SitesBLAST
Comparing WP_011952462.1 NCBI__GCF_000016765.1:WP_011952462.1 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)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
30% identity, 96% coverage: 12:460/469 of query aligns to 8:476/478 of 3h0mA
- active site: K72 (= K82), S147 (= S157), S148 (= S158), S166 (≠ T176), T168 (≠ G178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (≠ C184)
- binding glutamine: M122 (≠ H132), G123 (≠ K133), D167 (= D177), T168 (≠ G178), G169 (= G179), G170 (= G180), S171 (= S181), F199 (≠ G209), Y302 (= Y308), R351 (≠ C338), D418 (≠ G396)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
30% identity, 96% coverage: 12:460/469 of query aligns to 8:476/478 of 3h0lA
- active site: K72 (= K82), S147 (= S157), S148 (= S158), S166 (≠ T176), T168 (≠ G178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (≠ C184)
- binding asparagine: G123 (≠ K133), S147 (= S157), G169 (= G179), G170 (= G180), S171 (= S181), Y302 (= Y308), R351 (≠ C338), D418 (≠ G396)
3kfuE Crystal structure of the transamidosome (see paper)
35% identity, 95% coverage: 18:462/469 of query aligns to 9:466/468 of 3kfuE
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
30% identity, 96% coverage: 6:455/469 of query aligns to 3:478/485 of 2f2aA
- active site: K79 (= K82), S154 (= S157), S155 (= S158), S173 (≠ T176), T175 (≠ G178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (≠ C184)
- binding glutamine: G130 (≠ K133), S154 (= S157), D174 (= D177), T175 (≠ G178), G176 (= G179), S178 (= S181), F206 (≠ G209), Y309 (= Y308), Y310 (≠ A309), R358 (≠ C338), D425 (≠ A401)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
30% identity, 96% coverage: 6:455/469 of query aligns to 3:478/485 of 2dqnA
- active site: K79 (= K82), S154 (= S157), S155 (= S158), S173 (≠ T176), T175 (≠ G178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (≠ C184)
- binding asparagine: M129 (≠ H132), G130 (≠ K133), T175 (≠ G178), G176 (= G179), S178 (= S181), Y309 (= Y308), Y310 (≠ A309), R358 (≠ C338), D425 (≠ A401)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
31% identity, 95% coverage: 5:450/469 of query aligns to 1:444/457 of 5h6sC
- active site: K77 (= K82), S152 (= S157), S153 (= S158), L173 (≠ G178), G174 (= G179), G175 (= G180), S176 (= S181)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A131), R128 (≠ K133), W129 (≠ V134), S152 (= S157), L173 (≠ G178), G174 (= G179), S176 (= S181), W306 (≠ Y308), F338 (≠ R343)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
30% identity, 94% coverage: 11:450/469 of query aligns to 8:473/490 of 4yjiA
- active site: K79 (= K82), S158 (= S157), S159 (= S158), G179 (= G178), G180 (= G179), G181 (= G180), A182 (≠ S181)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ N84), G132 (≠ A131), S158 (= S157), G179 (= G178), G180 (= G179), A182 (≠ S181)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 87% coverage: 47:452/469 of query aligns to 174:590/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A131), T258 (≠ V134), S281 (= S157), G302 (= G178), G303 (= G179), S305 (= S181), S472 (≠ C338), I532 (≠ P398), M539 (≠ H405)
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)
29% identity, 87% coverage: 47:452/469 of query aligns to 174:590/607 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 (= GGGS 178:181) binding substrate
- S305 (= S181) mutation to A: Loss of activity.
- R307 (= R183) mutation to A: Loss of activity.
- S360 (≠ P236) mutation to A: No effect.
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
29% identity, 87% coverage: 47:452/469 of query aligns to 174:590/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A131), G302 (= G178), G303 (= G179), G304 (= G180), A305 (≠ S181), V442 (≠ A309), I475 (≠ Q341), M539 (≠ H405)
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
29% identity, 87% coverage: 47:452/469 of query aligns to 174:590/605 of 8ey1D
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
33% identity, 96% coverage: 11:460/469 of query aligns to 7:478/482 of 3a2qA
- active site: K69 (= K82), S147 (= S157), S148 (= S158), N166 (≠ T176), A168 (≠ G178), A169 (≠ G179), G170 (= G180), A171 (≠ S181), I174 (≠ C184)
- binding 6-aminohexanoic acid: G121 (≠ A131), G121 (≠ A131), N122 (≠ H132), S147 (= S157), A168 (≠ G178), A168 (≠ G178), A169 (≠ G179), A171 (≠ S181), C313 (≠ A312)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
33% identity, 92% coverage: 18:450/469 of query aligns to 15:476/487 of 1m21A
- active site: K81 (= K82), S160 (= S157), S161 (= S158), T179 (= T176), T181 (≠ G178), D182 (≠ G179), G183 (= G180), S184 (= S181), C187 (= C184)
- binding : A129 (= A131), N130 (≠ H132), F131 (vs. gap), C158 (≠ G155), G159 (= G156), S160 (= S157), S184 (= S181), C187 (= C184), I212 (≠ D208), R318 (vs. gap), L321 (≠ F297), L365 (≠ C338), F426 (≠ Y393)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
33% identity, 92% coverage: 18:450/469 of query aligns to 10:448/457 of 6c6gA
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
33% identity, 78% coverage: 73:439/469 of query aligns to 63:427/461 of 4gysB
- active site: K72 (= K82), S146 (= S157), S147 (= S158), T165 (= T176), T167 (≠ G178), A168 (≠ G179), G169 (= G180), S170 (= S181), V173 (≠ C184)
- binding malonate ion: A120 (= A131), G122 (≠ K133), S146 (= S157), T167 (≠ G178), A168 (≠ G179), S170 (= S181), S193 (≠ E204), G194 (≠ A205), V195 (≠ M206), R200 (≠ G211), Y297 (= Y308), R305 (= R316)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 82% coverage: 72:454/469 of query aligns to 85:501/508 of 3a1iA
- active site: K95 (= K82), S170 (= S157), S171 (= S158), G189 (≠ T176), Q191 (≠ G178), G192 (= G179), G193 (= G180), A194 (≠ S181), I197 (≠ C184)
- binding benzamide: F145 (≠ H132), S146 (≠ K133), G147 (≠ V134), Q191 (≠ G178), G192 (= G179), G193 (= G180), A194 (≠ S181), W327 (≠ Y308)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
31% identity, 78% coverage: 73:439/469 of query aligns to 82:450/605 of Q936X2
- K91 (= K82) mutation to A: Loss of activity.
- S165 (= S157) mutation to A: Loss of activity.
- S189 (= S181) mutation to A: Loss of activity.
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 96% coverage: 4:454/469 of query aligns to 23:491/507 of Q84DC4
- T31 (= T12) 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 (= G179) 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 (≠ C184) 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 (≠ L304) 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 (≠ A347) 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 (≠ L404) 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.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
27% identity, 94% coverage: 14:453/469 of query aligns to 7:410/412 of 1o9oA
- active site: K62 (= K82), A131 (≠ S157), S132 (= S158), T150 (= T176), T152 (≠ G178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ C184)
- binding 3-amino-3-oxopropanoic acid: G130 (= G156), T152 (≠ G178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ C184), P359 (= P394)
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, 48% coverage: 1:224/469 of query aligns to 69:288/579 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 (≠ N189) mutation to A: Loss of activity.
Query Sequence
>WP_011952462.1 NCBI__GCF_000016765.1:WP_011952462.1
MTSEEVCFLPATRLARLIAARKLSPVDAVEAVLDRAQQLNPSLNAFAHLAADQARAAARR
AQAAVMAGDRLGPLHGVPITVKDNVAVAGLPLGHGSIAVEPVIPDQDAIAVARARAAGAV
IIGKTTLPEFAHKVLTVNNAQGVTHNPWNLAHSPGGSSGGGGAALAAGIGPLAIATDGGG
SIRCPASWNGVVGLKPTLGRIPGEAMPDGFGNFAYIGPMARHTDDLALLLSVMEGPSPAD
PFALRPPPADAPVTVQGMRIGWLPHVGEHRTDAVTAAITERAVGALANAGAEVETLFAPC
FEGLYAVYAVLASTARAARYGHILDTAGDRMTPTLRDCIVQGRGWSAVQWLAAHDRRTAL
FRAVQALFERFDILATPTTTTTAPRLDSIDPGYPGGYPAWAVALHPFNLSGHPALSTPAG
FTDDGLPVGLQLVGPWFGERRLLVASAALEAMLGLAEHRPPVAPVPAHI
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