SitesBLAST
Comparing WP_011320446.1 NCBI__GCF_000204075.1:WP_011320446.1 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)
57% identity, 97% coverage: 3:474/486 of query aligns to 6:467/478 of 3h0mA
- active site: K72 (= K75), S147 (= S150), S148 (= S151), S166 (= S169), T168 (= T171), G169 (= G172), G170 (= G173), S171 (= S174), Q174 (= Q177)
- binding glutamine: M122 (= M125), G123 (= G126), D167 (= D170), T168 (= T171), G169 (= G172), G170 (= G173), S171 (= S174), F199 (≠ Y202), Y302 (= Y308), R351 (= R357), D418 (= D424)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
57% identity, 97% coverage: 3:474/486 of query aligns to 6:467/478 of 3h0lA
- active site: K72 (= K75), S147 (= S150), S148 (= S151), S166 (= S169), T168 (= T171), G169 (= G172), G170 (= G173), S171 (= S174), Q174 (= Q177)
- binding asparagine: G123 (= G126), S147 (= S150), G169 (= G172), G170 (= G173), S171 (= S174), Y302 (= Y308), R351 (= R357), D418 (= D424)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
54% identity, 98% coverage: 3:479/486 of query aligns to 7:479/485 of 2f2aA
- active site: K79 (= K75), S154 (= S150), S155 (= S151), S173 (= S169), T175 (= T171), G176 (= G172), G177 (= G173), S178 (= S174), Q181 (= Q177)
- binding glutamine: G130 (= G126), S154 (= S150), D174 (= D170), T175 (= T171), G176 (= G172), S178 (= S174), F206 (≠ Y202), Y309 (= Y308), Y310 (= Y309), R358 (= R357), D425 (= D424)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
54% identity, 98% coverage: 3:479/486 of query aligns to 7:479/485 of 2dqnA
- active site: K79 (= K75), S154 (= S150), S155 (= S151), S173 (= S169), T175 (= T171), G176 (= G172), G177 (= G173), S178 (= S174), Q181 (= Q177)
- binding asparagine: M129 (= M125), G130 (= G126), T175 (= T171), G176 (= G172), S178 (= S174), Y309 (= Y308), Y310 (= Y309), R358 (= R357), D425 (= D424)
3kfuE Crystal structure of the transamidosome (see paper)
50% identity, 98% coverage: 6:483/486 of query aligns to 4:465/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
39% identity, 81% coverage: 67:458/486 of query aligns to 30:435/450 of 4n0iA
- active site: K38 (= K75), S116 (= S150), S117 (= S151), T135 (≠ S169), T137 (= T171), G138 (= G172), G139 (= G173), S140 (= S174), L143 (≠ Q177)
- binding glutamine: G89 (= G126), T137 (= T171), G138 (= G172), S140 (= S174), Y168 (= Y202), Y271 (= Y308), Y272 (= Y309), R320 (= R357), D404 (= D424)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
34% identity, 84% coverage: 65:474/486 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K75), S170 (= S150), S171 (= S151), G189 (≠ S169), Q191 (≠ T171), G192 (= G172), G193 (= G173), A194 (≠ S174), I197 (≠ Q177)
- binding benzamide: F145 (≠ M125), S146 (≠ G126), G147 (≠ S127), Q191 (≠ T171), G192 (= G172), G193 (= G173), A194 (≠ S174), W327 (≠ Y308)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
31% identity, 97% coverage: 4:474/486 of query aligns to 131:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A124), T258 (≠ S127), S281 (= S150), G302 (≠ T171), G303 (= G172), S305 (= S174), S472 (≠ T362), I532 (≠ A415), M539 (= M426)
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, 97% coverage: 4:474/486 of query aligns to 131:589/607 of Q7XJJ7
- K205 (= K75) mutation to A: Loss of activity.
- SS 281:282 (= SS 150:151) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 171:174) binding substrate
- S305 (= S174) mutation to A: Loss of activity.
- R307 (= R176) mutation to A: Loss of activity.
- S360 (≠ Y229) mutation to A: No effect.
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
30% identity, 97% coverage: 4:474/486 of query aligns to 131:589/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A124), G302 (≠ T171), G303 (= G172), G304 (= G173), A305 (≠ S174), V442 (≠ Y309), I475 (≠ L365), M539 (= M426)
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, 97% coverage: 4:474/486 of query aligns to 131:589/605 of 8ey1D
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
33% identity, 97% coverage: 6:475/486 of query aligns to 5:450/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
34% identity, 97% coverage: 4:476/486 of query aligns to 8:479/487 of 1m21A
- active site: K81 (= K75), S160 (= S150), S161 (= S151), T179 (≠ S169), T181 (= T171), D182 (≠ G172), G183 (= G173), S184 (= S174), C187 (≠ Q177)
- binding : A129 (= A124), N130 (≠ M125), F131 (≠ G126), C158 (≠ G148), G159 (= G149), S160 (= S150), S184 (= S174), C187 (≠ Q177), I212 (≠ Y202), R318 (≠ Y309), L321 (≠ A312), L365 (≠ I358), F426 (≠ D416)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 95% coverage: 11:473/486 of query aligns to 36:487/507 of Q84DC4
- K100 (= K75) mutation to A: Abolishes activity on mandelamide.
- S180 (= S150) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S151) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G172) 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 (= S174) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q177) 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 (vs. gap) 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 (≠ D371) 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 (≠ D424) 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)
28% identity, 97% coverage: 6:474/486 of query aligns to 9:445/457 of 5h6sC
- active site: K77 (= K75), S152 (= S150), S153 (= S151), L173 (≠ T171), G174 (= G172), G175 (= G173), S176 (= S174)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A124), R128 (≠ G126), W129 (≠ S127), S152 (= S150), L173 (≠ T171), G174 (= G172), S176 (= S174), W306 (≠ Y308), F338 (≠ I360)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
33% identity, 85% coverage: 61:472/486 of query aligns to 78:460/605 of Q936X2
- K91 (= K75) mutation to A: Loss of activity.
- S165 (= S150) mutation to A: Loss of activity.
- S189 (= S174) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
32% identity, 93% coverage: 20:469/486 of query aligns to 20:434/461 of 4gysB
- active site: K72 (= K75), S146 (= S150), S147 (= S151), T165 (≠ S169), T167 (= T171), A168 (≠ G172), G169 (= G173), S170 (= S174), V173 (≠ Q177)
- binding malonate ion: A120 (= A124), G122 (= G126), S146 (= S150), T167 (= T171), A168 (≠ G172), S170 (= S174), S193 (≠ Y197), G194 (= G198), V195 (≠ L199), R200 (≠ S204), Y297 (= Y309), R305 (= R322)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
29% identity, 98% coverage: 1:475/486 of query aligns to 1:409/412 of 1o9oA
- active site: K62 (= K75), A131 (≠ S150), S132 (= S151), T150 (≠ S169), T152 (= T171), G153 (= G172), G154 (= G173), S155 (= S174), R158 (≠ Q177)
- binding 3-amino-3-oxopropanoic acid: G130 (= G149), T152 (= T171), G153 (= G172), G154 (= G173), S155 (= S174), R158 (≠ Q177), P359 (= P417)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
29% identity, 98% coverage: 1:475/486 of query aligns to 1:409/412 of 1ocmA
- active site: K62 (= K75), S131 (= S150), S132 (= S151), T152 (= T171), G153 (= G172), G154 (= G173), S155 (= S174)
- binding pyrophosphate 2-: R113 (≠ G126), S131 (= S150), Q151 (≠ D170), T152 (= T171), G153 (= G172), G154 (= G173), S155 (= S174), R158 (≠ Q177), P359 (= P417)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
27% identity, 98% coverage: 3:478/486 of query aligns to 7:478/490 of 4yjiA
- active site: K79 (= K75), S158 (= S150), S159 (= S151), G179 (≠ T171), G180 (= G172), G181 (= G173), A182 (≠ S174)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ N77), G132 (≠ A124), S158 (= S150), G179 (≠ T171), G180 (= G172), A182 (≠ S174)
Query Sequence
>WP_011320446.1 NCBI__GCF_000204075.1:WP_011320446.1
MASIRELHEQLVKKERSAVEITQETLDHIQELEPKLHSFLHITAQQALEQARAVDAKIAA
GEEIGLLAGIPIGVKDNMCTKGIPTTCASRILENFVPPYESTVTQKLLDAGAVVVGKTNL
DEFAMGSSTENSAYQVTANPWDLSRVPGGSSGGSAAAVAAEECVVALGSDTGGSIRQPAS
FCGVVGLKPTYGLVSRYGLVAYASSLDQIGPFGKSVEDTAILLKAIAGYDPKDSTSLKVE
IPDYVASLKPDLKARGKLRIGVIKETFGEGLDSVVEQAVTKAIEQLQRLGAEIHVISCPN
FRYGVPSYYIIAPSEASANLARYDGVKYGWRAPEGDNLLSMYKRTRATGFGAEVKRRIMI
GTYALSAGYYDAYYLKAQKVRTLIKQDFENAFKNVDVLVSPTAPTTAFKAGEKTADPISM
YLNDLMTIPVNLAGLPGLSLPCGFDEQGLPIGLQLIGKVLREDQLLQVAYAYEQSTSWHL
SQPKIS
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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