SitesBLAST
Comparing WP_011814761.1 NCBI__GCF_000015585.1:WP_011814761.1 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)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
35% identity, 96% coverage: 12:464/470 of query aligns to 7:481/490 of 4yjiA
- active site: K79 (= K84), S158 (= S160), S159 (= S161), G179 (≠ A181), G180 (= G182), G181 (= G183), A182 (≠ S184)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ V86), G132 (= G134), S158 (= S160), G179 (≠ A181), G180 (= G182), A182 (≠ S184)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
34% identity, 82% coverage: 74:457/470 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K84), S170 (= S160), S171 (= S161), G189 (≠ T179), Q191 (≠ A181), G192 (= G182), G193 (= G183), A194 (≠ S184), I197 (= I187)
- binding benzamide: F145 (≠ W135), S146 (≠ K136), G147 (= G137), Q191 (≠ A181), G192 (= G182), G193 (= G183), A194 (≠ S184), W327 (≠ F312)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
29% identity, 96% coverage: 12:463/470 of query aligns to 7:480/485 of 2f2aA
- active site: K79 (= K84), S154 (= S160), S155 (= S161), S173 (≠ T179), T175 (≠ A181), G176 (= G182), G177 (= G183), S178 (= S184), Q181 (≠ I187)
- binding glutamine: G130 (≠ K136), S154 (= S160), D174 (= D180), T175 (≠ A181), G176 (= G182), S178 (= S184), F206 (= F212), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ E334), D425 (≠ T407)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
29% identity, 96% coverage: 12:463/470 of query aligns to 7:480/485 of 2dqnA
- active site: K79 (= K84), S154 (= S160), S155 (= S161), S173 (≠ T179), T175 (≠ A181), G176 (= G182), G177 (= G183), S178 (= S184), Q181 (≠ I187)
- binding asparagine: M129 (≠ W135), G130 (≠ K136), T175 (≠ A181), G176 (= G182), S178 (= S184), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ E334), D425 (≠ T407)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
29% identity, 95% coverage: 20:467/470 of query aligns to 138:598/607 of Q7XJJ7
- K205 (= K84) mutation to A: Loss of activity.
- SS 281:282 (= SS 160:161) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ AGGS 181:184) binding
- S305 (= S184) mutation to A: Loss of activity.
- R307 (= R186) mutation to A: Loss of activity.
- S360 (≠ T238) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 95% coverage: 20:467/470 of query aligns to 138:598/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G134), T258 (≠ G137), S281 (= S160), G302 (≠ A181), G303 (= G182), S305 (= S184), S472 (≠ A342), I532 (≠ P395), M539 (≠ T407)
Sites not aligning to the query:
3kfuE Crystal structure of the transamidosome (see paper)
33% identity, 95% coverage: 13:458/470 of query aligns to 2:456/468 of 3kfuE
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
29% identity, 96% coverage: 11:460/470 of query aligns to 5:448/457 of 5h6sC
- active site: K77 (= K84), S152 (= S160), S153 (= S161), L173 (≠ A181), G174 (= G182), G175 (= G183), S176 (= S184)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G134), R128 (≠ K136), W129 (≠ G137), S152 (= S160), L173 (≠ A181), G174 (= G182), S176 (= S184), W306 (≠ F312), F338 (≠ A343)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
31% identity, 95% coverage: 21:466/470 of query aligns to 15:478/482 of 3a2qA
- active site: K69 (= K84), S147 (= S160), S148 (= S161), N166 (≠ T179), A168 (= A181), A169 (≠ G182), G170 (= G183), A171 (≠ S184), I174 (= I187)
- binding 6-aminohexanoic acid: G121 (= G134), G121 (= G134), N122 (≠ W135), S147 (= S160), A168 (= A181), A168 (= A181), A169 (≠ G182), A171 (≠ S184), C313 (≠ G318)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
31% identity, 95% coverage: 11:457/470 of query aligns to 1:449/457 of 6c6gA
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 95% coverage: 12:457/470 of query aligns to 6:467/478 of 3h0mA
- active site: K72 (= K84), S147 (= S160), S148 (= S161), S166 (≠ T179), T168 (≠ A181), G169 (= G182), G170 (= G183), S171 (= S184), Q174 (≠ I187)
- binding glutamine: M122 (≠ W135), G123 (≠ K136), D167 (= D180), T168 (≠ A181), G169 (= G182), G170 (= G183), S171 (= S184), F199 (= F212), Y302 (≠ F305), R351 (≠ A333), D418 (≠ P408)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 95% coverage: 12:457/470 of query aligns to 6:467/478 of 3h0lA
- active site: K72 (= K84), S147 (= S160), S148 (= S161), S166 (≠ T179), T168 (≠ A181), G169 (= G182), G170 (= G183), S171 (= S184), Q174 (≠ I187)
- binding asparagine: G123 (≠ K136), S147 (= S160), G169 (= G182), G170 (= G183), S171 (= S184), Y302 (≠ F305), R351 (≠ A333), D418 (≠ P408)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 96% coverage: 1:453/470 of query aligns to 18:484/507 of Q84DC4
- T31 (≠ S14) 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 (= S160) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S161) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G182) 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 (= S184) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I187) 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 (≠ A281) 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 (≠ M351) 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.
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
30% identity, 90% coverage: 36:457/470 of query aligns to 44:462/605 of Q936X2
- K91 (= K84) mutation to A: Loss of activity.
- S165 (= S160) mutation to A: Loss of activity.
- S189 (= S184) mutation to A: Loss of activity.
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)
32% identity, 60% coverage: 15:295/470 of query aligns to 81:357/579 of Q9TUI8
- S217 (= S160) mutation to A: Loss of activity.
- S218 (= S161) mutation to A: Lowers activity by at least 98%.
- D237 (= D180) mutation D->E,N: Loss of activity.
- S241 (= S184) mutation to A: Loss of activity.
- C249 (≠ S192) mutation to A: Loss of activity.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
29% identity, 96% coverage: 6:457/470 of query aligns to 6:477/487 of 1m21A
- active site: K81 (= K84), S160 (= S160), S161 (= S161), T179 (= T179), T181 (≠ A181), D182 (≠ G182), G183 (= G183), S184 (= S184), C187 (≠ I187)
- binding : A129 (≠ L133), N130 (≠ G134), F131 (≠ W135), C158 (≠ G158), G159 (= G159), S160 (= S160), S184 (= S184), C187 (≠ I187), I212 (≠ A209), R318 (≠ A311), L321 (= L314), L365 (≠ C338), F426 (≠ V394)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
29% identity, 94% coverage: 11:452/470 of query aligns to 2:403/412 of 1ocmA
- active site: K62 (= K84), S131 (= S160), S132 (= S161), T152 (≠ A181), G153 (= G182), G154 (= G183), S155 (= S184)
- binding pyrophosphate 2-: R113 (≠ K136), S131 (= S160), Q151 (≠ D180), T152 (≠ A181), G153 (= G182), G154 (= G183), S155 (= S184), R158 (≠ I187), P359 (= P401)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
29% identity, 94% coverage: 11:452/470 of query aligns to 2:403/412 of 1o9oA
- active site: K62 (= K84), A131 (≠ S160), S132 (= S161), T150 (= T179), T152 (≠ A181), G153 (= G182), G154 (= G183), S155 (= S184), R158 (≠ I187)
- binding 3-amino-3-oxopropanoic acid: G130 (= G159), T152 (≠ A181), G153 (= G182), G154 (= G183), S155 (= S184), R158 (≠ I187), P359 (= P401)
2vyaA Crystal structure of fatty acid amide hydrolase conjugated with the drug-like inhibitor pf-750 (see paper)
30% identity, 69% coverage: 17:339/470 of query aligns to 51:369/543 of 2vyaA
- active site: K110 (= K84), S185 (= S160), S186 (= S161), T204 (= T179), I206 (≠ A181), G207 (= G182), G208 (= G183), S209 (= S184), F212 (≠ I187)
- binding 4-(quinolin-3-ylmethyl)piperidine-1-carboxylic acid: F160 (≠ W135), S161 (≠ K136), I206 (≠ A181), G207 (= G182), S209 (= S184)
Sites not aligning to the query:
3oj8A Alpha-ketoheterocycle inhibitors of fatty acid amide hydrolase containing additional conformational contraints in the acyl side chain (see paper)
30% identity, 69% coverage: 17:339/470 of query aligns to 51:369/542 of 3oj8A
- active site: K110 (= K84), S185 (= S160), S186 (= S161), T204 (= T179), I206 (≠ A181), G207 (= G182), G208 (= G183), S209 (= S184), F212 (≠ I187)
- binding (S)-[(2S)-6-phenoxy-1,2,3,4-tetrahydronaphthalen-2-yl](5-pyridin-2-yl-1,3-oxazol-2-yl)methanol: M159 (≠ G134), F160 (≠ W135), S185 (= S160), D205 (= D180), I206 (≠ A181), G207 (= G182), S209 (= S184), L246 (vs. gap), F349 (vs. gap)
Sites not aligning to the query:
Query Sequence
>WP_011814761.1 NCBI__GCF_000015585.1:WP_011814761.1
MSSHPTAIADLTASELLRRYRSGSLSPVEATEAALARIRAHNETVNAFCLVDETTTLAAA
RRAEQRYLNTSPMGELDGVPVAIKDVFLTRGWPNLKGSKTVDPAGPWEQDAPAVSALRRH
GFVPLGKTTTPELGWKGVTDCPCYGVTRNPFDPDKTAGGSSGGSASSVVLGMGPLALGTD
AGGSIRIPAGFSGLVGHKPTQGRVPLWPASPFGQLAHPGPMTWTVEDAARLMNVIAETDP
RDPTLPAAGGDYVAALAGGVGGLRVAFSPNLGYVQVDAEIARSVAEAARMFEALGARVEE
VDPGFADPREAFDLLFFGGAANALRSIPEERHAEMDPCLIEAAGSVRDASMLDYLAAMNE
RAALIERTSLFHQQYDLLLTPTLPIPAFTAGREVPEGWHDPRWPSWTPFTYPFNMTGQPA
CSVPCGFTGQGLPIGLQIVGPRHADALVLRAAHAYQQAAPLTDHRPAWAR
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