SitesBLAST
Comparing Ac3H11_1012 FitnessBrowser__acidovorax_3H11:Ac3H11_1012 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)
29% identity, 93% coverage: 29:492/499 of query aligns to 7:480/490 of 4yjiA
- active site: K79 (= K102), S158 (= S177), S159 (= S178), G179 (≠ M198), G180 (≠ M199), G181 (= G200), A182 (≠ S201)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ I104), G132 (= G151), S158 (= S177), G179 (≠ M198), G180 (≠ M199), A182 (≠ S201)
3kfuE Crystal structure of the transamidosome (see paper)
35% identity, 93% coverage: 33:497/499 of query aligns to 1:466/468 of 3kfuE
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
28% identity, 94% coverage: 29:496/499 of query aligns to 6:455/457 of 5h6sC
- active site: K77 (= K102), S152 (= S177), S153 (= S178), L173 (≠ M198), G174 (≠ M199), G175 (= G200), S176 (= S201)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G151), R128 (≠ G153), W129 (≠ G154), S152 (= S177), L173 (≠ M198), G174 (≠ M199), S176 (= S201), W306 (= W333), F338 (≠ E364)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
26% identity, 90% coverage: 37:485/499 of query aligns to 15:473/485 of 2f2aA
- active site: K79 (= K102), S154 (= S177), S155 (= S178), S173 (= S196), T175 (≠ M198), G176 (≠ M199), G177 (= G200), S178 (= S201), Q181 (≠ T204)
- binding glutamine: G130 (= G153), S154 (= S177), D174 (= D197), T175 (≠ M198), G176 (≠ M199), S178 (= S201), F206 (= F230), Y309 (≠ F327), Y310 (≠ N328), R358 (≠ G372), D425 (≠ T428)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
26% identity, 90% coverage: 37:485/499 of query aligns to 15:473/485 of 2dqnA
- active site: K79 (= K102), S154 (= S177), S155 (= S178), S173 (= S196), T175 (≠ M198), G176 (≠ M199), G177 (= G200), S178 (= S201), Q181 (≠ T204)
- binding asparagine: M129 (≠ L152), G130 (= G153), T175 (≠ M198), G176 (≠ M199), S178 (= S201), Y309 (≠ F327), Y310 (≠ N328), R358 (≠ G372), D425 (≠ T428)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 89% coverage: 41:486/499 of query aligns to 18:467/478 of 3h0mA
- active site: K72 (= K102), S147 (= S177), S148 (= S178), S166 (= S196), T168 (≠ M198), G169 (≠ M199), G170 (= G200), S171 (= S201), Q174 (≠ T204)
- binding glutamine: M122 (≠ L152), G123 (= G153), D167 (= D197), T168 (≠ M198), G169 (≠ M199), G170 (= G200), S171 (= S201), F199 (= F230), Y302 (≠ F327), R351 (≠ E368), D418 (≠ T428)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
28% identity, 89% coverage: 41:486/499 of query aligns to 18:467/478 of 3h0lA
- active site: K72 (= K102), S147 (= S177), S148 (= S178), S166 (= S196), T168 (≠ M198), G169 (≠ M199), G170 (= G200), S171 (= S201), Q174 (≠ T204)
- binding asparagine: G123 (= G153), S147 (= S177), G169 (≠ M199), G170 (= G200), S171 (= S201), Y302 (≠ F327), R351 (≠ E368), D418 (≠ T428)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
31% identity, 80% coverage: 90:489/499 of query aligns to 83:501/508 of 3a1iA
- active site: K95 (= K102), S170 (= S177), S171 (= S178), G189 (≠ S196), Q191 (≠ M198), G192 (≠ M199), G193 (= G200), A194 (≠ S201), I197 (≠ T204)
- binding benzamide: F145 (≠ L152), S146 (≠ G153), G147 (= G154), Q191 (≠ M198), G192 (≠ M199), G193 (= G200), A194 (≠ S201), W327 (= W333)
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, 84% coverage: 70:486/499 of query aligns to 173:589/607 of Q7XJJ7
- K205 (= K102) mutation to A: Loss of activity.
- SS 281:282 (= SS 177:178) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ MMGS 198:201) binding
- S305 (= S201) mutation to A: Loss of activity.
- R307 (= R203) mutation to A: Loss of activity.
- S360 (≠ F257) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
26% identity, 84% coverage: 70:486/499 of query aligns to 173:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G151), T258 (≠ G154), S281 (= S177), G302 (≠ M198), G303 (≠ M199), S305 (= S201), S472 (≠ R358), I532 (≠ M429), M539 (= M436)
Sites not aligning to the query:
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
29% identity, 92% coverage: 37:495/499 of query aligns to 10:457/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
30% identity, 90% coverage: 37:486/499 of query aligns to 15:477/487 of 1m21A
- active site: K81 (= K102), S160 (= S177), S161 (= S178), T179 (≠ S196), T181 (≠ M198), D182 (≠ M199), G183 (= G200), S184 (= S201), C187 (≠ T204)
- binding : A129 (≠ G151), N130 (vs. gap), F131 (vs. gap), C158 (≠ A171), G159 (= G176), S160 (= S177), S184 (= S201), C187 (≠ T204), I212 (≠ V229), R318 (vs. gap), L321 (vs. gap), L365 (vs. gap), F426 (≠ M429)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
26% identity, 94% coverage: 22:489/499 of query aligns to 22:491/507 of Q84DC4
- T31 (= T31) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K102) mutation to A: Abolishes activity on mandelamide.
- S180 (= S177) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S178) mutation to A: Significantly decreases activity on mandelamide.
- G202 (≠ M199) 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 (= S201) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ T204) 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 (= Q379) 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 (≠ M436) 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.
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
27% identity, 95% coverage: 21:496/499 of query aligns to 15:475/605 of Q936X2
- K91 (= K102) mutation to A: Loss of activity.
- S165 (= S177) mutation to A: Loss of activity.
- S189 (= S201) 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)
31% identity, 47% coverage: 24:258/499 of query aligns to 1:240/564 of 6te4A
Sites not aligning to the query:
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
34% identity, 45% coverage: 30:256/499 of query aligns to 7:228/482 of 3a2qA
- active site: K69 (= K102), S147 (= S177), S148 (= S178), N166 (≠ S196), A168 (≠ M198), A169 (≠ M199), G170 (= G200), A171 (≠ S201), I174 (≠ T204)
- binding 6-aminohexanoic acid: G121 (= G151), G121 (= G151), N122 (≠ L152), S147 (= S177), A168 (≠ M198), A168 (≠ M198), A169 (≠ M199), A171 (≠ S201)
Sites not aligning to the query:
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
25% identity, 85% coverage: 66:488/499 of query aligns to 39:451/461 of 4gysB
- active site: K72 (= K102), S146 (= S177), S147 (= S178), T165 (≠ S196), T167 (≠ M198), A168 (≠ M199), G169 (= G200), S170 (= S201), V173 (≠ T204)
- binding malonate ion: A120 (≠ G151), G122 (= G153), S146 (= S177), T167 (≠ M198), A168 (≠ M199), S170 (= S201), S193 (≠ G224), G194 (≠ P225), V195 (≠ T226), R200 (≠ Q232), Y297 (≠ N334), R305 (= R340)
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, 42% coverage: 33:244/499 of query aligns to 82:287/579 of Q9TUI8
- S217 (= S177) mutation to A: Loss of activity.
- S218 (= S178) mutation to A: Lowers activity by at least 98%.
- D237 (= D197) mutation D->E,N: Loss of activity.
- S241 (= S201) mutation to A: Loss of activity.
- C249 (≠ N209) mutation to A: Loss of activity.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
34% identity, 31% coverage: 67:222/499 of query aligns to 27:176/412 of 1o9oA
- active site: K62 (= K102), A131 (≠ S177), S132 (= S178), T150 (≠ S196), T152 (≠ M198), G153 (≠ M199), G154 (= G200), S155 (= S201), R158 (≠ T204)
- binding 3-amino-3-oxopropanoic acid: G130 (= G176), T152 (≠ M198), G153 (≠ M199), G154 (= G200), S155 (= S201), R158 (≠ T204)
Sites not aligning to the query:
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)
27% identity, 42% coverage: 35:244/499 of query aligns to 84:287/579 of P97612
- K142 (= K102) mutation to A: Lowers activity 40000-fold. Lowers activity 70000-fold; when associated with A-217.
- S217 (= S177) mutation to A: Lowers activity 3000-fold. Lowers activity 70000-fold; when associated with A-142.
Query Sequence
>Ac3H11_1012 FitnessBrowser__acidovorax_3H11:Ac3H11_1012
MTHSPAPAPMPSATSVTPGGTPSHIVDYTATGLSRAIHAREVSCAEVLDAYLAQVDRLNP
VVNALVAMVDRDALRVQAAERDAQLARGESLGPLHGFPQAPKDIMPAAGMVTTRGSPIFA
GQVSATDAVVFERMRASGALFIGRSNSPEFGLGGHTYNPVYGTTRNAHNPAVSAGGSSGG
AAVAVALHMLPVADGSDMMGSLRTPAAFNNVYGLRTSFGLVPHGPTEEVFFQQFSVSGPM
ARNIPDLALLQSVQAGFDARLPLTRRHEDVALLGQPLERDWRGARIGWLGDLGGHLPAEP
GVLATCEQALEHFRTLGCTVESVVPTFNLEQLWNAWIDLRSFSVAGANAALYRDAQTRAL
LKPEAVWEIERGMRLTALQVYDAARVRSAWYQVLRGLFEQFDFLVLPAAQVFPFDAGLDW
PHEVGGRTMDTYHRWMEAVVPATMAGLPALAAPAGFGPGGLPAGLQILGPAQQDAAVLQI
GHAYDQASGYARVASPLLG
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