SitesBLAST
Comparing HSERO_RS23305 FitnessBrowser__HerbieS:HSERO_RS23305 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)
47% identity, 98% coverage: 5:483/488 of query aligns to 7:479/485 of 2f2aA
- active site: K79 (= K74), S154 (= S149), S155 (= S150), S173 (≠ T168), T175 (= T170), G176 (= G171), G177 (= G172), S178 (= S173), Q181 (= Q176)
- binding glutamine: A128 (= A123), M129 (= M124), G130 (= G125), S154 (= S149), D174 (= D169), T175 (= T170), G176 (= G171), G177 (= G172), S178 (= S173), F206 (= F201), Y309 (= Y304), Y310 (= Y305), R358 (= R353), D425 (= D424)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
47% identity, 98% coverage: 5:483/488 of query aligns to 7:479/485 of 2dqnA
- active site: K79 (= K74), S154 (= S149), S155 (= S150), S173 (≠ T168), T175 (= T170), G176 (= G171), G177 (= G172), S178 (= S173), Q181 (= Q176)
- binding asparagine: A128 (= A123), M129 (= M124), G130 (= G125), S154 (= S149), T175 (= T170), G176 (= G171), G177 (= G172), S178 (= S173), F206 (= F201), Y309 (= Y304), Y310 (= Y305), R358 (= R353), D425 (= D424)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
47% identity, 100% coverage: 1:487/488 of query aligns to 2:476/478 of 3h0mA
- active site: K72 (= K74), S147 (= S149), S148 (= S150), S166 (≠ T168), T168 (= T170), G169 (= G171), G170 (= G172), S171 (= S173), Q174 (= Q176)
- binding glutamine: A121 (= A123), M122 (= M124), G123 (= G125), D167 (= D169), T168 (= T170), G169 (= G171), G170 (= G172), S171 (= S173), F199 (= F201), Y302 (= Y304), Y303 (= Y305), R351 (= R353), D418 (= D424)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
47% identity, 100% coverage: 1:487/488 of query aligns to 2:476/478 of 3h0lA
- active site: K72 (= K74), S147 (= S149), S148 (= S150), S166 (≠ T168), T168 (= T170), G169 (= G171), G170 (= G172), S171 (= S173), Q174 (= Q176)
- binding asparagine: A121 (= A123), M122 (= M124), G123 (= G125), S124 (= S126), G146 (= G148), S147 (= S149), G169 (= G171), G170 (= G172), S171 (= S173), F199 (= F201), Y302 (= Y304), Y303 (= Y305), R351 (= R353), D418 (= D424)
3kfuE Crystal structure of the transamidosome (see paper)
46% identity, 98% coverage: 8:487/488 of query aligns to 4:465/468 of 3kfuE
- active site: K65 (= K74), S140 (= S149), S141 (= S150), S159 (≠ T168), T161 (= T170), G162 (= G171), G163 (= G172), S164 (= S173), Q167 (= Q176)
- binding : S350 (≠ H363), G351 (= G364), Y352 (= Y365), Y353 (= Y366), E354 (≠ D367)
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
36% identity, 83% coverage: 66:471/488 of query aligns to 30:444/450 of 4n0iA
- active site: K38 (= K74), S116 (= S149), S117 (= S150), T135 (= T168), T137 (= T170), G138 (= G171), G139 (= G172), S140 (= S173), L143 (≠ Q176)
- binding glutamine: G87 (≠ A123), M88 (= M124), G89 (= G125), S90 (= S126), S116 (= S149), D136 (= D169), T137 (= T170), G138 (= G171), G139 (= G172), S140 (= S173), Y168 (≠ F201), Y271 (= Y304), Y272 (= Y305), R320 (= R353), D404 (= D424)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
33% identity, 85% coverage: 64:478/488 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K74), S170 (= S149), S171 (= S150), G189 (≠ T168), Q191 (≠ T170), G192 (= G171), G193 (= G172), A194 (≠ S173), I197 (≠ Q176)
- binding benzamide: C144 (≠ A123), F145 (≠ M124), S146 (≠ G125), G147 (≠ S126), G169 (= G148), D190 (= D169), Q191 (≠ T170), G192 (= G171), G193 (= G172), A194 (≠ S173), W327 (≠ Y304), I449 (≠ S429)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
32% identity, 97% coverage: 1:474/488 of query aligns to 25:484/507 of Q84DC4
- T31 (≠ K7) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K74) mutation to A: Abolishes activity on mandelamide.
- S180 (= S149) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S150) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G171) 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 (= S173) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q176) 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 (= S300) 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 (≠ R352) 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 (≠ L428) 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)
31% identity, 97% coverage: 6:480/488 of query aligns to 8:479/487 of 1m21A
- active site: K81 (= K74), S160 (= S149), S161 (= S150), T179 (= T168), T181 (= T170), D182 (≠ G171), G183 (= G172), S184 (= S173), C187 (≠ Q176)
- binding : A129 (= A123), N130 (≠ M124), F131 (≠ G125), S138 (vs. gap), C158 (≠ G147), G159 (= G148), S160 (= S149), T181 (= T170), D182 (≠ G171), S184 (= S173), C187 (≠ Q176), I212 (≠ F201), R318 (≠ Y305), L321 (≠ A308), L365 (= L355), W417 (= W408), 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: 10:477/488 of query aligns to 12:448/457 of 6c6gA