SitesBLAST
Comparing WP_086508848.1 NCBI__GCF_002151265.1:WP_086508848.1 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)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 96% coverage: 11:458/467 of query aligns to 30:494/507 of Q84DC4
- T31 (≠ R12) 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 (≠ T155) mutation to A: Significantly decreases activity on mandelamide.
- S181 (≠ P156) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ A181) 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 (= S183) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I186) 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 (≠ F305) 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 (≠ L402) 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.
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
28% identity, 87% coverage: 47:451/467 of query aligns to 170:588/607 of Q7XJJ7
- K205 (= K82) mutation to A: Loss of activity.
- SS 281:282 (= SS 159:160) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TAGS 180:183) binding
- S305 (= S183) mutation to A: Loss of activity.
- R307 (= R185) mutation to A: Loss of activity.
- S360 (vs. gap) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 87% coverage: 47:451/467 of query aligns to 170:588/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A131), T258 (≠ G134), S281 (= S159), G302 (≠ T180), G303 (≠ A181), S305 (= S183), S472 (≠ P332), I532 (≠ P395), M539 (≠ L402)
Sites not aligning to the query:
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 96% coverage: 9:454/467 of query aligns to 5:469/478 of 3h0mA
- active site: K72 (= K82), S147 (= S159), S148 (= S160), S166 (≠ T178), T168 (= T180), G169 (≠ A181), G170 (= G182), S171 (= S183), Q174 (≠ I186)
- binding glutamine: M122 (≠ F132), G123 (= G133), D167 (= D179), T168 (= T180), G169 (≠ A181), G170 (= G182), S171 (= S183), F199 (≠ L211), Y302 (≠ F305), R351 (= R337), D418 (≠ A397)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 96% coverage: 9:454/467 of query aligns to 5:469/478 of 3h0lA
- active site: K72 (= K82), S147 (= S159), S148 (= S160), S166 (≠ T178), T168 (= T180), G169 (≠ A181), G170 (= G182), S171 (= S183), Q174 (≠ I186)
- binding asparagine: G123 (= G133), S147 (= S159), G169 (≠ A181), G170 (= G182), S171 (= S183), Y302 (≠ F305), R351 (= R337), D418 (≠ A397)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
33% identity, 90% coverage: 38:457/467 of query aligns to 44:468/605 of Q936X2
- K91 (= K82) mutation to A: Loss of activity.
- S165 (= S159) mutation to A: Loss of activity.
- S189 (= S183) mutation to A: Loss of activity.
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
28% identity, 88% coverage: 45:453/467 of query aligns to 42:475/485 of 2f2aA
- active site: K79 (= K82), S154 (= S159), S155 (= S160), S173 (≠ T178), T175 (= T180), G176 (≠ A181), G177 (= G182), S178 (= S183), Q181 (≠ I186)
- binding glutamine: G130 (= G133), S154 (= S159), D174 (= D179), T175 (= T180), G176 (≠ A181), S178 (= S183), F206 (≠ L211), Y309 (≠ K307), Y310 (≠ G308), R358 (= R337), D425 (≠ A397)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
28% identity, 88% coverage: 45:453/467 of query aligns to 42:475/485 of 2dqnA
- active site: K79 (= K82), S154 (= S159), S155 (= S160), S173 (≠ T178), T175 (= T180), G176 (≠ A181), G177 (= G182), S178 (= S183), Q181 (≠ I186)
- binding asparagine: M129 (≠ F132), G130 (= G133), T175 (= T180), G176 (≠ A181), S178 (= S183), Y309 (≠ K307), Y310 (≠ G308), R358 (= R337), D425 (≠ A397)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
29% identity, 93% coverage: 20:451/467 of query aligns to 12:448/457 of 6c6gA
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 87% coverage: 52:459/467 of query aligns to 45:448/461 of 4gysB
- active site: K72 (= K82), S146 (= S159), S147 (= S160), T165 (= T178), T167 (= T180), A168 (= A181), G169 (= G182), S170 (= S183), V173 (≠ I186)
- binding malonate ion: A120 (= A131), G122 (= G133), S146 (= S159), T167 (= T180), A168 (= A181), S170 (= S183), S193 (≠ Q206), G194 (≠ Q207), V195 (≠ I208), R200 (≠ T213), Y297 (≠ Q306), R305 (≠ E314)
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)
26% identity, 82% coverage: 74:454/467 of query aligns to 28:425/425 of Q9FR37
- K36 (= K82) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S159) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S160) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D179) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S183) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (≠ T191) mutation C->A,S: Reduces catalytic activity 10-fold.
- S214 (≠ G258) mutation to T: Slightly reduces catalytic activity.
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
29% identity, 82% coverage: 73:453/467 of query aligns to 72:478/487 of 1m21A
- active site: K81 (= K82), S160 (= S159), S161 (= S160), T179 (= T178), T181 (= T180), D182 (≠ A181), G183 (= G182), S184 (= S183), C187 (≠ I186)
- binding : A129 (= A131), N130 (vs. gap), F131 (= F132), C158 (≠ G157), G159 (= G158), S160 (= S159), S184 (= S183), C187 (≠ I186), I212 (≠ L211), R318 (≠ E300), L321 (≠ E303), L365 (≠ V334), F426 (≠ Y394)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
26% identity, 83% coverage: 72:458/467 of query aligns to 85:504/508 of 3a1iA
- active site: K95 (= K82), S170 (= S159), S171 (= S160), G189 (≠ T178), Q191 (≠ T180), G192 (≠ A181), G193 (= G182), A194 (≠ S183), I197 (= I186)
- binding benzamide: F145 (= F132), S146 (≠ G133), G147 (= G134), Q191 (≠ T180), G192 (≠ A181), G193 (= G182), A194 (≠ S183), W327 (≠ F305)
3kfuE Crystal structure of the transamidosome (see paper)
34% identity, 83% coverage: 66:451/467 of query aligns to 48:454/468 of 3kfuE
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 88% coverage: 44:453/467 of query aligns to 40:446/457 of 5h6sC
- active site: K77 (= K82), S152 (= S159), S153 (= S160), L173 (≠ T180), G174 (≠ A181), G175 (= G182), S176 (= S183)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A131), R128 (≠ G133), W129 (≠ G134), S152 (= S159), L173 (≠ T180), G174 (≠ A181), S176 (= S183), W306 (≠ F305), F338 (≠ M344)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
30% identity, 85% coverage: 56:454/467 of query aligns to 38:410/412 of 1o9oA
- active site: K62 (= K82), A131 (≠ S159), S132 (= S160), T150 (= T178), T152 (= T180), G153 (≠ A181), G154 (= G182), S155 (= S183), R158 (≠ I186)
- binding 3-amino-3-oxopropanoic acid: G130 (= G158), T152 (= T180), G153 (≠ A181), G154 (= G182), S155 (= S183), R158 (≠ I186), P359 (= P395)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
29% identity, 85% coverage: 56:454/467 of query aligns to 38:410/412 of 1ocmA
- active site: K62 (= K82), S131 (≠ A163), S132 (≠ G164), T152 (= T180), G153 (≠ A181), G154 (= G182), S155 (= S183)
- binding pyrophosphate 2-: R113 (= R145), S131 (≠ A163), Q151 (≠ D179), T152 (= T180), G153 (≠ A181), G154 (= G182), S155 (= S183), R158 (≠ I186), P359 (= P395)
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)
25% identity, 96% coverage: 10:457/467 of query aligns to 78:575/579 of Q9TUI8
- S217 (≠ G157) mutation to A: Loss of activity.
- S218 (≠ G158) mutation to A: Lowers activity by at least 98%.
- D237 (= D179) mutation D->E,N: Loss of activity.
- S241 (= S183) mutation to A: Loss of activity.
- C249 (≠ T191) mutation to A: Loss of activity.
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
33% identity, 52% coverage: 7:250/467 of query aligns to 3:238/482 of 3a2qA
- active site: K69 (= K82), S147 (= S159), S148 (= S160), N166 (≠ T178), A168 (≠ T180), A169 (= A181), G170 (= G182), A171 (≠ S183), I174 (= I186)
- binding 6-aminohexanoic acid: G121 (≠ A131), G121 (≠ A131), N122 (≠ F132), S147 (= S159), A168 (≠ T180), A168 (≠ T180), A169 (= A181), A171 (≠ S183)
Sites not aligning to the query:
4hbpA Crystal structure of faah in complex with inhibitor (see paper)
23% identity, 84% coverage: 60:451/467 of query aligns to 78:527/531 of 4hbpA
- active site: K100 (= K82), S175 (≠ G157), S176 (≠ G158), T194 (= T178), I196 (≠ T180), G197 (≠ A181), G198 (= G182), S199 (= S183), F202 (≠ I186)
- binding 4-(3-phenyl-1,2,4-thiadiazol-5-yl)-N-(pyridin-3-yl)piperazine-1-carboxamide: S151 (≠ G133), F152 (≠ G134), I196 (≠ T180), G197 (≠ A181), S199 (= S183), F339 (≠ A311), M394 (≠ L359), T446 (= T377)
Query Sequence
>WP_086508848.1 NCBI__GCF_002151265.1:WP_086508848.1
MTTNSPLLQPLRQQAAALRNGTLSASELAEAACAAYASRGKHDNAYLTWQGEAALAFARA
TDALIAQGGDSGPLMGIPVSIKDIYAVPGLPTYAGSSRRLPASWERPGPIVEALLAQLPS
LMGKTHTVEFAFGGLGTNAHWGAPRNPWDSQAHRTPGGSSSGAGVSLISGTAGLALGTDT
AGSVRIPASMTGVAGLKTTAGRWPAQQIVPLSTTLDTPGLLARRVDDLAYAFDALDANLS
PRPSPVSATPELADLTFGVPESFFWDDCSPGIAEAVQQAIRQLEAAGARVVTLELPNTDE
AYELFQKGGLAAAELAAFLKAELPEMEDALDPNVAARIRAADDMPAWEYVRRRSLLDELC
TAATERMGQVDAVLTPTVAITPPTLESLEPEGAYPKANMKALRNTVMANFMGLCGLTLPV
GRDAAGMPVGLQVLAGPWQEARLLAIGQAIEAKLGTGPDILGEPSAP
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