SitesBLAST
Comparing WP_011766088.1 NCBI__GCF_000061505.1:WP_011766088.1 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)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
30% identity, 96% coverage: 9:484/497 of query aligns to 5:444/457 of 5h6sC
- active site: K77 (= K82), S152 (= S157), S153 (= S158), L173 (≠ I178), G174 (≠ A179), G175 (= G180), S176 (= S181)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A131), R128 (≠ A133), W129 (≠ P134), S152 (= S157), L173 (≠ I178), G174 (≠ A179), S176 (= S181), W306 (≠ F326), F338 (≠ A362)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 96% coverage: 18:496/497 of query aligns to 14:478/478 of 3h0mA
- active site: K72 (= K82), S147 (= S157), S148 (= S158), S166 (= S176), T168 (≠ I178), G169 (≠ A179), G170 (= G180), S171 (= S181), Q174 (≠ I184)
- binding glutamine: M122 (≠ G132), G123 (≠ A133), D167 (= D177), T168 (≠ I178), G169 (≠ A179), G170 (= G180), S171 (= S181), F199 (≠ H209), Y302 (≠ D316), R351 (≠ D356), D418 (≠ E426)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 96% coverage: 18:496/497 of query aligns to 14:478/478 of 3h0lA
- active site: K72 (= K82), S147 (= S157), S148 (= S158), S166 (= S176), T168 (≠ I178), G169 (≠ A179), G170 (= G180), S171 (= S181), Q174 (≠ I184)
- binding asparagine: G123 (≠ A133), S147 (= S157), G169 (≠ A179), G170 (= G180), S171 (= S181), Y302 (≠ D316), R351 (≠ D356), D418 (≠ E426)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 90% coverage: 36:484/497 of query aligns to 33:473/485 of 2f2aA
- active site: K79 (= K82), S154 (= S157), S155 (= S158), S173 (= S176), T175 (≠ I178), G176 (≠ A179), G177 (= G180), S178 (= S181), Q181 (≠ I184)
- binding glutamine: G130 (≠ A133), S154 (= S157), D174 (= D177), T175 (≠ I178), G176 (≠ A179), S178 (= S181), F206 (≠ H209), Y309 (≠ F326), Y310 (≠ G327), R358 (= R372), D425 (≠ I436)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 90% coverage: 36:484/497 of query aligns to 33:473/485 of 2dqnA
- active site: K79 (= K82), S154 (= S157), S155 (= S158), S173 (= S176), T175 (≠ I178), G176 (≠ A179), G177 (= G180), S178 (= S181), Q181 (≠ I184)
- binding asparagine: M129 (≠ G132), G130 (≠ A133), T175 (≠ I178), G176 (≠ A179), S178 (= S181), Y309 (≠ F326), Y310 (≠ G327), R358 (= R372), D425 (≠ I436)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
30% identity, 96% coverage: 9:485/497 of query aligns to 1:449/457 of 6c6gA
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 87% coverage: 46:477/497 of query aligns to 169:581/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A131), T258 (≠ P134), S281 (= S157), G302 (≠ I178), G303 (≠ A179), S305 (= S181), S472 (≠ L345), I532 (≠ L429), M539 (≠ I436)
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)
28% identity, 87% coverage: 46:477/497 of query aligns to 169:581/607 of Q7XJJ7
- K205 (= K82) mutation to A: Loss of activity.
- SS 281:282 (= SS 157:158) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ IAGS 178:181) binding substrate
- S305 (= S181) mutation to A: Loss of activity.
- R307 (= R183) mutation to A: Loss of activity.
- S360 (≠ P247) mutation to A: No effect.
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
27% identity, 87% coverage: 46:477/497 of query aligns to 169:581/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A131), G302 (≠ I178), G303 (≠ A179), G304 (= G180), A305 (≠ S181), V442 (≠ A325), I475 (≠ A348), M539 (≠ I436)
Sites not aligning to the query:
8ey1D Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with n-(3-oxododecanoyl)-l-homoserine lactone
27% identity, 87% coverage: 46:477/497 of query aligns to 169:581/605 of 8ey1D
3kfuE Crystal structure of the transamidosome (see paper)
31% identity, 94% coverage: 21:486/497 of query aligns to 12:456/468 of 3kfuE
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
28% identity, 85% coverage: 74:493/497 of query aligns to 87:506/508 of 3a1iA
- active site: K95 (= K82), S170 (= S157), S171 (= S158), G189 (≠ S176), Q191 (≠ I178), G192 (≠ A179), G193 (= G180), A194 (≠ S181), I197 (= I184)
- binding benzamide: F145 (≠ G132), S146 (≠ A133), G147 (≠ P134), Q191 (≠ I178), G192 (≠ A179), G193 (= G180), A194 (≠ S181), W327 (vs. gap)
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, 69% coverage: 13:355/497 of query aligns to 81:428/579 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 (= C189) mutation to A: Loss of activity.
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
30% identity, 95% coverage: 18:487/497 of query aligns to 14:471/482 of 3a2qA
- active site: K69 (= K82), S147 (= S157), S148 (= S158), N166 (≠ S176), A168 (≠ I178), A169 (= A179), G170 (= G180), A171 (≠ S181), I174 (= I184)
- binding 6-aminohexanoic acid: G121 (≠ A131), G121 (≠ A131), N122 (≠ G132), S147 (= S157), A168 (≠ I178), A168 (≠ I178), A169 (= A179), A171 (≠ S181), C313 (≠ G330)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
37% identity, 47% coverage: 18:251/497 of query aligns to 15:243/487 of 1m21A
- active site: K81 (= K82), S160 (= S157), S161 (= S158), T179 (≠ S176), T181 (≠ I178), D182 (≠ A179), G183 (= G180), S184 (= S181), C187 (≠ I184)
- binding : A129 (= A131), N130 (≠ G132), F131 (vs. gap), C158 (≠ G155), G159 (= G156), S160 (= S157), S184 (= S181), C187 (≠ I184), I212 (vs. gap)
Sites not aligning to the query:
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
26% identity, 97% coverage: 8:488/497 of query aligns to 27:491/507 of Q84DC4
- T31 (≠ A12) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K82) 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 (≠ A179) 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 (≠ W323) 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 (≠ R373) 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 (= I436) 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.
3ppmA Crystal structure of a noncovalently bound alpha-ketoheterocycle inhibitor (phenhexyl/oxadiazole/pyridine) to a humanized variant of fatty acid amide hydrolase (see paper)
31% identity, 61% coverage: 15:317/497 of query aligns to 51:336/546 of 3ppmA
- active site: K110 (= K82), S185 (= S157), S186 (= S158), T204 (≠ S176), I206 (= I178), G207 (≠ A179), G208 (= G180), S209 (= S181), F212 (≠ I184)
- binding fluoride ion: D205 (= D177), I206 (= I178), G207 (≠ A179), S209 (= S181)
- binding 7-phenyl-1-[5-(pyridin-2-yl)-1,3,4-oxadiazol-2-yl]heptan-1-one: M159 (≠ A131), F160 (≠ G132), S185 (= S157), T204 (≠ S176), I206 (= I178), S209 (= S181), G236 (= G215), L246 (= L225)
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)
31% identity, 61% coverage: 15:317/497 of query aligns to 51:336/546 of 3k84A
- active site: K110 (= K82), S185 (= S157), S186 (= S158), T204 (≠ S176), I206 (= I178), G207 (≠ A179), G208 (= G180), S209 (= S181), F212 (≠ I184)
- binding (9Z)-1-(5-pyridin-2-yl-1,3,4-oxadiazol-2-yl)octadec-9-en-1-one: M159 (≠ A131), F160 (≠ G132), S161 (≠ A133), S185 (= S157), T204 (≠ S176), I206 (= I178), G207 (≠ A179), S209 (= S181)
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)
31% identity, 61% coverage: 15:317/497 of query aligns to 51:336/546 of 3k83A
- active site: K110 (= K82), S185 (= S157), S186 (= S158), T204 (≠ S176), I206 (= I178), G207 (≠ A179), G208 (= G180), S209 (= S181), F212 (≠ I184)
- binding 6-[2-(3-biphenyl-4-ylpropanoyl)-1,3-oxazol-5-yl]pyridine-2-carboxylic acid: M159 (≠ A131), F160 (≠ G132), S161 (≠ A133), S185 (= S157), D205 (= D177), I206 (= I178), G207 (≠ A179), S209 (= S181), G236 (= G215), C237 (≠ G216), V238 (≠ P217), L246 (= L225)
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)
31% identity, 61% coverage: 15:317/497 of query aligns to 51:336/546 of 2wj2A
- active site: K110 (= K82), S185 (= S157), S186 (= S158), T204 (≠ S176), I206 (= I178), G207 (≠ A179), G208 (= G180), S209 (= S181), F212 (≠ I184)
- binding 7-phenyl-1-(5-pyridin-2-yl-1,3-oxazol-2-yl)heptane-1,1-diol: M159 (≠ A131), F160 (≠ G132), S185 (= S157), T204 (≠ S176), D205 (= D177), I206 (= I178), G207 (≠ A179), S209 (= S181), C237 (≠ G216), L246 (= L225)
Sites not aligning to the query:
Query Sequence
>WP_011766088.1 NCBI__GCF_000061505.1:WP_011766088.1
MSAPDFQHLTAAQAVRDLRAGRYSAEQLVLACQARIDRFNPTLNALVTLNREGALAAARG
ADRRLAQGGLAPALLGVPVSIKDAFATRDMLTTASHRPLAAYRPGADATVVARWREAGAV
LMGKSNLPELAGAPHCWSPLFGLTRNPWNPALTPGGSSGGAAVAVAAGFSLLDIGSDIAG
SIRIPAAYCGIAGLKATENRIPRTGHIPHLPPEFGGPGRSVWHMLAFGVLARSVEDLQLG
YGLLAGPDGVDCTVPPFLPEPPSLPTTARAVAPMRIALWDDFAGMPLCPRIRRGLQNMAG
KLRASGHEVVRCAPADFDVGAAWHAFGLIGGAEIGLGMPGWQRRLFLALRPLLPRDHVIT
RAVAAGMRFDLRRYNQALNQREGLIRSLERFVGEWDAVICPVAPTGPYPGEPMPPTRKPP
RLNVGEATLPYLEATIAMTAPFSLTGSPVLSLPVGIEDGLPVGVQVIGKRWQEHALLETG
RRLENALGGFVPPPLAA
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