SitesBLAST
Comparing WP_013076676.1 NCBI__GCF_000092905.1:WP_013076676.1 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)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
32% identity, 85% coverage: 62:444/448 of query aligns to 197:591/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A118), T258 (≠ V121), S281 (= S139), G302 (≠ T160), G303 (= G161), S305 (= S163), S472 (≠ R325), I532 (≠ V385), M539 (≠ V392)
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)
32% identity, 85% coverage: 62:444/448 of query aligns to 197:591/607 of Q7XJJ7
- K205 (= K70) mutation to A: Loss of activity.
- SS 281:282 (= SS 139:140) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 160:163) binding substrate
- S305 (= S163) mutation to A: Loss of activity.
- R307 (= R165) mutation to A: Loss of activity.
- S360 (≠ D221) mutation to A: No effect.
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
32% identity, 85% coverage: 62:444/448 of query aligns to 197:591/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A118), G302 (≠ T160), G303 (= G161), G304 (= G162), A305 (≠ S163), V442 (≠ L295), I475 (≠ P328), M539 (≠ V392)
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
32% identity, 85% coverage: 62:444/448 of query aligns to 197:591/605 of 8ey1D
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
30% identity, 97% coverage: 9:441/448 of query aligns to 9:466/478 of 3h0mA
- active site: K72 (= K70), S147 (= S139), S148 (= S140), S166 (≠ T158), T168 (= T160), G169 (= G161), G170 (= G162), S171 (= S163), Q174 (≠ I166)
- binding glutamine: M122 (≠ Y119), G123 (= G120), D167 (= D159), T168 (= T160), G169 (= G161), G170 (= G162), S171 (= S163), F199 (≠ L191), Y302 (≠ L295), R351 (vs. gap), D418 (= D389)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
30% identity, 97% coverage: 9:441/448 of query aligns to 9:466/478 of 3h0lA
- active site: K72 (= K70), S147 (= S139), S148 (= S140), S166 (≠ T158), T168 (= T160), G169 (= G161), G170 (= G162), S171 (= S163), Q174 (≠ I166)
- binding asparagine: G123 (= G120), S147 (= S139), G169 (= G161), G170 (= G162), S171 (= S163), Y302 (≠ L295), R351 (vs. gap), D418 (= D389)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 99% coverage: 4:447/448 of query aligns to 5:479/485 of 2f2aA
- active site: K79 (= K70), S154 (= S139), S155 (= S140), S173 (≠ T158), T175 (= T160), G176 (= G161), G177 (= G162), S178 (= S163), Q181 (≠ I166)
- binding glutamine: G130 (= G120), S154 (= S139), D174 (= D159), T175 (= T160), G176 (= G161), S178 (= S163), F206 (≠ L191), Y309 (vs. gap), Y310 (vs. gap), R358 (= R325), D425 (vs. gap)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 99% coverage: 4:447/448 of query aligns to 5:479/485 of 2dqnA
- active site: K79 (= K70), S154 (= S139), S155 (= S140), S173 (≠ T158), T175 (= T160), G176 (= G161), G177 (= G162), S178 (= S163), Q181 (≠ I166)
- binding asparagine: M129 (≠ Y119), G130 (= G120), T175 (= T160), G176 (= G161), S178 (= S163), Y309 (vs. gap), Y310 (vs. gap), R358 (= R325), D425 (vs. gap)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
28% identity, 97% coverage: 7:441/448 of query aligns to 8:476/487 of 1m21A
- active site: K81 (= K70), S160 (= S139), S161 (= S140), T179 (= T158), T181 (= T160), D182 (≠ G161), G183 (= G162), S184 (= S163), C187 (≠ I166)
- binding : A129 (= A118), N130 (vs. gap), F131 (vs. gap), C158 (≠ G137), G159 (= G138), S160 (= S139), S184 (= S163), C187 (≠ I166), I212 (≠ L191), R318 (≠ L295), L321 (≠ R298), L365 (= L322), F426 (≠ V385)
3kfuE Crystal structure of the transamidosome (see paper)
31% identity, 97% coverage: 9:443/448 of query aligns to 4:456/468 of 3kfuE
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
31% identity, 85% coverage: 61:440/448 of query aligns to 82:460/605 of Q936X2
- K91 (= K70) mutation to A: Loss of activity.
- S165 (= S139) mutation to A: Loss of activity.
- S189 (= S163) 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)
31% identity, 87% coverage: 61:448/448 of query aligns to 65:455/457 of 6c6gA
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)
43% identity, 35% coverage: 62:218/448 of query aligns to 28:193/425 of Q9FR37
- K36 (= K70) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S139) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S140) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D159) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S163) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C171) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 91% coverage: 38:445/448 of query aligns to 60:491/507 of Q84DC4
- K100 (= K70) mutation to A: Abolishes activity on mandelamide.
- S180 (= S139) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S140) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G161) 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 (= S163) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I166) 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 (≠ W290) 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 (vs. gap) 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 (≠ V392) 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.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
32% identity, 85% coverage: 54:433/448 of query aligns to 56:430/461 of 4gysB
- active site: K72 (= K70), S146 (= S139), S147 (= S140), T165 (= T158), T167 (= T160), A168 (≠ G161), G169 (= G162), S170 (= S163), V173 (≠ I166)
- binding malonate ion: A120 (= A118), G122 (= G120), S146 (= S139), T167 (= T160), A168 (≠ G161), S170 (= S163), S193 (≠ Q186), G194 (= G187), V195 (= V188), R200 (≠ T193), Y297 (≠ V297), R305 (≠ T305)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
41% identity, 50% coverage: 5:226/448 of query aligns to 2:221/412 of 1o9oA
- active site: K62 (= K70), A131 (≠ S139), S132 (= S140), T150 (= T158), T152 (= T160), G153 (= G161), G154 (= G162), S155 (= S163), R158 (≠ I166)
- binding 3-amino-3-oxopropanoic acid: G130 (= G138), T152 (= T160), G153 (= G161), G154 (= G162), S155 (= S163), R158 (≠ I166)
Sites not aligning to the query:
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
42% identity, 50% coverage: 5:226/448 of query aligns to 2:221/412 of 1ocmA
- active site: K62 (= K70), S131 (= S139), S132 (= S140), T152 (= T160), G153 (= G161), G154 (= G162), S155 (= S163)
- binding pyrophosphate 2-: R113 (≠ G120), S131 (= S139), Q151 (≠ D159), T152 (= T160), G153 (= G161), G154 (= G162), S155 (= S163), R158 (≠ I166)
Sites not aligning to the query:
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
26% identity, 97% coverage: 2:434/448 of query aligns to 2:437/457 of 5h6sC
- active site: K77 (= K70), S152 (= S139), S153 (= S140), L173 (≠ T160), G174 (= G161), G175 (= G162), S176 (= S163)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A118), R128 (vs. gap), W129 (vs. gap), S152 (= S139), L173 (≠ T160), G174 (= G161), S176 (= S163), W306 (≠ T296), F338 (≠ A323)
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
27% identity, 91% coverage: 30:437/448 of query aligns to 7:446/450 of 4n0iA
- active site: K38 (= K70), S116 (= S139), S117 (= S140), T135 (= T158), T137 (= T160), G138 (= G161), G139 (= G162), S140 (= S163), L143 (≠ I166)
- binding glutamine: G89 (= G120), T137 (= T160), G138 (= G161), S140 (= S163), Y168 (≠ L191), Y271 (≠ Q294), Y272 (≠ L295), R320 (= R325), D404 (= D389)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
42% identity, 39% coverage: 56:228/448 of query aligns to 81:258/508 of 3a1iA
- active site: K95 (= K70), S170 (= S139), S171 (= S140), G189 (≠ T158), Q191 (≠ T160), G192 (= G161), G193 (= G162), A194 (≠ S163), I197 (= I166)
- binding benzamide: F145 (≠ Y119), S146 (vs. gap), G147 (vs. gap), Q191 (≠ T160), G192 (= G161), G193 (= G162), A194 (≠ S163)
Sites not aligning to the query:
Query Sequence
>WP_013076676.1 NCBI__GCF_000092905.1:WP_013076676.1
MTDYMTVLEMLSALERGTMTREALATRVRERLNVLEPKVQAFLYVDPEAADRIADPPGSG
PLSGIPVGVKDMIDVAGMPTTGGSRAYHRMPAEDAPCVAKLRKAGAVIVGKTNTQELAYG
VITPPTRNPRNLDYIPGGSSGGSAAAVAAGMVAAALGTDTGGSVRIPASCCGIVGFKPTR
DRISTQGVMPLSTTYDHVGLLTHTASDARYLFHLLTEHPGDSPIRAADGRTERPRPGGRA
SHDRVLAVPWDYIRERTDPEIVQIFEDVLGVFRRLGYGFEAVEMEPFDEWKALQLTVRLP
EAYLTHREVLEGPRRGLLQRDLAERLDPGRDISALDYLAAQAIRREKIADWTRKMESYAG
LVMPTLPCPVPKVGQEQVRIPGSEVPVWDALVSMTAPWNVVGFPAVSVPCGVDSRGLPVG
LQVVGSPMDDDGLLDLAAQFQAAAGIRL
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