SitesBLAST
Comparing WP_011840201.1 NCBI__GCF_000015985.1:WP_011840201.1 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)
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, 87% coverage: 54:437/441 of query aligns to 180:588/607 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 (≠ G233) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 87% coverage: 54:437/441 of query aligns to 180:588/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A128), T258 (≠ G131), S281 (= S154), G302 (≠ T175), G303 (= G176), S305 (= S178), S472 (≠ R326), I532 (≠ V385), M539 (≠ L392)
Sites not aligning to the query:
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 100% coverage: 2:441/441 of query aligns to 23:491/507 of Q84DC4
- T31 (≠ A9) 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 (≠ I181) 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 (≠ A292) 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 (≠ E337) 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 (≠ L392) 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.
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
29% identity, 87% coverage: 54:437/441 of query aligns to 180:588/605 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 (≠ A292), I475 (≠ S329), M539 (≠ L392)
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, 87% coverage: 54:437/441 of query aligns to 180:588/605 of 8ey1D
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 96% coverage: 15:437/441 of query aligns to 15:473/485 of 2f2aA
- active site: K79 (= K79), S154 (= S154), S155 (= S155), S173 (= S173), T175 (= T175), G176 (= G176), G177 (= G177), S178 (= S178), Q181 (≠ I181)
- binding glutamine: G130 (≠ S130), S154 (= S154), D174 (= D174), T175 (= T175), G176 (= G176), S178 (= S178), F206 (≠ L206), Y309 (vs. gap), Y310 (vs. gap), R358 (vs. gap), D425 (≠ N388)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 96% coverage: 15:437/441 of query aligns to 15:473/485 of 2dqnA
- active site: K79 (= K79), S154 (= S154), S155 (= S155), S173 (= S173), T175 (= T175), G176 (= G176), G177 (= G177), S178 (= S178), Q181 (≠ I181)
- binding asparagine: M129 (≠ F129), G130 (≠ S130), T175 (= T175), G176 (= G176), S178 (= S178), Y309 (vs. gap), Y310 (vs. gap), R358 (vs. gap), D425 (≠ N388)
3kfuE Crystal structure of the transamidosome (see paper)
33% identity, 98% coverage: 8:439/441 of query aligns to 2:456/468 of 3kfuE
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
31% identity, 89% coverage: 42:435/441 of query aligns to 54:459/605 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.
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 99% coverage: 4:440/441 of query aligns to 2:469/478 of 3h0mA
- active site: K72 (= K79), S147 (= S154), S148 (= S155), S166 (= S173), T168 (= T175), G169 (= G176), G170 (= G177), S171 (= S178), Q174 (≠ I181)
- binding glutamine: M122 (≠ F129), G123 (≠ S130), D167 (= D174), T168 (= T175), G169 (= G176), G170 (= G177), S171 (= S178), F199 (≠ L206), Y302 (≠ A296), R351 (= R326), D418 (≠ E387)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 99% coverage: 4:440/441 of query aligns to 2:469/478 of 3h0lA
- active site: K72 (= K79), S147 (= S154), S148 (= S155), S166 (= S173), T168 (= T175), G169 (= G176), G170 (= G177), S171 (= S178), Q174 (≠ I181)
- binding asparagine: G123 (≠ S130), S147 (= S154), G169 (= G176), G170 (= G177), S171 (= S178), Y302 (≠ A296), R351 (= R326), D418 (≠ E387)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
38% identity, 54% coverage: 9:246/441 of query aligns to 9:252/487 of 1m21A
- active site: K81 (= K79), S160 (= S154), S161 (= S155), T179 (≠ S173), T181 (= T175), D182 (≠ G176), G183 (= G177), S184 (= S178), C187 (≠ I181)
- binding : A129 (= A128), N130 (≠ F129), F131 (vs. gap), C158 (= C143), G159 (= G153), S160 (= S154), S184 (= S178), C187 (≠ I181), I212 (≠ L206)
Sites not aligning to the query:
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
29% identity, 85% coverage: 69:441/441 of query aligns to 85:501/508 of 3a1iA
- active site: K95 (= K79), S170 (= S154), S171 (= S155), G189 (≠ S173), Q191 (≠ T175), G192 (= G176), G193 (= G177), A194 (≠ S178), I197 (= I181)
- binding benzamide: F145 (= F129), S146 (= S130), G147 (= G131), Q191 (≠ T175), G192 (= G176), G193 (= G177), A194 (≠ S178), W327 (vs. gap)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
39% identity, 53% coverage: 6:237/441 of query aligns to 1:233/457 of 6c6gA
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 82% coverage: 70:429/441 of query aligns to 63:430/461 of 4gysB
- active site: K72 (= K79), S146 (= S154), S147 (= S155), T165 (≠ S173), T167 (= T175), A168 (≠ G176), G169 (= G177), S170 (= S178), V173 (≠ I181)
- binding malonate ion: A120 (= A128), G122 (≠ S130), S146 (= S154), T167 (= T175), A168 (≠ G176), S170 (= S178), S193 (≠ A201), G194 (= G202), V195 (≠ T203), R200 (≠ A208), Y297 (≠ A296), R305 (≠ A304)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
27% identity, 98% coverage: 6:438/441 of query aligns to 5:445/457 of 5h6sC
- active site: K77 (= K79), S152 (= S154), S153 (= S155), L173 (≠ T175), G174 (= G176), G175 (= G177), S176 (= S178)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A128), R128 (≠ S130), W129 (≠ L134), S152 (= S154), L173 (≠ T175), G174 (= G176), S176 (= S178), W306 (vs. gap), F338 (≠ L324)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
35% identity, 53% coverage: 6:240/441 of query aligns to 5:245/564 of 6te4A
Sites not aligning to the query:
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)
40% identity, 34% coverage: 71:218/441 of query aligns to 28:177/425 of Q9FR37
- K36 (= K79) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S154) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S155) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D174) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S178) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ N186) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
25% identity, 98% coverage: 6:437/441 of query aligns to 2:398/412 of 1o9oA
- active site: K62 (= K79), A131 (vs. gap), S132 (vs. gap), T150 (≠ S173), T152 (= T175), G153 (= G176), G154 (= G177), S155 (= S178), R158 (≠ I181)
- binding 3-amino-3-oxopropanoic acid: G130 (vs. gap), T152 (= T175), G153 (= G176), G154 (= G177), S155 (= S178), R158 (≠ I181), P359 (≠ S382)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
27% identity, 98% coverage: 6:437/441 of query aligns to 2:398/412 of 1ocmA
- active site: K62 (= K79), S131 (= S154), S132 (= S155), T152 (= T175), G153 (= G176), G154 (= G177), S155 (= S178)
- binding pyrophosphate 2-: R113 (≠ L134), S131 (= S154), Q151 (≠ D174), T152 (= T175), G153 (= G176), G154 (= G177), S155 (= S178), R158 (≠ I181), P359 (≠ S382)
Query Sequence
>WP_011840201.1 NCBI__GCF_000015985.1:WP_011840201.1
MDRLWMTAAELGRGIEAGRIHPVELAEAFLAAAADHPEGTRIYARLCPTRARTEAMAAAE
RAKRGLRRGPLDGVPVSWKDLFDTAGVATEAGSALLKGRVPEEDAAVLGTATLGGLVCLG
KTHMSELAFSGLGLNPVTATPPCVNDPAAVAGGSSSGAAASVAFGLAPAAIGSDTGGSVR
IPAAWNDLAGLKTTAGRLSLAGTVPLAARFDTVGPLARTVEDCALLLAVLEGGRPADLRG
ASLAGRRFLVLETLALEDLREAPARGFEEAVARLARAGARIERGAAPEVVEAMAMAGPLF
TGEAYATWAEVIEGAPDLMFPRILERFRSGASITAVEFVTAWQRLEALRAAWAARTAGYD
AVLVPTSPILPPDAKRLLTDESYYVGENLLALRNTRIANLMGLPALTLPTGQPSCGISLM
GQPMGEERLLRLGAAAERALG
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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