SitesBLAST
Comparing WP_012408531.1 NCBI__GCF_000020025.1:WP_012408531.1 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)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
32% identity, 93% coverage: 22:451/462 of query aligns to 20:473/485 of 2f2aA
- active site: K79 (= K81), S154 (= S164), S155 (= S165), S173 (≠ T183), T175 (= T185), G176 (= G186), G177 (= G187), S178 (= S188), Q181 (≠ V191)
- binding glutamine: G130 (≠ D140), S154 (= S164), D174 (= D184), T175 (= T185), G176 (= G186), S178 (= S188), F206 (≠ R216), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ D343), D425 (≠ Q402)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
32% identity, 93% coverage: 22:451/462 of query aligns to 20:473/485 of 2dqnA
- active site: K79 (= K81), S154 (= S164), S155 (= S165), S173 (≠ T183), T175 (= T185), G176 (= G186), G177 (= G187), S178 (= S188), Q181 (≠ V191)
- binding asparagine: M129 (≠ A139), G130 (≠ D140), T175 (= T185), G176 (= G186), S178 (= S188), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ D343), D425 (≠ Q402)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
31% identity, 96% coverage: 10:454/462 of query aligns to 8:479/487 of 1m21A
- active site: K81 (= K81), S160 (= S164), S161 (= S165), T179 (= T183), T181 (= T185), D182 (≠ G186), G183 (= G187), S184 (= S188), C187 (≠ V191)
- binding : A129 (= A138), N130 (vs. gap), F131 (vs. gap), C158 (≠ G162), G159 (= G163), S160 (= S164), S184 (= S188), C187 (≠ V191), I212 (≠ R216), R318 (≠ S314), L321 (≠ A317), L365 (vs. gap), F426 (≠ A393)
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, 94% coverage: 18:451/462 of query aligns to 139:588/607 of Q7XJJ7
- K205 (= K81) mutation to A: Loss of activity.
- SS 281:282 (= SS 164:165) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 185:188) binding substrate
- S305 (= S188) mutation to A: Loss of activity.
- R307 (= R190) mutation to A: Loss of activity.
- S360 (≠ P243) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 94% coverage: 18:451/462 of query aligns to 139:588/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A138), T258 (≠ L141), S281 (= S164), G302 (≠ T185), G303 (= G186), S305 (= S188), S472 (≠ D343), I532 (vs. gap), M539 (≠ Q402)
Sites not aligning to the query:
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
29% identity, 94% coverage: 18:451/462 of query aligns to 139:588/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A138), G302 (≠ T185), G303 (= G186), G304 (= G187), A305 (≠ S188), V442 (vs. gap), I475 (≠ K346), M539 (≠ Q402)
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, 94% coverage: 18:451/462 of query aligns to 139:588/605 of 8ey1D
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 96% coverage: 8:451/462 of query aligns to 5:466/478 of 3h0mA
- active site: K72 (= K81), S147 (= S164), S148 (= S165), S166 (≠ T183), T168 (= T185), G169 (= G186), G170 (= G187), S171 (= S188), Q174 (≠ V191)
- binding glutamine: M122 (≠ A139), G123 (≠ D140), D167 (= D184), T168 (= T185), G169 (= G186), G170 (= G187), S171 (= S188), F199 (≠ R216), Y302 (vs. gap), R351 (≠ D343), D418 (≠ Q402)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 96% coverage: 8:451/462 of query aligns to 5:466/478 of 3h0lA
- active site: K72 (= K81), S147 (= S164), S148 (= S165), S166 (≠ T183), T168 (= T185), G169 (= G186), G170 (= G187), S171 (= S188), Q174 (≠ V191)
- binding asparagine: G123 (≠ D140), S147 (= S164), G169 (= G186), G170 (= G187), S171 (= S188), Y302 (vs. gap), R351 (≠ D343), D418 (≠ Q402)
3kfuE Crystal structure of the transamidosome (see paper)
32% identity, 95% coverage: 16:455/462 of query aligns to 8:458/468 of 3kfuE
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
31% identity, 95% coverage: 15:451/462 of query aligns to 8:448/457 of 6c6gA
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
31% identity, 95% coverage: 9:447/462 of query aligns to 29:483/507 of Q84DC4
- T31 (≠ A11) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K81) mutation to A: Abolishes activity on mandelamide.
- S180 (= S164) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S165) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G186) 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 (= S188) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ V191) 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 (≠ F308) 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 (vs. gap) 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 (≠ M405) 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, 96% coverage: 9:453/462 of query aligns to 3:409/412 of 1o9oA
- active site: K62 (= K81), A131 (≠ S164), S132 (= S165), T150 (= T183), T152 (= T185), G153 (= G186), G154 (= G187), S155 (= S188), R158 (≠ V191)
- binding 3-amino-3-oxopropanoic acid: G130 (= G163), T152 (= T185), G153 (= G186), G154 (= G187), S155 (= S188), R158 (≠ V191), P359 (≠ Q402)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
27% identity, 96% coverage: 9:453/462 of query aligns to 3:409/412 of 1ocmA
- active site: K62 (= K81), S131 (= S164), S132 (= S165), T152 (= T185), G153 (= G186), G154 (= G187), S155 (= S188)
- binding pyrophosphate 2-: R113 (vs. gap), S131 (= S164), Q151 (≠ D184), T152 (= T185), G153 (= G186), G154 (= G187), S155 (= S188), R158 (≠ V191), P359 (≠ Q402)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
28% identity, 82% coverage: 71:451/462 of query aligns to 85:497/508 of 3a1iA
- active site: K95 (= K81), S170 (= S164), S171 (= S165), G189 (≠ T183), Q191 (≠ T185), G192 (= G186), G193 (= G187), A194 (≠ S188), I197 (≠ V191)
- binding benzamide: F145 (≠ A139), S146 (≠ D140), G147 (≠ L141), Q191 (≠ T185), G192 (= G186), G193 (= G187), A194 (≠ S188), W327 (vs. gap)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 86% coverage: 45:443/462 of query aligns to 55:453/605 of Q936X2
- K91 (= K81) mutation to A: Loss of activity.
- S165 (= S164) mutation to A: Loss of activity.
- S189 (= S188) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
31% identity, 80% coverage: 73:440/462 of query aligns to 64:427/461 of 4gysB
- active site: K72 (= K81), S146 (= S164), S147 (= S165), T165 (= T183), T167 (= T185), A168 (≠ G186), G169 (= G187), S170 (= S188), V173 (= V191)
- binding malonate ion: A120 (= A138), G122 (≠ D140), S146 (= S164), T167 (= T185), A168 (≠ G186), S170 (= S188), S193 (≠ K211), G194 (= G212), V195 (≠ I213), R200 (= R218), Y297 (= Y313), R305 (≠ F321)
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)
26% identity, 82% coverage: 73:450/462 of query aligns to 28:421/425 of Q9FR37
- K36 (= K81) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S164) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S165) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D184) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S188) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ S196) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ T246) mutation to T: Slightly reduces catalytic activity.
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
27% identity, 83% coverage: 62:444/462 of query aligns to 19:443/450 of 4n0iA
- active site: K38 (= K81), S116 (= S164), S117 (= S165), T135 (= T183), T137 (= T185), G138 (= G186), G139 (= G187), S140 (= S188), L143 (≠ V191)
- binding glutamine: G89 (≠ D140), T137 (= T185), G138 (= G186), S140 (= S188), Y168 (≠ R216), Y271 (vs. gap), Y272 (vs. gap), R320 (≠ D343), D404 (≠ Q402)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
29% identity, 98% coverage: 4:456/462 of query aligns to 2:473/482 of 3a2qA
- active site: K69 (≠ H74), S147 (= S164), S148 (= S165), N166 (≠ T183), A168 (≠ T185), A169 (≠ G186), G170 (= G187), A171 (≠ S188), I174 (≠ V191)
- binding 6-aminohexanoic acid: G121 (≠ A138), G121 (≠ A138), N122 (≠ A139), S147 (= S164), A168 (≠ T185), A168 (≠ T185), A169 (≠ G186), A171 (≠ S188), C313 (≠ A317)
Query Sequence
>WP_012408531.1 NCBI__GCF_000020025.1:WP_012408531.1
MQADFIPKTIAQASQQMQSGLLTSSMLVKHYLASIKKLNYTLNAFITVLEQQALEAAIQK
DFERINGQNCGLLHGIPIVVKDNIDTAEVKTTVGSQLFCELTNQGLRDRIPLSDSVIVQK
LKAAGAVILGKTNLSEFAADLSGNNLFYGNTCNFWNHNHSSGGSSSGSATAIAARLCLAG
IGTDTGGSIRVPASWSGVVGLRPTYRLLSNKGIFPRTRSFDTVGFLTNCVEDIAILLDAV
LFPISTNLKQLYPLPTNINGLKLGILNNYTFRGIEPEIAKAISNAISILKKLGAEIITIN
SPFLIEGFDEVTYSTIALYEFHQVLQAEYATNPNKFGAKVQSDLSKGVKISHHSYKKAKQ
KREECFLQRQKLFQEVDILLTPTTPIVAPLIDADAKIYRLNQRFMLPFSFLGLPAISLPC
GQSTQGLPIGLQLVGNSYTEALILRVAFALQVATTFSEDSLL
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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