SitesBLAST
Comparing PP_2932 FitnessBrowser__Putida:PP_2932 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)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
87% identity, 99% coverage: 3:566/567 of query aligns to 1:564/564 of 6te4A
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
28% identity, 98% coverage: 6:562/567 of query aligns to 5:486/487 of 1m21A
- active site: K81 (= K84), S160 (= S162), S161 (= S163), T179 (≠ E181), T181 (= T183), D182 (≠ W184), G183 (≠ S185), S184 (= S186), C187 (≠ G189)
- binding : A129 (= A133), N130 (= N134), F131 (vs. gap), C158 (≠ S160), G159 (= G161), S160 (= S162), S184 (= S186), C187 (≠ G189), I212 (≠ L214), R318 (≠ L369), L321 (≠ E372), L365 (= L419), F426 (≠ V488)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
37% identity, 44% coverage: 11:258/567 of query aligns to 5:247/457 of 6c6gA
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
25% identity, 98% coverage: 6:563/567 of query aligns to 27:499/507 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 (= K84) mutation to A: Abolishes activity on mandelamide.
- S180 (vs. gap) mutation to A: Significantly decreases activity on mandelamide.
- S181 (vs. gap) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ W184) 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 (≠ G189) 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 (vs. gap) 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 (≠ A421) 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 (≠ V500) 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.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
39% identity, 31% coverage: 55:230/567 of query aligns to 46:214/461 of 4gysB
- active site: K72 (= K84), S146 (= S162), S147 (= S163), T165 (≠ E181), T167 (= T183), A168 (≠ W184), G169 (≠ S185), S170 (= S186), V173 (≠ G189)
- binding malonate ion: A120 (= A133), G122 (= G135), S146 (= S162), T167 (= T183), A168 (≠ W184), S170 (= S186), S193 (≠ R209), G194 (= G210), V195 (≠ N211), R200 (≠ P216)
Sites not aligning to the query:
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
32% identity, 40% coverage: 3:231/567 of query aligns to 1:227/457 of 5h6sC
- active site: K77 (= K84), S152 (= S162), S153 (= S163), L173 (≠ T183), G174 (≠ W184), G175 (≠ S185), S176 (= S186)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A133), R128 (≠ N134), W129 (≠ G135), S152 (= S162), L173 (≠ T183), G174 (≠ W184), S176 (= S186)
Sites not aligning to the query:
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
24% identity, 58% coverage: 8:337/567 of query aligns to 6:348/478 of 3h0mA
- active site: K72 (= K84), S147 (≠ F158), S148 (≠ A159), S166 (≠ E181), T168 (= T183), G169 (≠ W184), G170 (≠ S185), S171 (= S186), Q174 (≠ G189)
- binding glutamine: M122 (≠ N134), G123 (= G135), D167 (≠ E182), T168 (= T183), G169 (≠ W184), G170 (≠ S185), S171 (= S186), F199 (≠ L214), Y302 (≠ M289)
Sites not aligning to the query:
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
24% identity, 58% coverage: 8:337/567 of query aligns to 6:348/478 of 3h0lA
- active site: K72 (= K84), S147 (≠ F158), S148 (≠ A159), S166 (≠ E181), T168 (= T183), G169 (≠ W184), G170 (≠ S185), S171 (= S186), Q174 (≠ G189)
- binding asparagine: G123 (= G135), S147 (≠ F158), G169 (≠ W184), G170 (≠ S185), S171 (= S186), Y302 (≠ M289)
Sites not aligning to the query:
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
34% identity, 32% coverage: 66:244/567 of query aligns to 74:247/605 of Q936X2
- K91 (= K84) mutation to A: Loss of activity.
- S165 (≠ F158) mutation to A: Loss of activity.
- S189 (= S186) mutation to A: Loss of activity.
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
25% identity, 44% coverage: 11:257/567 of query aligns to 130:376/607 of Q7XJJ7
- K205 (= K84) mutation to A: Loss of activity.
- SS 281:282 (= SS 162:163) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TWSS 183:186) binding substrate
- S305 (= S186) mutation to A: Loss of activity.
- R307 (= R188) mutation to A: Loss of activity.
- S360 (≠ D241) mutation to A: No effect.
3kfuE Crystal structure of the transamidosome (see paper)
27% identity, 41% coverage: 11:242/567 of query aligns to 4:220/468 of 3kfuE
Sites not aligning to the query:
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
25% identity, 44% coverage: 11:257/567 of query aligns to 130:376/616 of 6diiH
Sites not aligning to the query:
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
24% identity, 53% coverage: 35:337/567 of query aligns to 28:355/485 of 2f2aA
- active site: K79 (= K84), S154 (= S160), S155 (≠ G161), S173 (≠ E181), T175 (= T183), G176 (≠ W184), G177 (≠ S185), S178 (= S186), Q181 (≠ G189)
- binding glutamine: G130 (= G135), S154 (= S160), D174 (≠ E182), T175 (= T183), G176 (≠ W184), S178 (= S186), F206 (≠ L214), Y309 (≠ M289), Y310 (= Y290)
Sites not aligning to the query:
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
24% identity, 53% coverage: 35:337/567 of query aligns to 28:355/485 of 2dqnA