SitesBLAST
Comparing AO356_18110 FitnessBrowser__pseudo5_N2C3_1:AO356_18110 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)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
29% identity, 97% coverage: 7:465/471 of query aligns to 5:455/457 of 5h6sC
- active site: K77 (= K81), S152 (= S156), S153 (= S157), L173 (≠ A177), G174 (≠ C178), G175 (= G179), S176 (= S180)
- binding 4-oxidanylbenzohydrazide: C126 (= C130), R128 (≠ A132), W129 (≠ F133), S152 (= S156), L173 (≠ A177), G174 (≠ C178), S176 (= S180), W306 (= W312), F338 (≠ S348)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 97% coverage: 8:463/471 of query aligns to 6:475/478 of 3h0mA
- active site: K72 (= K81), S147 (= S156), S148 (= S157), S166 (= S175), T168 (≠ A177), G169 (≠ C178), G170 (= G179), S171 (= S180), Q174 (≠ I183)
- binding glutamine: M122 (= M131), G123 (≠ A132), D167 (= D176), T168 (≠ A177), G169 (≠ C178), G170 (= G179), S171 (= S180), F199 (≠ L216), Y302 (≠ L311), R351 (≠ L344), D418 (vs. gap)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 97% coverage: 8:463/471 of query aligns to 6:475/478 of 3h0lA
- active site: K72 (= K81), S147 (= S156), S148 (= S157), S166 (= S175), T168 (≠ A177), G169 (≠ C178), G170 (= G179), S171 (= S180), Q174 (≠ I183)
- binding asparagine: G123 (≠ A132), S147 (= S156), G169 (≠ C178), G170 (= G179), S171 (= S180), Y302 (≠ L311), R351 (≠ L344), D418 (vs. gap)
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, 89% coverage: 55:471/471 of query aligns to 179:601/607 of Q7XJJ7
- K205 (= K81) mutation to A: Loss of activity.
- SS 281:282 (= SS 156:157) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ ACGS 177:180) binding
- S305 (= S180) mutation to A: Loss of activity.
- R307 (= R182) mutation to A: Loss of activity.
- S360 (≠ A240) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 89% coverage: 55:471/471 of query aligns to 179:601/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ C130), T258 (≠ F133), S281 (= S156), G302 (≠ A177), G303 (≠ C178), S305 (= S180), S472 (= S336), I532 (vs. gap), M539 (≠ Y404)
Sites not aligning to the query:
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 96% coverage: 7:459/471 of query aligns to 28:492/507 of Q84DC4
- T31 (≠ R10) 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 (= S156) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S157) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ C178) 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 (= S180) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I183) 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 (≠ V296) 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 (≠ E349) 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 (≠ F408) 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.
3kfuE Crystal structure of the transamidosome (see paper)
31% identity, 95% coverage: 18:465/471 of query aligns to 11:465/468 of 3kfuE
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
29% identity, 90% coverage: 34:456/471 of query aligns to 33:475/485 of 2f2aA
- active site: K79 (= K81), S154 (= S156), S155 (= S157), S173 (= S175), T175 (≠ A177), G176 (≠ C178), G177 (= G179), S178 (= S180), Q181 (≠ I183)
- binding glutamine: G130 (≠ A132), S154 (= S156), D174 (= D176), T175 (≠ A177), G176 (≠ C178), S178 (= S180), F206 (≠ L216), Y309 (≠ L311), Y310 (≠ W312), R358 (≠ W362), D425 (vs. gap)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
29% identity, 90% coverage: 34:456/471 of query aligns to 33:475/485 of 2dqnA
- active site: K79 (= K81), S154 (= S156), S155 (= S157), S173 (= S175), T175 (≠ A177), G176 (≠ C178), G177 (= G179), S178 (= S180), Q181 (≠ I183)
- binding asparagine: M129 (= M131), G130 (≠ A132), T175 (≠ A177), G176 (≠ C178), S178 (= S180), Y309 (≠ L311), Y310 (≠ W312), R358 (≠ W362), D425 (vs. gap)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
32% identity, 97% coverage: 13:467/471 of query aligns to 11:478/482 of 3a2qA
- active site: K69 (= K81), S147 (= S156), S148 (= S157), N166 (≠ S175), A168 (= A177), A169 (≠ C178), G170 (= G179), A171 (≠ S180), I174 (= I183)
- binding 6-aminohexanoic acid: G121 (≠ C130), G121 (≠ C130), N122 (≠ M131), S147 (= S156), A168 (= A177), A168 (= A177), A169 (≠ C178), A171 (≠ S180), C313 (≠ L345)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
30% identity, 82% coverage: 71:455/471 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K81), S170 (= S156), S171 (= S157), G189 (≠ S175), Q191 (≠ A177), G192 (≠ C178), G193 (= G179), A194 (≠ S180), I197 (= I183)
- binding benzamide: F145 (≠ M131), S146 (≠ A132), G147 (≠ F133), Q191 (≠ A177), G192 (≠ C178), G193 (= G179), A194 (≠ S180), W327 (= W312)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
38% identity, 49% coverage: 19:251/471 of query aligns to 18:250/487 of 1m21A
- active site: K81 (= K81), S160 (= S156), S161 (= S157), T179 (≠ S175), T181 (≠ A177), D182 (≠ C178), G183 (= G179), S184 (= S180), C187 (≠ I183)
- binding : A129 (≠ C130), N130 (≠ M131), F131 (= F133), C158 (≠ G154), G159 (= G155), S160 (= S156), S184 (= S180), C187 (≠ I183), I212 (≠ N208)
Sites not aligning to the query:
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
29% identity, 93% coverage: 19:454/471 of query aligns to 13:448/457 of 6c6gA
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)
29% identity, 73% coverage: 3:347/471 of query aligns to 66:407/579 of Q9TUI8
- S217 (= S156) mutation to A: Loss of activity.
- S218 (= S157) mutation to A: Lowers activity by at least 98%.
- D237 (= D176) mutation D->E,N: Loss of activity.
- S241 (= S180) mutation to A: Loss of activity.
- C249 (≠ N188) mutation to A: Loss of activity.
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
32% identity, 51% coverage: 7:247/471 of query aligns to 5:243/564 of 6te4A
Sites not aligning to the query:
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
23% identity, 94% coverage: 11:455/471 of query aligns to 10:474/490 of 4yjiA
- active site: K79 (= K81), S158 (= S156), S159 (= S157), G179 (≠ A177), G180 (≠ C178), G181 (= G179), A182 (≠ S180)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ V83), G132 (≠ C130), S158 (= S156), G179 (≠ A177), G180 (≠ C178), A182 (≠ S180)
3ppmA Crystal structure of a noncovalently bound alpha-ketoheterocycle inhibitor (phenhexyl/oxadiazole/pyridine) to a humanized variant of fatty acid amide hydrolase (see paper)
29% identity, 67% coverage: 16:330/471 of query aligns to 54:361/546 of 3ppmA
- active site: K110 (= K81), S185 (= S156), S186 (= S157), T204 (≠ S175), I206 (≠ A177), G207 (≠ C178), G208 (= G179), S209 (= S180), F212 (≠ I183)
- binding fluoride ion: D205 (= D176), I206 (≠ A177), G207 (≠ C178), S209 (= S180)
- binding 7-phenyl-1-[5-(pyridin-2-yl)-1,3,4-oxadiazol-2-yl]heptan-1-one: M159 (≠ C130), F160 (≠ M131), S185 (= S156), T204 (≠ S175), I206 (≠ A177), S209 (= S180), G236 (≠ N208), L246 (≠ S218)
Sites not aligning to the query:
3k84A Crystal structure analysis of a oleyl/oxadiazole/pyridine inhibitor bound to a humanized variant of fatty acid amide hydrolase (see paper)
29% identity, 67% coverage: 16:330/471 of query aligns to 54:361/546 of 3k84A
- active site: K110 (= K81), S185 (= S156), S186 (= S157), T204 (≠ S175), I206 (≠ A177), G207 (≠ C178), G208 (= G179), S209 (= S180), F212 (≠ I183)
- binding (9Z)-1-(5-pyridin-2-yl-1,3,4-oxadiazol-2-yl)octadec-9-en-1-one: M159 (≠ C130), F160 (≠ M131), S161 (≠ A132), S185 (= S156), T204 (≠ S175), I206 (≠ A177), G207 (≠ C178), S209 (= S180), T345 (= T317)
Sites not aligning to the query:
3k83A Crystal structure analysis of a biphenyl/oxazole/carboxypyridine alpha-ketoheterocycle inhibitor bound to a humanized variant of fatty acid amide hydrolase (see paper)
29% identity, 67% coverage: 16:330/471 of query aligns to 54:361/546 of 3k83A
- active site: K110 (= K81), S185 (= S156), S186 (= S157), T204 (≠ S175), I206 (≠ A177), G207 (≠ C178), G208 (= G179), S209 (= S180), F212 (≠ I183)
- binding 6-[2-(3-biphenyl-4-ylpropanoyl)-1,3-oxazol-5-yl]pyridine-2-carboxylic acid: M159 (≠ C130), F160 (≠ M131), S161 (≠ A132), S185 (= S156), D205 (= D176), I206 (≠ A177), G207 (≠ C178), S209 (= S180), G236 (≠ N208), C237 (≠ D209), V238 (≠ R210), L246 (≠ S218)
Sites not aligning to the query:
2wj2A 3d-crystal structure of humanized-rat fatty acid amide hydrolase (faah) conjugated with 7-phenyl-1-(5-(pyridin-2-yl)oxazol-2-yl) heptan- 1-one, an alpha-ketooxazole (see paper)
29% identity, 67% coverage: 16:330/471 of query aligns to 54:361/546 of 2wj2A
- active site: K110 (= K81), S185 (= S156), S186 (= S157), T204 (≠ S175), I206 (≠ A177), G207 (≠ C178), G208 (= G179), S209 (= S180), F212 (≠ I183)
- binding 7-phenyl-1-(5-pyridin-2-yl-1,3-oxazol-2-yl)heptane-1,1-diol: M159 (≠ C130), F160 (≠ M131), S185 (= S156), T204 (≠ S175), D205 (= D176), I206 (≠ A177), G207 (≠ C178), S209 (= S180), C237 (≠ D209), L246 (≠ S218)
Sites not aligning to the query:
Query Sequence
>AO356_18110 FitnessBrowser__pseudo5_N2C3_1:AO356_18110
MFNPDTLTLREMAGLLRRGVLTSVTLLEFYLQRIAERNRQINALIQLAPVEDLRRQAREA
DEMARIGQISGPLHGIPITVKDVLHVRGFKMSRGVGELMGDVSQEDATAVARLRQAGAII
LGISNVPELCMAFETENLIYGRTLNPHDLLRSAGGSSGGEAAAIAAGCSPAGLASDACGS
VRIPAHFNGICGLKLTQGRVPLTGQFPNDRSGLFHLTSAFGVMGRYVDDLALLGPLISGA
DGHDPDTVDVPFAASEPLADLRIALFSASSRTPVSAAVSQVLQQVERCLSPVVTQVSEVA
PPMLDEACDVLWRVFITGADAGRGWRRLFESMNKRSFTPAIAQLLDMSEAVELSVDEVKR
DWIMIDTFRYQLAKFFKQHDLFICPVFPDVAFRHGASLEDRDQYAFVFPFSLSGSPAVVI
RAGVDPSTGMPIGIQIVGPHWQEERLLAVAAFLERELERWSPVAPRPVSTY
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