SitesBLAST
Comparing WP_057687391.1 NCBI__GCF_001431535.1:WP_057687391.1 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)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
32% identity, 93% coverage: 24:482/492 of query aligns to 5:448/457 of 5h6sC
- active site: K77 (= K97), S152 (= S172), S153 (= S173), L173 (≠ I193), G174 (= G194), G175 (= G195), S176 (= S196)
- binding 4-oxidanylbenzohydrazide: C126 (≠ S146), R128 (≠ S148), W129 (= W149), S152 (= S172), L173 (≠ I193), G174 (= G194), S176 (= S196), W306 (= W330), F338 (≠ W368)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 93% coverage: 22:481/492 of query aligns to 3:469/478 of 3h0mA
- active site: K72 (= K97), S147 (= S172), S148 (= S173), S166 (≠ N191), T168 (≠ I193), G169 (= G194), G170 (= G195), S171 (= S196), Q174 (≠ H199)
- binding glutamine: M122 (≠ F147), G123 (≠ S148), D167 (= D192), T168 (≠ I193), G169 (= G194), G170 (= G195), S171 (= S196), F199 (≠ P222), Y302 (≠ W330), R351 (vs. gap), D418 (= D419)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 93% coverage: 22:481/492 of query aligns to 3:469/478 of 3h0lA
- active site: K72 (= K97), S147 (= S172), S148 (= S173), S166 (≠ N191), T168 (≠ I193), G169 (= G194), G170 (= G195), S171 (= S196), Q174 (≠ H199)
- binding asparagine: G123 (≠ S148), S147 (= S172), G169 (= G194), G170 (= G195), S171 (= S196), Y302 (≠ W330), R351 (vs. gap), D418 (= D419)
3kfuE Crystal structure of the transamidosome (see paper)
32% identity, 92% coverage: 26:480/492 of query aligns to 2:456/468 of 3kfuE
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
35% identity, 79% coverage: 89:478/492 of query aligns to 87:497/508 of 3a1iA
- active site: K95 (= K97), S170 (= S172), S171 (= S173), G189 (≠ N191), Q191 (≠ I193), G192 (= G194), G193 (= G195), A194 (≠ S196), I197 (≠ H199)
- binding benzamide: F145 (= F147), S146 (= S148), G147 (≠ W149), Q191 (≠ I193), G192 (= G194), G193 (= G195), A194 (≠ S196), W327 (= W330)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 91% coverage: 31:479/492 of query aligns to 13:474/485 of 2f2aA
- active site: K79 (= K97), S154 (= S172), S155 (= S173), S173 (≠ N191), T175 (≠ I193), G176 (= G194), G177 (= G195), S178 (= S196), Q181 (≠ H199)
- binding glutamine: G130 (≠ S148), S154 (= S172), D174 (= D192), T175 (≠ I193), G176 (= G194), S178 (= S196), F206 (≠ P222), Y309 (≠ W330), Y310 (≠ W331), R358 (≠ E366), D425 (≠ P432)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 91% coverage: 31:479/492 of query aligns to 13:474/485 of 2dqnA
- active site: K79 (= K97), S154 (= S172), S155 (= S173), S173 (≠ N191), T175 (≠ I193), G176 (= G194), G177 (= G195), S178 (= S196), Q181 (≠ H199)
- binding asparagine: M129 (≠ F147), G130 (≠ S148), T175 (≠ I193), G176 (= G194), S178 (= S196), Y309 (≠ W330), Y310 (≠ W331), R358 (≠ E366), D425 (≠ P432)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 85% coverage: 65:483/492 of query aligns to 173:593/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ S146), T258 (≠ W149), S281 (= S172), G302 (≠ I193), G303 (= G194), S305 (= S196), S472 (≠ E366), I532 (≠ A418), M539 (≠ A425)
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)
30% identity, 85% coverage: 65:483/492 of query aligns to 173:593/607 of Q7XJJ7
- K205 (= K97) mutation to A: Loss of activity.
- SS 281:282 (= SS 172:173) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ IGGS 193:196) binding
- S305 (= S196) mutation to A: Loss of activity.
- R307 (= R198) mutation to A: Loss of activity.
- S360 (≠ F257) mutation to A: No effect.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
31% identity, 93% coverage: 19:478/492 of query aligns to 1:476/487 of 1m21A
- active site: K81 (= K97), S160 (= S172), S161 (= S173), T179 (≠ N191), T181 (≠ I193), D182 (≠ G194), G183 (= G195), S184 (= S196), C187 (≠ H199)
- binding : A129 (≠ S146), N130 (vs. gap), F131 (vs. gap), C158 (≠ G170), G159 (= G171), S160 (= S172), S184 (= S196), C187 (≠ H199), I212 (≠ G218), R318 (= R328), L321 (≠ V334), L365 (vs. gap), F426 (≠ K412)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
28% identity, 93% coverage: 25:482/492 of query aligns to 7:477/490 of 4yjiA
- active site: K79 (= K97), S158 (= S172), S159 (= S173), G179 (≠ I193), G180 (= G194), G181 (= G195), A182 (≠ S196)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ N99), G132 (≠ S146), S158 (= S172), G179 (≠ I193), G180 (= G194), A182 (≠ S196)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 93% coverage: 22:481/492 of query aligns to 26:490/507 of Q84DC4
- T31 (= T27) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K97) mutation to A: Abolishes activity on mandelamide.
- S180 (= S172) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S173) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G194) 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 (= S196) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ H199) 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 (≠ W327) 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 (≠ N379) 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 (= I427) 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.
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
31% identity, 93% coverage: 25:482/492 of query aligns to 6:472/482 of 3a2qA
- active site: K69 (= K97), S147 (= S172), S148 (= S173), N166 (= N191), A168 (≠ I193), A169 (≠ G194), G170 (= G195), A171 (≠ S196), I174 (≠ H199)
- binding 6-aminohexanoic acid: G121 (≠ S146), G121 (≠ S146), N122 (≠ F147), S147 (= S172), A168 (≠ I193), A168 (≠ I193), A169 (≠ G194), A171 (≠ S196), C313 (≠ E336)
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)
33% identity, 58% coverage: 33:315/492 of query aligns to 86:360/579 of Q9TUI8
- S217 (= S172) mutation to A: Loss of activity.
- S218 (= S173) mutation to A: Lowers activity by at least 98%.
- D237 (= D192) mutation D->E,N: Loss of activity.
- S241 (= S196) mutation to A: Loss of activity.
- C249 (= C204) mutation to A: Loss of activity.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
29% identity, 90% coverage: 36:478/492 of query aligns to 13:448/457 of 6c6gA
3ppmA Crystal structure of a noncovalently bound alpha-ketoheterocycle inhibitor (phenhexyl/oxadiazole/pyridine) to a humanized variant of fatty acid amide hydrolase (see paper)
32% identity, 58% coverage: 33:315/492 of query aligns to 54:328/546 of 3ppmA
- active site: K110 (= K97), S185 (= S172), S186 (= S173), T204 (≠ N191), I206 (= I193), G207 (= G194), G208 (= G195), S209 (= S196), F212 (≠ H199)
- binding fluoride ion: D205 (= D192), I206 (= I193), G207 (= G194), S209 (= S196)
- binding 7-phenyl-1-[5-(pyridin-2-yl)-1,3,4-oxadiazol-2-yl]heptan-1-one: M159 (≠ S146), F160 (= F147), S185 (= S172), T204 (≠ N191), I206 (= I193), S209 (= S196), G236 (≠ S221), L246 (= L231)
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)
32% identity, 58% coverage: 33:315/492 of query aligns to 54:328/546 of 3k84A
- active site: K110 (= K97), S185 (= S172), S186 (= S173), T204 (≠ N191), I206 (= I193), G207 (= G194), G208 (= G195), S209 (= S196), F212 (≠ H199)
- binding (9Z)-1-(5-pyridin-2-yl-1,3,4-oxadiazol-2-yl)octadec-9-en-1-one: M159 (≠ S146), F160 (= F147), S161 (= S148), S185 (= S172), T204 (≠ N191), I206 (= I193), G207 (= G194), S209 (= S196)
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)
32% identity, 58% coverage: 33:315/492 of query aligns to 54:328/546 of 3k83A
- active site: K110 (= K97), S185 (= S172), S186 (= S173), T204 (≠ N191), I206 (= I193), G207 (= G194), G208 (= G195), S209 (= S196), F212 (≠ H199)
- binding 6-[2-(3-biphenyl-4-ylpropanoyl)-1,3-oxazol-5-yl]pyridine-2-carboxylic acid: M159 (≠ S146), F160 (= F147), S161 (= S148), S185 (= S172), D205 (= D192), I206 (= I193), G207 (= G194), S209 (= S196), G236 (≠ S221), C237 (≠ P222), V238 (≠ A223), L246 (= L231)
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)
32% identity, 58% coverage: 33:315/492 of query aligns to 54:328/546 of 2wj2A
- active site: K110 (= K97), S185 (= S172), S186 (= S173), T204 (≠ N191), I206 (= I193), G207 (= G194), G208 (= G195), S209 (= S196), F212 (≠ H199)
- binding 7-phenyl-1-(5-pyridin-2-yl-1,3-oxazol-2-yl)heptane-1,1-diol: M159 (≠ S146), F160 (= F147), S185 (= S172), T204 (≠ N191), D205 (= D192), I206 (= I193), G207 (= G194), S209 (= S196), C237 (≠ P222), L246 (= L231)
Sites not aligning to the query:
4j5pA Crystal structure of a covalently bound alpha-ketoheterocycle inhibitor (phenhexyl/oxadiazole/pyridine) to a humanized variant of fatty acid amide hydrolase (see paper)
32% identity, 58% coverage: 33:315/492 of query aligns to 54:328/544 of 4j5pA
- active site: K110 (= K97), S185 (= S172), S186 (= S173), T204 (≠ N191), I206 (= I193), G207 (= G194), G208 (= G195), S209 (= S196), F212 (≠ H199)
- binding (1S)-1-{5-[5-(bromomethyl)pyridin-2-yl]-1,3-oxazol-2-yl}-7-phenylheptan-1-ol: S158 (≠ F145), M159 (≠ S146), F160 (= F147), S161 (= S148), S185 (= S172), T204 (≠ N191), D205 (= D192), I206 (= I193), G207 (= G194), G208 (= G195), S209 (= S196), C237 (≠ P222)
Sites not aligning to the query:
Query Sequence
>WP_057687391.1 NCBI__GCF_001431535.1:WP_057687391.1
MVPAAAQVPPLSLRSPGSLPAWALSATDASALLRRGELSAVELTRSCLGRIAVVNPVVNA
LNFVDEAAAIRAAEQADAALARGAVSAPLHGIPVAIKDNTDVRGQPMTNGIVALKDNIAS
ADAPQVARLRAAGAIVLGRSNTPCFSFSWDARNDLHGTTWNPWSRAHTPGGSSGGAACAV
ATGMVPLAHGNDIGGSIRHPAYCCGVAGLRPTPGRVPGLFSPAKGDEALGLQLMLVDGPI
ARGVADLRLMLESMTGFDPRVPGSLPLPLPFPASPLLPGTRIGVLREDDVKPRTPTVAAA
LERAVVALQQAGFTVEEVRLPELAEAWRLWWLLVMEETRALLPSIERDGDAPIKAWIGFN
YDVASEMWGRQPSLTDYINGYARRARLIASLQQKLRRYPVILMPVASEEPFKQGQHYADL
ASARAAIASGWPLMAIPVLGFPALAVPTGCVDGLPTGVQLMGRRFHERDVLQVGAALEAA
MPVLTPMDPLRT
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