SitesBLAST
Comparing AO353_25440 FitnessBrowser__pseudo3_N2E3:AO353_25440 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)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
30% identity, 95% coverage: 14:473/483 of query aligns to 8:478/490 of 4yjiA
- active site: K79 (= K86), S158 (= S161), S159 (= S162), G179 (≠ M182), G180 (≠ M183), G181 (= G184), A182 (≠ S185)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L88), G132 (= G135), S158 (= S161), G179 (≠ M182), G180 (≠ M183), A182 (≠ S185)
3kfuE Crystal structure of the transamidosome (see paper)
34% identity, 95% coverage: 14:471/483 of query aligns to 2:457/468 of 3kfuE
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 96% coverage: 16:478/483 of query aligns to 9:476/478 of 3h0mA
- active site: K72 (= K86), S147 (= S161), S148 (= S162), S166 (= S180), T168 (≠ M182), G169 (≠ M183), G170 (= G184), S171 (= S185), Q174 (≠ N188)
- binding glutamine: M122 (≠ L136), G123 (= G137), D167 (= D181), T168 (≠ M182), G169 (≠ M183), G170 (= G184), S171 (= S185), F199 (= F207), Y302 (≠ H324), R351 (≠ G355), D418 (= D413)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 96% coverage: 16:478/483 of query aligns to 9:476/478 of 3h0lA
- active site: K72 (= K86), S147 (= S161), S148 (= S162), S166 (= S180), T168 (≠ M182), G169 (≠ M183), G170 (= G184), S171 (= S185), Q174 (≠ N188)
- binding asparagine: G123 (= G137), S147 (= S161), G169 (≠ M183), G170 (= G184), S171 (= S185), Y302 (≠ H324), R351 (≠ G355), D418 (= D413)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
28% identity, 94% coverage: 14:468/483 of query aligns to 8:473/485 of 2f2aA
- active site: K79 (= K86), S154 (= S161), S155 (= S162), S173 (= S180), T175 (≠ M182), G176 (≠ M183), G177 (= G184), S178 (= S185), Q181 (≠ N188)
- binding glutamine: G130 (= G137), S154 (= S161), D174 (= D181), T175 (≠ M182), G176 (≠ M183), S178 (= S185), F206 (= F214), Y309 (≠ W325), Y310 (≠ M326), R358 (vs. gap), D425 (≠ S411)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
28% identity, 94% coverage: 14:468/483 of query aligns to 8:473/485 of 2dqnA
- active site: K79 (= K86), S154 (= S161), S155 (= S162), S173 (= S180), T175 (≠ M182), G176 (≠ M183), G177 (= G184), S178 (= S185), Q181 (≠ N188)
- binding asparagine: M129 (≠ L136), G130 (= G137), T175 (≠ M182), G176 (≠ M183), S178 (= S185), Y309 (≠ W325), Y310 (≠ M326), R358 (vs. gap), D425 (≠ S411)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 98% coverage: 8:480/483 of query aligns to 27:496/507 of Q84DC4
- T31 (≠ L12) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K86) mutation to A: Abolishes activity on mandelamide.
- S180 (= S161) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S162) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ M183) 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 (= S185) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ N188) 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 (≠ A360) 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 (≠ M419) 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, 96% coverage: 5:469/483 of query aligns to 122:589/607 of Q7XJJ7
- K205 (= K86) mutation to A: Loss of activity.
- SS 281:282 (= SS 161:162) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ MMGS 182:185) binding
- S305 (= S185) mutation to A: Loss of activity.
- R307 (= R187) mutation to A: Loss of activity.
- S360 (≠ A241) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 96% coverage: 5:469/483 of query aligns to 122:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G135), T258 (≠ S138), S281 (= S161), G302 (≠ M182), G303 (≠ M183), S305 (= S185), S472 (≠ G355), I532 (= I407), M539 (= M419)
Sites not aligning to the query:
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
26% identity, 97% coverage: 8:475/483 of query aligns to 1:451/457 of 5h6sC
- active site: K77 (= K86), S152 (= S161), S153 (= S162), L173 (≠ M182), G174 (≠ M183), G175 (= G184), S176 (= S185)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G135), R128 (≠ G137), W129 (≠ S138), S152 (= S161), L173 (≠ M182), G174 (≠ M183), S176 (= S185), W306 (≠ D295), F338 (≠ G332)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
27% identity, 96% coverage: 18:481/483 of query aligns to 11:481/482 of 3a2qA
- active site: K69 (= K86), S147 (= S161), S148 (= S162), N166 (≠ S180), A168 (≠ M182), A169 (≠ M183), G170 (= G184), A171 (≠ S185), I174 (≠ N188)
- binding 6-aminohexanoic acid: G121 (= G135), G121 (= G135), N122 (≠ L136), S147 (= S161), A168 (≠ M182), A168 (≠ M182), A169 (≠ M183), A171 (≠ S185), C313 (≠ R323)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
30% identity, 93% coverage: 25:472/483 of query aligns to 19:480/487 of 1m21A
- active site: K81 (= K86), S160 (= S161), S161 (= S162), T179 (≠ S180), T181 (≠ M182), D182 (≠ M183), G183 (= G184), S184 (= S185), C187 (≠ N188)
- binding : A129 (≠ G135), N130 (vs. gap), F131 (vs. gap), C158 (≠ G159), G159 (= G160), S160 (= S161), S184 (= S185), C187 (≠ N188), I212 (≠ L213), R318 (= R320), L321 (≠ R323), L365 (= L358), F426 (≠ M412)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
28% identity, 84% coverage: 76:480/483 of query aligns to 85:506/508 of 3a1iA
- active site: K95 (= K86), S170 (= S161), S171 (= S162), G189 (≠ S180), Q191 (≠ M182), G192 (≠ M183), G193 (= G184), A194 (≠ S185), I197 (≠ N188)
- binding benzamide: F145 (≠ L136), S146 (≠ G137), G147 (≠ S138), Q191 (≠ M182), G192 (≠ M183), G193 (= G184), A194 (≠ S185), W327 (= W325)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
27% identity, 91% coverage: 12:451/483 of query aligns to 1:431/457 of 6c6gA
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
29% identity, 84% coverage: 50:457/483 of query aligns to 39:427/461 of 4gysB
- active site: K72 (= K86), S146 (= S161), S147 (= S162), T165 (≠ S180), T167 (≠ M182), A168 (≠ M183), G169 (= G184), S170 (= S185), V173 (≠ N188)
- binding malonate ion: A120 (≠ G135), G122 (= G137), S146 (= S161), T167 (≠ M182), A168 (≠ M183), S170 (= S185), S193 (vs. gap), G194 (= G203), V195 (≠ R204), R200 (≠ D209), Y297 (≠ W316), R305 (= R323)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
28% identity, 88% coverage: 43:469/483 of query aligns to 52:462/605 of Q936X2
- K91 (= K86) mutation to A: Loss of activity.
- S165 (= S161) mutation to A: Loss of activity.
- S189 (= S185) mutation to A: Loss of activity.
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
30% identity, 49% coverage: 8:242/483 of query aligns to 1:240/564 of 6te4A
Sites not aligning to the query:
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
25% identity, 81% coverage: 78:466/483 of query aligns to 30:448/450 of 4n0iA
- active site: K38 (= K86), S116 (= S161), S117 (= S162), T135 (≠ S180), T137 (≠ M182), G138 (≠ M183), G139 (= G184), S140 (= S185), L143 (≠ N188)
- binding glutamine: G89 (= G137), T137 (≠ M182), G138 (≠ M183), S140 (= S185), Y168 (≠ F214), Y271 (≠ W319), Y272 (≠ R320), R320 (≠ G355), D404 (≠ M419)
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)
27% identity, 46% coverage: 7:229/483 of query aligns to 71:288/579 of Q9TUI8
- S217 (= S161) mutation to A: Loss of activity.
- S218 (= S162) mutation to A: Lowers activity by at least 98%.
- D237 (= D181) mutation D->E,N: Loss of activity.
- S241 (= S185) mutation to A: Loss of activity.
- C249 (≠ N193) mutation to A: Loss of activity.
P97612 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 Rattus norvegicus (Rat) (see paper)
28% identity, 43% coverage: 25:231/483 of query aligns to 90:287/579 of P97612
- K142 (= K86) mutation to A: Lowers activity 40000-fold. Lowers activity 70000-fold; when associated with A-217.
- S217 (= S161) mutation to A: Lowers activity 3000-fold. Lowers activity 70000-fold; when associated with A-142.
Query Sequence
>AO353_25440 FitnessBrowser__pseudo3_N2E3:AO353_25440
MTSTPISELVLLKAHELADCIRLRQVSCREVMQAYLSHIERFNPWVNALISLQAPEDLLA
QADQRDAELASGLYRGWMHGLPHAIKDLSLTRGIRTTFGSPLFEDFLPDRDGIMCERIKA
AGAIIIGKTNTPEFGLGSQTYNPLFGATGCAYDPSKTAGGSSGGAASALAMHLVPVADGS
DMMGSLRNPAAFNNVFGFRPSQGRVPFDDSADLFIDQLGYEGPMGRCVRDAALLLSVQAG
ADARAPLSIAESGAAFAAPLERDFSGTRLGWLGDFNGYLPMEKGILDLCQKAFTDFESLG
CSIEPASVDFAPEQLWNSWRTLRHWMVAGSLGSAYANPSQRARLKEEACWEVENGLRLSA
SDVFAASVARSHWYRAISNLFKRFDYLLLPTAQVFPFDKNLPWPTSIEGVSMDTYHRWME
VVIPGTLSGCPVANVQVGFNRNGLPMGLQIIGKHQADFAVLQLAHAYEQASRWFERCPSP
LLK
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