SitesBLAST
Comparing WP_010966260.1 NCBI__GCF_000008765.1:WP_010966260.1 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)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
55% identity, 100% coverage: 1:477/478 of query aligns to 1:475/485 of 2f2aA
- active site: K79 (= K79), S154 (= S154), S155 (= S155), S173 (= S173), T175 (= T175), G176 (= G176), G177 (= G177), S178 (= S178), Q181 (= Q181)
- binding glutamine: G130 (= G130), S154 (= S154), D174 (= D174), T175 (= T175), G176 (= G176), S178 (= S178), F206 (= F206), Y309 (= Y310), Y310 (= Y311), R358 (= R359), D425 (= D426)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
55% identity, 100% coverage: 1:477/478 of query aligns to 1:475/485 of 2dqnA
- active site: K79 (= K79), S154 (= S154), S155 (= S155), S173 (= S173), T175 (= T175), G176 (= G176), G177 (= G177), S178 (= S178), Q181 (= Q181)
- binding asparagine: M129 (= M129), G130 (= G130), T175 (= T175), G176 (= G176), S178 (= S178), Y309 (= Y310), Y310 (= Y311), R358 (= R359), D425 (= D426)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
52% identity, 99% coverage: 3:477/478 of query aligns to 2:468/478 of 3h0mA
- active site: K72 (= K79), S147 (= S154), S148 (= S155), S166 (= S173), T168 (= T175), G169 (= G176), G170 (= G177), S171 (= S178), Q174 (= Q181)
- binding glutamine: M122 (= M129), G123 (= G130), D167 (= D174), T168 (= T175), G169 (= G176), G170 (= G177), S171 (= S178), F199 (= F206), Y302 (= Y310), R351 (= R359), D418 (= D426)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
52% identity, 99% coverage: 3:477/478 of query aligns to 2:468/478 of 3h0lA
- active site: K72 (= K79), S147 (= S154), S148 (= S155), S166 (= S173), T168 (= T175), G169 (= G176), G170 (= G177), S171 (= S178), Q174 (= Q181)
- binding asparagine: G123 (= G130), S147 (= S154), G169 (= G176), G170 (= G177), S171 (= S178), Y302 (= Y310), R351 (= R359), D418 (= D426)
3kfuE Crystal structure of the transamidosome (see paper)
47% identity, 98% coverage: 9:476/478 of query aligns to 3:455/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
39% identity, 83% coverage: 64:461/478 of query aligns to 23:436/450 of 4n0iA
- active site: K38 (= K79), S116 (= S154), S117 (= S155), T135 (≠ S173), T137 (= T175), G138 (= G176), G139 (= G177), S140 (= S178), L143 (≠ Q181)
- binding glutamine: G89 (= G130), T137 (= T175), G138 (= G176), S140 (= S178), Y168 (≠ F206), Y271 (= Y310), Y272 (= Y311), R320 (= R359), D404 (= D426)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
31% identity, 98% coverage: 6:475/478 of query aligns to 1:448/457 of 6c6gA
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 86% coverage: 69:478/478 of query aligns to 85:500/508 of 3a1iA
- active site: K95 (= K79), S170 (= S154), S171 (= S155), G189 (≠ S173), Q191 (≠ T175), G192 (= G176), G193 (= G177), A194 (≠ S178), I197 (≠ Q181)
- binding benzamide: F145 (≠ M129), S146 (≠ G130), G147 (≠ S131), Q191 (≠ T175), G192 (= G176), G193 (= G177), A194 (≠ S178), W327 (≠ Y310)
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, 89% coverage: 52:476/478 of query aligns to 178:589/607 of Q7XJJ7
- K205 (= K79) mutation to A: Loss of activity.
- SS 281:282 (= SS 154:155) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 175:178) binding substrate
- S305 (= S178) mutation to A: Loss of activity.
- R307 (= R180) mutation to A: Loss of activity.
- S360 (≠ E233) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 89% coverage: 52:476/478 of query aligns to 178:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A128), T258 (≠ S131), S281 (= S154), G302 (≠ T175), G303 (= G176), S305 (= S178), S472 (≠ T364), I532 (vs. gap), M539 (≠ L420)
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
29% identity, 89% coverage: 52:476/478 of query aligns to 178:589/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A128), G302 (≠ T175), G303 (= G176), G304 (= G177), A305 (≠ S178), V442 (≠ Y311), I475 (≠ L367), M539 (≠ L420)
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, 89% coverage: 52:476/478 of query aligns to 178:589/605 of 8ey1D
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
30% identity, 98% coverage: 8:477/478 of query aligns to 8:478/487 of 1m21A
- active site: K81 (= K79), S160 (= S154), S161 (= S155), T179 (≠ S173), T181 (= T175), D182 (≠ G176), G183 (= G177), S184 (= S178), C187 (≠ Q181)
- binding : A129 (= A128), N130 (≠ M129), F131 (≠ G130), C158 (≠ G152), G159 (= G153), S160 (= S154), S184 (= S178), C187 (≠ Q181), I212 (≠ F206), R318 (≠ Y311), L321 (≠ S314), L365 (≠ M361), F426 (≠ D418)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 99% coverage: 2:476/478 of query aligns to 24:488/507 of Q84DC4
- T31 (≠ E9) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K79) mutation to A: Abolishes activity on mandelamide.
- S180 (= S154) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S155) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G176) 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 (= S178) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q181) 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 (≠ G306) 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 (≠ S369) 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 (= I427) 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.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
27% identity, 99% coverage: 2:476/478 of query aligns to 1:445/457 of 5h6sC
- active site: K77 (= K79), S152 (= S154), S153 (= S155), L173 (≠ T175), G174 (= G176), G175 (= G177), S176 (= S178)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A128), R128 (≠ G130), W129 (≠ S131), S152 (= S154), L173 (≠ T175), G174 (= G176), S176 (= S178), W306 (≠ Y310), F338 (≠ L362)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
28% identity, 99% coverage: 4:477/478 of query aligns to 1:440/461 of 4gysB
- active site: K72 (= K79), S146 (= S154), S147 (= S155), T165 (≠ S173), T167 (= T175), A168 (≠ G176), G169 (= G177), S170 (= S178), V173 (≠ Q181)
- binding malonate ion: A120 (= A128), G122 (= G130), S146 (= S154), T167 (= T175), A168 (≠ G176), S170 (= S178), S193 (≠ F201), G194 (= G202), V195 (≠ L203), R200 (≠ S208), Y297 (= Y310), R305 (≠ S315)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
28% identity, 96% coverage: 18:476/478 of query aligns to 18:474/490 of 4yjiA
- active site: K79 (= K79), S158 (= S154), S159 (= S155), G179 (≠ T175), G180 (= G176), G181 (= G177), A182 (≠ S178)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ N81), G132 (≠ A128), S158 (= S154), G179 (≠ T175), G180 (= G176), A182 (≠ S178)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 94% coverage: 24:474/478 of query aligns to 37:460/605 of Q936X2
- K91 (= K79) mutation to A: Loss of activity.
- S165 (= S154) mutation to A: Loss of activity.
- S189 (= S178) mutation to A: Loss of activity.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
27% identity, 89% coverage: 39:463/478 of query aligns to 15:394/412 of 1o9oA
- active site: K62 (= K79), A131 (≠ S154), S132 (= S155), T150 (≠ S173), T152 (= T175), G153 (= G176), G154 (= G177), S155 (= S178), R158 (≠ Q181)
- binding 3-amino-3-oxopropanoic acid: G130 (= G153), T152 (= T175), G153 (= G176), G154 (= G177), S155 (= S178), R158 (≠ Q181), P359 (= P419)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
27% identity, 89% coverage: 39:463/478 of query aligns to 15:394/412 of 1ocmA
- active site: K62 (= K79), S131 (= S154), S132 (= S155), T152 (= T175), G153 (= G176), G154 (= G177), S155 (= S178)
- binding pyrophosphate 2-: R113 (≠ G130), S131 (= S154), Q151 (≠ D174), T152 (= T175), G153 (= G176), G154 (= G177), S155 (= S178), R158 (≠ Q181), P359 (= P419)
Query Sequence
>WP_010966260.1 NCBI__GCF_000008765.1:WP_010966260.1
MEILDMTVEQLRNAILDKHLKSEDIVKAYFDNIKRNEPEINAYITLCEDYALKEAKDVDK
KIANGDKVGRLAGIPIAIKDNICTDGIKTTCASKMLYDFVPPYDATVIKKLKAEDAIIIG
KVNMDEFAMGSSTENSAFKITKNPRDITRVPGGSSGGSAAVVAAKMAPISLGSDTGGSIR
QPAAFCGVVGLKPTYGLVSRFGLIAFASSLDQIGPLGKTVKDCAELLEVISGEDELDNTS
SKKHEKEDYLEGIDDGIKGMKIGMPKEFLNDGLDPEIRKCIDDTIEKLKSLGAEVCEMSL
PITEEGLSAYYIISSAEASSNLARFDGIRYGYRPDDFEDVYDLMETSRSEAFGDEVKRRI
MLGTYALSSGYYDAYYKRALKLKKKIKNEFKEAFENYDLILSPVSPVLPFKIGEKKADPL
QMYLADIYTVNINLAGIPAISLPCSVSKEGLPIGLQLLGPHFGEKKIFRAARALEKER
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