SitesBLAST
Comparing WP_013683061.1 NCBI__GCF_000194625.1:WP_013683061.1 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, 92% coverage: 34:461/463 of query aligns to 36:471/478 of 3h0mA
- active site: K72 (= K71), S147 (= S146), S148 (= S147), S166 (= S165), T168 (= T167), G169 (= G168), G170 (= G169), S171 (= S170), Q174 (≠ C173)
- binding glutamine: M122 (= M121), G123 (= G122), D167 (= D166), T168 (= T167), G169 (= G168), G170 (= G169), S171 (= S170), F199 (≠ Y198), Y302 (= Y293), R351 (= R342), D418 (= D408)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
54% identity, 92% coverage: 34:461/463 of query aligns to 36:471/478 of 3h0lA
- active site: K72 (= K71), S147 (= S146), S148 (= S147), S166 (= S165), T168 (= T167), G169 (= G168), G170 (= G169), S171 (= S170), Q174 (≠ C173)
- binding asparagine: G123 (= G122), S147 (= S146), G169 (= G168), G170 (= G169), S171 (= S170), Y302 (= Y293), R351 (= R342), D418 (= D408)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
50% identity, 94% coverage: 20:456/463 of query aligns to 21:473/485 of 2f2aA
- active site: K79 (= K71), S154 (= S146), S155 (= S147), S173 (= S165), T175 (= T167), G176 (= G168), G177 (= G169), S178 (= S170), Q181 (≠ C173)
- binding glutamine: G130 (= G122), S154 (= S146), D174 (= D166), T175 (= T167), G176 (= G168), S178 (= S170), F206 (≠ Y198), Y309 (= Y293), Y310 (= Y294), R358 (= R342), D425 (= D408)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
50% identity, 94% coverage: 20:456/463 of query aligns to 21:473/485 of 2dqnA
- active site: K79 (= K71), S154 (= S146), S155 (= S147), S173 (= S165), T175 (= T167), G176 (= G168), G177 (= G169), S178 (= S170), Q181 (≠ C173)
- binding asparagine: M129 (= M121), G130 (= G122), T175 (= T167), G176 (= G168), S178 (= S170), Y309 (= Y293), Y310 (= Y294), R358 (= R342), D425 (= D408)
3kfuE Crystal structure of the transamidosome (see paper)
47% identity, 95% coverage: 16:457/463 of query aligns to 17:455/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
36% identity, 92% coverage: 25:452/463 of query aligns to 2:446/450 of 4n0iA
- active site: K38 (= K71), S116 (= S146), S117 (= S147), T135 (≠ S165), T137 (= T167), G138 (= G168), G139 (= G169), S140 (= S170), L143 (≠ C173)
- binding glutamine: G89 (= G122), T137 (= T167), G138 (= G168), S140 (= S170), Y168 (= Y198), Y271 (= Y293), Y272 (= Y294), R320 (= R342), D404 (= D408)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
34% identity, 86% coverage: 60:458/463 of query aligns to 84:499/508 of 3a1iA
- active site: K95 (= K71), S170 (= S146), S171 (= S147), G189 (≠ S165), Q191 (≠ T167), G192 (= G168), G193 (= G169), A194 (≠ S170), I197 (≠ C173)
- binding benzamide: F145 (≠ M121), S146 (≠ G122), G147 (≠ T123), Q191 (≠ T167), G192 (= G168), G193 (= G169), A194 (≠ S170), W327 (≠ Y293)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 87% coverage: 54:458/463 of query aligns to 188:590/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A120), T258 (= T123), S281 (= S146), G302 (≠ T167), G303 (= G168), S305 (= S170), S472 (= S347), I532 (≠ D400), M539 (= M407)
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, 87% coverage: 54:458/463 of query aligns to 188:590/607 of Q7XJJ7
- K205 (= K71) mutation to A: Loss of activity.
- SS 281:282 (= SS 146:147) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 167:170) binding substrate
- S305 (= S170) mutation to A: Loss of activity.
- R307 (= R172) mutation to A: Loss of activity.
- S360 (≠ K225) mutation to A: No effect.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
35% identity, 88% coverage: 56:462/463 of query aligns to 59:450/457 of 6c6gA
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
30% identity, 87% coverage: 54:458/463 of query aligns to 188:590/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A120), G302 (≠ T167), G303 (= G168), G304 (= G169), A305 (≠ S170), V442 (≠ I295), I475 (≠ L350), M539 (= M407)
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
30% identity, 87% coverage: 54:458/463 of query aligns to 188:590/605 of 8ey1D
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
31% identity, 98% coverage: 6:460/463 of query aligns to 5:480/487 of 1m21A
- active site: K81 (= K71), S160 (= S146), S161 (= S147), T179 (≠ S165), T181 (= T167), D182 (≠ G168), G183 (= G169), S184 (= S170), C187 (= C173)
- binding : A129 (= A120), N130 (vs. gap), F131 (vs. gap), C158 (≠ G144), G159 (= G145), S160 (= S146), S184 (= S170), C187 (= C173), I212 (≠ Y198), R318 (≠ Y294), L321 (≠ A297), L365 (≠ M344), F426 (≠ D400)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
31% identity, 97% coverage: 13:459/463 of query aligns to 39:490/507 of Q84DC4
- K100 (= K71) mutation to A: Abolishes activity on mandelamide.
- S180 (= S146) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S147) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G168) 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 (= S170) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ C173) 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 (≠ A289) 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 (≠ K357) 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 (≠ D408) 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.
Sites not aligning to the query:
- 31 T→I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
27% identity, 99% coverage: 6:462/463 of query aligns to 4:450/457 of 5h6sC
- active site: K77 (= K71), S152 (= S146), S153 (= S147), L173 (≠ T167), G174 (= G168), G175 (= G169), S176 (= S170)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A120), R128 (≠ G122), W129 (≠ T123), S152 (= S146), L173 (≠ T167), G174 (= G168), S176 (= S170), W306 (≠ Y293), F338 (≠ L345)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
33% identity, 93% coverage: 23:451/463 of query aligns to 37:456/605 of Q936X2
- K91 (= K71) mutation to A: Loss of activity.
- S165 (= S146) mutation to A: Loss of activity.
- S189 (= S170) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
31% identity, 90% coverage: 46:460/463 of query aligns to 46:442/461 of 4gysB
- active site: K72 (= K71), S146 (= S146), S147 (= S147), T165 (≠ S165), T167 (= T167), A168 (≠ G168), G169 (= G169), S170 (= S170), V173 (≠ C173)
- binding malonate ion: A120 (= A120), G122 (= G122), S146 (= S146), T167 (= T167), A168 (≠ G168), S170 (= S170), S193 (≠ Y193), G194 (= G194), V195 (≠ L195), R200 (≠ N200), Y297 (= Y315), R305 (≠ Q319)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
30% identity, 87% coverage: 61:462/463 of query aligns to 59:474/482 of 3a2qA
- active site: K69 (= K71), S147 (= S146), S148 (= S147), N166 (≠ S165), A168 (≠ T167), A169 (≠ G168), G170 (= G169), A171 (≠ S170), I174 (≠ C173)
- binding 6-aminohexanoic acid: G121 (≠ A120), G121 (≠ A120), N122 (≠ M121), S147 (= S146), A168 (≠ T167), A168 (≠ T167), A169 (≠ G168), A171 (≠ S170), C313 (≠ A297)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
28% identity, 94% coverage: 25:459/463 of query aligns to 4:410/412 of 1ocmA
- active site: K62 (= K71), S131 (= S146), S132 (= S147), T152 (= T167), G153 (= G168), G154 (= G169), S155 (= S170)
- binding pyrophosphate 2-: R113 (≠ G122), S131 (= S146), Q151 (≠ D166), T152 (= T167), G153 (= G168), G154 (= G169), S155 (= S170), R158 (≠ C173), P359 (= P401)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
28% identity, 94% coverage: 25:459/463 of query aligns to 4:410/412 of 1o9oA
- active site: K62 (= K71), A131 (≠ S146), S132 (= S147), T150 (≠ S165), T152 (= T167), G153 (= G168), G154 (= G169), S155 (= S170), R158 (≠ C173)
- binding 3-amino-3-oxopropanoic acid: G130 (= G145), T152 (= T167), G153 (= G168), G154 (= G169), S155 (= S170), R158 (≠ C173), P359 (= P401)
Query Sequence
>WP_013683061.1 NCBI__GCF_000194625.1:WP_013683061.1
MSGKGQISIAEWKQRLESEKAYDLVAEMLERIEKSKFNAYITVNGDALKLAEEYDKGKLE
GKLAGIPIAVKDNISTKGMRTTCASKILEDYVPVFDAHVVERIKQEGAIIIGKTNLDEFA
MGTTTETSYFGVVRNPHDENRVAGGSSGGSGAAIAAGETVLSLGSDTGGSIRCPASFCGV
VGLKPTYGLVSRYGLIPYANSLDQIGPMASCVEDLALLLEVISGKDERDSTNAGKPFVFT
PKFRKFRIGVISEMGGNDDVMKCFEEAVEVIKGMGCEVGEVSMPSFKYALAAYYIIAMGE
ASSNLARYDGVRYGYALPQLDSWTRYFSKVRAEGFGSEVKRRIMLGSYALSAGYYGKYYL
KALKVRTLVKNDFQRAFKDYDLLISPTMPSLPFRIGELADPLTMYKMDVNTVPINLAGLP
ALSMPIGFVKGLPVGMQVIGNYFEENAILSFALELEKMMKEVT
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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