SitesBLAST
Comparing WP_013705468.1 NCBI__GCF_000195295.1:WP_013705468.1 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)
54% identity, 99% coverage: 5:487/487 of query aligns to 3:477/478 of 3h0mA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (= S174), T168 (= T176), G169 (= G177), G170 (= G178), S171 (= S179), Q174 (= Q182)
- binding glutamine: M122 (= M130), G123 (= G131), D167 (= D175), T168 (= T176), G169 (= G177), G170 (= G178), S171 (= S179), F199 (= F207), Y302 (= Y310), R351 (= R359), D418 (= D426)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
54% identity, 99% coverage: 5:487/487 of query aligns to 3:477/478 of 3h0lA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (= S174), T168 (= T176), G169 (= G177), G170 (= G178), S171 (= S179), Q174 (= Q182)
- binding asparagine: G123 (= G131), S147 (= S155), G169 (= G177), G170 (= G178), S171 (= S179), Y302 (= Y310), R351 (= R359), D418 (= D426)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
54% identity, 99% coverage: 1:481/487 of query aligns to 1:479/485 of 2f2aA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (= S174), T175 (= T176), G176 (= G177), G177 (= G178), S178 (= S179), Q181 (= Q182)
- binding glutamine: G130 (= G131), S154 (= S155), D174 (= D175), T175 (= T176), G176 (= G177), S178 (= S179), F206 (= F207), Y309 (= Y310), Y310 (= Y311), R358 (= R359), D425 (= D426)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
54% identity, 99% coverage: 1:481/487 of query aligns to 1:479/485 of 2dqnA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (= S174), T175 (= T176), G176 (= G177), G177 (= G178), S178 (= S179), Q181 (= Q182)
- binding asparagine: M129 (= M130), G130 (= G131), T175 (= T176), G176 (= G177), S178 (= S179), Y309 (= Y310), Y310 (= Y311), R358 (= R359), D425 (= D426)
3kfuE Crystal structure of the transamidosome (see paper)
50% identity, 96% coverage: 19:487/487 of query aligns to 11:466/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
37% identity, 86% coverage: 49:468/487 of query aligns to 4:443/450 of 4n0iA
- active site: K38 (= K80), S116 (= S155), S117 (= S156), T135 (≠ S174), T137 (= T176), G138 (= G177), G139 (= G178), S140 (= S179), L143 (≠ Q182)
- binding glutamine: G89 (= G131), T137 (= T176), G138 (= G177), S140 (= S179), Y168 (≠ F207), Y271 (= Y310), Y272 (= Y311), R320 (= R359), D404 (= D426)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
36% identity, 83% coverage: 72:476/487 of query aligns to 87:498/508 of 3a1iA
- active site: K95 (= K80), S170 (= S155), S171 (= S156), G189 (≠ S174), Q191 (≠ T176), G192 (= G177), G193 (= G178), A194 (≠ S179), I197 (≠ Q182)
- binding benzamide: F145 (≠ M130), S146 (≠ G131), G147 (≠ S132), Q191 (≠ T176), G192 (= G177), G193 (= G178), A194 (≠ S179), W327 (≠ Y310)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
34% identity, 98% coverage: 10:486/487 of query aligns to 8:485/487 of 1m21A
- active site: K81 (= K80), S160 (= S155), S161 (= S156), T179 (≠ S174), T181 (= T176), D182 (≠ G177), G183 (= G178), S184 (= S179), C187 (≠ Q182)
- binding : A129 (= A129), N130 (≠ M130), F131 (≠ G131), C158 (≠ G153), G159 (= G154), S160 (= S155), S184 (= S179), C187 (≠ Q182), I212 (≠ F207), R318 (≠ Y311), L321 (≠ A314), L365 (≠ M361), F426 (≠ Y423)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
31% identity, 89% coverage: 46:476/487 of query aligns to 170:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A129), T258 (≠ S132), S281 (= S155), G302 (≠ T176), G303 (= G177), S305 (= S179), S472 (vs. gap), I532 (≠ D417), M539 (≠ L424)
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)
31% identity, 89% coverage: 46:476/487 of query aligns to 170:589/607 of Q7XJJ7
- K205 (= K80) mutation to A: Loss of activity.
- SS 281:282 (= SS 155:156) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 176:179) binding substrate
- S305 (= S179) mutation to A: Loss of activity.
- R307 (= R181) mutation to A: Loss of activity.
- S360 (≠ Y234) mutation to A: No effect.
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
31% identity, 89% coverage: 46:476/487 of query aligns to 170:589/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A129), G302 (≠ T176), G303 (= G177), G304 (= G178), A305 (≠ S179), V442 (≠ Y311), I475 (vs. gap), M539 (≠ L424)
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
31% identity, 89% coverage: 46:476/487 of query aligns to 170:589/605 of 8ey1D
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
33% identity, 95% coverage: 20:482/487 of query aligns to 13:455/457 of 6c6gA
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
29% identity, 96% coverage: 8:476/487 of query aligns to 5:445/457 of 5h6sC
- active site: K77 (= K80), S152 (= S155), S153 (= S156), L173 (≠ T176), G174 (= G177), G175 (= G178), S176 (= S179)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A129), R128 (≠ G131), W129 (≠ S132), S152 (= S155), L173 (≠ T176), G174 (= G177), S176 (= S179), W306 (≠ Y310), F338 (≠ Y344)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
31% identity, 97% coverage: 5:475/487 of query aligns to 26:487/507 of Q84DC4
- T31 (≠ Q11) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K80) mutation to A: Abolishes activity on mandelamide.
- S180 (= S155) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S156) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G177) 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 (= S179) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q182) 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 (≠ A306) 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 (≠ D373) 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 (= I430) 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.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
33% identity, 95% coverage: 7:467/487 of query aligns to 2:430/461 of 4gysB
- active site: K72 (= K80), S146 (= S155), S147 (= S156), T165 (≠ S174), T167 (= T176), A168 (≠ G177), G169 (= G178), S170 (= S179), V173 (≠ Q182)
- binding malonate ion: A120 (= A129), G122 (= G131), S146 (= S155), T167 (= T176), A168 (≠ G177), S170 (= S179), S193 (≠ F202), G194 (= G203), V195 (≠ L204), R200 (≠ S209), Y297 (= Y310), R305 (= R324)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
29% identity, 98% coverage: 3:480/487 of query aligns to 3:478/490 of 4yjiA
- active site: K79 (= K80), S158 (= S155), S159 (= S156), G179 (≠ T176), G180 (= G177), G181 (= G178), A182 (≠ S179)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L82), G132 (≠ A129), S158 (= S155), G179 (≠ T176), G180 (= G177), A182 (≠ S179)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
38% identity, 53% coverage: 5:264/487 of query aligns to 4:259/482 of 3a2qA
- active site: K69 (= K80), S147 (= S155), S148 (= S156), N166 (≠ S174), A168 (≠ T176), A169 (≠ G177), G170 (= G178), A171 (≠ S179), I174 (≠ Q182)
- binding 6-aminohexanoic acid: G121 (≠ A129), G121 (≠ A129), N122 (≠ M130), S147 (= S155), A168 (≠ T176), A168 (≠ T176), A169 (≠ G177), A171 (≠ S179)
Sites not aligning to the query:
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
30% identity, 87% coverage: 51:474/487 of query aligns to 62:460/605 of Q936X2
- K91 (= K80) mutation to A: Loss of activity.
- S165 (= S155) mutation to A: Loss of activity.
- S189 (= S179) 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)
43% identity, 32% coverage: 72:229/487 of query aligns to 28:192/425 of Q9FR37
- K36 (= K80) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S155) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S156) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D175) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S179) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C187) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
Query Sequence
>WP_013705468.1 NCBI__GCF_000195295.1:WP_013705468.1
MTVSWQSLTIQQLHPLMLRGEISPVELTQGFLDRISQFDDTLHCYITVEAQQALAQAQEA
TRRLASGRATPLTGIPLAIKDLIVTQGLRTTCASRSLENYVPPYDATVMHRLREAGAVIL
GKVNMDEFAMGSSTENSAFGATRNPWRLDCIPGGSSGGSAAAVAADLCLASLGSDTGGSI
RQPASHCGVVGLKPTYGRVSRFGLVAFASSLDQIGPITKDVADCALLLQFLAGYDPKDST
SAPVPTPDYSQALNQDIKGLKIGVPQEYFIAGMEEEVEQAVRAALETFKGLGAELVEVSL
PHTQYAVAVYYLIATAEASSNLARYDGVKYGFRAAEANDLMDMYCATRAQGLGAEVRRRI
MLGTYALSAGYYDAYYKKASQVRTLIRRDFDEVFQTCQIVATPVAPTTAFRLGEKMDDPL
TMYLSDIFTISANLAGIPGISVPCGLNSGGLPIGLQLLARHFDESTLLKAAHAFEQASTF
HLLKPPI
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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