SitesBLAST
Comparing WP_006748066.1 NCBI__GCF_000227685.2:WP_006748066.1 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)
31% identity, 93% coverage: 5:469/500 of query aligns to 6:444/457 of 5h6sC
- active site: K77 (= K76), S152 (= S151), S153 (= S152), L173 (≠ I172), G174 (= G173), G175 (= G174), S176 (= S175)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A125), R128 (≠ T127), W129 (≠ P128), S152 (= S151), L173 (≠ I172), G174 (= G173), S176 (= S175), W306 (≠ Y311), F338 (≠ K350)
3kfuE Crystal structure of the transamidosome (see paper)
34% identity, 94% coverage: 6:474/500 of query aligns to 2:459/468 of 3kfuE
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 93% coverage: 7:469/500 of query aligns to 9:473/485 of 2f2aA
- active site: K79 (= K76), S154 (= S151), S155 (= S152), S173 (= S170), T175 (≠ I172), G176 (= G173), G177 (= G174), S178 (= S175), Q181 (≠ I178)
- binding glutamine: G130 (≠ T127), S154 (= S151), D174 (= D171), T175 (≠ I172), G176 (= G173), S178 (= S175), F206 (≠ H203), Y309 (= Y311), Y310 (≠ G312), R358 (vs. gap), D425 (= D410)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 93% coverage: 7:469/500 of query aligns to 9:473/485 of 2dqnA
- active site: K79 (= K76), S154 (= S151), S155 (= S152), S173 (= S170), T175 (≠ I172), G176 (= G173), G177 (= G174), S178 (= S175), Q181 (≠ I178)
- binding asparagine: M129 (≠ G126), G130 (≠ T127), T175 (≠ I172), G176 (= G173), S178 (= S175), Y309 (= Y311), Y310 (≠ G312), R358 (vs. gap), D425 (= D410)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 92% coverage: 8:465/500 of query aligns to 9:462/478 of 3h0mA
- active site: K72 (= K76), S147 (= S151), S148 (= S152), S166 (= S170), T168 (≠ I172), G169 (= G173), G170 (= G174), S171 (= S175), Q174 (≠ I178)
- binding glutamine: M122 (≠ G126), G123 (≠ T127), D167 (= D171), T168 (≠ I172), G169 (= G173), G170 (= G174), S171 (= S175), F199 (≠ H203), Y302 (= Y311), R351 (vs. gap), D418 (= D410)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 92% coverage: 8:465/500 of query aligns to 9:462/478 of 3h0lA
- active site: K72 (= K76), S147 (= S151), S148 (= S152), S166 (= S170), T168 (≠ I172), G169 (= G173), G170 (= G174), S171 (= S175), Q174 (≠ I178)
- binding asparagine: G123 (≠ T127), S147 (= S151), G169 (= G173), G170 (= G174), S171 (= S175), Y302 (= Y311), R351 (vs. gap), D418 (= D410)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
32% identity, 91% coverage: 8:462/500 of query aligns to 5:441/457 of 6c6gA
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, 90% coverage: 22:471/500 of query aligns to 147:590/607 of Q7XJJ7
- K205 (= K76) mutation to A: Loss of activity.
- SS 281:282 (= SS 151:152) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ IGGS 172:175) binding substrate
- S305 (= S175) mutation to A: Loss of activity.
- R307 (= R177) mutation to A: Loss of activity.
- S360 (≠ P237) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 90% coverage: 22:471/500 of query aligns to 147:590/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A125), T258 (≠ P128), S281 (= S151), G302 (≠ I172), G303 (= G173), S305 (= S175), S472 (≠ Y347), I532 (≠ L414), M539 (≠ V421)
Sites not aligning to the query:
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
28% identity, 90% coverage: 22:471/500 of query aligns to 147:590/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A125), G302 (≠ I172), G303 (= G173), G304 (= G174), A305 (≠ S175), V442 (≠ A310), I475 (≠ K350), M539 (≠ V421)
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
28% identity, 90% coverage: 22:471/500 of query aligns to 147:590/605 of 8ey1D
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
30% identity, 82% coverage: 68:478/500 of query aligns to 87:506/508 of 3a1iA
- active site: K95 (= K76), S170 (= S151), S171 (= S152), G189 (≠ S170), Q191 (≠ I172), G192 (= G173), G193 (= G174), A194 (≠ S175), I197 (= I178)
- binding benzamide: F145 (≠ G126), S146 (≠ T127), G147 (≠ P128), Q191 (≠ I172), G192 (= G173), G193 (= G174), A194 (≠ S175), W327 (= W308)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 94% coverage: 5:474/500 of query aligns to 43:492/507 of Q84DC4
- K100 (= K76) mutation to A: Abolishes activity on mandelamide.
- S180 (= S151) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S152) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G173) 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 (= S175) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I178) 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 (≠ D305) 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 (≠ R358) 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 (≠ V421) 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.
Sites not aligning to the query:
- 31 T→I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
35% identity, 48% coverage: 9:248/500 of query aligns to 11:250/487 of 1m21A
- active site: K81 (= K76), S160 (= S151), S161 (= S152), T179 (≠ S170), T181 (≠ I172), D182 (≠ G173), G183 (= G174), S184 (= S175), C187 (≠ I178)
- binding : A129 (= A125), N130 (≠ G126), F131 (≠ T127), C158 (≠ G149), G159 (= G150), S160 (= S151), S184 (= S175), C187 (≠ I178), I212 (≠ L215)
Sites not aligning to the query:
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)
37% identity, 52% coverage: 8:265/500 of query aligns to 81:331/579 of Q9TUI8
- S217 (= S151) mutation to A: Loss of activity.
- S218 (= S152) mutation to A: Lowers activity by at least 98%.
- D237 (= D171) mutation D->E,N: Loss of activity.
- S241 (= S175) mutation to A: Loss of activity.
- C249 (= C183) mutation to A: Loss of activity.
4j5pA Crystal structure of a covalently bound alpha-ketoheterocycle inhibitor (phenhexyl/oxadiazole/pyridine) to a humanized variant of fatty acid amide hydrolase (see paper)
35% identity, 51% coverage: 10:265/500 of query aligns to 51:299/544 of 4j5pA
- active site: K110 (= K76), S185 (= S151), S186 (= S152), T204 (≠ S170), I206 (= I172), G207 (= G173), G208 (= G174), S209 (= S175), F212 (≠ I178)
- binding (1S)-1-{5-[5-(bromomethyl)pyridin-2-yl]-1,3-oxazol-2-yl}-7-phenylheptan-1-ol: S158 (≠ L124), M159 (≠ A125), F160 (≠ G126), S161 (≠ T127), S185 (= S151), T204 (≠ S170), D205 (= D171), I206 (= I172), G207 (= G173), G208 (= G174), S209 (= S175), C237 (≠ L204)
Sites not aligning to the query:
3pr0A Crystal structure of a covalently bound alpha-ketoheterocycle inhibitor (phenhexyl/oxadiazole/pyridine) to a humanized variant of fatty acid amide hydrolase (see paper)
35% identity, 51% coverage: 10:265/500 of query aligns to 51:299/545 of 3pr0A
- active site: K110 (= K76), S185 (= S151), S186 (= S152), T204 (≠ S170), I206 (= I172), G207 (= G173), G208 (= G174), S209 (= S175), F212 (≠ I178)
- binding 7-phenyl-1-[5-(pyridin-2-yl)-1,3,4-oxadiazol-2-yl]heptane-1,1-diol: M159 (≠ A125), F160 (≠ G126), S161 (≠ T127), S185 (= S151), D205 (= D171), I206 (= I172), G207 (= G173), S209 (= S175)
Sites not aligning to the query:
3lj7A 3d-crystal structure of humanized-rat fatty acid amide hydrolase (faah) conjugated with carbamate inhibitor urb597 (see paper)
35% identity, 51% coverage: 10:265/500 of query aligns to 51:299/545 of 3lj7A
- active site: K110 (= K76), S185 (= S151), S186 (= S152), T204 (≠ S170), I206 (= I172), G207 (= G173), G208 (= G174), S209 (= S175), F212 (≠ I178)
- binding cyclohexane aminocarboxylic acid: F160 (≠ G126), I206 (= I172), G207 (= G173), S209 (= S175)
3k83B Crystal structure analysis of a biphenyl/oxazole/carboxypyridine alpha-ketoheterocycle inhibitor bound to a humanized variant of fatty acid amide hydrolase (see paper)
35% identity, 51% coverage: 10:265/500 of query aligns to 51:299/545 of 3k83B
- active site: K110 (= K76), S185 (= S151), S186 (= S152), T204 (≠ S170), I206 (= I172), G207 (= G173), G208 (= G174), S209 (= S175), F212 (≠ I178)
- binding 1-dodecanol: S114 (≠ A80), S132 (≠ P98), K235 (≠ P202)
- binding 6-[2-(3-biphenyl-4-ylpropanoyl)-1,3-oxazol-5-yl]pyridine-2-carboxylic acid: M159 (≠ A125), F160 (≠ G126), S161 (≠ T127), S185 (= S151), D205 (= D171), I206 (= I172), G207 (= G173), S209 (= S175), G236 (≠ H203), C237 (≠ L204), V238 (≠ P205)
Sites not aligning to the query:
3ppmA Crystal structure of a noncovalently bound alpha-ketoheterocycle inhibitor (phenhexyl/oxadiazole/pyridine) to a humanized variant of fatty acid amide hydrolase (see paper)
36% identity, 51% coverage: 10:265/500 of query aligns to 51:299/546 of 3ppmA
- active site: K110 (= K76), S185 (= S151), S186 (= S152), T204 (≠ S170), I206 (= I172), G207 (= G173), G208 (= G174), S209 (= S175), F212 (≠ I178)
- binding fluoride ion: D205 (= D171), I206 (= I172), G207 (= G173), S209 (= S175)
- binding 7-phenyl-1-[5-(pyridin-2-yl)-1,3,4-oxadiazol-2-yl]heptan-1-one: M159 (≠ A125), F160 (≠ G126), S185 (= S151), T204 (≠ S170), I206 (= I172), S209 (= S175), G236 (≠ H203), L246 (= L215)
Sites not aligning to the query:
Query Sequence
>WP_006748066.1 NCBI__GCF_000227685.2:WP_006748066.1
MLMPTSRQLLAQLHSGQLDFTEVAERYLQHIERYNPTVNAVVTLNRAGALQQAQALQQLR
EQGRLPPLAGLPLTIKDAFATAGLRTTSSHPPLADYVPVRDATLVARLREAGGLLLGKTN
LPRLAGTPHCDSPLFGRTNNPWDPSRTPGGSSAGSAAAVAMGFSCLDLGSDIGGSIRIPA
AFCGVAGFKATENRLPRTGHIPHLPDGERSVRHCLSFGLLARDVDSLQLGFKHLDGPDGE
DTEVPTLPQMSTVLRKRPLRIAWWDDFAGLPMCRRTTDVLARTVEVLKARGVEVERRKPE
GFDFDRAWYAYGIVAGSEVGLGMPGIERRGLTLAGRLLPPSQRLAGYFIKGLRFSLRRYN
DALNLRERLIIELEMFLDHWDAWLCPVAPTVAHPHVPGKGLNPLPAIRFDEHRLPWLEAM
VSMTTPFSLTGSPVVVLPAGIEQGLPVGLQFIGKRWQDERLLSICREIEAITGRYVPPPG
VISQDESRSGENFAVRGTVK
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