SitesBLAST
Comparing WP_037572612.1 NCBI__GCF_000744815.1:WP_037572612.1 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)
50% identity, 97% coverage: 10:492/499 of query aligns to 6:477/478 of 3h0mA
- active site: K72 (= K82), S147 (= S157), S148 (≠ G158), S166 (≠ T176), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (= Q184)
- binding glutamine: M122 (= M132), G123 (= G133), D167 (= D177), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), F199 (= F209), Y302 (= Y313), R351 (= R364), D418 (= D431)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
50% identity, 97% coverage: 10:492/499 of query aligns to 6:477/478 of 3h0lA
- active site: K72 (= K82), S147 (= S157), S148 (≠ G158), S166 (≠ T176), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (= Q184)
- binding asparagine: G123 (= G133), S147 (= S157), G169 (= G179), G170 (= G180), S171 (= S181), Y302 (= Y313), R351 (= R364), D418 (= D431)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
47% identity, 96% coverage: 8:485/499 of query aligns to 4:477/485 of 2f2aA
- active site: K79 (= K82), S154 (= S157), S155 (≠ G158), S173 (≠ T176), T175 (= T178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (= Q184)
- binding glutamine: G130 (= G133), S154 (= S157), D174 (= D177), T175 (= T178), G176 (= G179), S178 (= S181), F206 (= F209), Y309 (= Y313), Y310 (= Y314), R358 (= R364), D425 (= D431)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
47% identity, 96% coverage: 8:485/499 of query aligns to 4:477/485 of 2dqnA
- active site: K79 (= K82), S154 (= S157), S155 (≠ G158), S173 (≠ T176), T175 (= T178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (= Q184)
- binding asparagine: M129 (= M132), G130 (= G133), T175 (= T178), G176 (= G179), S178 (= S181), Y309 (= Y313), Y310 (= Y314), R358 (= R364), D425 (= D431)
3kfuE Crystal structure of the transamidosome (see paper)
51% identity, 95% coverage: 11:483/499 of query aligns to 2:456/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
37% identity, 78% coverage: 74:464/499 of query aligns to 30:433/450 of 4n0iA
- active site: K38 (= K82), S116 (= S157), S117 (≠ G158), T135 (= T176), T137 (= T178), G138 (= G179), G139 (= G180), S140 (= S181), L143 (≠ Q184)
- binding glutamine: G89 (= G133), T137 (= T178), G138 (= G179), S140 (= S181), Y168 (≠ F209), Y271 (= Y313), Y272 (= Y314), R320 (= R364), D404 (= D431)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
36% identity, 94% coverage: 13:481/499 of query aligns to 5:448/457 of 6c6gA
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
32% identity, 95% coverage: 10:481/499 of query aligns to 29:487/507 of Q84DC4
- T31 (≠ A12) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K82) mutation to A: Abolishes activity on mandelamide.
- S180 (= S157) mutation to A: Significantly decreases activity on mandelamide.
- S181 (≠ G158) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G179) 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 (= S181) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q184) 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 (≠ A309) 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 (≠ D431) 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.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
36% identity, 93% coverage: 18:482/499 of query aligns to 15:477/487 of 1m21A
- active site: K81 (= K82), S160 (= S157), S161 (≠ G158), T179 (= T176), T181 (= T178), D182 (≠ G179), G183 (= G180), S184 (= S181), C187 (≠ Q184)
- binding : A129 (= A131), N130 (≠ M132), F131 (≠ G133), C158 (≠ G155), G159 (= G156), S160 (= S157), S184 (= S181), C187 (≠ Q184), I212 (≠ F209), R318 (≠ Y314), L321 (≠ A317), L365 (≠ M366), F426 (vs. gap)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
33% identity, 82% coverage: 72:482/499 of query aligns to 85:498/508 of 3a1iA