SitesBLAST
Comparing WP_011798409.1 NCBI__GCF_000015505.1:WP_011798409.1 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)
30% identity, 91% coverage: 11:470/506 of query aligns to 8:485/490 of 4yjiA
- active site: K79 (= K82), S158 (= S157), S159 (= S158), G179 (≠ T178), G180 (= G179), G181 (= G180), A182 (≠ S181)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L84), G132 (= G131), S158 (= S157), G179 (≠ T178), G180 (= G179), A182 (≠ S181)
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, 80% coverage: 57:459/506 of query aligns to 180:589/607 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 (≠ TGGS 178:181) binding substrate
- S305 (= S181) mutation to A: Loss of activity.
- R307 (= R183) mutation to A: Loss of activity.
- S360 (≠ V236) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 80% coverage: 57:459/506 of query aligns to 180:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G131), T258 (≠ A134), S281 (= S157), G302 (≠ T178), G303 (= G179), S305 (= S181), S472 (≠ N341), I532 (= I397), M539 (≠ L409)
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
28% identity, 80% coverage: 57:459/506 of query aligns to 180:589/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (= G131), G302 (≠ T178), G303 (= G179), G304 (= G180), A305 (≠ S181), V442 (≠ D312), I475 (≠ M344), M539 (≠ L409)
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
28% identity, 80% coverage: 57:459/506 of query aligns to 180:589/605 of 8ey1D
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 88% coverage: 17:461/506 of query aligns to 14:476/485 of 2f2aA
- active site: K79 (= K82), S154 (= S157), S155 (= S158), S173 (= S176), T175 (= T178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (≠ I184)
- binding glutamine: G130 (= G133), S154 (= S157), D174 (= D177), T175 (= T178), G176 (= G179), S178 (= S181), F206 (≠ G209), Y309 (≠ C310), Y310 (≠ F311), R358 (≠ N341), D425 (≠ L409)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 88% coverage: 17:461/506 of query aligns to 14:476/485 of 2dqnA
- active site: K79 (= K82), S154 (= S157), S155 (= S158), S173 (= S176), T175 (= T178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (≠ I184)
- binding asparagine: M129 (≠ A132), G130 (= G133), T175 (= T178), G176 (= G179), S178 (= S181), Y309 (≠ C310), Y310 (≠ F311), R358 (≠ N341), D425 (≠ L409)
3kfuE Crystal structure of the transamidosome (see paper)
33% identity, 90% coverage: 11:464/506 of query aligns to 2:460/468 of 3kfuE
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
29% identity, 89% coverage: 9:459/506 of query aligns to 5:445/457 of 5h6sC
- active site: K77 (= K82), S152 (= S157), S153 (= S158), L173 (≠ T178), G174 (= G179), G175 (= G180), S176 (= S181)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G131), R128 (≠ G133), W129 (≠ A134), S152 (= S157), L173 (≠ T178), G174 (= G179), S176 (= S181), W306 (≠ L300), F338 (≠ R339)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 90% coverage: 12:467/506 of query aligns to 8:475/478 of 3h0mA
- active site: K72 (= K82), S147 (= S157), S148 (= S158), S166 (= S176), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (≠ I184)
- binding glutamine: M122 (≠ A132), G123 (= G133), D167 (= D177), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), F199 (≠ G209), Y302 (vs. gap), R351 (≠ N341), D418 (vs. gap)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 90% coverage: 12:467/506 of query aligns to 8:475/478 of 3h0lA
- active site: K72 (= K82), S147 (= S157), S148 (= S158), S166 (= S176), T168 (= T178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (≠ I184)
- binding asparagine: G123 (= G133), S147 (= S157), G169 (= G179), G170 (= G180), S171 (= S181), Y302 (vs. gap), R351 (≠ N341), D418 (vs. gap)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
32% identity, 86% coverage: 9:441/506 of query aligns to 1:431/457 of 6c6gA
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 77% coverage: 72:459/506 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K82), S170 (= S157), S171 (= S158), G189 (≠ S176), Q191 (≠ T178), G192 (= G179), G193 (= G180), A194 (≠ S181), I197 (= I184)
- binding benzamide: F145 (≠ A132), S146 (≠ G133), G147 (≠ A134), Q191 (≠ T178), G192 (= G179), G193 (= G180), A194 (≠ S181), W327 (≠ C297)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
41% identity, 38% coverage: 11:201/506 of query aligns to 7:191/482 of 3a2qA
- active site: K69 (= K82), S147 (= S157), S148 (= S158), N166 (≠ S176), A168 (≠ T178), A169 (≠ G179), G170 (= G180), A171 (≠ S181), I174 (= I184)
- binding 6-aminohexanoic acid: G121 (= G131), G121 (= G131), N122 (≠ A132), S147 (= S157), A168 (≠ T178), A168 (≠ T178), A169 (≠ G179), A171 (≠ S181)
Sites not aligning to the query:
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 80% coverage: 57:459/506 of query aligns to 50:439/461 of 4gysB
- active site: K72 (= K82), S146 (= S157), S147 (= S158), T165 (≠ S176), T167 (= T178), A168 (≠ G179), G169 (= G180), S170 (= S181), V173 (≠ I184)
- binding malonate ion: A120 (≠ G131), G122 (= G133), S146 (= S157), T167 (= T178), A168 (≠ G179), S170 (= S181), S193 (= S204), G194 (≠ R205), V195 (≠ K206), R200 (≠ T211), Y297 (≠ R315), R305 (≠ M323)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 90% coverage: 4:458/506 of query aligns to 23:487/507 of Q84DC4
- T31 (= T12) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- 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 (≠ C297) 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 (≠ C353) 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 (≠ L409) 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.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
38% identity, 46% coverage: 13:243/506 of query aligns to 10:246/487 of 1m21A
- active site: K81 (= K82), S160 (= S157), S161 (= S158), T179 (≠ S176), T181 (= T178), D182 (≠ G179), G183 (= G180), S184 (= S181), C187 (≠ I184)
- binding : A129 (≠ G131), N130 (≠ A132), F131 (vs. gap), C158 (≠ G155), G159 (= G156), S160 (= S157), S184 (= S181), C187 (≠ I184), I212 (= I213)
Sites not aligning to the query:
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
30% identity, 89% coverage: 13:463/506 of query aligns to 6:412/412 of 1o9oA
- active site: K62 (= K82), A131 (≠ S157), S132 (= S158), T150 (≠ S176), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ I184)
- binding 3-amino-3-oxopropanoic acid: G130 (= G156), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ I184), P359 (≠ Q401)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
30% identity, 89% coverage: 13:463/506 of query aligns to 6:412/412 of 1ocmA
- active site: K62 (= K82), S131 (= S157), S132 (= S158), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181)
- binding pyrophosphate 2-: R113 (= R137), S131 (= S157), Q151 (≠ D177), T152 (= T178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ I184), P359 (≠ Q401)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
27% identity, 77% coverage: 74:465/506 of query aligns to 83:464/605 of Q936X2
- K91 (= K82) mutation to A: Loss of activity.
- S165 (= S157) mutation to A: Loss of activity.
- S189 (= S181) mutation to A: Loss of activity.
Query Sequence
>WP_011798409.1 NCBI__GCF_000015505.1:WP_011798409.1
MNAEDLIALPATEMRRMIGARQLSPVELLNACIARIEAVNPYVNAVTATCFDRARTEARA
AEAAVMAGGPLGLLHGLPLGVKDLEDTEGLLTTHGSPIYRGNVPTRDNVLVARLRAAGAI
VTGKTNVPEMGAGANSRNPVWGATGNPFNPNLNAGGSSGGSAAALALDMLPVCTGSDTGG
SLRIPAAKCGVVGFRPSPGVVPSSRKPLGWTPISVVGPMGRTVADACLQLAATAGVSATD
PLTYEVDPLSFLLPQDLDLGGLRVGYTEDFGACAVDDGIRGVFREKIAAMRHLFRSCEPL
ALDLGEVHHCFDVLRAEAFVAGMRSAYERDPSSLGPNPRANYEMGAAMSLLDCAWAQAEQ
TRILARFQAAYCDVDIILAPTTPVSPFPWMLAHATHINGEQQENYYRWLSLTYVTTLTTH
PSLSLPCGTDHAGMPFGLQIVGRFRADRHTLGVAQAMERAFASSEALRRPRPNARSLRHA
EPALTSIVTAPPMLGGQASGMAASAV
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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