SitesBLAST
Comparing WP_011606923.1 NCBI__GCF_000058485.1:WP_011606923.1 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)
50% identity, 90% coverage: 40:504/519 of query aligns to 14:469/478 of 3h0mA
- active site: K72 (= K104), S147 (= S179), S148 (= S180), S166 (≠ T198), T168 (= T200), G169 (= G201), G170 (= G202), S171 (= S203), Q174 (= Q206)
- binding glutamine: M122 (= M154), G123 (= G155), D167 (= D199), T168 (= T200), G169 (= G201), G170 (= G202), S171 (= S203), F199 (= F231), Y302 (= Y335), R351 (= R386), D418 (= D453)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
50% identity, 90% coverage: 40:504/519 of query aligns to 14:469/478 of 3h0lA
- active site: K72 (= K104), S147 (= S179), S148 (= S180), S166 (≠ T198), T168 (= T200), G169 (= G201), G170 (= G202), S171 (= S203), Q174 (= Q206)
- binding asparagine: G123 (= G155), S147 (= S179), G169 (= G201), G170 (= G202), S171 (= S203), Y302 (= Y335), R351 (= R386), D418 (= D453)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
50% identity, 89% coverage: 40:501/519 of query aligns to 15:473/485 of 2f2aA
- active site: K79 (= K104), S154 (= S179), S155 (= S180), S173 (≠ T198), T175 (= T200), G176 (= G201), G177 (= G202), S178 (= S203), Q181 (= Q206)
- binding glutamine: G130 (= G155), S154 (= S179), D174 (= D199), T175 (= T200), G176 (= G201), S178 (= S203), F206 (= F231), Y309 (= Y335), Y310 (= Y336), R358 (= R386), D425 (= D453)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
50% identity, 89% coverage: 40:501/519 of query aligns to 15:473/485 of 2dqnA
- active site: K79 (= K104), S154 (= S179), S155 (= S180), S173 (≠ T198), T175 (= T200), G176 (= G201), G177 (= G202), S178 (= S203), Q181 (= Q206)
- binding asparagine: M129 (= M154), G130 (= G155), T175 (= T200), G176 (= G201), S178 (= S203), Y309 (= Y335), Y310 (= Y336), R358 (= R386), D425 (= D453)
3kfuE Crystal structure of the transamidosome (see paper)
53% identity, 90% coverage: 38:503/519 of query aligns to 7:456/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
36% identity, 76% coverage: 96:491/519 of query aligns to 30:439/450 of 4n0iA
- active site: K38 (= K104), S116 (= S179), S117 (= S180), T135 (= T198), T137 (= T200), G138 (= G201), G139 (= G202), S140 (= S203), L143 (≠ Q206)
- binding glutamine: G89 (= G155), T137 (= T200), G138 (= G201), S140 (= S203), Y168 (≠ F231), Y271 (= Y335), Y272 (= Y336), R320 (= R386), D404 (= D453)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
38% identity, 89% coverage: 40:502/519 of query aligns to 10:449/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
38% identity, 94% coverage: 22:508/519 of query aligns to 2:483/487 of 1m21A
- active site: K81 (= K104), S160 (= S179), S161 (= S180), T179 (= T198), T181 (= T200), D182 (≠ G201), G183 (= G202), S184 (= S203), C187 (≠ Q206)
- binding : A129 (= A153), N130 (≠ M154), F131 (≠ G155), C158 (≠ G177), G159 (= G178), S160 (= S179), S184 (= S203), C187 (≠ Q206), I212 (≠ F231), R318 (≠ Y336), L321 (≠ A339), L365 (≠ I388), F426 (vs. gap)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
38% identity, 79% coverage: 94:502/519 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K104), S170 (= S179), S171 (= S180), G189 (≠ T198), Q191 (≠ T200), G192 (= G201), G193 (= G202), A194 (≠ S203), I197 (≠ Q206)
- binding benzamide: F145 (≠ M154), S146 (≠ G155), G147 (≠ S156), Q191 (≠ T200), G192 (= G201), G193 (= G202), A194 (≠ S203), W327 (≠ Y335)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
33% identity, 92% coverage: 30:504/519 of query aligns to 27:490/507 of Q84DC4
- T31 (≠ A34) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K104) mutation to A: Abolishes activity on mandelamide.
- S180 (= S179) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S180) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G201) 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 (= S203) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q206) 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 (≠ A331) 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 (≠ A401) 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.
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, 84% coverage: 68:502/519 of query aligns to 169:589/607 of Q7XJJ7
- K205 (= K104) mutation to A: Loss of activity.
- SS 281:282 (= SS 179:180) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 200:203) binding substrate
- S305 (= S203) mutation to A: Loss of activity.
- R307 (= R205) mutation to A: Loss of activity.
- S360 (≠ H258) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
31% identity, 84% coverage: 68:502/519 of query aligns to 169:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A153), T258 (≠ S156), S281 (= S179), G302 (≠ T200), G303 (= G201), S305 (= S203), S472 (≠ G378), I532 (≠ A448), M539 (≠ C455)
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
30% identity, 84% coverage: 68:502/519 of query aligns to 169:589/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A153), G302 (≠ T200), G303 (= G201), G304 (= G202), A305 (≠ S203), V442 (≠ Y336), I475 (= I388), M539 (≠ C455)
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, 84% coverage: 68:502/519 of query aligns to 169:589/605 of 8ey1D
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
34% identity, 88% coverage: 54:510/519 of query aligns to 25:447/461 of 4gysB
- active site: K72 (= K104), S146 (= S179), S147 (= S180), T165 (= T198), T167 (= T200), A168 (≠ G201), G169 (= G202), S170 (= S203), V173 (≠ Q206)
- binding malonate ion: A120 (= A153), G122 (= G155), S146 (= S179), T167 (= T200), A168 (≠ G201), S170 (= S203), S193 (≠ Y226), G194 (= G227), V195 (≠ L228), R200 (≠ S233), Y297 (= Y336), R305 (= R349)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
29% identity, 86% coverage: 27:473/519 of query aligns to 1:424/457 of 5h6sC
- active site: K77 (= K104), S152 (= S179), S153 (= S180), L173 (≠ T200), G174 (= G201), G175 (= G202), S176 (= S203)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A153), R128 (≠ G155), W129 (≠ S156), S152 (= S179), L173 (≠ T200), G174 (= G201), S176 (= S203), W306 (≠ Y335), F338 (≠ L389)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
29% identity, 92% coverage: 29:503/519 of query aligns to 3:475/490 of 4yjiA
- active site: K79 (= K104), S158 (= S179), S159 (= S180), G179 (≠ T200), G180 (= G201), G181 (= G202), A182 (≠ S203)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ V106), G132 (≠ A153), S158 (= S179), G179 (≠ T200), G180 (= G201), A182 (≠ S203)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
33% identity, 83% coverage: 74:502/519 of query aligns to 62:462/605 of Q936X2
- K91 (= K104) mutation to A: Loss of activity.
- S165 (= S179) mutation to A: Loss of activity.
- S189 (= S203) mutation to A: Loss of activity.
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
41% identity, 45% coverage: 33:263/519 of query aligns to 7:234/482 of 3a2qA
- active site: K69 (= K104), S147 (= S179), S148 (= S180), N166 (≠ T198), A168 (≠ T200), A169 (≠ G201), G170 (= G202), A171 (≠ S203), I174 (≠ Q206)
- binding 6-aminohexanoic acid: G121 (≠ A153), G121 (≠ A153), N122 (≠ M154), S147 (= S179), A168 (≠ T200), A168 (≠ T200), A169 (≠ G201), A171 (≠ S203)
Sites not aligning to the query:
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
30% identity, 90% coverage: 40:504/519 of query aligns to 11:410/412 of 1o9oA
- active site: K62 (= K104), A131 (≠ S179), S132 (= S180), T150 (= T198), T152 (= T200), G153 (= G201), G154 (= G202), S155 (= S203), R158 (≠ Q206)
- binding 3-amino-3-oxopropanoic acid: G130 (= G178), T152 (= T200), G153 (= G201), G154 (= G202), S155 (= S203), R158 (≠ Q206), P359 (= P446)
Query Sequence
>WP_011606923.1 NCBI__GCF_000058485.1:WP_011606923.1
MTDHPTPSTPTTVTAATAPATPVAAADVVHLTAAATAAAIAAGELSAVEATQAALDRIAK
VDDTIHAFLHVDTEGALAAARSVDERRAAGERLGPLAGVPLALKDVLTARGMPTTCGSRI
LEGWHAPYDATVVGRLRAADVVLLGKVNMDEFAMGSSTENSAYGPTRNPWDTTRIPGGSS
GGSAAAVAAFEAPLAIGTDTGGSIRQPAAVCGLVGVKPTYGGVSRYGLVAFSSSLDQAGP
LARTVTDAALLHAAIAGHDPLDSTSVDVPVPAVVEAAGRRDIRGLRIGVVRELAGEGYDP
GVQAAFAAAVETLTELGAEVVEVSCPHFTYALAAYYLIAPSECSSNLARFDAMRFGLRVG
DDGQAGAEEVMSRTREAGFGPEVKRRIILGTYALSSGYYDAYYGQAQKVRTLISRDFAAA
YERVDVLVSPTTPTPAFPLGSKVDDPVAMYLSDLCTIPSNLAGGPAMSLPAGLADGLPVG
IQIMAPPFADDRLYLVGGALEEALDAQRGHSLLDEAPAL
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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