SitesBLAST
Comparing WP_013721238.1 NCBI__GCF_000204645.1:WP_013721238.1 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)
48% identity, 99% coverage: 5:493/496 of query aligns to 1:476/478 of 3h0mA
- active site: K72 (= K80), S147 (= S163), S148 (= S164), S166 (≠ T182), T168 (= T184), G169 (= G185), G170 (= G186), S171 (= S187), Q174 (= Q190)
- binding glutamine: M122 (= M130), G123 (= G131), D167 (= D183), T168 (= T184), G169 (= G185), G170 (= G186), S171 (= S187), F199 (= F215), Y302 (= Y319), R351 (= R368), D418 (= D434)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
48% identity, 99% coverage: 5:493/496 of query aligns to 1:476/478 of 3h0lA
- active site: K72 (= K80), S147 (= S163), S148 (= S164), S166 (≠ T182), T168 (= T184), G169 (= G185), G170 (= G186), S171 (= S187), Q174 (= Q190)
- binding asparagine: G123 (= G131), S147 (= S163), G169 (= G185), G170 (= G186), S171 (= S187), Y302 (= Y319), R351 (= R368), D418 (= D434)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
47% identity, 90% coverage: 42:489/496 of query aligns to 40:479/485 of 2f2aA
- active site: K79 (= K80), S154 (= S163), S155 (= S164), S173 (≠ T182), T175 (= T184), G176 (= G185), G177 (= G186), S178 (= S187), Q181 (= Q190)
- binding glutamine: G130 (= G131), S154 (= S163), D174 (= D183), T175 (= T184), G176 (= G185), S178 (= S187), F206 (= F215), Y309 (= Y319), Y310 (= Y320), R358 (= R368), D425 (= D434)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
47% identity, 90% coverage: 42:489/496 of query aligns to 40:479/485 of 2dqnA
- active site: K79 (= K80), S154 (= S163), S155 (= S164), S173 (≠ T182), T175 (= T184), G176 (= G185), G177 (= G186), S178 (= S187), Q181 (= Q190)
- binding asparagine: M129 (= M130), G130 (= G131), T175 (= T184), G176 (= G185), S178 (= S187), Y309 (= Y319), Y310 (= Y320), R358 (= R368), D425 (= D434)
3kfuE Crystal structure of the transamidosome (see paper)
50% identity, 96% coverage: 21:495/496 of query aligns to 12:467/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
36% identity, 85% coverage: 62:482/496 of query aligns to 20:449/450 of 4n0iA
- active site: K38 (= K80), S116 (= S163), S117 (= S164), T135 (= T182), T137 (= T184), G138 (= G185), G139 (= G186), S140 (= S187), L143 (≠ Q190)
- binding glutamine: G89 (= G131), T137 (= T184), G138 (= G185), S140 (= S187), Y168 (≠ F215), Y271 (= Y319), Y272 (= Y320), R320 (= R368), D404 (= D434)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
34% identity, 96% coverage: 11:486/496 of query aligns to 8:479/487 of 1m21A
- active site: K81 (= K80), S160 (= S163), S161 (= S164), T179 (= T182), T181 (= T184), D182 (≠ G185), G183 (= G186), S184 (= S187), C187 (≠ Q190)
- binding : A129 (= A129), N130 (vs. gap), F131 (≠ M130), C158 (≠ G161), G159 (= G162), S160 (= S163), S184 (= S187), C187 (≠ Q190), I212 (≠ F215), R318 (≠ Y320), L321 (≠ A323), L365 (≠ V375), F426 (≠ Y431)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
34% identity, 96% coverage: 9:483/496 of query aligns to 1:448/457 of 6c6gA
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
31% identity, 96% coverage: 6:483/496 of query aligns to 25:487/507 of Q84DC4
- T31 (≠ A12) 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 (= S163) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S164) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G185) 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 (= S187) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q190) 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 (= S315) 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 (≠ D382) 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.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 89% coverage: 46:484/496 of query aligns to 170:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A129), T258 (≠ G132), S281 (= S163), G302 (≠ T184), G303 (= G185), S305 (= S187), S472 (≠ T373), I532 (≠ D426), M539 (≠ A433)
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, 89% coverage: 46:484/496 of query aligns to 170:589/607 of Q7XJJ7
- K205 (= K80) mutation to A: Loss of activity.
- SS 281:282 (= SS 163:164) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 184:187) binding substrate
- S305 (= S187) mutation to A: Loss of activity.
- R307 (= R189) mutation to A: Loss of activity.
- S360 (≠ D243) 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, 89% coverage: 46:484/496 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 (≠ T184), G303 (= G185), G304 (= G186), A305 (≠ S187), V442 (≠ Y320), I475 (≠ L376), M539 (≠ A433)
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, 89% coverage: 46:484/496 of query aligns to 170:589/605 of 8ey1D
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 83% coverage: 72:484/496 of query aligns to 87:498/508 of 3a1iA
- active site: K95 (= K80), S170 (= S163), S171 (= S164), G189 (≠ T182), Q191 (≠ T184), G192 (= G185), G193 (= G186), A194 (≠ S187), I197 (≠ Q190)
- binding benzamide: F145 (≠ M130), S146 (≠ G131), G147 (= G132), Q191 (≠ T184), G192 (= G185), G193 (= G186), A194 (≠ S187), W327 (≠ Y319)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
33% identity, 94% coverage: 19:484/496 of query aligns to 14:439/461 of 4gysB
- active site: K72 (= K80), S146 (= S163), S147 (= S164), T165 (= T182), T167 (= T184), A168 (≠ G185), G169 (= G186), S170 (= S187), V173 (≠ Q190)
- binding malonate ion: A120 (= A129), G122 (= G131), S146 (= S163), T167 (= T184), A168 (≠ G185), S170 (= S187), S193 (≠ Y210), G194 (= G211), V195 (≠ M212), R200 (vs. gap), Y297 (≠ F334), R305 (= R342)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 94% coverage: 13:478/496 of query aligns to 9:439/457 of 5h6sC
- active site: K77 (= K80), S152 (= S163), S153 (= S164), L173 (≠ T184), G174 (= G185), G175 (= G186), S176 (= S187)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A129), R128 (≠ N134), W129 (≠ E135), S152 (= S163), L173 (≠ T184), G174 (= G185), S176 (= S187), W306 (≠ Y319), F338 (≠ Y353)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
29% identity, 86% coverage: 60:485/496 of query aligns to 42:409/412 of 1o9oA
- active site: K62 (= K80), A131 (≠ S163), S132 (= S164), T150 (= T182), T152 (= T184), G153 (= G185), G154 (= G186), S155 (= S187), R158 (≠ Q190)
- binding 3-amino-3-oxopropanoic acid: G130 (= G162), T152 (= T184), G153 (= G185), G154 (= G186), S155 (= S187), R158 (≠ Q190), P359 (= P427)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
29% identity, 86% coverage: 60:485/496 of query aligns to 42:409/412 of 1ocmA
- active site: K62 (= K80), S131 (= S163), S132 (= S164), T152 (= T184), G153 (= G185), G154 (= G186), S155 (= S187)
- binding pyrophosphate 2-: R113 (≠ D145), S131 (= S163), Q151 (≠ D183), T152 (= T184), G153 (= G185), G154 (= G186), S155 (= S187), R158 (≠ Q190), P359 (= P427)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
31% identity, 82% coverage: 67:472/496 of query aligns to 78:450/605 of Q936X2
- K91 (= K80) mutation to A: Loss of activity.
- S165 (= S163) mutation to A: Loss of activity.
- S189 (= S187) 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)
46% identity, 27% coverage: 106:240/496 of query aligns to 64:187/425 of Q9FR37
- S113 (= S163) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S164) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D183) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S187) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C195) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 36 active site, Charge relay system; K→A: Loss of catalytic activity.; K→R: Reduces catalytic activity 10-fold.
- 214 S→T: Slightly reduces catalytic activity.
Query Sequence
>WP_013721238.1 NCBI__GCF_000204645.1:WP_013721238.1
MSSTVLHDMGVAQLAAALRGGQVSAVEAAQHFLARAKSHQHLGAYVALNEDATLAQARAQ
DASIAAGTAAPLAGVPIAHKDIFVTRDFPTTAASRMLAGYRSPFDATVVARLAEAGCVTL
GKLNCDEFAMGGTNENSAVAPVGFDAPRPVRNPWDGARVPGGSSGGSAAAVAARLAPAVT
GTDTGGSIRQPASFCGVTGIKPTYGRASRYGMIAFASSLDQAGPMARSAEDCALLLSAMC
GPDPDRDSTSLDRPAEDFGRALGDSLEGLRIGVPAEFFGEGLAADVHAAVDAALKEYEKL
GARLVPITLPRTDLSVPVYYILAPAEASSNLSRFDGVRYGYRAKDYADLLDMYKKTRAQG
FGDEVKRRIMIGTYVLSEGYYDAYYLQAQKLRRMIADDFQAAFKECDLIAGPVAPTTAWR
LGSQNDPVANYLADIYTLPASLAGLPGMSVPAGFGEGGLPVGLQLIGNYFQEARLLNAAH
RLQQATDFHLRAPEGI
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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