SitesBLAST
Comparing WP_011651681.1 NCBI__GCF_000009265.1:WP_011651681.1 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)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
47% identity, 95% coverage: 16:481/493 of query aligns to 15:473/485 of 2f2aA
- active site: K79 (= K79), S154 (= S159), S155 (= S160), S173 (≠ T178), T175 (= T180), G176 (= G181), G177 (= G182), S178 (= S183), Q181 (= Q186)
- binding glutamine: G130 (= G130), S154 (= S159), D174 (= D179), T175 (= T180), G176 (= G181), S178 (= S183), F206 (= F211), Y309 (= Y314), Y310 (= Y315), R358 (= R362), D425 (= D432)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
47% identity, 95% coverage: 16:481/493 of query aligns to 15:473/485 of 2dqnA
- active site: K79 (= K79), S154 (= S159), S155 (= S160), S173 (≠ T178), T175 (= T180), G176 (= G181), G177 (= G182), S178 (= S183), Q181 (= Q186)
- binding asparagine: M129 (= M129), G130 (= G130), T175 (= T180), G176 (= G181), S178 (= S183), Y309 (= Y314), Y310 (= Y315), R358 (= R362), D425 (= D432)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
46% identity, 97% coverage: 8:487/493 of query aligns to 6:472/478 of 3h0mA
- active site: K72 (= K79), S147 (= S159), S148 (= S160), S166 (≠ T178), T168 (= T180), G169 (= G181), G170 (= G182), S171 (= S183), Q174 (= Q186)
- binding glutamine: M122 (= M129), G123 (= G130), D167 (= D179), T168 (= T180), G169 (= G181), G170 (= G182), S171 (= S183), F199 (= F211), Y302 (= Y314), R351 (= R362), D418 (= D432)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
46% identity, 97% coverage: 8:487/493 of query aligns to 6:472/478 of 3h0lA
- active site: K72 (= K79), S147 (= S159), S148 (= S160), S166 (≠ T178), T168 (= T180), G169 (= G181), G170 (= G182), S171 (= S183), Q174 (= Q186)
- binding asparagine: G123 (= G130), S147 (= S159), G169 (= G181), G170 (= G182), S171 (= S183), Y302 (= Y314), R351 (= R362), D418 (= D432)
3kfuE Crystal structure of the transamidosome (see paper)
43% identity, 97% coverage: 11:486/493 of query aligns to 4:459/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
36% identity, 82% coverage: 71:474/493 of query aligns to 30:443/450 of 4n0iA
- active site: K38 (= K79), S116 (= S159), S117 (= S160), T135 (= T178), T137 (= T180), G138 (= G181), G139 (= G182), S140 (= S183), L143 (≠ Q186)
- binding glutamine: G89 (= G130), T137 (= T180), G138 (= G181), S140 (= S183), Y168 (≠ F211), Y271 (= Y314), Y272 (= Y315), R320 (= R362), D404 (= D432)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
35% identity, 96% coverage: 9:482/493 of query aligns to 8:477/487 of 1m21A
- active site: K81 (= K79), S160 (= S159), S161 (= S160), T179 (= T178), T181 (= T180), D182 (≠ G181), G183 (= G182), S184 (= S183), C187 (≠ Q186)
- binding : A129 (= A128), N130 (≠ M129), F131 (≠ G130), C158 (≠ G157), G159 (= G158), S160 (= S159), S184 (= S183), C187 (≠ Q186), I212 (≠ F211), R318 (≠ Y315), L321 (≠ A318), L365 (≠ M364), F426 (≠ I433)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
31% identity, 98% coverage: 3:486/493 of query aligns to 24:492/507 of Q84DC4
- T31 (≠ A10) 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 (= S159) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S160) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G181) 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 (= Q186) 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 (≠ L311) 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 (≠ D376) 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 (= I433) 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.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
29% identity, 96% coverage: 7:481/493 of query aligns to 1:448/457 of 6c6gA
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 95% coverage: 17:484/493 of query aligns to 139:591/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A128), T258 (≠ S131), S281 (= S159), G302 (≠ T180), G303 (= G181), S305 (= S183), S472 (≠ T367), I532 (≠ L421), M539 (= M428)
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)
28% identity, 95% coverage: 17:484/493 of query aligns to 139:591/607 of Q7XJJ7
- K205 (≠ G86) mutation to A: Loss of activity.
- SS 281:282 (= SS 159:160) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 180:183) binding
- S305 (= S183) mutation to A: Loss of activity.
- R307 (= R185) mutation to A: Loss of activity.
- S360 (≠ V238) mutation to A: No effect.
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
30% identity, 86% coverage: 69:491/493 of query aligns to 85:508/508 of 3a1iA
- active site: K95 (= K79), S170 (= S159), S171 (= S160), G189 (≠ T178), Q191 (≠ T180), G192 (= G181), G193 (= G182), A194 (≠ S183), I197 (≠ Q186)
- binding benzamide: F145 (≠ M129), S146 (≠ G130), G147 (≠ S131), Q191 (≠ T180), G192 (= G181), G193 (= G182), A194 (≠ S183), W327 (≠ Y314)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
29% identity, 92% coverage: 10:465/493 of query aligns to 9:457/490 of 4yjiA
- active site: K79 (= K79), S158 (= S159), S159 (= S160), G179 (≠ T180), G180 (= G181), G181 (= G182), A182 (≠ S183)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L81), G132 (≠ A128), S158 (= S159), G179 (≠ T180), G180 (= G181), A182 (≠ S183)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 92% coverage: 17:470/493 of query aligns to 10:450/605 of Q936X2
- K91 (= K79) mutation to A: Loss of activity.
- S165 (≠ N151) mutation to A: Loss of activity.
- S189 (= S183) mutation to A: Loss of activity.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
26% identity, 99% coverage: 3:490/493 of query aligns to 1:456/457 of 5h6sC
- active site: K77 (= K79), S152 (= S159), S153 (= S160), L173 (≠ T180), G174 (= G181), G175 (= G182), S176 (= S183)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A128), R128 (≠ G130), W129 (≠ S131), S152 (= S159), L173 (≠ T180), G174 (= G181), S176 (= S183), W306 (≠ G296), F338 (≠ Y347)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 85% coverage: 56:473/493 of query aligns to 51:430/461 of 4gysB
- active site: K72 (= K79), S146 (= S159), S147 (= S160), T165 (= T178), T167 (= T180), A168 (≠ G181), G169 (= G182), S170 (= S183), V173 (≠ Q186)
- binding malonate ion: A120 (= A128), G122 (= G130), S146 (= S159), T167 (= T180), A168 (≠ G181), S170 (= S183), S193 (≠ W206), G194 (= G207), V195 (≠ T208), R200 (≠ S213), Y297 (= Y329), R305 (= R337)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
30% identity, 61% coverage: 3:305/493 of query aligns to 1:341/564 of 6te4A
Sites not aligning to the query:
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
31% identity, 51% coverage: 16:268/493 of query aligns to 14:259/482 of 3a2qA
- active site: K69 (= K79), S147 (= S159), S148 (= S160), N166 (≠ T178), A168 (≠ T180), A169 (≠ G181), G170 (= G182), A171 (≠ S183), I174 (≠ Q186)
- binding 6-aminohexanoic acid: G121 (≠ A128), G121 (≠ A128), N122 (≠ M129), S147 (= S159), A168 (≠ T180), A168 (≠ T180), A169 (≠ G181), A171 (≠ S183)
Sites not aligning to the query:
4do3A Structure of faah with a non-steroidal anti-inflammatory drug (see paper)
28% identity, 43% coverage: 14:225/493 of query aligns to 52:255/543 of 4do3A
- active site: K110 (= K79), S185 (= S159), S186 (= S160), T204 (= T178), I206 (≠ T180), G207 (= G181), G208 (= G182), S209 (= S183), F212 (≠ Q186)
- binding (2S)-2-(6-chloro-9H-carbazol-2-yl)propanoic acid: L160 (≠ M129)
- binding cyclohexane aminocarboxylic acid: L160 (≠ M129), I206 (≠ T180), G207 (= G181), S209 (= S183)
Sites not aligning to the query:
1mt5A Crystal structure of fatty acid amide hydrolase (see paper)
28% identity, 43% coverage: 14:225/493 of query aligns to 48:251/537 of 1mt5A
- active site: K106 (= K79), S181 (= S159), S182 (= S160), T200 (= T178), I202 (≠ T180), G203 (= G181), G204 (= G182), S205 (= S183), F208 (≠ Q186)
- binding methyl arachidonyl fluorophosphonate: M155 (≠ A128), L156 (≠ M129), S157 (≠ G130), S181 (= S159), D201 (= D179), I202 (≠ T180), G203 (= G181), S205 (= S183)
Sites not aligning to the query:
Query Sequence
>WP_011651681.1 NCBI__GCF_000009265.1:WP_011651681.1
MSELTSLTIAEARQKLRAKEITAIELTEAYISAIDAANGRLNAYIKVTPDLARVMAKNSD
ERIAAGKAGELEGIPLGIKDLFATVGVHTQACSHILDGFEPRYESTVTQNLWDDGAVMLG
KLNMDEFAMGSSNETSYYGPVINPWRAAGSNQQLVPGGSSGGSAAAVAAHLCAGATATDT
GGSIRQPAAFTGTVGIKPTYGRCSRWGTVAFASSLDQAGPIARDVRDAAILLKSMASVDA
KDTTSVDLPVPDYEAALGQSLKGMKIGIPNEYRVDGMPDEIETLWRQGIAWLKEAGAEIV
DISLPHTKYALPAYYIVAPAEASSNLARYDGVRYGLRVDGKDIVDMYEKTRAAGFGKEVK
RRIMIGTYVLSAGYYDAYYIRAQKVRTLIKRDFELAFDAGVDAILTPATPSSAFGVADEN
LAADPVKMYLNDIFTVTVNMAGLPGIAVPAGLDHKGLPLGLQLIGKPFDEETLFKTAHVI
EQAAGRFTPAKWW
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