SitesBLAST
Comparing WP_338063076.1 NCBI__GCF_001431535.1:WP_338063076.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
32% identity, 92% coverage: 30:488/498 of query aligns to 5:448/457 of 5h6sC
- active site: K77 (= K103), S152 (= S178), S153 (= S179), L173 (≠ I199), G174 (= G200), G175 (= G201), S176 (= S202)
- binding 4-oxidanylbenzohydrazide: C126 (≠ S152), R128 (≠ S154), W129 (= W155), S152 (= S178), L173 (≠ I199), G174 (= G200), S176 (= S202), W306 (= W336), F338 (≠ W374)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 92% coverage: 28:487/498 of query aligns to 3:469/478 of 3h0mA
- active site: K72 (= K103), S147 (= S178), S148 (= S179), S166 (≠ N197), T168 (≠ I199), G169 (= G200), G170 (= G201), S171 (= S202), Q174 (≠ H205)
- binding glutamine: M122 (≠ F153), G123 (≠ S154), D167 (= D198), T168 (≠ I199), G169 (= G200), G170 (= G201), S171 (= S202), F199 (≠ P228), Y302 (≠ W336), R351 (vs. gap), D418 (= D425)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 92% coverage: 28:487/498 of query aligns to 3:469/478 of 3h0lA
- active site: K72 (= K103), S147 (= S178), S148 (= S179), S166 (≠ N197), T168 (≠ I199), G169 (= G200), G170 (= G201), S171 (= S202), Q174 (≠ H205)
- binding asparagine: G123 (≠ S154), S147 (= S178), G169 (= G200), G170 (= G201), S171 (= S202), Y302 (≠ W336), R351 (vs. gap), D418 (= D425)
9fz1A umg-sp3 (see paper)
33% identity, 92% coverage: 30:487/498 of query aligns to 3:436/438 of 9fz1A
3kfuE Crystal structure of the transamidosome (see paper)
32% identity, 91% coverage: 32:486/498 of query aligns to 2:456/468 of 3kfuE
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
35% identity, 78% coverage: 95:484/498 of query aligns to 87:497/508 of 3a1iA
- active site: K95 (= K103), S170 (= S178), S171 (= S179), G189 (≠ N197), Q191 (≠ I199), G192 (= G200), G193 (= G201), A194 (≠ S202), I197 (≠ H205)
- binding benzamide: F145 (= F153), S146 (= S154), G147 (≠ W155), Q191 (≠ I199), G192 (= G200), G193 (= G201), A194 (≠ S202), W327 (= W336)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 90% coverage: 37:485/498 of query aligns to 13:474/485 of 2f2aA
- active site: K79 (= K103), S154 (= S178), S155 (= S179), S173 (≠ N197), T175 (≠ I199), G176 (= G200), G177 (= G201), S178 (= S202), Q181 (≠ H205)
- binding glutamine: G130 (≠ S154), S154 (= S178), D174 (= D198), T175 (≠ I199), G176 (= G200), S178 (= S202), F206 (≠ P228), Y309 (≠ W336), Y310 (≠ W337), R358 (≠ E372), D425 (≠ P438)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 90% coverage: 37:485/498 of query aligns to 13:474/485 of 2dqnA
- active site: K79 (= K103), S154 (= S178), S155 (= S179), S173 (≠ N197), T175 (≠ I199), G176 (= G200), G177 (= G201), S178 (= S202), Q181 (≠ H205)
- binding asparagine: M129 (≠ F153), G130 (≠ S154), T175 (≠ I199), G176 (= G200), S178 (= S202), Y309 (≠ W336), Y310 (≠ W337), R358 (≠ E372), D425 (≠ P438)
8xtcA umgsp2-mut (see paper)
33% identity, 92% coverage: 30:487/498 of query aligns to 5:438/440 of 8xtcA
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, 84% coverage: 71:489/498 of query aligns to 173:593/607 of Q7XJJ7
- K205 (= K103) mutation to A: Loss of activity.
- SS 281:282 (= SS 178:179) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ IGGS 199:202) binding substrate
- S305 (= S202) mutation to A: Loss of activity.
- R307 (= R204) mutation to A: Loss of activity.
- S360 (≠ F263) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
30% identity, 84% coverage: 71:489/498 of query aligns to 173:593/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ S152), T258 (≠ W155), S281 (= S178), G302 (≠ I199), G303 (= G200), S305 (= S202), S472 (≠ E372), I532 (≠ A424), M539 (≠ A431)
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: 71:489/498 of query aligns to 173:593/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ S152), G302 (≠ I199), G303 (= G200), G304 (= G201), A305 (≠ S202), V442 (≠ W337), I475 (≠ W374), M539 (≠ A431)
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: 71:489/498 of query aligns to 173:593/605 of 8ey1D
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
31% identity, 92% coverage: 25:484/498 of query aligns to 1:476/487 of 1m21A
- active site: K81 (= K103), S160 (= S178), S161 (= S179), T179 (≠ N197), T181 (≠ I199), D182 (≠ G200), G183 (= G201), S184 (= S202), C187 (≠ H205)
- binding : A129 (≠ S152), N130 (vs. gap), F131 (vs. gap), C158 (≠ G176), G159 (= G177), S160 (= S178), S184 (= S202), C187 (≠ H205), I212 (≠ G224), R318 (= R334), L321 (≠ V340), L365 (vs. gap), F426 (≠ K418)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
28% identity, 92% coverage: 31:488/498 of query aligns to 7:477/490 of 4yjiA
- active site: K79 (= K103), S158 (= S178), S159 (= S179), G179 (≠ I199), G180 (= G200), G181 (= G201), A182 (≠ S202)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ N105), G132 (≠ S152), S158 (= S178), G179 (≠ I199), G180 (= G200), A182 (≠ S202)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 92% coverage: 28:487/498 of query aligns to 26:490/507 of Q84DC4
- T31 (= T33) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K103) mutation to A: Abolishes activity on mandelamide.
- S180 (= S178) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S179) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G200) 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 (= S202) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ H205) 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 (≠ W333) 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 (≠ N385) 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 (= I433) 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.
Q5XVM9 Lipoamidase; Lipoyl-X hydrolase; Pyruvate dehydrogenase inactivase; EC 3.5.1.138 from Enterococcus faecalis (Streptococcus faecalis) (see paper)
27% identity, 93% coverage: 31:492/498 of query aligns to 93:555/725 of Q5XVM9
- K159 (= K103) mutation to A: Strong decrease in activity on the lipoyl domain substrate and on lipoylated small molecules substrates.
- S235 (= S178) mutation to A: Loss of activity on the lipoyl domain substrate and on lipoylated small molecules substrates.
- S259 (= S202) mutation to A: Loss of activity on the lipoyl domain substrate and on lipoylated small molecules substrates.
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
31% identity, 92% coverage: 31:488/498 of query aligns to 6:472/482 of 3a2qA
- active site: K69 (= K103), S147 (= S178), S148 (= S179), N166 (= N197), A168 (≠ I199), A169 (≠ G200), G170 (= G201), A171 (≠ S202), I174 (≠ H205)
- binding 6-aminohexanoic acid: G121 (≠ S152), G121 (≠ S152), N122 (≠ F153), S147 (= S178), A168 (≠ I199), A168 (≠ I199), A169 (≠ G200), A171 (≠ S202), C313 (≠ E342)
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)
33% identity, 57% coverage: 39:321/498 of query aligns to 86:360/579 of Q9TUI8
- S217 (= S178) mutation to A: Loss of activity.
- S218 (= S179) mutation to A: Lowers activity by at least 98%.
- D237 (= D198) mutation D->E,N: Loss of activity.
- S241 (= S202) mutation to A: Loss of activity.
- C249 (= C210) mutation to A: Loss of activity.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
29% identity, 89% coverage: 42:484/498 of query aligns to 13:448/457 of 6c6gA
Query Sequence
>WP_338063076.1 NCBI__GCF_001431535.1:WP_338063076.1
MAGTGGMVPAAAQVPPLSLRSPGSLPAWALSATDASALLRRGELSAVELTRSCLGRIAVV
NPVVNALNFVDEAAAIRAAEQADAALARGAVSAPLHGIPVAIKDNTDVRGQPMTNGIVAL
KDNIASADAPQVARLRAAGAIVLGRSNTPCFSFSWDARNDLHGTTWNPWSRAHTPGGSSG
GAACAVATGMVPLAHGNDIGGSIRHPAYCCGVAGLRPTPGRVPGLFSPAKGDEALGLQLM
LVDGPIARGVADLRLMLESMTGFDPRVPGSLPLPLPFPASPLLPGTRIGVLREDDVKPRT
PTVAAALERAVVALQQAGFTVEEVRLPELAEAWRLWWLLVMEETRALLPSIERDGDAPIK
AWIGFNYDVASEMWGRQPSLTDYINGYARRARLIASLQQKLRRYPVILMPVASEEPFKQG
QHYADLASARAAIASGWPLMAIPVLGFPALAVPTGCVDGLPTGVQLMGRRFHERDVLQVG
AALEAAMPVLTPMDPLRT
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