SitesBLAST
Comparing WP_084276351.1 NCBI__GCF_900176045.1:WP_084276351.1 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)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
58% identity, 88% coverage: 44:432/443 of query aligns to 66:460/478 of 3h0mA
- active site: K72 (= K50), S147 (= S125), S148 (= S126), S166 (= S144), T168 (= T146), G169 (= G147), G170 (= G148), S171 (= S149), Q174 (= Q152)
- binding glutamine: M122 (= M100), G123 (= G101), D167 (= D145), T168 (= T146), G169 (= G147), G170 (= G148), S171 (= S149), F199 (≠ Y177), Y302 (= Y276), R351 (= R324), D418 (= D390)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
58% identity, 88% coverage: 44:432/443 of query aligns to 66:460/478 of 3h0lA
- active site: K72 (= K50), S147 (= S125), S148 (= S126), S166 (= S144), T168 (= T146), G169 (= G147), G170 (= G148), S171 (= S149), Q174 (= Q152)
- binding asparagine: G123 (= G101), S147 (= S125), G169 (= G147), G170 (= G148), S171 (= S149), Y302 (= Y276), R351 (= R324), D418 (= D390)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
54% identity, 98% coverage: 3:438/443 of query aligns to 39:473/485 of 2f2aA
- active site: K79 (= K50), S154 (= S125), S155 (= S126), S173 (= S144), T175 (= T146), G176 (= G147), G177 (= G148), S178 (= S149), Q181 (= Q152)
- binding glutamine: G130 (= G101), S154 (= S125), D174 (= D145), T175 (= T146), G176 (= G147), S178 (= S149), F206 (≠ Y177), Y309 (= Y276), Y310 (= Y277), R358 (= R324), D425 (= D390)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
54% identity, 98% coverage: 3:438/443 of query aligns to 39:473/485 of 2dqnA
- active site: K79 (= K50), S154 (= S125), S155 (= S126), S173 (= S144), T175 (= T146), G176 (= G147), G177 (= G148), S178 (= S149), Q181 (= Q152)
- binding asparagine: M129 (= M100), G130 (= G101), T175 (= T146), G176 (= G147), S178 (= S149), Y309 (= Y276), Y310 (= Y277), R358 (= R324), D425 (= D390)
3kfuE Crystal structure of the transamidosome (see paper)
50% identity, 89% coverage: 44:438/443 of query aligns to 59:454/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
35% identity, 95% coverage: 18:437/443 of query aligns to 2:449/450 of 4n0iA
- active site: K38 (= K50), S116 (= S125), S117 (= S126), T135 (≠ S144), T137 (= T146), G138 (= G147), G139 (= G148), S140 (= S149), L143 (≠ Q152)
- binding glutamine: G89 (= G101), T137 (= T146), G138 (= G147), S140 (= S149), Y168 (= Y177), Y271 (= Y276), Y272 (= Y277), R320 (= R324), D404 (= D390)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
32% identity, 90% coverage: 43:440/443 of query aligns to 198:590/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A99), T258 (≠ S102), S281 (= S125), G302 (≠ T146), G303 (= G147), S305 (= S149), S472 (≠ T329), I532 (≠ S382), M539 (≠ S389)
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, 90% coverage: 43:440/443 of query aligns to 198:590/607 of Q7XJJ7
- K205 (= K50) mutation to A: Loss of activity.
- SS 281:282 (= SS 125:126) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 146:149) binding substrate
- S305 (= S149) mutation to A: Loss of activity.
- R307 (= R151) mutation to A: Loss of activity.
- S360 (≠ V204) 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, 90% coverage: 43:440/443 of query aligns to 198:590/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A99), G302 (≠ T146), G303 (= G147), G304 (= G148), A305 (≠ S149), V442 (≠ Y277), I475 (≠ L332), M539 (≠ S389)
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, 90% coverage: 43:440/443 of query aligns to 198:590/605 of 8ey1D
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
32% identity, 89% coverage: 44:438/443 of query aligns to 68:448/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
30% identity, 96% coverage: 17:443/443 of query aligns to 48:481/487 of 1m21A
- active site: K81 (= K50), S160 (= S125), S161 (= S126), T179 (≠ S144), T181 (= T146), D182 (≠ G147), G183 (= G148), S184 (= S149), C187 (≠ Q152)
- binding : A129 (= A99), N130 (≠ M100), F131 (≠ G101), C158 (≠ G123), G159 (= G124), S160 (= S125), S184 (= S149), C187 (≠ Q152), I212 (≠ Y177), R318 (≠ Y277), L321 (≠ A280), L365 (= L326), F426 (≠ Y387)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 99% coverage: 2:441/443 of query aligns to 28:490/507 of Q84DC4
- T31 (≠ K5) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K50) mutation to A: Abolishes activity on mandelamide.
- S180 (= S125) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S126) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G147) 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 (= S149) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q152) 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 (≠ D272) 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 (≠ D338) 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 (≠ V391) 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.
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
30% identity, 89% coverage: 47:440/443 of query aligns to 92:499/508 of 3a1iA
- active site: K95 (= K50), S170 (= S125), S171 (= S126), G189 (≠ S144), Q191 (≠ T146), G192 (= G147), G193 (= G148), A194 (≠ S149), I197 (≠ Q152)
- binding benzamide: F145 (≠ M100), S146 (≠ G101), G147 (≠ S102), Q191 (≠ T146), G192 (= G147), G193 (= G148), A194 (≠ S149), W327 (vs. gap)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 90% coverage: 43:439/443 of query aligns to 70:445/457 of 5h6sC
- active site: K77 (= K50), S152 (= S125), S153 (= S126), L173 (≠ T146), G174 (= G147), G175 (= G148), S176 (= S149)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A99), R128 (≠ G101), W129 (≠ S102), S152 (= S125), L173 (≠ T146), G174 (= G147), S176 (= S149), W306 (≠ L288), F338 (≠ L327)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
31% identity, 87% coverage: 44:427/443 of query aligns to 85:450/605 of Q936X2
- K91 (= K50) mutation to A: Loss of activity.
- S165 (= S125) mutation to A: Loss of activity.
- S189 (= S149) mutation to A: Loss of activity.
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)
36% identity, 49% coverage: 44:262/443 of query aligns to 136:361/579 of Q9TUI8
- S217 (= S125) mutation to A: Loss of activity.
- S218 (= S126) mutation to A: Lowers activity by at least 98%.
- D237 (= D145) mutation D->E,N: Loss of activity.
- S241 (= S149) mutation to A: Loss of activity.
- C249 (= C157) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 93% coverage: 28:439/443 of query aligns to 50:439/461 of 4gysB
- active site: K72 (= K50), S146 (= S125), S147 (= S126), T165 (≠ S144), T167 (= T146), A168 (≠ G147), G169 (= G148), S170 (= S149), V173 (≠ Q152)
- binding malonate ion: A120 (= A99), G122 (= G101), S146 (= S125), T167 (= T146), A168 (≠ G147), S170 (= S149), S193 (≠ Y172), G194 (= G173), V195 (≠ L174), R200 (≠ S179), Y297 (= Y291), R305 (= R299)
4hbpA Crystal structure of faah in complex with inhibitor (see paper)
34% identity, 49% coverage: 44:262/443 of query aligns to 94:319/531 of 4hbpA
- active site: K100 (= K50), S175 (= S125), S176 (= S126), T194 (≠ S144), I196 (≠ T146), G197 (= G147), G198 (= G148), S199 (= S149), F202 (≠ Q152)
- binding 4-(3-phenyl-1,2,4-thiadiazol-5-yl)-N-(pyridin-3-yl)piperazine-1-carboxamide: S151 (≠ G101), F152 (≠ S102), I196 (≠ T146), G197 (= G147), S199 (= S149)
Sites not aligning to the query:
4do3A Structure of faah with a non-steroidal anti-inflammatory drug (see paper)
34% identity, 49% coverage: 44:262/443 of query aligns to 104:329/543 of 4do3A
- active site: K110 (= K50), S185 (= S125), S186 (= S126), T204 (≠ S144), I206 (≠ T146), G207 (= G147), G208 (= G148), S209 (= S149), F212 (≠ Q152)
- binding (2S)-2-(6-chloro-9H-carbazol-2-yl)propanoic acid: L160 (≠ M100)
- binding cyclohexane aminocarboxylic acid: L160 (≠ M100), I206 (≠ T146), G207 (= G147), S209 (= S149)
Sites not aligning to the query:
Query Sequence
>WP_084276351.1 NCBI__GCF_900176045.1:WP_084276351.1
MITLKEALQLPKEELEEIKKDLIKKAKEQKELNAYIALDSAGEGVPIAIKDNIQVDGWEV
TCASKILQGYIAPYDATVIEKLKSAGCAPFGRTNMDEFAMGSTTESSCYGKTLNPRDPSR
VPGGSSGGSAAVVAAGIAIAALGSDTGGSIRQPAAFCGIVGMKPTYGRVSRYGLAAYGSS
LDQIGPMTQNVEDAIILYNMIAGVDERDSTSARVPFEPVVPNADRKLTIGVVPNYVKDAS
AAVQKAYDKAVAALKEAGHEIVEVSLMDAKYDIASYYITAMAEASTNLSRYDGVRYGYRA
EASNLKEMYKKTRSEGFGEEVKRRILLGTFVLSSGYYDAYYIKAQRVRHLIKDEYSKVFE
KVDLILSPVAPDVAYKFGELKSPLEMYLSDVYTIGVNLAGLPAISLPVDEHEGLPVGLQL
IGKAFDEQTLFDGAMSLERVVRS
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