SitesBLAST
Comparing GFF2305 FitnessBrowser__psRCH2:GFF2305 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)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
46% identity, 96% coverage: 25:599/600 of query aligns to 37:605/605 of Q936X2
- K91 (= K78) mutation to A: Loss of activity.
- S165 (= S152) mutation to A: Loss of activity.
- S189 (= S176) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
51% identity, 64% coverage: 69:449/600 of query aligns to 63:440/461 of 4gysB
- active site: K72 (= K78), S146 (= S152), S147 (= S153), T165 (= T171), T167 (= T173), A168 (= A174), G169 (= G175), S170 (= S176), V173 (= V179)
- binding malonate ion: A120 (= A126), G122 (= G128), S146 (= S152), T167 (= T173), A168 (= A174), S170 (= S176), S193 (≠ A199), G194 (= G200), V195 (= V201), R200 (= R206), Y297 (= Y306), R305 (= R314)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 73% coverage: 9:443/600 of query aligns to 7:462/478 of 3h0mA
- active site: K72 (= K78), S147 (= S152), S148 (= S153), S166 (≠ T171), T168 (= T173), G169 (≠ A174), G170 (= G175), S171 (= S176), Q174 (≠ V179)
- binding glutamine: M122 (≠ T127), G123 (= G128), D167 (= D172), T168 (= T173), G169 (≠ A174), G170 (= G175), S171 (= S176), F199 (≠ A204), Y302 (vs. gap), R351 (≠ V336), D418 (= D396)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 73% coverage: 9:443/600 of query aligns to 7:462/478 of 3h0lA
- active site: K72 (= K78), S147 (= S152), S148 (= S153), S166 (≠ T171), T168 (= T173), G169 (≠ A174), G170 (= G175), S171 (= S176), Q174 (≠ V179)
- binding asparagine: G123 (= G128), S147 (= S152), G169 (≠ A174), G170 (= G175), S171 (= S176), Y302 (vs. gap), R351 (≠ V336), D418 (= D396)
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)
26% identity, 68% coverage: 38:446/600 of query aligns to 4:421/425 of Q9FR37
- K36 (= K78) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S152) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S153) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D172) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S176) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ N184) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ P242) mutation to T: Slightly reduces catalytic activity.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
39% identity, 29% coverage: 69:242/600 of query aligns to 72:250/487 of 1m21A
- active site: K81 (= K78), S160 (= S152), S161 (= S153), T179 (= T171), T181 (= T173), D182 (≠ A174), G183 (= G175), S184 (= S176), C187 (≠ V179)
- binding : A129 (= A126), N130 (≠ T127), F131 (vs. gap), C158 (≠ G150), G159 (= G151), S160 (= S152), S184 (= S176), C187 (≠ V179), I212 (≠ A204)
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, 73% coverage: 8:447/600 of query aligns to 130:588/607 of Q7XJJ7
- K205 (= K78) mutation to A: Loss of activity.
- SS 281:282 (= SS 152:153) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TAGS 173:176) binding substrate
- S305 (= S176) mutation to A: Loss of activity.
- R307 (= R178) mutation to A: Loss of activity.
- S360 (≠ L231) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
26% identity, 74% coverage: 8:448/600 of query aligns to 130:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A126), T258 (≠ L129), S281 (= S152), G302 (≠ T173), G303 (≠ A174), S305 (= S176), S472 (≠ V336), I532 (≠ V391), M539 (≠ G398)
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
26% identity, 73% coverage: 8:447/600 of query aligns to 130:588/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A126), G302 (≠ T173), G303 (≠ A174), G304 (= G175), A305 (≠ S176), V442 (≠ E307), I475 (≠ K339), M539 (≠ G398)
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
26% identity, 73% coverage: 8:447/600 of query aligns to 130:588/605 of 8ey1D
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
38% identity, 34% coverage: 5:210/600 of query aligns to 26:238/507 of Q84DC4