SitesBLAST
Comparing WP_092993132.1 NCBI__GCF_900102855.1:WP_092993132.1 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)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
34% identity, 95% coverage: 9:460/478 of query aligns to 7:480/490 of 4yjiA
- active site: K79 (= K81), S158 (= S157), S159 (= S158), G179 (≠ A178), G180 (= G179), G181 (= G180), A182 (≠ S181)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ V83), G132 (= G131), S158 (= S157), G179 (≠ A178), G180 (= G179), A182 (≠ S181)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
29% identity, 93% coverage: 9:453/478 of query aligns to 7:473/485 of 2f2aA
- active site: K79 (= K81), S154 (= S157), S155 (= S158), S173 (≠ T176), T175 (≠ A178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (≠ I184)
- binding glutamine: G130 (≠ K133), S154 (= S157), D174 (= D177), T175 (≠ A178), G176 (= G179), S178 (= S181), F206 (vs. gap), Y309 (≠ L312), Y310 (≠ F313), R358 (vs. gap), D425 (≠ T404)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
29% identity, 93% coverage: 9:453/478 of query aligns to 7:473/485 of 2dqnA
- active site: K79 (= K81), S154 (= S157), S155 (= S158), S173 (≠ T176), T175 (≠ A178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (≠ I184)
- binding asparagine: M129 (≠ W132), G130 (≠ K133), T175 (≠ A178), G176 (= G179), S178 (= S181), Y309 (≠ L312), Y310 (≠ F313), R358 (vs. gap), D425 (≠ T404)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
34% identity, 81% coverage: 69:454/478 of query aligns to 83:498/508 of 3a1iA
- active site: K95 (= K81), S170 (= S157), S171 (= S158), G189 (≠ T176), Q191 (≠ A178), G192 (= G179), G193 (= G180), A194 (≠ S181), I197 (= I184)
- binding benzamide: F145 (≠ W132), S146 (≠ K133), G147 (= G134), Q191 (≠ A178), G192 (= G179), G193 (= G180), A194 (≠ S181), W327 (≠ F309)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 95% coverage: 12:465/478 of query aligns to 133:600/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G131), T258 (≠ G134), S281 (= S157), G302 (≠ A178), G303 (= G179), S305 (= S181), S472 (≠ D333), I532 (vs. gap), M539 (≠ T404)
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)
29% identity, 95% coverage: 12:465/478 of query aligns to 133:600/607 of Q7XJJ7
- K205 (= K81) mutation to A: Loss of activity.
- SS 281:282 (= SS 157:158) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ AGGS 178:181) binding
- S305 (= S181) mutation to A: Loss of activity.
- R307 (= R183) mutation to A: Loss of activity.
- S360 (vs. gap) mutation to A: No effect.
3kfuE Crystal structure of the transamidosome (see paper)
35% identity, 91% coverage: 22:455/478 of query aligns to 14:456/468 of 3kfuE
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 95% coverage: 9:464/478 of query aligns to 6:477/478 of 3h0mA
- active site: K72 (= K81), S147 (= S157), S148 (= S158), S166 (≠ T176), T168 (≠ A178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (≠ I184)
- binding glutamine: M122 (≠ W132), G123 (≠ K133), D167 (= D177), T168 (≠ A178), G169 (= G179), G170 (= G180), S171 (= S181), F199 (= F209), Y302 (≠ F302), R351 (vs. gap), D418 (≠ T404)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 95% coverage: 9:464/478 of query aligns to 6:477/478 of 3h0lA
- active site: K72 (= K81), S147 (= S157), S148 (= S158), S166 (≠ T176), T168 (≠ A178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (≠ I184)
- binding asparagine: G123 (≠ K133), S147 (= S157), G169 (= G179), G170 (= G180), S171 (= S181), Y302 (≠ F302), R351 (vs. gap), D418 (≠ T404)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
33% identity, 90% coverage: 26:453/478 of query aligns to 19:448/457 of 6c6gA
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
29% identity, 94% coverage: 8:457/478 of query aligns to 5:448/457 of 5h6sC
- active site: K77 (= K81), S152 (= S157), S153 (= S158), L173 (≠ A178), G174 (= G179), G175 (= G180), S176 (= S181)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G131), R128 (≠ K133), W129 (≠ G134), S152 (= S157), L173 (≠ A178), G174 (= G179), S176 (= S181), W306 (≠ F309), F338 (≠ V337)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 94% coverage: 7:453/478 of query aligns to 27:487/507 of Q84DC4
- T31 (≠ A11) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K81) mutation to A: Abolishes activity on mandelamide.
- S180 (= S157) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S158) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G179) 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 (= S181) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I184) 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 (≠ A278) 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 (≠ L348) 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 (≠ T404) 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.
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, 66% coverage: 12:327/478 of query aligns to 81:395/579 of Q9TUI8
- S217 (= S157) mutation to A: Loss of activity.
- S218 (= S158) mutation to A: Lowers activity by at least 98%.
- D237 (= D177) mutation D->E,N: Loss of activity.
- S241 (= S181) mutation to A: Loss of activity.
- C249 (≠ S189) mutation to A: Loss of activity.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
27% identity, 97% coverage: 2:463/478 of query aligns to 5:485/487 of 1m21A
- active site: K81 (= K81), S160 (= S157), S161 (= S158), T179 (= T176), T181 (≠ A178), D182 (≠ G179), G183 (= G180), S184 (= S181), C187 (≠ I184)
- binding : A129 (≠ K133), N130 (≠ G134), F131 (≠ V135), C158 (≠ G155), G159 (= G156), S160 (= S157), S184 (= S181), C187 (≠ I184), I212 (≠ F209), R318 (vs. gap), L321 (vs. gap), L365 (= L336), F426 (≠ T404)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
35% identity, 47% coverage: 10:233/478 of query aligns to 7:227/482 of 3a2qA
- active site: K69 (= K81), S147 (= S157), S148 (= S158), N166 (≠ T176), A168 (= A178), A169 (≠ G179), G170 (= G180), A171 (≠ S181), I174 (= I184)
- binding 6-aminohexanoic acid: G121 (= G131), G121 (= G131), N122 (≠ W132), S147 (= S157), A168 (= A178), A168 (= A178), A169 (≠ G179), A171 (≠ S181)
Sites not aligning to the query:
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
29% identity, 89% coverage: 31:457/478 of query aligns to 25:443/461 of 4gysB
- active site: K72 (= K81), S146 (= S157), S147 (= S158), T165 (= T176), T167 (≠ A178), A168 (≠ G179), G169 (= G180), S170 (= S181), V173 (≠ I184)
- binding malonate ion: A120 (≠ G131), G122 (≠ K133), S146 (= S157), T167 (≠ A178), A168 (≠ G179), S170 (= S181), S193 (≠ W204), G194 (≠ P205), V195 (≠ G206), R200 (≠ G210), Y297 (≠ F314), R305 (≠ A320)
2wapA 3d-crystal structure of humanized-rat fatty acid amide hydrolase (faah) conjugated with the drug-like urea inhibitor pf-3845 (see paper)
39% identity, 32% coverage: 71:223/478 of query aligns to 100:256/541 of 2wapA
- active site: K110 (= K81), S185 (= S157), S186 (= S158), T204 (= T176), I206 (≠ A178), G207 (= G179), G208 (= G180), S209 (= S181), F212 (≠ I184)
- binding 4-(3-{[5-(trifluoromethyl)pyridin-2-yl]oxy}benzyl)piperidine-1-carboxylic acid: F160 (≠ W132), S161 (≠ K133), I206 (≠ A178), G207 (= G179), S209 (= S181)
Sites not aligning to the query:
2wj1A 3d-crystal structure of humanized-rat fatty acid amide hydrolase (faah) conjugated with 7-phenyl-1-(4-(pyridin-2-yl)oxazol-2-yl) heptan- 1-one, an alpha-ketooxazole (see paper)
39% identity, 32% coverage: 71:223/478 of query aligns to 99:255/543 of 2wj1A
- active site: K109 (= K81), S184 (= S157), S185 (= S158), T203 (= T176), I205 (≠ A178), G206 (= G179), G207 (= G180), S208 (= S181), F211 (≠ I184)
- binding 7-phenyl-1-(4-pyridin-2-yl-1,3-oxazol-2-yl)heptane-1,1-diol: S157 (≠ F130), M158 (≠ G131), F159 (≠ W132), S184 (= S157), T203 (= T176), D204 (= D177), I205 (≠ A178), G206 (= G179), S208 (= S181), C236 (≠ S207)
Sites not aligning to the query:
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
29% identity, 83% coverage: 61:455/478 of query aligns to 42:409/412 of 1ocmA
- active site: K62 (= K81), S131 (= S157), S132 (= S158), T152 (≠ A178), G153 (= G179), G154 (= G180), S155 (= S181)
- binding pyrophosphate 2-: R113 (≠ K133), S131 (= S157), Q151 (≠ D177), T152 (≠ A178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ I184), P359 (= P396)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
29% identity, 83% coverage: 61:455/478 of query aligns to 42:409/412 of 1o9oA
- active site: K62 (= K81), A131 (≠ S157), S132 (= S158), T150 (= T176), T152 (≠ A178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ I184)
- binding 3-amino-3-oxopropanoic acid: G130 (= G156), T152 (≠ A178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ I184), P359 (= P396)
Query Sequence
>WP_092993132.1 NCBI__GCF_900102855.1:WP_092993132.1
MDTDVADMTAAEMAAMFRHRLLSPVEAAEAALDRIRRYNPAVNAFCLVDEETTLKAARAA
EERHLRGESLGELDGVPVAIKDVFLTREWPTLKGSRTITPHQPWRTDAPAVAALRRHGAV
PVGKTTTPEFGWKGVTDNPVDGITRNPWDISRTAGGSSGGSAAAIPLGMGVLALGTDAGG
SIRIPAGFSGLFGHKPTHGRIPMWPGSPFGVLAHPGPMTKTVEDAALLMNVLTEPDRRDP
SLPPDHTDYVQALGGRIAGLHIAFSADFGFVDVDPEIADAVAEAARVFESLGATVEAVDP
GFPNPEESFERLFFGGAANALRDIDTDQRRLMDAGLVESAEAAAKMPLLEYLAAQNVRNE
LLEQMSRFHERFDLLLTPTLPIAAFEAGREVPPGWPKRRWPSWTPFTFPFNMTGQPASSV
PCGFTSEGLPIGLQLVGARHQDALVLRAAHAFEQAQPISRRPPLLDTPGTDDRETIYA
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