SitesBLAST
Comparing Ac3H11_417 FitnessBrowser__acidovorax_3H11:Ac3H11_417 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)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
26% identity, 98% coverage: 9:450/451 of query aligns to 11:470/478 of 3h0mA
- active site: K72 (= K69), S147 (= S152), S148 (= S153), S166 (= S171), T168 (= T173), G169 (= G174), G170 (= G175), S171 (= S176), Q174 (≠ I179)
- binding glutamine: M122 (≠ F120), G123 (vs. gap), D167 (= D172), T168 (= T173), G169 (= G174), G170 (= G175), S171 (= S176), F199 (≠ L204), Y302 (= Y292), R351 (= R321), D418 (≠ N395)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
26% identity, 98% coverage: 9:450/451 of query aligns to 11:470/478 of 3h0lA
- active site: K72 (= K69), S147 (= S152), S148 (= S153), S166 (= S171), T168 (= T173), G169 (= G174), G170 (= G175), S171 (= S176), Q174 (≠ I179)
- binding asparagine: G123 (vs. gap), S147 (= S152), G169 (= G174), G170 (= G175), S171 (= S176), Y302 (= Y292), R351 (= R321), D418 (≠ N395)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
27% identity, 89% coverage: 46:447/451 of query aligns to 182:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A119), T258 (≠ G122), S281 (= S152), G302 (≠ T173), G303 (= G174), S305 (= S176), S472 (≠ R319), I532 (≠ F391), M539 (≠ L398)
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)
27% identity, 89% coverage: 46:447/451 of query aligns to 182:589/607 of Q7XJJ7
- K205 (= K69) mutation to A: Loss of activity.
- SS 281:282 (= SS 152:153) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 173:176) binding substrate
- S305 (= S176) mutation to A: Loss of activity.
- R307 (= R178) mutation to A: Loss of activity.
- S360 (vs. gap) mutation to A: No effect.
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
27% identity, 89% coverage: 46:447/451 of query aligns to 182:589/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A119), G302 (≠ T173), G303 (= G174), G304 (= G175), A305 (≠ S176), V442 (vs. gap), I475 (= I322), M539 (≠ L398)
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, 89% coverage: 46:447/451 of query aligns to 182:589/605 of 8ey1D
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 90% coverage: 46:450/451 of query aligns to 50:442/461 of 4gysB
- active site: K72 (= K69), S146 (= S152), S147 (= S153), T165 (≠ S171), T167 (= T173), A168 (≠ G174), G169 (= G175), S170 (= S176), V173 (≠ I179)
- binding malonate ion: A120 (= A119), G122 (≠ S121), S146 (= S152), T167 (= T173), A168 (≠ G174), S170 (= S176), S193 (≠ T199), G194 (= G200), V195 (≠ A201), R200 (≠ T206), Y297 (≠ F294), R305 (vs. gap)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
41% identity, 38% coverage: 60:231/451 of query aligns to 72:239/487 of 1m21A
- active site: K81 (= K69), S160 (= S152), S161 (= S153), T179 (≠ S171), T181 (= T173), D182 (≠ G174), G183 (= G175), S184 (= S176), C187 (≠ I179)
- binding : A129 (= A119), N130 (vs. gap), F131 (= F120), C158 (≠ G150), G159 (= G151), S160 (= S152), S184 (= S176), C187 (≠ I179), I212 (≠ L204)
Sites not aligning to the query:
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)
30% identity, 81% coverage: 61:426/451 of query aligns to 28:402/425 of Q9FR37
- K36 (= K69) 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 (vs. gap) mutation to T: Slightly reduces catalytic activity.
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
25% identity, 86% coverage: 61:446/451 of query aligns to 71:473/485 of 2f2aA
- active site: K79 (= K69), S154 (≠ W135), S155 (≠ D136), S173 (= S171), T175 (= T173), G176 (= G174), G177 (= G175), S178 (= S176), Q181 (≠ I179)
- binding glutamine: G130 (≠ S121), S154 (≠ W135), D174 (= D172), T175 (= T173), G176 (= G174), S178 (= S176), F206 (≠ L204), Y309 (vs. gap), Y310 (vs. gap), R358 (= R321), D425 (≠ N395)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
25% identity, 86% coverage: 61:446/451 of query aligns to 71:473/485 of 2dqnA
- active site: K79 (= K69), S154 (≠ W135), S155 (≠ D136), S173 (= S171), T175 (= T173), G176 (= G174), G177 (= G175), S178 (= S176), Q181 (≠ I179)
- binding asparagine: M129 (≠ F120), G130 (≠ S121), T175 (= T173), G176 (= G174), S178 (= S176), Y309 (vs. gap), Y310 (vs. gap), R358 (= R321), D425 (≠ N395)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
32% identity, 69% coverage: 60:370/451 of query aligns to 65:380/457 of 6c6gA