SitesBLAST
Comparing Ac3H11_4128 FitnessBrowser__acidovorax_3H11:Ac3H11_4128 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)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
30% identity, 87% coverage: 13:463/520 of query aligns to 7:475/490 of 4yjiA
- active site: K79 (= K85), S158 (= S160), S159 (= S161), G179 (≠ T181), G180 (= G182), G181 (= G183), A182 (≠ S184)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L87), G132 (= G134), S158 (= S160), G179 (≠ T181), G180 (= G182), A182 (≠ S184)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
28% identity, 85% coverage: 21:464/520 of query aligns to 15:476/485 of 2f2aA
- active site: K79 (= K85), S154 (= S160), S155 (= S161), S173 (= S179), T175 (= T181), G176 (= G182), G177 (= G183), S178 (= S184), Q181 (≠ I187)
- binding glutamine: G130 (= G136), S154 (= S160), D174 (= D180), T175 (= T181), G176 (= G182), S178 (= S184), F206 (≠ G212), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ N344), D425 (≠ W411)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
28% identity, 85% coverage: 21:464/520 of query aligns to 15:476/485 of 2dqnA
- active site: K79 (= K85), S154 (= S160), S155 (= S161), S173 (= S179), T175 (= T181), G176 (= G182), G177 (= G183), S178 (= S184), Q181 (≠ I187)
- binding asparagine: M129 (≠ A135), G130 (= G136), T175 (= T181), G176 (= G182), S178 (= S184), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ N344), D425 (≠ W411)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 78% coverage: 60:462/520 of query aligns to 180:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G134), T258 (≠ A137), S281 (= S160), G302 (≠ T181), G303 (= G182), S305 (= S184), S472 (≠ N344), I532 (≠ G402), M539 (≠ Y409)
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, 78% coverage: 60:462/520 of query aligns to 180:589/607 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 (≠ TGGS 181:184) binding
- S305 (= S184) mutation to A: Loss of activity.
- R307 (= R186) mutation to A: Loss of activity.
- S360 (≠ M239) mutation to A: No effect.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
29% identity, 87% coverage: 12:462/520 of query aligns to 5:445/457 of 5h6sC
- active site: K77 (= K85), S152 (= S160), S153 (= S161), L173 (≠ T181), G174 (= G182), G175 (= G183), S176 (= S184)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G134), R128 (≠ G136), W129 (≠ A137), S152 (= S160), L173 (≠ T181), G174 (= G182), S176 (= S184), W306 (≠ L317), F338 (≠ R342)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 88% coverage: 9:465/520 of query aligns to 2:470/478 of 3h0mA
- active site: K72 (= K85), S147 (= S160), S148 (= S161), S166 (= S179), T168 (= T181), G169 (= G182), G170 (= G183), S171 (= S184), Q174 (≠ I187)
- binding glutamine: M122 (≠ A135), G123 (= G136), D167 (= D180), T168 (= T181), G169 (= G182), G170 (= G183), S171 (= S184), F199 (≠ G212), Y302 (vs. gap), R351 (≠ N344), D418 (≠ L412)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 88% coverage: 9:465/520 of query aligns to 2:470/478 of 3h0lA
- active site: K72 (= K85), S147 (= S160), S148 (= S161), S166 (= S179), T168 (= T181), G169 (= G182), G170 (= G183), S171 (= S184), Q174 (≠ I187)
- binding asparagine: G123 (= G136), S147 (= S160), G169 (= G182), G170 (= G183), S171 (= S184), Y302 (vs. gap), R351 (≠ N344), D418 (≠ L412)
3kfuE Crystal structure of the transamidosome (see paper)
31% identity, 87% coverage: 14:463/520 of query aligns to 2:456/468 of 3kfuE
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
32% identity, 85% coverage: 25:468/520 of query aligns to 18:475/482 of 3a2qA
- active site: K69 (= K85), S147 (= S160), S148 (= S161), N166 (≠ S179), A168 (≠ T181), A169 (≠ G182), G170 (= G183), A171 (≠ S184), I174 (= I187)
- binding 6-aminohexanoic acid: G121 (= G134), G121 (= G134), N122 (≠ A135), S147 (= S160), A168 (≠ T181), A168 (≠ T181), A169 (≠ G182), A171 (≠ S184), C313 (≠ A321)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
32% identity, 88% coverage: 16:470/520 of query aligns to 5:455/457 of 6c6gA
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 88% coverage: 6:461/520 of query aligns to 22:487/507 of Q84DC4
- T31 (≠ N15) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- 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 (= G182) 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 (≠ I187) 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 (≠ C300) 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 (≠ S356) 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 (= I400) 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)
30% identity, 75% coverage: 75:462/520 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K85), S170 (= S160), S171 (= S161), G189 (≠ S179), Q191 (≠ T181), G192 (= G182), G193 (= G183), A194 (≠ S184), I197 (= I187)
- binding benzamide: F145 (≠ A135), S146 (≠ G136), G147 (≠ A137), Q191 (≠ T181), G192 (= G182), G193 (= G183), A194 (≠ S184), W327 (≠ C300)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
28% identity, 79% coverage: 64:476/520 of query aligns to 71:478/605 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.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
29% identity, 74% coverage: 60:445/520 of query aligns to 50:422/461 of 4gysB
- active site: K72 (= K85), S146 (= S160), S147 (= S161), T165 (≠ S179), T167 (= T181), A168 (≠ G182), G169 (= G183), S170 (= S184), V173 (≠ I187)
- binding malonate ion: A120 (≠ G134), G122 (= G136), S146 (= S160), T167 (= T181), A168 (≠ G182), S170 (= S184), S193 (= S207), G194 (≠ R208), V195 (≠ K209), R200 (≠ T214), Y297 (≠ R318), R305 (≠ T326)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
29% identity, 86% coverage: 16:464/520 of query aligns to 6:410/412 of 1o9oA
- active site: K62 (= K85), A131 (≠ S160), S132 (= S161), T150 (≠ S179), T152 (= T181), G153 (= G182), G154 (= G183), S155 (= S184), R158 (≠ I187)
- binding 3-amino-3-oxopropanoic acid: G130 (= G159), T152 (= T181), G153 (= G182), G154 (= G183), S155 (= S184), R158 (≠ I187), P359 (= P404)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
37% identity, 45% coverage: 11:244/520 of query aligns to 5:244/487 of 1m21A
- active site: K81 (= K85), S160 (= S160), S161 (= S161), T179 (≠ S179), T181 (= T181), D182 (≠ G182), G183 (= G183), S184 (= S184), C187 (≠ I187)
- binding : A129 (≠ G134), N130 (≠ A135), F131 (vs. gap), C158 (≠ G158), G159 (= G159), S160 (= S160), S184 (= S184), C187 (≠ I187), I212 (= I216)
Sites not aligning to the query:
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
29% identity, 86% coverage: 16:464/520 of query aligns to 6:410/412 of 1ocmA
- active site: K62 (= K85), S131 (= S160), S132 (= S161), T152 (= T181), G153 (= G182), G154 (= G183), S155 (= S184)
- binding pyrophosphate 2-: R113 (= R140), S131 (= S160), Q151 (≠ D180), T152 (= T181), G153 (= G182), G154 (= G183), S155 (= S184), R158 (≠ I187), P359 (= P404)
6te4A Structural insights into pseudomonas aeruginosa type six secretion system exported effector 8: tse8 in complex with a peptide (see paper)
36% identity, 42% coverage: 9:228/520 of query aligns to 2:228/564 of 6te4A
Sites not aligning to the query:
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)
31% identity, 43% coverage: 7:227/520 of query aligns to 72:288/579 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 (= C192) mutation to A: Loss of activity.
Query Sequence
>Ac3H11_4128 FitnessBrowser__acidovorax_3H11:Ac3H11_4128
MTTTSPQALVELTANELRHHIGTREISPVELLDACIARIEAVNPHVNAVTATCYDRARTE
AKAAEQAVLRGEPLGLLHGLPMGVKDLEATAGLLTTYGSQIYREHIPAEDNVLVARLRAA
GAIVAGKTNIPEMGAGANSRNTVWGATGNPFNPNLNAGGSSGGSAAALACDMLPVCTGSD
TGGSLRIPASICGVVGFRPSPGVVPSSRKLLGWTPISVVGPMGRTVEEACLQLAASAGMS
AGDPLSYPLDPMSFLLPETVDLSRLRVATTEDFGACAVDNGIRTVFRRKVQAMKHLFARC
DAIDIDLGDVHRCFDVLRAEAFVASTREAYERDPASLGPNTRANYEMGAAMTLLDSAWAQ
AEQTRILARFQKLYEDYDIILAPTTPVSPFAWTELFASHINGEPQANYYRWLALTYVSTL
TTHPALSLPCGLDDAGMPFGLQIVGRFRADRHTLGVGHALEQAFKGIAGLARPRPDIAKL
VQTRAEPALTSIVTVAPDPRDARSLPRDDRAASAAQVSAV
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