SitesBLAST
Comparing WP_015797706.1 NCBI__GCF_000023265.1:WP_015797706.1 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)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
34% identity, 97% coverage: 9:468/472 of query aligns to 4:478/482 of 3a2qA
- active site: K69 (= K82), S147 (= S157), S148 (= S158), N166 (≠ S176), A168 (≠ G178), A169 (≠ G179), G170 (= G180), A171 (≠ S181), I174 (= I184)
- binding 6-aminohexanoic acid: G121 (= G131), G121 (= G131), N122 (≠ E132), S147 (= S157), A168 (≠ G178), A168 (≠ G178), A169 (≠ G179), A171 (≠ S181), C313 (≠ V314)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 96% coverage: 16:470/472 of query aligns to 135:599/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G131), T258 (≠ P134), S281 (= S157), G302 (= G178), G303 (= G179), S305 (= S181), S472 (≠ E336), I532 (≠ L403), M539 (≠ A409)
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)
29% identity, 96% coverage: 16:470/472 of query aligns to 135:599/607 of Q7XJJ7
- K205 (= K82) mutation to A: Loss of activity.
- SS 281:282 (= SS 157:158) mutation to AA: Loss of activity.
- GGGS 302:305 (= GGGS 178:181) binding substrate
- S305 (= S181) mutation to A: Loss of activity.
- R307 (= R183) mutation to A: Loss of activity.
- S360 (vs. gap) mutation to A: No effect.
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
29% identity, 96% coverage: 16:470/472 of query aligns to 135:599/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (= G131), G302 (= G178), G303 (= G179), G304 (= G180), A305 (≠ S181), V442 (≠ S311), I475 (≠ R339), M539 (≠ A409)
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, 96% coverage: 16:470/472 of query aligns to 135:599/605 of 8ey1D
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
29% identity, 94% coverage: 19:464/472 of query aligns to 15:479/490 of 4yjiA
- active site: K79 (= K82), S158 (= S157), S159 (= S158), G179 (= G178), G180 (= G179), G181 (= G180), A182 (≠ S181)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L84), G132 (= G131), S158 (= S157), G179 (= G178), G180 (= G179), A182 (≠ S181)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 96% coverage: 15:468/472 of query aligns to 10:476/478 of 3h0mA
- active site: K72 (= K82), S147 (= S157), S148 (= S158), S166 (= S176), T168 (≠ G178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (≠ I184)
- binding glutamine: M122 (≠ E132), G123 (≠ L133), D167 (= D177), T168 (≠ G178), G169 (= G179), G170 (= G180), S171 (= S181), F199 (= F209), Y302 (≠ E305), R351 (≠ Q351), D418 (≠ A409)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 96% coverage: 15:468/472 of query aligns to 10:476/478 of 3h0lA
- active site: K72 (= K82), S147 (= S157), S148 (= S158), S166 (= S176), T168 (≠ G178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (≠ I184)
- binding asparagine: G123 (≠ L133), S147 (= S157), G169 (= G179), G170 (= G180), S171 (= S181), Y302 (≠ E305), R351 (≠ Q351), D418 (≠ A409)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 91% coverage: 28:458/472 of query aligns to 23:444/457 of 5h6sC
- active site: K77 (= K82), S152 (= S157), S153 (= S158), L173 (≠ G178), G174 (= G179), G175 (= G180), S176 (= S181)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G131), R128 (≠ L133), W129 (≠ P134), S152 (= S157), L173 (≠ G178), G174 (= G179), S176 (= S181), W306 (≠ V310), F338 (≠ V349)
3kfuE Crystal structure of the transamidosome (see paper)
32% identity, 93% coverage: 21:459/472 of query aligns to 11:455/468 of 3kfuE
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 95% coverage: 14:462/472 of query aligns to 10:477/485 of 2f2aA
- active site: K79 (= K82), S154 (= S157), S155 (= S158), S173 (= S176), T175 (≠ G178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (≠ I184)
- binding glutamine: G130 (≠ L133), S154 (= S157), D174 (= D177), T175 (≠ G178), G176 (= G179), S178 (= S181), F206 (= F209), Y309 (≠ E305), Y310 (≠ L306), R358 (≠ L352), D425 (≠ A409)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 95% coverage: 14:462/472 of query aligns to 10:477/485 of 2dqnA
- active site: K79 (= K82), S154 (= S157), S155 (= S158), S173 (= S176), T175 (≠ G178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (≠ I184)
- binding asparagine: M129 (≠ E132), G130 (≠ L133), T175 (≠ G178), G176 (= G179), S178 (= S181), Y309 (≠ E305), Y310 (≠ L306), R358 (≠ L352), D425 (≠ A409)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
31% identity, 87% coverage: 52:460/472 of query aligns to 41:450/457 of 6c6gA
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 81% coverage: 81:460/472 of query aligns to 94:499/508 of 3a1iA
- active site: K95 (= K82), S170 (= S157), S171 (= S158), G189 (≠ S176), Q191 (≠ G178), G192 (= G179), G193 (= G180), A194 (≠ S181), I197 (= I184)
- binding benzamide: F145 (≠ E132), S146 (≠ L133), G147 (≠ P134), Q191 (≠ G178), G192 (= G179), G193 (= G180), A194 (≠ S181), W327 (≠ V310)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
34% identity, 48% coverage: 8:232/472 of query aligns to 4:237/487 of 1m21A
- active site: K81 (= K82), S160 (= S157), S161 (= S158), T179 (≠ S176), T181 (≠ G178), D182 (≠ G179), G183 (= G180), S184 (= S181), C187 (≠ I184)
- binding : A129 (≠ G131), N130 (≠ E132), F131 (≠ L133), C158 (≠ G155), G159 (= G156), S160 (= S157), S184 (= S181), C187 (≠ I184), I212 (≠ P207)
Sites not aligning to the query:
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
27% identity, 94% coverage: 16:460/472 of query aligns to 34:489/507 of Q84DC4
- K100 (= K82) mutation to A: Abolishes activity on mandelamide.
- S180 (= S157) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S158) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G179) 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 (= S181) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I184) 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 (≠ T299) 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 (≠ R357) 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 (≠ A396) 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.
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)
37% identity, 27% coverage: 76:201/472 of query aligns to 30:157/425 of Q9FR37
- K36 (= K82) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S157) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S158) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D177) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S181) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C189) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
27% identity, 95% coverage: 13:459/472 of query aligns to 2:408/412 of 1o9oA
- active site: K62 (= K82), A131 (≠ S157), S132 (= S158), T150 (≠ S176), T152 (≠ G178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ I184)
- binding 3-amino-3-oxopropanoic acid: G130 (= G156), T152 (≠ G178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ I184), P359 (= P401)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 82% coverage: 63:450/472 of query aligns to 51:430/461 of 4gysB
- active site: K72 (= K82), S146 (= S157), S147 (= S158), T165 (≠ S176), T167 (≠ G178), A168 (≠ G179), G169 (= G180), S170 (= S181), V173 (≠ I184)
- binding malonate ion: A120 (≠ G131), G122 (≠ L133), S146 (= S157), T167 (≠ G178), A168 (≠ G179), S170 (= S181), S193 (≠ E214), G194 (= G215), V195 (= V216), R200 (= R219), Y297 (≠ V314), R305 (vs. gap)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
28% identity, 95% coverage: 13:459/472 of query aligns to 2:408/412 of 1ocmA
- active site: K62 (= K82), S131 (= S157), S132 (= S158), T152 (≠ G178), G153 (= G179), G154 (= G180), S155 (= S181)
- binding pyrophosphate 2-: R113 (≠ L133), S131 (= S157), Q151 (≠ D177), T152 (≠ G178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ I184), P359 (= P401)
Query Sequence
>WP_015797706.1 NCBI__GCF_000023265.1:WP_015797706.1
MSTIDLAAYVDGVSLAAALRRREVGVLEVLQATLELIDERNPALGAIVWLDRDDARRRAE
RAARRLDADDPAPFLGVPLPVKDLHPVAGWPITYGSWGGPEGVSARSSIAVEALEEAGFV
LVGRSATPELGELPATEGDRYGVTRNPWDLSRTPGGSSGGAAAAVAGGMVTVAHGSDGGG
SLRIPAAACGLVGLKPSRGRVPARSAPWFGLSTEGVVTRSIRDQAACLAVLAAPRRGAWL
PQPPAGFGDGGWHVAPTRLRVGVVTEPPFGLPIDDARRLAVGEVARLVADLGHEVREVTL
ALPDELIEAVSVVVGAGVAEHDDLDWSRVEPHTAAEYERAKALPATELVRQLMVLERTGS
DLAAALPGDVDVLLTPTTAIAPPPVGTVLEAAHAAAHTGLPALEVVSLAIFTLPWNIAGL
PAISLPTHLDVDGLPIGVQLVGPPAGEATLLALGAALEEVYEWTTRRPPVQR
Or try a new SitesBLAST search
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