SitesBLAST

K100 (= K119) mutation to A: Abolishes activity on mandelamide.
S180 (= S194) mutation to A: Significantly decreases activity on mandelamide.
S181 (= S195) mutation to A: Significantly decreases activity on mandelamide.
G202 (= G216) 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 (= S218) mutation to A: Abolishes activity on mandelamide.
Q207 (≠ N221) 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 (≠ G393) 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 (≠ M452) 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)
25% identity, 88% coverage: 49:503/518 of query aligns to 9:467/478 of 3h0mA

query
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active site: K72 (= K119), S147 (= S194), S148 (= S195), S166 (= S213), T168 (≠ F215), G169 (= G216), G170 (= G217), S171 (= S218), Q174 (≠ N221)
binding glutamine: M122 (≠ L169), G123 (= G170), D167 (= D214), T168 (≠ F215), G169 (= G216), G170 (= G217), S171 (= S218), F199 (= F247), Y302 (vs. gap), R351 (≠ Q376), D418 (= D446)

3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
25% identity, 88% coverage: 49:503/518 of query aligns to 9:467/478 of 3h0lA

query
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active site: K72 (= K119), S147 (= S194), S148 (= S195), S166 (= S213), T168 (≠ F215), G169 (= G216), G170 (= G217), S171 (= S218), Q174 (≠ N221)
binding asparagine: G123 (= G170), S147 (= S194), G169 (= G216), G170 (= G217), S171 (= S218), Y302 (vs. gap), R351 (≠ Q376), D418 (= D446)

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, 79% coverage: 100:506/518 of query aligns to 181:592/607 of Q7XJJ7

query
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Q7XJJ7

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