SitesBLAST
Comparing Ac3H11_3338 FitnessBrowser__acidovorax_3H11:Ac3H11_3338 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)
48% identity, 98% coverage: 6:494/497 of query aligns to 2:476/478 of 3h0mA
- active site: K72 (= K80), S147 (= S163), S148 (= S164), S166 (≠ T182), T168 (= T184), G169 (= G185), G170 (= G186), S171 (= S187), Q174 (= Q190)
- binding glutamine: M122 (= M130), G123 (= G131), D167 (= D183), T168 (= T184), G169 (= G185), G170 (= G186), S171 (= S187), F199 (= F215), Y302 (= Y319), R351 (= R368), D418 (= D435)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
48% identity, 98% coverage: 6:494/497 of query aligns to 2:476/478 of 3h0lA
- active site: K72 (= K80), S147 (= S163), S148 (= S164), S166 (≠ T182), T168 (= T184), G169 (= G185), G170 (= G186), S171 (= S187), Q174 (= Q190)
- binding asparagine: G123 (= G131), S147 (= S163), G169 (= G185), G170 (= G186), S171 (= S187), Y302 (= Y319), R351 (= R368), D418 (= D435)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
44% identity, 97% coverage: 11:490/497 of query aligns to 8:479/485 of 2f2aA
- active site: K79 (= K80), S154 (= S163), S155 (= S164), S173 (≠ T182), T175 (= T184), G176 (= G185), G177 (= G186), S178 (= S187), Q181 (= Q190)
- binding glutamine: G130 (= G131), S154 (= S163), D174 (= D183), T175 (= T184), G176 (= G185), S178 (= S187), F206 (= F215), Y309 (= Y319), Y310 (= Y320), R358 (= R368), D425 (= D435)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
44% identity, 97% coverage: 11:490/497 of query aligns to 8:479/485 of 2dqnA
- active site: K79 (= K80), S154 (= S163), S155 (= S164), S173 (≠ T182), T175 (= T184), G176 (= G185), G177 (= G186), S178 (= S187), Q181 (= Q190)
- binding asparagine: M129 (= M130), G130 (= G131), T175 (= T184), G176 (= G185), S178 (= S187), Y309 (= Y319), Y310 (= Y320), R358 (= R368), D425 (= D435)
3kfuE Crystal structure of the transamidosome (see paper)
47% identity, 97% coverage: 14:496/497 of query aligns to 1:467/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
36% identity, 83% coverage: 72:483/497 of query aligns to 30:449/450 of 4n0iA
- active site: K38 (= K80), S116 (= S163), S117 (= S164), T135 (= T182), T137 (= T184), G138 (= G185), G139 (= G186), S140 (= S187), L143 (≠ Q190)
- binding glutamine: G89 (= G131), T137 (= T184), G138 (= G185), S140 (= S187), Y168 (≠ F215), Y271 (= Y319), Y272 (= Y320), R320 (= R368), D404 (= D435)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
33% identity, 98% coverage: 11:497/497 of query aligns to 8:487/487 of 1m21A
- active site: K81 (= K80), S160 (= S163), S161 (= S164), T179 (= T182), T181 (= T184), D182 (≠ G185), G183 (= G186), S184 (= S187), C187 (≠ Q190)
- binding : A129 (= A129), N130 (≠ M130), F131 (≠ G131), C158 (≠ G161), G159 (= G162), S160 (= S163), S184 (= S187), C187 (≠ Q190), I212 (≠ F215), R318 (≠ Y320), L321 (≠ A323), L365 (≠ I369), F426 (vs. gap)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
31% identity, 96% coverage: 6:484/497 of query aligns to 25:487/507 of Q84DC4
- T31 (≠ A12) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K80) mutation to A: Abolishes activity on mandelamide.
- S180 (= S163) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S164) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G185) 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 (= S187) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q190) 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 (= S315) 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 (≠ D382) 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 (vs. gap) 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)
31% identity, 84% coverage: 70:485/497 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K80), S170 (= S163), S171 (= S164), G189 (≠ T182), Q191 (≠ T184), G192 (= G185), G193 (= G186), A194 (≠ S187), I197 (≠ Q190)
- binding benzamide: F145 (≠ M130), S146 (≠ G131), G147 (≠ S132), Q191 (≠ T184), G192 (= G185), G193 (= G186), A194 (≠ S187), W327 (≠ Y319)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
35% identity, 93% coverage: 22:484/497 of query aligns to 14:448/457 of 6c6gA
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
31% identity, 83% coverage: 72:485/497 of query aligns to 197:589/607 of Q7XJJ7
- K205 (= K80) mutation to A: Loss of activity.
- SS 281:282 (= SS 163:164) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 184:187) binding
- S305 (= S187) mutation to A: Loss of activity.
- R307 (= R189) mutation to A: Loss of activity.
- S360 (≠ P242) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
31% identity, 83% coverage: 72:485/497 of query aligns to 197:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A129), T258 (≠ S132), S281 (= S163), G302 (≠ T184), G303 (= G185), S305 (= S187), S472 (≠ A373), I532 (≠ N426), M539 (≠ L433)
Sites not aligning to the query:
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
33% identity, 91% coverage: 34:485/497 of query aligns to 27:439/461 of 4gysB
- active site: K72 (= K80), S146 (= S163), S147 (= S164), T165 (= T182), T167 (= T184), A168 (≠ G185), G169 (= G186), S170 (= S187), V173 (≠ Q190)
- binding malonate ion: A120 (= A129), G122 (= G131), S146 (= S163), T167 (= T184), A168 (≠ G185), S170 (= S187), S193 (≠ Y210), G194 (= G211), V195 (≠ M212), R200 (≠ S217), Y297 (≠ F334), R305 (= R342)
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)
45% identity, 34% coverage: 72:240/497 of query aligns to 28:187/425 of Q9FR37
- K36 (= K80) active site, Charge relay system; mutation to A: Loss of catalytic activity.; mutation to R: Reduces catalytic activity 10-fold.
- S113 (= S163) active site, Charge relay system; mutation S->A,T: Loss of catalytic activity.
- S114 (= S164) mutation to A: Loss of catalytic activity.; mutation to T: Reduces catalytic activity 400-fold.
- D133 (= D183) mutation to A: Loss of catalytic activity.; mutation to E: Reduces catalytic activity 600-fold.
- S137 (= S187) active site, Acyl-ester intermediate; mutation to A: Reduces catalytic activity 170-fold.; mutation to T: Loss of catalytic activity.
- C145 (= C195) mutation C->A,S: Reduces catalytic activity 10-fold.
Sites not aligning to the query:
- 214 S→T: Slightly reduces catalytic activity.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 94% coverage: 15:479/497 of query aligns to 7:439/457 of 5h6sC
- active site: K77 (= K80), S152 (= S163), S153 (= S164), L173 (≠ T184), G174 (= G185), G175 (= G186), S176 (= S187)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A129), R128 (≠ N134), W129 (≠ E135), S152 (= S163), L173 (≠ T184), G174 (= G185), S176 (= S187), W306 (≠ Y319), F338 (≠ I371)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
29% identity, 86% coverage: 60:486/497 of query aligns to 42:409/412 of 1o9oA
- active site: K62 (= K80), A131 (≠ S163), S132 (= S164), T150 (= T182), T152 (= T184), G153 (= G185), G154 (= G186), S155 (= S187), R158 (≠ Q190)
- binding 3-amino-3-oxopropanoic acid: G130 (= G162), T152 (= T184), G153 (= G185), G154 (= G186), S155 (= S187), R158 (≠ Q190), P359 (= P428)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
29% identity, 86% coverage: 60:486/497 of query aligns to 42:409/412 of 1ocmA
- active site: K62 (= K80), S131 (= S163), S132 (= S164), T152 (= T184), G153 (= G185), G154 (= G186), S155 (= S187)
- binding pyrophosphate 2-: R113 (≠ D145), S131 (= S163), Q151 (≠ D183), T152 (= T184), G153 (= G185), G154 (= G186), S155 (= S187), R158 (≠ Q190), P359 (= P428)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
30% identity, 82% coverage: 67:473/497 of query aligns to 78:450/605 of Q936X2
- K91 (= K80) mutation to A: Loss of activity.
- S165 (= S163) mutation to A: Loss of activity.
- S189 (= S187) mutation to A: Loss of activity.
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
26% identity, 97% coverage: 6:489/497 of query aligns to 3:478/490 of 4yjiA
- active site: K79 (= K80), S158 (= S163), S159 (= S164), G179 (≠ T184), G180 (= G185), G181 (= G186), A182 (≠ S187)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ I82), G132 (≠ A129), S158 (= S163), G179 (≠ T184), G180 (= G185), A182 (≠ S187)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
35% identity, 46% coverage: 47:273/497 of query aligns to 34:259/482 of 3a2qA
- active site: K69 (= K80), S147 (= S163), S148 (= S164), N166 (≠ T182), A168 (≠ T184), A169 (≠ G185), G170 (= G186), A171 (≠ S187), I174 (≠ Q190)
- binding 6-aminohexanoic acid: G121 (≠ A129), G121 (≠ A129), N122 (≠ M130), S147 (= S163), A168 (≠ T184), A168 (≠ T184), A169 (≠ G185), A171 (≠ S187)
Sites not aligning to the query:
Query Sequence
>Ac3H11_3338 FitnessBrowser__acidovorax_3H11:Ac3H11_3338
MTSTALHDLGVAQLATELRERRVSAVEAAQHFLDRAQAHQNLGAYVAVNPEITLAQARAQ
DAAIAAGTAGPLAGVPIAHKDIFVTKGFPSTAGSKMLAGYQSPFDATVVTKLADAGAVTL
GKLNCDEFAMGSANENSAVAPVGTDAPAPVRNPWATDRIPGGSSGGSAVAVAARLAPAVT
GTDTGGSIRQPASFCGITGIKPTYGRASRYGMIAFASSLDQAGPMARSAEDCALLLSAMC
GPDPDRDSTSLDVPAENFSAKLNDSIEGLRIGIPAEFFGEGLAPDVRAAVDGALKEYEKL
GAKLVPISLPRTQLSIPVYYIIAPAEASSNLSRFDGVKFGHRAKDYSDLVDMYKKTRAEG
FGDEVKRRIMIGAYVLSHGYYDAYYLQAQKIRRMIADDFQNAFKSCDLIAGPVAPTVAWK
LGDHGNDPLADYLADIFTLPGSLAGLPGMSVPAGFGEGGMPVGLQLLGNYFQEARLLNAA
HRLQQATDFHLRRPEGF
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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