SitesBLAST
Comparing WP_037574269.1 NCBI__GCF_000744815.1:WP_037574269.1 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)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
33% identity, 96% coverage: 8:459/472 of query aligns to 7:475/490 of 4yjiA
- active site: K79 (= K80), S158 (= S156), S159 (= S157), G179 (= G177), G180 (= G178), G181 (= G179), A182 (≠ S180)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L82), G132 (= G130), S158 (= S156), G179 (= G177), G180 (= G178), A182 (≠ S180)
3kfuE Crystal structure of the transamidosome (see paper)
36% identity, 96% coverage: 9:459/472 of query aligns to 2:456/468 of 3kfuE
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
30% identity, 90% coverage: 15:440/472 of query aligns to 137:571/607 of Q7XJJ7
- K205 (= K80) mutation to A: Loss of activity.
- SS 281:282 (= SS 156:157) mutation to AA: Loss of activity.
- GGGS 302:305 (= GGGS 177:180) binding substrate
- S305 (= S180) mutation to A: Loss of activity.
- R307 (= R182) mutation to A: Loss of activity.
- S360 (≠ P234) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 90% coverage: 15:440/472 of query aligns to 137:571/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G130), T258 (≠ G133), S281 (= S156), G302 (= G177), G303 (= G178), S305 (= S180), S472 (≠ G348), I532 (≠ L402), M539 (≠ T409)
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, 90% coverage: 15:440/472 of query aligns to 137:571/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (= G130), G302 (= G177), G303 (= G178), G304 (= G179), A305 (≠ S180), V442 (≠ T316), I475 (≠ K351), M539 (≠ T409)
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, 90% coverage: 15:440/472 of query aligns to 137:571/605 of 8ey1D
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 94% coverage: 8:453/472 of query aligns to 7:469/485 of 2f2aA
- active site: K79 (= K80), S154 (= S156), S155 (= S157), S173 (≠ T175), T175 (≠ G177), G176 (= G178), G177 (= G179), S178 (= S180), Q181 (≠ I183)
- binding glutamine: G130 (≠ K132), S154 (= S156), D174 (= D176), T175 (≠ G177), G176 (= G178), S178 (= S180), F206 (= F208), Y309 (= Y314), Y310 (≠ H315), R358 (= R363), D425 (≠ T409)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 94% coverage: 8:453/472 of query aligns to 7:469/485 of 2dqnA
- active site: K79 (= K80), S154 (= S156), S155 (= S157), S173 (≠ T175), T175 (≠ G177), G176 (= G178), G177 (= G179), S178 (= S180), Q181 (≠ I183)
- binding asparagine: M129 (≠ W131), G130 (≠ K132), T175 (≠ G177), G176 (= G178), S178 (= S180), Y309 (= Y314), Y310 (≠ H315), R358 (= R363), D425 (≠ T409)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
30% identity, 96% coverage: 3:453/472 of query aligns to 1:439/457 of 5h6sC
- active site: K77 (= K80), S152 (= S156), S153 (= S157), L173 (≠ G177), G174 (= G178), G175 (= G179), S176 (= S180)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G130), R128 (≠ K132), W129 (≠ G133), S152 (= S156), L173 (≠ G177), G174 (= G178), S176 (= S180), W306 (≠ Y314), F338 (vs. gap)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
32% identity, 81% coverage: 70:451/472 of query aligns to 85:491/508 of 3a1iA
- active site: K95 (= K80), S170 (= S156), S171 (= S157), G189 (≠ T175), Q191 (≠ G177), G192 (= G178), G193 (= G179), A194 (≠ S180), I197 (= I183)
- binding benzamide: F145 (≠ W131), S146 (≠ K132), G147 (= G133), Q191 (≠ G177), G192 (= G178), G193 (= G179), A194 (≠ S180), W327 (= W318)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 96% coverage: 5:456/472 of query aligns to 3:464/478 of 3h0mA
- active site: K72 (= K80), S147 (= S156), S148 (= S157), S166 (≠ T175), T168 (≠ G177), G169 (= G178), G170 (= G179), S171 (= S180), Q174 (≠ I183)
- binding glutamine: M122 (≠ W131), G123 (≠ K132), D167 (= D176), T168 (≠ G177), G169 (= G178), G170 (= G179), S171 (= S180), F199 (= F208), Y302 (= Y314), R351 (= R363), D418 (≠ T409)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 96% coverage: 5:456/472 of query aligns to 3:464/478 of 3h0lA
- active site: K72 (= K80), S147 (= S156), S148 (= S157), S166 (≠ T175), T168 (≠ G177), G169 (= G178), G170 (= G179), S171 (= S180), Q174 (≠ I183)
- binding asparagine: G123 (≠ K132), S147 (= S156), G169 (= G178), G170 (= G179), S171 (= S180), Y302 (= Y314), R351 (= R363), D418 (≠ T409)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
33% identity, 96% coverage: 9:460/472 of query aligns to 7:471/482 of 3a2qA
- active site: K69 (= K80), S147 (= S156), S148 (= S157), N166 (≠ T175), A168 (≠ G177), A169 (≠ G178), G170 (= G179), A171 (≠ S180), I174 (= I183)
- binding 6-aminohexanoic acid: G121 (= G130), G121 (= G130), N122 (≠ W131), S147 (= S156), A168 (≠ G177), A168 (≠ G177), A169 (≠ G178), A171 (≠ S180), C313 (≠ W318)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
32% identity, 96% coverage: 7:457/472 of query aligns to 1:448/457 of 6c6gA
Q9AHE8 Urethanase; Enantioselective amidase; Ethyl carbamate-degrading amidase; EC 3.5.1.75 from Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter) (see 3 papers)
28% identity, 82% coverage: 66:450/472 of query aligns to 84:501/517 of Q9AHE8
- R94 (≠ P76) mutation to P: No change in activity.
- I97 (= I79) mutation to L: 1.12-fold increase in specific activity toward ethyl carbamate, shows higher ethanol tolerance. 3.1-fold increase in specific activity toward ethyl carbamate and 1.5-fold increase in ethanol tolerance, shows lower pH tolerance; when associated with A-195.
- K98 (= K80) mutation to A: Almost loss of activity.
- P163 (= P146) mutation to A: Decrease in activity.
- A172 (≠ G155) mutation to G: Changes substrate specificity. Decrease in activity.
- S173 (= S156) mutation to A: Almost loss of activity.
- N175 (≠ G158) mutation to G: Decrease in activity.; mutation to S: Changes substrate specificity.
- G195 (= G178) mutation to A: 1.86-fold increase in specific activity toward ethyl carbamate, shows lower pH tolerance, causes a decrease in the thermostability. 3.1-fold increase in specific activity toward ethyl carbamate and 1.5-fold increase in ethanol tolerance, shows lower pH tolerance; when associated with L-97.
- S197 (= S180) mutation to A: Almost loss of activity.
- L200 (≠ I183) mutation to C: Decrease in activity.
9fz1A umg-sp3 (see paper)
30% identity, 97% coverage: 7:462/472 of query aligns to 3:438/438 of 9fz1A
Q5XVM9 Lipoamidase; Lipoyl-X hydrolase; Pyruvate dehydrogenase inactivase; EC 3.5.1.138 from Enterococcus faecalis (Streptococcus faecalis) (see paper)
28% identity, 95% coverage: 8:457/472 of query aligns to 93:547/725 of Q5XVM9
- K159 (≠ D73) mutation to A: Strong decrease in activity on the lipoyl domain substrate and on lipoylated small molecules substrates.
- S235 (= S156) mutation to A: Loss of activity on the lipoyl domain substrate and on lipoylated small molecules substrates.
- S259 (= S180) mutation to A: Loss of activity on the lipoyl domain substrate and on lipoylated small molecules substrates.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
37% identity, 50% coverage: 4:238/472 of query aligns to 2:243/487 of 1m21A
- active site: K81 (= K80), S160 (= S156), S161 (= S157), T179 (= T175), T181 (≠ G177), D182 (≠ G178), G183 (= G179), S184 (= S180), C187 (≠ I183)
- binding : A129 (≠ K132), N130 (≠ G133), F131 (≠ V134), C158 (≠ G154), G159 (= G155), S160 (= S156), S184 (= S180), C187 (≠ I183), I212 (≠ F208)
Sites not aligning to the query:
8xtcA umgsp2-mut (see paper)
30% identity, 96% coverage: 7:460/472 of query aligns to 5:438/440 of 8xtcA
Q9TUI8 Fatty-acid amide hydrolase 1; Anandamide amidase; Anandamide amidohydrolase 1; Fatty acid ester hydrolase; Oleamide hydrolase 1; EC 3.5.1.99; EC 3.1.1.- from Sus scrofa (Pig) (see paper)
38% identity, 46% coverage: 6:222/472 of query aligns to 76:288/579 of Q9TUI8
- S217 (= S156) mutation to A: Loss of activity.
- S218 (= S157) mutation to A: Lowers activity by at least 98%.
- D237 (= D176) mutation D->E,N: Loss of activity.
- S241 (= S180) mutation to A: Loss of activity.
- C249 (= C188) mutation to A: Loss of activity.
Query Sequence
>WP_037574269.1 NCBI__GCF_000744815.1:WP_037574269.1
MTEPYAMTATELVAAYESKELSPVEATASVLDRIEAADPVLNAYCLVEADAAMEEARRSE
DRWSRGEPAGLLDGVPVSIKDLLYTRGRPTLRGSLSISAEREWAEDAPSVARMREQGAVF
VGKTTTPEFGWKGVTDNPLTGITRNPWNPSTTSGGSSGGSAAAVAAGMAPLSVGTDGGGS
VRIPAAFCGIFGMKPTYGRIPLYPASPFGTLAHAGPMARTVEDAALLMDVVTGPDSRDWS
ALESPRGGYRAAVAEALAMGSLAGLRIAYAPTLAGAEVDPEVAARVEAVAGLLERLGADV
ETADPGFADPVEAYHTLWFSGAAKVVEQLGPEQFARLDPGLQEICREGAAKSALEYLGAV
DERMALGVWMGRFHETYDLLLTPTIPIPAFEAGVEVPPGSGLRRWTGWTPFTYPFNLTQQ
PAATVPAGLAGGLPVGAQLVAARHGDELVLRASAVLHAALCAEGVVGTGPVG
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