SitesBLAST
Comparing WP_097029915.1 NCBI__GCF_900207575.1:WP_097029915.1 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)
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, 89% coverage: 47:438/441 of query aligns to 166:589/607 of Q7XJJ7
- K205 (= K79) mutation to A: Loss of activity.
- SS 281:282 (= SS 154:155) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 175:178) binding substrate
- S305 (= S178) mutation to A: Loss of activity.
- R307 (= R180) mutation to A: Loss of activity.
- S360 (≠ R233) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 89% coverage: 47:438/441 of query aligns to 166:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A128), T258 (≠ G131), S281 (= S154), G302 (≠ T175), G303 (= G176), S305 (= S178), S472 (≠ I323), I532 (≠ Y383), M539 (≠ L392)
Sites not aligning to the query:
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
30% identity, 89% coverage: 47:438/441 of query aligns to 166:589/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A128), G302 (≠ T175), G303 (= G176), G304 (= G177), A305 (≠ S178), V442 (≠ G297), I475 (≠ R326), M539 (≠ L392)
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, 89% coverage: 47:438/441 of query aligns to 166:589/605 of 8ey1D
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
28% identity, 99% coverage: 1:437/441 of query aligns to 1:473/485 of 2f2aA
- active site: K79 (= K79), S154 (= S154), S155 (= S155), S173 (= S173), T175 (= T175), G176 (= G176), G177 (= G177), S178 (= S178), Q181 (≠ I181)
- binding glutamine: G130 (≠ S130), S154 (= S154), D174 (= D174), T175 (= T175), G176 (= G176), S178 (= S178), F206 (≠ L206), Y309 (≠ A296), Y310 (≠ G297), R358 (vs. gap), D425 (≠ N388)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
28% identity, 99% coverage: 1:437/441 of query aligns to 1:473/485 of 2dqnA
- active site: K79 (= K79), S154 (= S154), S155 (= S155), S173 (= S173), T175 (= T175), G176 (= G176), G177 (= G177), S178 (= S178), Q181 (≠ I181)
- binding asparagine: M129 (≠ F129), G130 (≠ S130), T175 (= T175), G176 (= G176), S178 (= S178), Y309 (≠ A296), Y310 (≠ G297), R358 (vs. gap), D425 (≠ N388)
3kfuE Crystal structure of the transamidosome (see paper)
35% identity, 96% coverage: 15:439/441 of query aligns to 9:456/468 of 3kfuE
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 84% coverage: 71:441/441 of query aligns to 92:491/507 of Q84DC4
- K100 (= K79) mutation to A: Abolishes activity on mandelamide.
- S180 (= S154) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S155) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G176) 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 (= S178) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I181) 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 (vs. gap) 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 (vs. gap) 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 (≠ L392) 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.
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 100% coverage: 1:440/441 of query aligns to 1:469/478 of 3h0mA
- active site: K72 (= K79), S147 (= S154), S148 (= S155), S166 (= S173), T168 (= T175), G169 (= G176), G170 (= G177), S171 (= S178), Q174 (≠ I181)
- binding glutamine: M122 (≠ F129), G123 (≠ S130), D167 (= D174), T168 (= T175), G169 (= G176), G170 (= G177), S171 (= S178), F199 (≠ L206), Y302 (≠ A296), R351 (≠ P321), D418 (≠ E387)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 100% coverage: 1:440/441 of query aligns to 1:469/478 of 3h0lA
- active site: K72 (= K79), S147 (= S154), S148 (= S155), S166 (= S173), T168 (= T175), G169 (= G176), G170 (= G177), S171 (= S178), Q174 (≠ I181)
- binding asparagine: G123 (≠ S130), S147 (= S154), G169 (= G176), G170 (= G177), S171 (= S178), Y302 (≠ A296), R351 (≠ P321), D418 (≠ E387)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
36% identity, 63% coverage: 9:288/441 of query aligns to 9:309/487 of 1m21A