SitesBLAST
Comparing WP_012566706.1 NCBI__GCF_000016185.1:WP_012566706.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
46% identity, 97% coverage: 2:508/521 of query aligns to 1:473/485 of 2f2aA
- active site: K79 (= K78), S154 (= S189), S155 (= S190), S173 (≠ T208), T175 (= T210), G176 (= G211), G177 (= G212), S178 (= S213), Q181 (= Q216)
- binding glutamine: G130 (= G129), S154 (= S189), D174 (= D209), T175 (= T210), G176 (= G211), S178 (= S213), F206 (= F241), Y309 (= Y344), Y310 (= Y345), R358 (= R392), D425 (= D459)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
46% identity, 97% coverage: 2:508/521 of query aligns to 1:473/485 of 2dqnA
- active site: K79 (= K78), S154 (= S189), S155 (= S190), S173 (≠ T208), T175 (= T210), G176 (= G211), G177 (= G212), S178 (= S213), Q181 (= Q216)
- binding asparagine: M129 (= M128), G130 (= G129), T175 (= T210), G176 (= G211), S178 (= S213), Y309 (= Y344), Y310 (= Y345), R358 (= R392), D425 (= D459)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
47% identity, 96% coverage: 8:509/521 of query aligns to 6:467/478 of 3h0mA
- active site: K72 (= K78), S147 (= S189), S148 (= S190), S166 (≠ T208), T168 (= T210), G169 (= G211), G170 (= G212), S171 (= S213), Q174 (= Q216)
- binding glutamine: M122 (= M128), G123 (= G129), D167 (= D209), T168 (= T210), G169 (= G211), G170 (= G212), S171 (= S213), F199 (= F241), Y302 (= Y344), R351 (= R392), D418 (= D459)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
47% identity, 96% coverage: 8:509/521 of query aligns to 6:467/478 of 3h0lA
- active site: K72 (= K78), S147 (= S189), S148 (= S190), S166 (≠ T208), T168 (= T210), G169 (= G211), G170 (= G212), S171 (= S213), Q174 (= Q216)
- binding asparagine: G123 (= G129), S147 (= S189), G169 (= G211), G170 (= G212), S171 (= S213), Y302 (= Y344), R351 (= R392), D418 (= D459)
3kfuE Crystal structure of the transamidosome (see paper)
44% identity, 94% coverage: 19:510/521 of query aligns to 12:456/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
35% identity, 83% coverage: 70:501/521 of query aligns to 30:443/450 of 4n0iA
- active site: K38 (= K78), S116 (= S189), S117 (= S190), T135 (= T208), T137 (= T210), G138 (= G211), G139 (= G212), S140 (= S213), L143 (≠ Q216)
- binding glutamine: G89 (= G129), T137 (= T210), G138 (= G211), S140 (= S213), Y168 (≠ F241), Y271 (= Y344), Y272 (= Y345), R320 (= R392), D404 (= D459)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
29% identity, 86% coverage: 70:517/521 of query aligns to 87:506/508 of 3a1iA
- active site: K95 (= K78), S170 (≠ E177), S171 (≠ W178), G189 (≠ T208), Q191 (≠ T210), G192 (= G211), G193 (= G212), A194 (≠ S213), I197 (≠ Q216)
- binding benzamide: F145 (≠ M128), S146 (≠ G129), G147 (≠ S130), Q191 (≠ T210), G192 (= G211), G193 (= G212), A194 (≠ S213), W327 (≠ Y344)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
33% identity, 96% coverage: 9:509/521 of query aligns to 8:477/487 of 1m21A
- active site: K81 (= K78), S160 (= S189), S161 (= S190), T179 (= T208), T181 (= T210), D182 (≠ G211), G183 (= G212), S184 (= S213), C187 (≠ Q216)
- binding : A129 (= A127), N130 (≠ M128), F131 (≠ G129), C158 (≠ G187), G159 (= G188), S160 (= S189), S184 (= S213), C187 (≠ Q216), I212 (≠ F241), R318 (≠ Y345), L321 (≠ A348), L365 (= L394), F426 (≠ Y456)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 98% coverage: 7:517/521 of query aligns to 28:496/507 of Q84DC4
- T31 (≠ A10) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K78) mutation to A: Abolishes activity on mandelamide.
- S180 (= S189) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S190) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G211) 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 (= S213) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q216) 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 (≠ A325) 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 (≠ D406) 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.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 89% coverage: 48:511/521 of query aligns to 174:591/616 of 6diiH