), G169 (= G177), G170 (= G178), S171 (= S179), Q174 (≠ I182)
- binding glutamine: M122 (≠ F130), G123 (≠ S131), D167 (= D175), T168 (= T176), G169 (= G177), G170 (= G178), S171 (= S179), F199 (≠ L207), Y302 (≠ S297), R351 (= R327), D418 (≠ S388)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 98% coverage: 7:441/442 of query aligns to 5:469/478 of 3h0lA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (= S174), T168 (= T176), G169 (= G177), G170 (= G178), S171 (= S179), Q174 (≠ I182)
- binding asparagine: G123 (≠ S131), S147 (= S155), G169 (= G177), G170 (= G178), S171 (= S179), Y302 (≠ S297), R351 (= R327), D418 (≠ S388)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 84% coverage: 72:441/442 of query aligns to 92:490/507 of Q84DC4
- K100 (= K80) mutation to A: Abolishes activity on mandelamide.
- S180 (= S155) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S156) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G177) 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 (= S179) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I182) 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 (≠ A293) 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 (≠ L355) 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 (≠ L393) 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.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 84% coverage: 49:418/442 of query aligns to 44:414/461 of 4gysB