SitesBLAST
Comparing WP_110206069.1 NCBI__GCF_003194585.1:WP_110206069.1 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)
48% identity, 94% coverage: 10:502/522 of query aligns to 5:477/478 of 3h0mA
- active site: K72 (= K87), S147 (= S162), S148 (≠ G163), S166 (≠ T181), T168 (= T183), G169 (= G184), G170 (= G185), S171 (= S186), Q174 (= Q189)
- binding glutamine: M122 (= M137), G123 (= G138), D167 (= D182), T168 (= T183), G169 (= G184), G170 (= G185), S171 (= S186), F199 (≠ M214), Y302 (= Y321), R351 (= R374), D418 (= D441)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
48% identity, 94% coverage: 10:502/522 of query aligns to 5:477/478 of 3h0lA
- active site: K72 (= K87), S147 (= S162), S148 (≠ G163), S166 (≠ T181), T168 (= T183), G169 (= G184), G170 (= G185), S171 (= S186), Q174 (= Q189)
- binding asparagine: G123 (= G138), S147 (= S162), G169 (= G184), G170 (= G185), S171 (= S186), Y302 (= Y321), R351 (= R374), D418 (= D441)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
51% identity, 85% coverage: 48:491/522 of query aligns to 40:473/485 of 2f2aA
- active site: K79 (= K87), S154 (= S162), S155 (≠ G163), S173 (≠ T181), T175 (= T183), G176 (= G184), G177 (= G185), S178 (= S186), Q181 (= Q189)
- binding glutamine: G130 (= G138), S154 (= S162), D174 (= D182), T175 (= T183), G176 (= G184), S178 (= S186), F206 (≠ M214), Y309 (= Y321), Y310 (= Y322), R358 (= R374), D425 (= D441)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
51% identity, 85% coverage: 48:491/522 of query aligns to 40:473/485 of 2dqnA
- active site: K79 (= K87), S154 (= S162), S155 (≠ G163), S173 (≠ T181), T175 (= T183), G176 (= G184), G177 (= G185), S178 (= S186), Q181 (= Q189)
- binding asparagine: M129 (= M137), G130 (= G138), T175 (= T183), G176 (= G184), S178 (= S186), Y309 (= Y321), Y310 (= Y322), R358 (= R374), D425 (= D441)
3kfuE Crystal structure of the transamidosome (see paper)
52% identity, 92% coverage: 12:491/522 of query aligns to 2:454/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
36% identity, 78% coverage: 75:481/522 of query aligns to 26:440/450 of 4n0iA
- active site: K38 (= K87), S116 (= S162), S117 (≠ G163), T135 (= T181), T137 (= T183), G138 (= G184), G139 (= G185), S140 (= S186), L143 (≠ Q189)
- binding glutamine: G89 (= G138), T137 (= T183), G138 (= G184), S140 (= S186), Y168 (≠ M214), Y271 (= Y321), Y272 (= Y322), R320 (= R374), D404 (= D441)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
34% identity, 92% coverage: 14:491/522 of query aligns to 5:448/457 of 6c6gA
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
35% identity, 80% coverage: 79:493/522 of query aligns to 87:499/508 of 3a1iA
- active site: K95 (= K87), S170 (= S162), S171 (≠ G163), G189 (≠ T181), Q191 (≠ T183), G192 (= G184), G193 (= G185), A194 (≠ S186), I197 (≠ Q189)
- binding benzamide: F145 (≠ M137), S146 (≠ G138), G147 (≠ S139), Q191 (≠ T183), G192 (= G184), G193 (= G185), A194 (≠ S186), W327 (≠ Y321)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
32% identity, 96% coverage: 14:514/522 of query aligns to 32:503/507 of Q84DC4
- K100 (= K87) mutation to A: Abolishes activity on mandelamide.
- S180 (= S162) mutation to A: Significantly decreases activity on mandelamide.
- S181 (≠ G163) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G184) 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 (= S186) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q189) 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 (≠ T320) 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 (≠ D388) 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 (vs. gap) 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.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
34% identity, 92% coverage: 13:491/522 of query aligns to 9:476/487 of 1m21A