SitesBLAST
Comparing WP_048066007.1 NCBI__GCF_000007345.1:WP_048066007.1 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)
53% identity, 98% coverage: 6:471/475 of query aligns to 6:476/478 of 3h0mA
- active site: K72 (= K69), S147 (= S144), S148 (= S145), S166 (= S163), T168 (= T165), G169 (= G166), G170 (= G167), S171 (= S168), Q174 (≠ C171)
- binding glutamine: M122 (= M119), G123 (= G120), D167 (= D164), T168 (= T165), G169 (= G166), G170 (= G167), S171 (= S168), F199 (≠ Y196), Y302 (= Y298), R351 (= R346), D418 (= D413)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
53% identity, 98% coverage: 6:471/475 of query aligns to 6:476/478 of 3h0lA
- active site: K72 (= K69), S147 (= S144), S148 (= S145), S166 (= S163), T168 (= T165), G169 (= G166), G170 (= G167), S171 (= S168), Q174 (≠ C171)
- binding asparagine: G123 (= G120), S147 (= S144), G169 (= G166), G170 (= G167), S171 (= S168), Y302 (= Y298), R351 (= R346), D418 (= D413)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
54% identity, 89% coverage: 43:467/475 of query aligns to 49:479/485 of 2f2aA
- active site: K79 (= K69), S154 (= S144), S155 (= S145), S173 (= S163), T175 (= T165), G176 (= G166), G177 (= G167), S178 (= S168), Q181 (≠ C171)
- binding glutamine: G130 (= G120), S154 (= S144), D174 (= D164), T175 (= T165), G176 (= G166), S178 (= S168), F206 (≠ Y196), Y309 (= Y298), Y310 (= Y299), R358 (= R346), D425 (= D413)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
54% identity, 89% coverage: 43:467/475 of query aligns to 49:479/485 of 2dqnA
- active site: K79 (= K69), S154 (= S144), S155 (= S145), S173 (= S163), T175 (= T165), G176 (= G166), G177 (= G167), S178 (= S168), Q181 (≠ C171)
- binding asparagine: M129 (= M119), G130 (= G120), T175 (= T165), G176 (= G166), S178 (= S168), Y309 (= Y298), Y310 (= Y299), R358 (= R346), D425 (= D413)
3kfuE Crystal structure of the transamidosome (see paper)
50% identity, 96% coverage: 16:471/475 of query aligns to 13:465/468 of 3kfuE
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
39% identity, 85% coverage: 58:462/475 of query aligns to 84:498/508 of 3a1iA
- active site: K95 (= K69), S170 (= S144), S171 (= S145), G189 (≠ S163), Q191 (≠ T165), G192 (= G166), G193 (= G167), A194 (≠ S168), I197 (≠ C171)
- binding benzamide: F145 (≠ M119), S146 (≠ G120), G147 (≠ S121), Q191 (≠ T165), G192 (= G166), G193 (= G167), A194 (≠ S168), W327 (≠ Y298)
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
39% identity, 83% coverage: 61:454/475 of query aligns to 30:443/450 of 4n0iA
- active site: K38 (= K69), S116 (= S144), S117 (= S145), T135 (≠ S163), T137 (= T165), G138 (= G166), G139 (= G167), S140 (= S168), L143 (≠ C171)
- binding glutamine: G89 (= G120), T137 (= T165), G138 (= G166), S140 (= S168), Y168 (= Y196), Y271 (= Y298), Y272 (= Y299), R320 (= R346), D404 (= D413)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
33% identity, 98% coverage: 9:473/475 of query aligns to 12:486/487 of 1m21A
- active site: K81 (= K69), S160 (= S144), S161 (= S145), T179 (≠ S163), T181 (= T165), D182 (≠ G166), G183 (= G167), S184 (= S168), C187 (= C171)
- binding : A129 (= A118), N130 (vs. gap), F131 (vs. gap), C158 (≠ G142), G159 (= G143), S160 (= S144), S184 (= S168), C187 (= C171), I212 (≠ Y196), R318 (≠ Y299), L321 (≠ A302), L365 (= L348), F426 (≠ L411)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
34% identity, 94% coverage: 16:461/475 of query aligns to 14:448/457 of 6c6gA
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 97% coverage: 5:463/475 of query aligns to 5:446/457 of 5h6sC
- active site: K77 (= K69), S152 (= S144), S153 (= S145), L173 (≠ T165), G174 (= G166), G175 (= G167), S176 (= S168)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A118), R128 (≠ G120), W129 (≠ S121), S152 (= S144), L173 (≠ T165), G174 (= G166), S176 (= S168), W306 (≠ Y298), F338 (≠ L349)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
31% identity, 92% coverage: 28:462/475 of query aligns to 176:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A118), T258 (≠ S121), S281 (= S144), G302 (≠ T165), G303 (= G166), S305 (= S168), S472 (≠ W327), I532 (≠ E404), M539 (≠ L411)
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)
31% identity, 92% coverage: 28:462/475 of query aligns to 176:589/607 of Q7XJJ7
- K205 (= K69) mutation to A: Loss of activity.
- SS 281:282 (= SS 144:145) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 165:168) binding substrate
- S305 (= S168) mutation to A: Loss of activity.
- R307 (= R170) mutation to A: Loss of activity.
- S360 (≠ Y223) mutation to A: No effect.
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
32% identity, 94% coverage: 17:461/475 of query aligns to 43:487/507 of Q84DC4
- K100 (= K69) mutation to A: Abolishes activity on mandelamide.
- S180 (= S144) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S145) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G166) 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 (= S168) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ C171) 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 (≠ A294) 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 (≠ K361) 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 (≠ D413) 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.
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
30% identity, 92% coverage: 28:462/475 of query aligns to 176:589/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A118), G302 (≠ T165), G303 (= G166), G304 (= G167), A305 (≠ S168), V442 (≠ Y299), I475 (≠ M330), M539 (≠ L411)
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, 92% coverage: 28:462/475 of query aligns to 176:589/605 of 8ey1D
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
33% identity, 85% coverage: 46:450/475 of query aligns to 68:450/605 of Q936X2
- K91 (= K69) mutation to A: Loss of activity.
- S165 (= S144) mutation to A: Loss of activity.
- S189 (= S168) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
34% identity, 86% coverage: 43:450/475 of query aligns to 45:427/461 of 4gysB
- active site: K72 (= K69), S146 (= S144), S147 (= S145), T165 (≠ S163), T167 (= T165), A168 (≠ G166), G169 (= G167), S170 (= S168), V173 (≠ C171)
- binding malonate ion: A120 (= A118), G122 (= G120), S146 (= S144), T167 (= T165), A168 (≠ G166), S170 (= S168), S193 (≠ Y191), G194 (= G192), V195 (= V193), R200 (≠ N198), Y297 (= Y318), R305 (≠ N326)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
29% identity, 97% coverage: 4:466/475 of query aligns to 5:478/490 of 4yjiA
- active site: K79 (= K69), S158 (= S144), S159 (= S145), G179 (≠ T165), G180 (= G166), G181 (= G167), A182 (≠ S168)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ N71), G132 (≠ A118), S158 (= S144), G179 (≠ T165), G180 (= G166), A182 (≠ S168)
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)
30% identity, 81% coverage: 61:446/475 of query aligns to 28:407/425 of Q9FR37
- K36 (= K69) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S144) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S145) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D164) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S168) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C176) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ G251) mutation to T: Slightly reduces catalytic activity.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
28% identity, 96% coverage: 5:461/475 of query aligns to 2:407/412 of 1o9oA
- active site: K62 (= K69), A131 (≠ S144), S132 (= S145), T150 (≠ S163), T152 (= T165), G153 (= G166), G154 (= G167), S155 (= S168), R158 (≠ C171)
- binding 3-amino-3-oxopropanoic acid: G130 (= G143), T152 (= T165), G153 (= G166), G154 (= G167), S155 (= S168), R158 (≠ C171), P359 (= P406)
Query Sequence
>WP_048066007.1 NCBI__GCF_000007345.1:WP_048066007.1
MAKWMSVAQVKDKIKESSAEEVTAGYLEVIEKSKINGYITVSDKALEQAKKIDVEGHEGP
LAGVPIAIKDNISVVGLPNSCGSKILEGYVPPFNAHVIEKLLDAGAVILGKTNLDEFAMG
SSTETSYYGPTANPWDLERVPGGSSGGSAAVVAAGEAPFALGSDTGGSVRCPAAFCGVVG
LKPTYGAVSRYGVVAYANSLEQVGPLANNVEDIAILMDVIAGYDRRDSTSIDSKTEYQKA
LVDDVKGLKIGVPKEFFGEGIHPGVEKAVWNAIHKFESLGATRQEVSMPNINYALASYYI
IAMSEASSNLARFDGTRYGFRANGENWHAMVSKTRAEGFGTEVKRRILLGTYALSAGYHD
KYYLKALKVRTLVKQDFDKALSTVDLLMAPTMPNPAFRIGEKIEDPLTLYLSDVNTCPIN
LAGVPSVSVPCGFTDGLPVGLQIMGKPFDEPTVLRAAYTFEKNTDYHTKRPPEVA
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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