SitesBLAST
Comparing PP_0613 FitnessBrowser__Putida:PP_0613 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)
31% identity, 95% coverage: 15:458/469 of query aligns to 11:476/485 of 2f2aA
- active site: K79 (= K83), S154 (= S159), S155 (= S160), S173 (= S178), T175 (≠ A180), G176 (= G181), G177 (= G182), S178 (= S183), Q181 (≠ I186)
- binding glutamine: G130 (≠ K135), S154 (= S159), D174 (= D179), T175 (≠ A180), G176 (= G181), S178 (= S183), F206 (≠ M211), Y309 (≠ F304), Y310 (vs. gap), R358 (≠ Q347), D425 (≠ W402)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
31% identity, 95% coverage: 15:458/469 of query aligns to 11:476/485 of 2dqnA
- active site: K79 (= K83), S154 (= S159), S155 (= S160), S173 (= S178), T175 (≠ A180), G176 (= G181), G177 (= G182), S178 (= S183), Q181 (≠ I186)
- binding asparagine: M129 (≠ W134), G130 (≠ K135), T175 (≠ A180), G176 (= G181), S178 (= S183), Y309 (≠ F304), Y310 (vs. gap), R358 (≠ Q347), D425 (≠ W402)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
32% identity, 97% coverage: 11:466/469 of query aligns to 7:485/490 of 4yjiA
- active site: K79 (= K83), S158 (= S159), S159 (= S160), G179 (≠ A180), G180 (= G181), G181 (= G182), A182 (≠ S183)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L85), G132 (= G133), S158 (= S159), G179 (≠ A180), G180 (= G181), A182 (≠ S183)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
33% identity, 82% coverage: 73:456/469 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K83), S170 (= S159), S171 (= S160), G189 (≠ S178), Q191 (≠ A180), G192 (= G181), G193 (= G182), A194 (≠ S183), I197 (= I186)
- binding benzamide: F145 (≠ W134), S146 (≠ K135), G147 (= G136), Q191 (≠ A180), G192 (= G181), G193 (= G182), A194 (≠ S183), W327 (≠ F311)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 97% coverage: 14:468/469 of query aligns to 9:478/478 of 3h0mA
- active site: K72 (= K83), S147 (= S159), S148 (= S160), S166 (= S178), T168 (≠ A180), G169 (= G181), G170 (= G182), S171 (= S183), Q174 (≠ I186)
- binding glutamine: M122 (≠ W134), G123 (≠ K135), D167 (= D179), T168 (≠ A180), G169 (= G181), G170 (= G182), S171 (= S183), F199 (≠ M211), Y302 (≠ F304), R351 (≠ Q347), D418 (≠ T406)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 97% coverage: 14:468/469 of query aligns to 9:478/478 of 3h0lA
- active site: K72 (= K83), S147 (= S159), S148 (= S160), S166 (= S178), T168 (≠ A180), G169 (= G181), G170 (= G182), S171 (= S183), Q174 (≠ I186)
- binding asparagine: G123 (≠ K135), S147 (= S159), G169 (= G181), G170 (= G182), S171 (= S183), Y302 (≠ F304), R351 (≠ Q347), D418 (≠ T406)
3kfuE Crystal structure of the transamidosome (see paper)
32% identity, 95% coverage: 21:467/469 of query aligns to 11:466/468 of 3kfuE
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
26% identity, 97% coverage: 10:466/469 of query aligns to 5:455/457 of 5h6sC
- active site: K77 (= K83), S152 (= S159), S153 (= S160), L173 (≠ A180), G174 (= G181), G175 (= G182), S176 (= S183)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G133), R128 (≠ K135), W129 (≠ G136), S152 (= S159), L173 (≠ A180), G174 (= G181), S176 (= S183), W306 (≠ F311), F338 (vs. gap)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
26% identity, 94% coverage: 19:459/469 of query aligns to 138:592/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G133), T258 (≠ G136), S281 (= S159), G302 (≠ A180), G303 (= G181), S305 (= S183), S472 (≠ G345), I532 (≠ V393), M539 (≠ A400)
Sites not aligning to the query:
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
26% identity, 94% coverage: 19:459/469 of query aligns to 138:592/607 of Q7XJJ7
- K205 (= K83) mutation to A: Loss of activity.
- SS 281:282 (= SS 159:160) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ AGGS 180:183) binding
- S305 (= S183) mutation to A: Loss of activity.
- R307 (= R185) mutation to A: Loss of activity.
- S360 (≠ P237) mutation to A: No effect.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
29% identity, 95% coverage: 10:456/469 of query aligns to 1:449/457 of 6c6gA
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
28% identity, 94% coverage: 17:459/469 of query aligns to 12:472/482 of 3a2qA
- active site: K69 (= K83), S147 (= S159), S148 (= S160), N166 (≠ S178), A168 (= A180), A169 (≠ G181), G170 (= G182), A171 (≠ S183), I174 (= I186)
- binding 6-aminohexanoic acid: G121 (= G133), G121 (= G133), N122 (≠ W134), S147 (= S159), A168 (= A180), A168 (= A180), A169 (≠ G181), A171 (≠ S183), C313 (≠ W315)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
28% identity, 92% coverage: 28:457/469 of query aligns to 37:463/605 of Q936X2
- K91 (= K83) mutation to A: Loss of activity.
- S165 (= S159) mutation to A: Loss of activity.
- S189 (= S183) mutation to A: Loss of activity.
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
26% identity, 95% coverage: 9:455/469 of query aligns to 27:487/507 of Q84DC4
- T31 (≠ V13) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K83) mutation to A: Abolishes activity on mandelamide.
- S180 (= S159) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S160) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G181) 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 (= S183) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I186) 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 (≠ D301) 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 (≠ E352) 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 (≠ T406) 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)
27% identity, 99% coverage: 1:462/469 of query aligns to 11:483/487 of 1m21A
- active site: K81 (= K83), S160 (= S159), S161 (= S160), T179 (≠ S178), T181 (≠ A180), D182 (≠ G181), G183 (= G182), S184 (= S183), C187 (≠ I186)
- binding : A129 (≠ K135), N130 (≠ G136), F131 (≠ V137), C158 (≠ G157), G159 (= G158), S160 (= S159), S184 (= S183), C187 (≠ I186), I212 (≠ M211), R318 (≠ N312), L321 (≠ W315), L365 (= L357), F426 (≠ Y410)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
28% identity, 84% coverage: 53:447/469 of query aligns to 45:430/461 of 4gysB
- active site: K72 (= K83), S146 (= S159), S147 (= S160), T165 (≠ S178), T167 (≠ A180), A168 (≠ G181), G169 (= G182), S170 (= S183), V173 (≠ I186)
- binding malonate ion: A120 (≠ G133), G122 (≠ K135), S146 (= S159), T167 (≠ A180), A168 (≠ G181), S170 (= S183), S193 (= S215), G194 (≠ H216), V195 (≠ L217), R200 (= R222), Y297 (≠ F316), R305 (= R321)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
26% identity, 90% coverage: 23:445/469 of query aligns to 15:396/412 of 1o9oA
- active site: K62 (= K83), A131 (≠ S159), S132 (= S160), T150 (≠ S178), T152 (≠ A180), G153 (= G181), G154 (= G182), S155 (= S183), R158 (≠ I186)
- binding 3-amino-3-oxopropanoic acid: G130 (= G158), T152 (≠ A180), G153 (= G181), G154 (= G182), S155 (= S183), R158 (≠ I186), P359 (vs. gap)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
27% identity, 90% coverage: 23:445/469 of query aligns to 15:396/412 of 1ocmA
- active site: K62 (= K83), S131 (= S159), S132 (= S160), T152 (≠ A180), G153 (= G181), G154 (= G182), S155 (= S183)
- binding pyrophosphate 2-: R113 (≠ K135), S131 (= S159), Q151 (≠ D179), T152 (≠ A180), G153 (= G181), G154 (= G182), S155 (= S183), R158 (≠ I186), P359 (≠ T406)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
30% identity, 53% coverage: 7:253/469 of query aligns to 2:254/564 of 6te4A
Sites not aligning to the query:
Q9TUI8 Fatty-acid amide hydrolase 1; Anandamide amidase; Anandamide amidohydrolase 1; Fatty acid ester hydrolase; Oleamide hydrolase 1; EC 3.5.1.99; EC 3.1.1.- from Sus scrofa (Pig) (see paper)
36% identity, 33% coverage: 73:225/469 of query aligns to 132:288/579 of Q9TUI8
- S217 (= S159) mutation to A: Loss of activity.
- S218 (= S160) mutation to A: Lowers activity by at least 98%.
- D237 (= D179) mutation D->E,N: Loss of activity.
- S241 (= S183) mutation to A: Loss of activity.
- C249 (≠ T191) mutation to A: Loss of activity.
Query Sequence
>PP_0613 FitnessBrowser__Putida:PP_0613
MTQKTAIGELTAVELLELYHRRQLSPVEVVDDVLARIDLHNPAVNAFCHVDGEGARAAAR
ASEQRWQRGQPCGRLDGVPASIKDLTLTRGMPTRKGSRTTSGAGPWEIDAPFSAFMREAG
AVLVGKTTTPEFGWKGVTDNPLYGITRNPWDTRLTAGGSSGGAAAAAALNLGVLHQGSDA
GGSIRIPCAFTGTFGIKPTFGYVPQWPASAMTVLSHLGPMTRTVDDSVLMLDCVARPDAR
DGLAGAPRQAPWLSQQQDLSGLRIAYSANFGYVQVDPQIQALVAQAVQRLARLGAQVEEV
DPGFSDPLETFNTLWFAGAARLASALSDEQKALLDPGLRWIAEQGAQISLGEYTQALEAR
AELIAKMNAFHQRYDVLVSPMLPLVAFEAGHNVPPGSGMAQWMEWTPLSYPFNLTQQPAA
SVPCGFTREGLPVGLQVVAGRFADEQVLRVCKVYEQHYPSRHLQAPITG
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory