SitesBLAST
Comparing WP_011886344.1 NCBI__GCF_000016205.1:WP_011886344.1 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)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
47% identity, 99% coverage: 1:493/496 of query aligns to 2:476/478 of 3h0mA
- active site: K72 (= K75), S147 (= S150), S148 (= S151), S166 (≠ T169), T168 (= T171), G169 (= G172), G170 (= G173), S171 (= S174), Q174 (= Q177)
- binding glutamine: M122 (= M125), G123 (= G126), D167 (= D170), T168 (= T171), G169 (= G172), G170 (= G173), S171 (= S174), F199 (= F202), Y302 (= Y315), R351 (= R364), D418 (= D431)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
47% identity, 99% coverage: 1:493/496 of query aligns to 2:476/478 of 3h0lA
- active site: K72 (= K75), S147 (= S150), S148 (= S151), S166 (≠ T169), T168 (= T171), G169 (= G172), G170 (= G173), S171 (= S174), Q174 (= Q177)
- binding asparagine: G123 (= G126), S147 (= S150), G169 (= G172), G170 (= G173), S171 (= S174), Y302 (= Y315), R351 (= R364), D418 (= D431)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
49% identity, 91% coverage: 37:489/496 of query aligns to 40:479/485 of 2f2aA
- active site: K79 (= K75), S154 (= S150), S155 (= S151), S173 (≠ T169), T175 (= T171), G176 (= G172), G177 (= G173), S178 (= S174), Q181 (= Q177)
- binding glutamine: G130 (= G126), S154 (= S150), D174 (= D170), T175 (= T171), G176 (= G172), S178 (= S174), F206 (= F202), Y309 (= Y315), Y310 (= Y316), R358 (= R364), D425 (= D431)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
49% identity, 91% coverage: 37:489/496 of query aligns to 40:479/485 of 2dqnA
- active site: K79 (= K75), S154 (= S150), S155 (= S151), S173 (≠ T169), T175 (= T171), G176 (= G172), G177 (= G173), S178 (= S174), Q181 (= Q177)
- binding asparagine: M129 (= M125), G130 (= G126), T175 (= T171), G176 (= G172), S178 (= S174), Y309 (= Y315), Y310 (= Y316), R358 (= R364), D425 (= D431)
3kfuE Crystal structure of the transamidosome (see paper)
48% identity, 98% coverage: 8:495/496 of query aligns to 4:467/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
35% identity, 84% coverage: 67:482/496 of query aligns to 30:449/450 of 4n0iA
- active site: K38 (= K75), S116 (= S150), S117 (= S151), T135 (= T169), T137 (= T171), G138 (= G172), G139 (= G173), S140 (= S174), L143 (≠ Q177)
- binding glutamine: G89 (= G126), T137 (= T171), G138 (= G172), S140 (= S174), Y168 (≠ F202), Y271 (= Y315), Y272 (= Y316), R320 (= R364), D404 (= D431)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
32% identity, 97% coverage: 6:486/496 of query aligns to 8:479/487 of 1m21A
- active site: K81 (= K75), S160 (= S150), S161 (= S151), T179 (= T169), T181 (= T171), D182 (≠ G172), G183 (= G173), S184 (= S174), C187 (≠ Q177)
- binding : A129 (= A124), N130 (≠ M125), F131 (≠ G126), C158 (≠ G148), G159 (= G149), S160 (= S150), S184 (= S174), C187 (≠ Q177), I212 (≠ F202), R318 (≠ Y316), L321 (≠ A319), L365 (≠ V371), F426 (vs. gap)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
34% identity, 96% coverage: 7:483/496 of query aligns to 4:448/457 of 6c6gA
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
31% identity, 97% coverage: 5:483/496 of query aligns to 29:487/507 of Q84DC4
- T31 (= T7) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K75) mutation to A: Abolishes activity on mandelamide.
- S180 (= S150) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S151) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G172) 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 (= S174) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q177) 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 (= S311) 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 (≠ D378) 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 (≠ L435) 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.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 90% coverage: 40:484/496 of query aligns to 169:589/616 of 6diiH