SitesBLAST
Comparing WP_011388738.1 NCBI__GCF_000013085.1:WP_011388738.1 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)
3kfuE Crystal structure of the transamidosome (see paper)
36% identity, 95% coverage: 9:470/485 of query aligns to 1:457/468 of 3kfuE
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
30% identity, 92% coverage: 20:467/485 of query aligns to 15:473/485 of 2f2aA
- active site: K79 (= K85), S154 (= S160), S155 (= S161), S173 (= S179), T175 (≠ M181), G176 (≠ M182), G177 (= G183), S178 (= S184), Q181 (≠ N187)
- binding glutamine: G130 (= G136), S154 (= S160), D174 (= D180), T175 (≠ M181), G176 (≠ M182), S178 (= S184), F206 (= F213), Y309 (≠ L314), Y310 (≠ W315), R358 (vs. gap), D425 (= D412)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
30% identity, 92% coverage: 20:467/485 of query aligns to 15:473/485 of 2dqnA
- active site: K79 (= K85), S154 (= S160), S155 (= S161), S173 (= S179), T175 (≠ M181), G176 (≠ M182), G177 (= G183), S178 (= S184), Q181 (≠ N187)
- binding asparagine: M129 (≠ L135), G130 (= G136), T175 (≠ M181), G176 (≠ M182), S178 (= S184), Y309 (≠ L314), Y310 (≠ W315), R358 (vs. gap), D425 (= D412)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
30% identity, 94% coverage: 20:477/485 of query aligns to 15:489/490 of 4yjiA
- active site: K79 (= K85), S158 (= S160), S159 (= S161), G179 (≠ M181), G180 (≠ M182), G181 (= G183), A182 (≠ S184)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L87), G132 (= G134), S158 (= S160), G179 (≠ M181), G180 (≠ M182), A182 (≠ S184)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
30% identity, 91% coverage: 25:467/485 of query aligns to 19:466/478 of 3h0mA
- active site: K72 (= K85), S147 (= S160), S148 (= S161), S166 (= S179), T168 (≠ M181), G169 (≠ M182), G170 (= G183), S171 (= S184), Q174 (≠ N187)
- binding glutamine: M122 (≠ L135), G123 (= G136), D167 (= D180), T168 (≠ M181), G169 (≠ M182), G170 (= G183), S171 (= S184), F199 (= F213), Y302 (≠ A317), R351 (vs. gap), D418 (= D412)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
30% identity, 91% coverage: 25:467/485 of query aligns to 19:466/478 of 3h0lA
- active site: K72 (= K85), S147 (= S160), S148 (= S161), S166 (= S179), T168 (≠ M181), G169 (≠ M182), G170 (= G183), S171 (= S184), Q174 (≠ N187)
- binding asparagine: G123 (= G136), S147 (= S160), G169 (≠ M182), G170 (= G183), S171 (= S184), Y302 (≠ A317), R351 (vs. gap), D418 (= D412)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 96% coverage: 13:480/485 of query aligns to 7:450/457 of 5h6sC
- active site: K77 (= K85), S152 (= S160), S153 (= S161), L173 (≠ M181), G174 (≠ M182), G175 (= G183), S176 (= S184)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G134), R128 (≠ G136), W129 (≠ S137), S152 (= S160), L173 (≠ M181), G174 (≠ M182), S176 (= S184), W306 (= W318), F338 (= F349)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
31% identity, 92% coverage: 20:464/485 of query aligns to 37:484/507 of Q84DC4
- K100 (= K85) mutation to A: Abolishes activity on mandelamide.
- S180 (= S160) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S161) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ M182) 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 (= S184) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ N187) 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 (vs. gap) 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 (≠ S366) 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 (≠ M418) 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.
Sites not aligning to the query:
- 31 T→I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
26% identity, 86% coverage: 53:467/485 of query aligns to 173:588/607 of Q7XJJ7
- K205 (= K85) mutation to A: Loss of activity.
- SS 281:282 (= SS 160:161) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ MMGS 181:184) binding substrate
- S305 (= S184) mutation to A: Loss of activity.
- R307 (= R186) mutation to A: Loss of activity.
- S360 (≠ F240) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
26% identity, 86% coverage: 53:467/485 of query aligns to 173:588/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G134), T258 (≠ S137), S281 (= S160), G302 (≠ M181), G303 (≠ M182), S305 (= S184), S472 (≠ E350), I532 (≠ M411), M539 (= M418)
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
26% identity, 86% coverage: 53:467/485 of query aligns to 173:588/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (= G134), G302 (≠ M181), G303 (≠ M182), G304 (= G183), A305 (≠ S184), V442 (≠ T319), I475 (≠ R353), M539 (= M418)
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
26% identity, 86% coverage: 53:467/485 of query aligns to 173:588/605 of 8ey1D
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
30% identity, 81% coverage: 73:467/485 of query aligns to 83:497/508 of 3a1iA
- active site: K95 (= K85), S170 (= S160), S171 (= S161), G189 (≠ S179), Q191 (≠ M181), G192 (≠ M182), G193 (= G183), A194 (≠ S184), I197 (≠ N187)
- binding benzamide: F145 (≠ L135), S146 (≠ G136), G147 (≠ S137), Q191 (≠ M181), G192 (≠ M182), G193 (= G183), A194 (≠ S184), W327 (= W315)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
31% identity, 90% coverage: 25:461/485 of query aligns to 15:442/457 of 6c6gA
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
29% identity, 96% coverage: 12:477/485 of query aligns to 6:478/482 of 3a2qA
- active site: K69 (= K85), S147 (= S160), S148 (= S161), N166 (≠ S179), A168 (≠ M181), A169 (≠ M182), G170 (= G183), A171 (≠ S184), I174 (≠ N187)
- binding 6-aminohexanoic acid: G121 (= G134), G121 (= G134), N122 (≠ L135), S147 (= S160), A168 (≠ M181), A168 (≠ M181), A169 (≠ M182), A171 (≠ S184), C313 (≠ R322)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
31% identity, 90% coverage: 26:463/485 of query aligns to 17:434/461 of 4gysB
- active site: K72 (= K85), S146 (= S160), S147 (= S161), T165 (≠ S179), T167 (≠ M181), A168 (≠ M182), G169 (= G183), S170 (= S184), V173 (≠ N187)
- binding malonate ion: A120 (≠ G134), G122 (= G136), S146 (= S160), T167 (≠ M181), A168 (≠ M182), S170 (= S184), S193 (≠ H206), G194 (= G207), V195 (= V208), R200 (≠ Q215), Y297 (≠ W315), R305 (= R322)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
37% identity, 44% coverage: 35:247/485 of query aligns to 33:246/487 of 1m21A
- active site: K81 (= K85), S160 (= S160), S161 (= S161), T179 (≠ S179), T181 (≠ M181), D182 (≠ M182), G183 (= G183), S184 (= S184), C187 (≠ N187)
- binding : A129 (≠ G134), N130 (vs. gap), F131 (vs. gap), C158 (≠ G158), G159 (= G159), S160 (= S160), S184 (= S184), C187 (≠ N187), I212 (≠ D211)
Sites not aligning to the query:
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
36% identity, 44% coverage: 29:241/485 of query aligns to 23:240/564 of 6te4A
Sites not aligning to the query:
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
27% identity, 93% coverage: 29:479/485 of query aligns to 37:476/605 of Q936X2
- K91 (= K85) mutation to A: Loss of activity.
- S165 (= S160) mutation to A: Loss of activity.
- S189 (= S184) 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)
32% identity, 34% coverage: 65:227/485 of query aligns to 122:287/579 of Q9TUI8
- S217 (= S160) mutation to A: Loss of activity.
- S218 (= S161) mutation to A: Lowers activity by at least 98%.
- D237 (= D180) mutation D->E,N: Loss of activity.
- S241 (= S184) mutation to A: Loss of activity.
- C249 (≠ N192) mutation to A: Loss of activity.
Query Sequence
>WP_011388738.1 NCBI__GCF_000013085.1:WP_011388738.1
MSPDPDDILAGDARALSRRIHHRAVSCREVMAATLARIDRFNPAVTALVSLRDREDLLRE
ADAKDALLGKGLSQGPLHGFPQAPKDLAATRGIATTRGSPLFRHQIPKQDAIFVERLRAG
GAIFVGKTNTPEFGLGSQTYNPVFGATGNAYDPRLTAGGSSGGAACALALGMLAVADGSD
MMGSLRNPAAFNNVFGFRPSAGRVPHGVVPDLFFQQLGYDGPMGRSVADLALLLSVMAGF
DARAPQSLAGDPAVFAQPLEGSVAGVRVGWLGDLGGYLAFEPGILELCQGALATLGDLGC
VVDEATAGFPLDALWTAWTDLRSFLVAGDLGPLYADPVKRAQMKPEAIFEIERGLALSGP
QVFAASARRSAWYRRMLVLFERFDVLALPSAQVFPFEHATPWPRAIAGRTMDSYHRWMEV
VVPASMAGVPVISVPVGFNAAGLPMGLQVIGKPRDDLSLLRLAHAYDLATRWPARRPPPV
LSPAS
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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