SitesBLAST
Comparing WP_013841350.1 NCBI__GCF_000215085.1:WP_013841350.1 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)
56% identity, 98% coverage: 3:475/485 of query aligns to 2:468/478 of 3h0mA
- active site: K72 (= K79), S147 (= S154), S148 (= S155), S166 (= S173), T168 (= T175), G169 (= G176), G170 (= G177), S171 (= S178), Q174 (= Q181)
- binding glutamine: M122 (= M129), G123 (= G130), D167 (= D174), T168 (= T175), G169 (= G176), G170 (= G177), S171 (= S178), F199 (= F206), Y302 (= Y309), R351 (= R358), D418 (= D425)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
56% identity, 98% coverage: 3:475/485 of query aligns to 2:468/478 of 3h0lA
- active site: K72 (= K79), S147 (= S154), S148 (= S155), S166 (= S173), T168 (= T175), G169 (= G176), G170 (= G177), S171 (= S178), Q174 (= Q181)
- binding asparagine: G123 (= G130), S147 (= S154), G169 (= G176), G170 (= G177), S171 (= S178), Y302 (= Y309), R351 (= R358), D418 (= D425)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
55% identity, 95% coverage: 15:473/485 of query aligns to 15:473/485 of 2f2aA
- active site: K79 (= K79), S154 (= S154), S155 (= S155), S173 (= S173), T175 (= T175), G176 (= G176), G177 (= G177), S178 (= S178), Q181 (= Q181)
- binding glutamine: G130 (= G130), S154 (= S154), D174 (= D174), T175 (= T175), G176 (= G176), S178 (= S178), F206 (= F206), Y309 (= Y309), Y310 (= Y310), R358 (= R358), D425 (= D425)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
55% identity, 95% coverage: 15:473/485 of query aligns to 15:473/485 of 2dqnA
- active site: K79 (= K79), S154 (= S154), S155 (= S155), S173 (= S173), T175 (= T175), G176 (= G176), G177 (= G177), S178 (= S178), Q181 (= Q181)
- binding asparagine: M129 (= M129), G130 (= G130), T175 (= T175), G176 (= G176), S178 (= S178), Y309 (= Y309), Y310 (= Y310), R358 (= R358), D425 (= D425)
3kfuE Crystal structure of the transamidosome (see paper)
47% identity, 98% coverage: 8:481/485 of query aligns to 2:462/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
36% identity, 86% coverage: 50:466/485 of query aligns to 4:443/450 of 4n0iA
- active site: K38 (= K79), S116 (= S154), S117 (= S155), T135 (≠ S173), T137 (= T175), G138 (= G176), G139 (= G177), S140 (= S178), L143 (≠ Q181)
- binding glutamine: G89 (= G130), T137 (= T175), G138 (= G176), S140 (= S178), Y168 (≠ F206), Y271 (= Y309), Y272 (= Y310), R320 (= R358), D404 (= D425)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
34% identity, 96% coverage: 13:477/485 of query aligns to 22:501/508 of 3a1iA
- active site: K95 (= K79), S170 (= S154), S171 (= S155), G189 (≠ S173), Q191 (≠ T175), G192 (= G176), G193 (= G177), A194 (≠ S178), I197 (≠ Q181)
- binding benzamide: F145 (≠ M129), S146 (≠ G130), G147 (≠ S131), Q191 (≠ T175), G192 (= G176), G193 (= G177), A194 (≠ S178), W327 (≠ Y309)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
33% identity, 97% coverage: 10:481/485 of query aligns to 5:455/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
32% identity, 96% coverage: 10:476/485 of query aligns to 10:479/487 of 1m21A
- active site: K81 (= K79), S160 (= S154), S161 (= S155), T179 (≠ S173), T181 (= T175), D182 (≠ G176), G183 (= G177), S184 (= S178), C187 (≠ Q181)
- binding : A129 (= A128), N130 (≠ M129), F131 (≠ G130), C158 (≠ G152), G159 (= G153), S160 (= S154), S184 (= S178), C187 (≠ Q181), I212 (≠ F206), R318 (≠ Y310), L321 (≠ A313), L365 (≠ M360), F426 (vs. gap)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
27% identity, 99% coverage: 4:482/485 of query aligns to 3:453/457 of 5h6sC
- active site: K77 (= K79), S152 (= S154), S153 (= S155), L173 (≠ T175), G174 (= G176), G175 (= G177), S176 (= S178)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A128), R128 (≠ G130), W129 (≠ S131), S152 (= S154), L173 (≠ T175), G174 (= G176), S176 (= S178), W306 (≠ Y309), F338 (= F343)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 88% coverage: 49:474/485 of query aligns to 175:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A128), T258 (≠ S131), S281 (= S154), G302 (≠ T175), G303 (= G176), S305 (= S178), S472 (≠ M342), I532 (≠ D417), M539 (≠ Q424)
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, 88% coverage: 49:474/485 of query aligns to 175:589/607 of Q7XJJ7
- K205 (= K79) mutation to A: Loss of activity.
- SS 281:282 (= SS 154:155) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 175:178) binding substrate
- S305 (= S178) mutation to A: Loss of activity.
- R307 (= R180) mutation to A: Loss of activity.
- S360 (≠ H233) mutation to A: No effect.
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
27% identity, 98% coverage: 3:477/485 of query aligns to 25:491/507 of Q84DC4
- T31 (≠ H9) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K79) mutation to A: Abolishes activity on mandelamide.
- S180 (= S154) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S155) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G176) 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 (= S178) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q181) 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 (≠ A305) 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 (≠ D372) 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 (vs. gap) 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.
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
28% identity, 88% coverage: 49:474/485 of query aligns to 175:589/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A128), G302 (≠ T175), G303 (= G176), G304 (= G177), A305 (≠ S178), V442 (≠ Y310), I475 (≠ R345), M539 (≠ Q424)
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, 88% coverage: 49:474/485 of query aligns to 175:589/605 of 8ey1D
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
28% identity, 98% coverage: 7:480/485 of query aligns to 7:480/490 of 4yjiA
- active site: K79 (= K79), S158 (= S154), S159 (= S155), G179 (≠ T175), G180 (= G176), G181 (= G177), A182 (≠ S178)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ N81), G132 (≠ A128), S158 (= S154), G179 (≠ T175), G180 (= G176), A182 (≠ S178)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
30% identity, 91% coverage: 24:465/485 of query aligns to 37:453/605 of Q936X2
- K91 (= K79) mutation to A: Loss of activity.
- S165 (= S154) mutation to A: Loss of activity.
- S189 (= S178) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 91% coverage: 24:465/485 of query aligns to 20:430/461 of 4gysB
- active site: K72 (= K79), S146 (= S154), S147 (= S155), T165 (≠ S173), T167 (= T175), A168 (≠ G176), G169 (= G177), S170 (= S178), V173 (≠ Q181)
- binding malonate ion: A120 (= A128), G122 (= G130), S146 (= S154), T167 (= T175), A168 (≠ G176), S170 (= S178), S193 (≠ Y201), G194 (= G202), V195 (≠ L203), R200 (≠ S208), Y297 (= Y309), R305 (= R323)
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: 71:226/485 of query aligns to 28:185/425 of Q9FR37
- K36 (= K79) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S154) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S155) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D174) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S178) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C186) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
34% identity, 51% coverage: 15:263/485 of query aligns to 14:259/482 of 3a2qA
- active site: K69 (= K79), S147 (= S154), S148 (= S155), N166 (≠ S173), A168 (≠ T175), A169 (≠ G176), G170 (= G177), A171 (≠ S178), I174 (≠ Q181)
- binding 6-aminohexanoic acid: G121 (≠ A128), G121 (≠ A128), N122 (≠ M129), S147 (= S154), A168 (≠ T175), A168 (≠ T175), A169 (≠ G176), A171 (≠ S178)
Sites not aligning to the query:
Query Sequence
>WP_013841350.1 NCBI__GCF_000215085.1:WP_013841350.1
MDLCQLTAHELHDKLQKKEISAVEIASSVFKRVDQVEEKVKSYLTITRDQAIEKAEEVDR
KIASGEKIGPLEGIPVAIKDNMCTEGVRTTCASKILYNFVPPYTATVVEKVHRAGMVMAG
KTNMDEFAMGSSTENSGFQLTRNPWDLERVPGGSSGGSASAVAAGEAIISLGSDTGGSIR
QPASFCGVVGLKPTYGAVSRYGLVAFASSLDQIGPFTRDVTDMAQMLNVICGHDPMDSTS
ANVQQSDYTQFLVNDIKGLKIGVPREYMADGIDPGVKERMKEAMGKLTELGAWVEETSMP
HTDYAMPAYYLIATAEASSNLARYDGVRYGLRVEDAEDVVDMFMRSRSQGFGTEVKRRIM
LGTYSLSAGYYDAYYLKALKVRTLIKRDFDRAFEKYDLLLSPASPSTAFKIGEMVNDPIQ
MYLQDICTIPVNLAGIPAVSIPCGLVNNLPVGLQFMGRAFDEGTLLRAAYTLEQNTGWTR
IAPEL
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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