SitesBLAST
Comparing AO356_25480 FitnessBrowser__pseudo5_N2C3_1:AO356_25480 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)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
36% identity, 96% coverage: 13:478/485 of query aligns to 5:478/482 of 3a2qA
- active site: K69 (= K80), S147 (= S156), S148 (= S157), N166 (= N175), A168 (≠ G177), A169 (≠ G178), G170 (= G179), A171 (≠ S180), I174 (≠ V183)
- binding 6-aminohexanoic acid: G121 (= G130), G121 (= G130), N122 (≠ T131), S147 (= S156), A168 (≠ G177), A168 (≠ G177), A169 (≠ G178), A171 (≠ S180), C313 (≠ I317)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
32% identity, 95% coverage: 13:473/485 of query aligns to 6:478/490 of 4yjiA
- active site: K79 (= K80), S158 (= S156), S159 (= S157), G179 (= G177), G180 (= G178), G181 (= G179), A182 (≠ S180)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L82), G132 (= G130), S158 (= S156), G179 (= G177), G180 (= G178), A182 (≠ S180)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 95% coverage: 16:478/485 of query aligns to 8:476/478 of 3h0mA
- active site: K72 (= K80), S147 (= S156), S148 (= S157), S166 (≠ N175), T168 (≠ G177), G169 (= G178), G170 (= G179), S171 (= S180), Q174 (≠ V183)
- binding glutamine: M122 (≠ T131), G123 (≠ S132), D167 (= D176), T168 (≠ G177), G169 (= G178), G170 (= G179), S171 (= S180), F199 (≠ E208), Y302 (≠ F314), R351 (= R346), D418 (≠ S419)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 95% coverage: 16:478/485 of query aligns to 8:476/478 of 3h0lA
- active site: K72 (= K80), S147 (= S156), S148 (= S157), S166 (≠ N175), T168 (≠ G177), G169 (= G178), G170 (= G179), S171 (= S180), Q174 (≠ V183)
- binding asparagine: G123 (≠ S132), S147 (= S156), G169 (= G178), G170 (= G179), S171 (= S180), Y302 (≠ F314), R351 (= R346), D418 (≠ S419)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
33% identity, 85% coverage: 65:478/485 of query aligns to 80:504/508 of 3a1iA
- active site: K95 (= K80), S170 (= S156), S171 (= S157), G189 (≠ N175), Q191 (≠ G177), G192 (= G178), G193 (= G179), A194 (≠ S180), I197 (≠ V183)
- binding benzamide: F145 (≠ T131), S146 (= S132), G147 (≠ Y133), Q191 (≠ G177), G192 (= G178), G193 (= G179), A194 (≠ S180), W327 (≠ F314)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
28% identity, 94% coverage: 13:468/485 of query aligns to 6:473/485 of 2f2aA
- active site: K79 (= K80), S154 (= S156), S155 (= S157), S173 (≠ N175), T175 (≠ G177), G176 (= G178), G177 (= G179), S178 (= S180), Q181 (≠ V183)
- binding glutamine: G130 (≠ S132), S154 (= S156), D174 (= D176), T175 (≠ G177), G176 (= G178), S178 (= S180), F206 (≠ E208), Y309 (≠ H312), Y310 (≠ V313), R358 (= R346), D425 (≠ Q410)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
28% identity, 94% coverage: 13:468/485 of query aligns to 6:473/485 of 2dqnA
- active site: K79 (= K80), S154 (= S156), S155 (= S157), S173 (≠ N175), T175 (≠ G177), G176 (= G178), G177 (= G179), S178 (= S180), Q181 (≠ V183)
- binding asparagine: M129 (≠ T131), G130 (≠ S132), T175 (≠ G177), G176 (= G178), S178 (= S180), Y309 (≠ H312), Y310 (≠ V313), R358 (= R346), D425 (≠ Q410)
3kfuE Crystal structure of the transamidosome (see paper)
31% identity, 93% coverage: 22:470/485 of query aligns to 9:456/468 of 3kfuE
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
30% identity, 94% coverage: 25:478/485 of query aligns to 18:484/487 of 1m21A
- active site: K81 (= K80), S160 (= S156), S161 (= S157), T179 (≠ N175), T181 (≠ G177), D182 (≠ G178), G183 (= G179), S184 (= S180), C187 (≠ V183)
- binding : A129 (≠ G130), N130 (≠ T131), F131 (vs. gap), C158 (≠ G154), G159 (= G155), S160 (= S156), S184 (= S180), C187 (≠ V183), I212 (≠ E208), R318 (vs. gap), L321 (≠ G305), L365 (≠ E339), F426 (≠ Q410)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 94% coverage: 15:472/485 of query aligns to 7:448/457 of 5h6sC
- active site: K77 (= K80), S152 (= S156), S153 (= S157), L173 (≠ G177), G174 (= G178), G175 (= G179), S176 (= S180)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G130), R128 (≠ S132), W129 (≠ Y133), S152 (= S156), L173 (≠ G177), G174 (= G178), S176 (= S180), W306 (≠ V313), F338 (≠ I347)
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, 61% coverage: 10:306/485 of query aligns to 69:372/579 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 (= C188) mutation to A: Loss of activity.
Q9FR37 Amidase 1; AtAMI1; Translocon at the outer membrane of chloroplasts 64-I; AtTOC64-I; EC 3.5.1.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
49% identity, 19% coverage: 109:198/485 of query aligns to 66:155/425 of Q9FR37
- S113 (= S156) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S157) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D176) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S180) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C188) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 36 active site, Charge relay system; K→A: Loss of catalytic activity.; K→R: Reduces catalytic activity 10-fold.
- 214 S→T: Slightly reduces catalytic activity.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
37% identity, 38% coverage: 18:200/485 of query aligns to 6:194/457 of 6c6gA
Sites not aligning to the query:
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
37% identity, 26% coverage: 71:198/485 of query aligns to 196:323/616 of 6diiH
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)
37% identity, 26% coverage: 71:198/485 of query aligns to 196:323/607 of Q7XJJ7
- K205 (= K80) mutation to A: Loss of activity.
- SS 281:282 (= SS 156:157) mutation to AA: Loss of activity.
- GGGS 302:305 (= GGGS 177:180) binding
- S305 (= S180) mutation to A: Loss of activity.
- R307 (= R182) mutation to A: Loss of activity.
Sites not aligning to the query:
- 360 S→A: No effect.
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)
29% identity, 59% coverage: 22:306/485 of query aligns to 53:339/543 of 2wj1A
- active site: K109 (= K80), S184 (= S156), S185 (= S157), T203 (≠ N175), I205 (≠ G177), G206 (= G178), G207 (= G179), S208 (= S180), F211 (≠ V183)
- binding 7-phenyl-1-(4-pyridin-2-yl-1,3-oxazol-2-yl)heptane-1,1-diol: S157 (≠ F129), M158 (≠ G130), F159 (≠ T131), S184 (= S156), T203 (≠ N175), D204 (= D176), I205 (≠ G177), G206 (= G178), S208 (= S180), C236 (≠ E208)
Sites not aligning to the query:
2vyaA Crystal structure of fatty acid amide hydrolase conjugated with the drug-like inhibitor pf-750 (see paper)
29% identity, 59% coverage: 22:306/485 of query aligns to 54:340/543 of 2vyaA
- active site: K110 (= K80), S185 (= S156), S186 (= S157), T204 (≠ N175), I206 (≠ G177), G207 (= G178), G208 (= G179), S209 (= S180), F212 (≠ V183)
- binding 4-(quinolin-3-ylmethyl)piperidine-1-carboxylic acid: F160 (≠ T131), S161 (= S132), I206 (≠ G177), G207 (= G178), S209 (= S180)
Sites not aligning to the query:
2wapA 3d-crystal structure of humanized-rat fatty acid amide hydrolase (faah) conjugated with the drug-like urea inhibitor pf-3845 (see paper)
29% identity, 59% coverage: 22:306/485 of query aligns to 54:340/541 of 2wapA
- active site: K110 (= K80), S185 (= S156), S186 (= S157), T204 (≠ N175), I206 (≠ G177), G207 (= G178), G208 (= G179), S209 (= S180), F212 (≠ V183)
- binding 4-(3-{[5-(trifluoromethyl)pyridin-2-yl]oxy}benzyl)piperidine-1-carboxylic acid: F160 (≠ T131), S161 (= S132), I206 (≠ G177), G207 (= G178), S209 (= S180), Y303 (≠ P272), L340 (= L306)
Sites not aligning to the query:
6mrgA Faah bound to non covalent inhibitor (see paper)
29% identity, 59% coverage: 22:306/485 of query aligns to 55:341/543 of 6mrgA
Sites not aligning to the query:
- active site: 48, 427, 453, 458, 459
- binding (1R)-2-{[6-(2,3-dihydro-1,4-benzodioxin-6-yl)pyrimidin-4-yl]amino}-1-phenylethan-1-ol: 373, 376, 401, 457, 464, 500
3k7fA Crystal structure analysis of a phenhexyl/oxazole/carboxypyridine alpha-ketoheterocycle inhibitor bound to a humanized variant of fatty acid amide hydrolase' (see paper)
29% identity, 59% coverage: 22:306/485 of query aligns to 55:341/543 of 3k7fA
- active site: K111 (= K80), S186 (= S156), S187 (= S157), T205 (≠ N175), I207 (≠ G177), G208 (= G178), G209 (= G179), S210 (= S180), F213 (≠ V183)
- binding 6-[2-(7-phenylheptanoyl)-1,3-oxazol-5-yl]pyridine-2-carboxylic acid: M160 (≠ G130), F161 (≠ T131), S162 (= S132), S186 (= S156), D206 (= D176), I207 (≠ G177), G208 (= G178), S210 (= S180), G237 (= G207), C238 (≠ E208), V239 (≠ G209)
Sites not aligning to the query:
Query Sequence
>AO356_25480 FitnessBrowser__pseudo5_N2C3_1:AO356_25480
MGMQDIHHLMDSEDATALAEWVRRGEVQPGELLETAIERLERVEPQLNAVAERLYDSARQ
AARTPQVGQGLLAGVPTLIKDLFSPVHGAAMTNGSRALGDFRADFESEVVTRLRRAGCQV
MGTSTSPEFGTSYSTESARFGATRNPWSSEHSAGGSSGGAAALVAARVVPFAHGNDGGGS
LRVPASCCGVFGFKPSRGLMPSGPIVGEGWAGMGTPHAITLSVRDSAALLDATAGMDLGA
PYAAPVQALPYTMAVQADPKPLRIALVEQLGPWPTAPQSLQAVGEAARLCEALGHRVEPV
NLPVGLLEFLDHVFTIIGASSRHYVDLLGQMRGFAVQAEELEVRTRIILRDKGNVSGAQY
AAAVEWIHALGRQLAVFMQDYDVILTPVLTREPVLIGELDLQDVCMSLDQLIERYHSYSP
FTALFNASGQPAMSVPLSWSANGLPMGAHFAGRFGEENTLLALAAQLERAQPWRGRVPAV
NACRR
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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