SitesBLAST
Comparing WP_197458471.1 NCBI__GCF_001636925.1:WP_197458471.1 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)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
54% identity, 84% coverage: 76:492/497 of query aligns to 73:485/487 of 1m21A
- active site: K81 (= K84), S160 (= S164), S161 (= S165), T179 (= T183), T181 (= T185), D182 (= D186), G183 (= G187), S184 (= S188), C187 (= C191)
- binding : A129 (= A133), N130 (= N134), F131 (≠ I135), C158 (= C162), G159 (= G163), S160 (= S164), S184 (= S188), C187 (= C191), I212 (= I216), R318 (≠ F322), L321 (= L325), L365 (≠ I371), F426 (≠ M433)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 84% coverage: 66:484/497 of query aligns to 54:467/478 of 3h0mA
- active site: K72 (= K84), S147 (= S164), S148 (= S165), S166 (≠ T183), T168 (= T185), G169 (≠ D186), G170 (= G187), S171 (= S188), Q174 (≠ C191)
- binding glutamine: M122 (≠ I135), G123 (≠ R136), D167 (≠ E184), T168 (= T185), G169 (≠ D186), G170 (= G187), S171 (= S188), F199 (≠ I216), Y302 (≠ G314), R351 (≠ A375), D418 (≠ Q439)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 84% coverage: 66:484/497 of query aligns to 54:467/478 of 3h0lA
- active site: K72 (= K84), S147 (= S164), S148 (= S165), S166 (≠ T183), T168 (= T185), G169 (≠ D186), G170 (= G187), S171 (= S188), Q174 (≠ C191)
- binding asparagine: G123 (≠ R136), S147 (= S164), G169 (≠ D186), G170 (= G187), S171 (= S188), Y302 (≠ G314), R351 (≠ A375), D418 (≠ Q439)
3kfuE Crystal structure of the transamidosome (see paper)
33% identity, 83% coverage: 76:486/497 of query aligns to 57:457/468 of 3kfuE
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 91% coverage: 43:492/497 of query aligns to 54:506/508 of 3a1iA
- active site: K95 (= K84), S170 (= S164), S171 (= S165), G189 (≠ T183), Q191 (≠ T185), G192 (≠ D186), G193 (= G187), A194 (≠ S188), I197 (≠ C191)
- binding benzamide: F145 (≠ N134), S146 (= S140), G147 (≠ I141), Q191 (≠ T185), G192 (≠ D186), G193 (= G187), A194 (≠ S188), W327 (≠ L333)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
28% identity, 89% coverage: 43:483/497 of query aligns to 38:473/485 of 2f2aA
- active site: K79 (= K84), S154 (= S164), S155 (= S165), S173 (≠ T183), T175 (= T185), G176 (≠ D186), G177 (= G187), S178 (= S188), Q181 (≠ C191)
- binding glutamine: G130 (≠ I135), S154 (= S164), D174 (≠ E184), T175 (= T185), G176 (≠ D186), S178 (= S188), F206 (≠ I216), Y309 (≠ G314), Y310 (≠ R315), R358 (≠ A375), D425 (≠ Q439)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
28% identity, 89% coverage: 43:483/497 of query aligns to 38:473/485 of 2dqnA
- active site: K79 (= K84), S154 (= S164), S155 (= S165), S173 (≠ T183), T175 (= T185), G176 (≠ D186), G177 (= G187), S178 (= S188), Q181 (≠ C191)
- binding asparagine: M129 (≠ N134), G130 (≠ I135), T175 (= T185), G176 (≠ D186), S178 (= S188), Y309 (≠ G314), Y310 (≠ R315), R358 (≠ A375), D425 (≠ Q439)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 84% coverage: 76:493/497 of query aligns to 92:496/507 of Q84DC4
- K100 (= K84) 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 (≠ D186) 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 (≠ C191) 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 (≠ I317) 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 (≠ E388) 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 (≠ L440) 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.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
26% identity, 86% coverage: 65:492/497 of query aligns to 184:597/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A133), T258 (≠ I141), S281 (= S164), G302 (≠ T185), G303 (≠ D186), S305 (= S188), S472 (≠ R374), I532 (≠ M433), M539 (≠ L440)
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)
26% identity, 86% coverage: 65:492/497 of query aligns to 184:597/607 of Q7XJJ7
- K205 (= K84) mutation to A: Loss of activity.
- SS 281:282 (= SS 164:165) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TDGS 185:188) binding substrate
- S305 (= S188) mutation to A: Loss of activity.
- R307 (≠ T190) mutation to A: Loss of activity.
- S360 (= S243) mutation to A: No effect.
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
26% identity, 86% coverage: 65:492/497 of query aligns to 184:597/605 of 8ey9B