SitesBLAST
Comparing WP_081423402.1 NCBI__GCF_000008325.1:WP_081423402.1 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)
Q9FR37 Amidase 1; AtAMI1; Translocon at the outer membrane of chloroplasts 64-I; AtTOC64-I; EC 3.5.1.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
38% identity, 90% coverage: 39:414/416 of query aligns to 28:425/425 of Q9FR37
- K36 (= K47) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S124) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S125) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D144) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S148) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C156) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (vs. gap) mutation to T: Slightly reduces catalytic activity.
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
37% identity, 90% coverage: 42:416/416 of query aligns to 64:456/593 of Q9MUK5
Sites not aligning to the query:
- 516 N→A: Loss of HSP90 binding, but no effect on HSP70 binding.
- 550 R→A: 80% decrease of HSP70 and HSP90 binding.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
43% identity, 46% coverage: 15:206/416 of query aligns to 39:232/457 of 6c6gA
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 92% coverage: 26:407/416 of query aligns to 51:462/478 of 3h0mA
- active site: K72 (= K47), S147 (= S124), S148 (= S125), S166 (≠ T143), T168 (= T145), G169 (≠ A146), G170 (= G147), S171 (= S148), Q174 (≠ L151)
- binding glutamine: M122 (≠ F99), G123 (= G100), D167 (= D144), T168 (= T145), G169 (≠ A146), G170 (= G147), S171 (= S148), F199 (≠ L176), Y302 (vs. gap), R351 (= R294), D418 (≠ R361)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 92% coverage: 26:407/416 of query aligns to 51:462/478 of 3h0lA
- active site: K72 (= K47), S147 (= S124), S148 (= S125), S166 (≠ T143), T168 (= T145), G169 (≠ A146), G170 (= G147), S171 (= S148), Q174 (≠ L151)
- binding asparagine: G123 (= G100), S147 (= S124), G169 (≠ A146), G170 (= G147), S171 (= S148), Y302 (vs. gap), R351 (= R294), D418 (≠ R361)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
28% identity, 88% coverage: 46:410/416 of query aligns to 204:587/607 of Q7XJJ7
- K205 (= K47) mutation to A: Loss of activity.
- SS 281:282 (= SS 124:125) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TAGS 145:148) binding substrate
- S305 (= S148) mutation to A: Loss of activity.
- R307 (= R150) mutation to A: Loss of activity.
- S360 (vs. gap) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 88% coverage: 46:410/416 of query aligns to 204:587/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A98), T258 (≠ L101), S281 (= S124), G302 (≠ T145), G303 (≠ A146), S305 (= S148), S472 (≠ N298), I532 (≠ D352), M539 (≠ F359)
Sites not aligning to the query:
3kfuE Crystal structure of the transamidosome (see paper)
32% identity, 88% coverage: 38:404/416 of query aligns to 56:447/468 of 3kfuE
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
27% identity, 88% coverage: 46:410/416 of query aligns to 204:587/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A98), G302 (≠ T145), G303 (≠ A146), G304 (= G147), A305 (≠ S148), V442 (≠ Q269), I475 (≠ L301), M539 (≠ F359)
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
27% identity, 88% coverage: 46:410/416 of query aligns to 204:587/605 of 8ey1D
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 91% coverage: 38:414/416 of query aligns to 91:490/507 of Q84DC4
- K100 (= K47) mutation to A: Abolishes activity on mandelamide.
- S180 (= S124) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S125) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ A146) 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 (= S148) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ L151) 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 (≠ W264) 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 (≠ R326) 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 (≠ L363) 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.
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
38% identity, 39% coverage: 26:189/416 of query aligns to 58:219/485 of 2f2aA
- active site: K79 (= K47), S154 (= S124), S155 (= S125), S173 (≠ T143), T175 (= T145), G176 (≠ A146), G177 (= G147), S178 (= S148), Q181 (≠ L151)
- binding glutamine: G130 (= G100), S154 (= S124), D174 (= D144), T175 (= T145), G176 (≠ A146), S178 (= S148), F206 (≠ L176)
Sites not aligning to the query:
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
38% identity, 39% coverage: 26:189/416 of query aligns to 58:219/485 of 2dqnA
- active site: K79 (= K47), S154 (= S124), S155 (= S125), S173 (≠ T143), T175 (= T145), G176 (≠ A146), G177 (= G147), S178 (= S148), Q181 (≠ L151)
- binding asparagine: M129 (≠ F99), G130 (= G100), T175 (= T145), G176 (≠ A146), S178 (= S148)
Sites not aligning to the query:
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
27% identity, 88% coverage: 46:411/416 of query aligns to 37:450/450 of 4n0iA