SitesBLAST
Comparing PfGW456L13_3622 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3622 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)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
36% identity, 96% coverage: 10:465/474 of query aligns to 6:471/482 of 3a2qA
- active site: K69 (= K74), S147 (= S151), S148 (= S152), N166 (≠ T170), A168 (≠ C172), A169 (≠ G173), G170 (= G174), A171 (≠ S175), I174 (≠ V178)
- binding 6-aminohexanoic acid: G121 (≠ A125), G121 (≠ A125), N122 (≠ G126), S147 (= S151), A168 (≠ C172), A168 (≠ C172), A169 (≠ G173), A171 (≠ S175), C313 (≠ F311)
3kfuE Crystal structure of the transamidosome (see paper)
32% identity, 95% coverage: 17:464/474 of query aligns to 8:456/468 of 3kfuE
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 94% coverage: 14:458/474 of query aligns to 10:462/478 of 3h0mA
- active site: K72 (= K74), S147 (= S151), S148 (= S152), S166 (≠ T170), T168 (≠ C172), G169 (= G173), G170 (= G174), S171 (= S175), Q174 (≠ V178)
- binding glutamine: M122 (≠ G126), G123 (≠ D127), D167 (= D171), T168 (≠ C172), G169 (= G173), G170 (= G174), S171 (= S175), F199 (= F204), Y302 (vs. gap), R351 (≠ W338), D418 (≠ S413)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 94% coverage: 14:458/474 of query aligns to 10:462/478 of 3h0lA
- active site: K72 (= K74), S147 (= S151), S148 (= S152), S166 (≠ T170), T168 (≠ C172), G169 (= G173), G170 (= G174), S171 (= S175), Q174 (≠ V178)
- binding asparagine: G123 (≠ D127), S147 (= S151), G169 (= G173), G170 (= G174), S171 (= S175), Y302 (vs. gap), R351 (≠ W338), D418 (≠ S413)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
31% identity, 95% coverage: 13:462/474 of query aligns to 10:473/485 of 2f2aA
- active site: K79 (= K74), S154 (= S151), S155 (= S152), S173 (≠ T170), T175 (≠ C172), G176 (= G173), G177 (= G174), S178 (= S175), Q181 (≠ V178)
- binding glutamine: G130 (≠ D127), S154 (= S151), D174 (= D171), T175 (≠ C172), G176 (= G173), S178 (= S175), F206 (= F204), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ W338), D425 (≠ S413)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
31% identity, 95% coverage: 13:462/474 of query aligns to 10:473/485 of 2dqnA
- active site: K79 (= K74), S154 (= S151), S155 (= S152), S173 (≠ T170), T175 (≠ C172), G176 (= G173), G177 (= G174), S178 (= S175), Q181 (≠ V178)
- binding asparagine: M129 (≠ G126), G130 (≠ D127), T175 (≠ C172), G176 (= G173), S178 (= S175), Y309 (vs. gap), Y310 (vs. gap), R358 (≠ W338), D425 (≠ S413)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 84% coverage: 66:462/474 of query aligns to 197:588/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A125), T258 (≠ F128), S281 (= S151), G302 (≠ C172), G303 (= G173), S305 (= S175), S472 (≠ F343), I532 (≠ L402), M539 (≠ S413)
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)
30% identity, 84% coverage: 66:462/474 of query aligns to 197:588/607 of Q7XJJ7
- K205 (= K74) mutation to A: Loss of activity.
- SS 281:282 (= SS 151:152) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ CGGS 172:175) binding
- S305 (= S175) mutation to A: Loss of activity.
- R307 (= R177) mutation to A: Loss of activity.
- S360 (≠ Y231) mutation to A: No effect.
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
29% identity, 98% coverage: 2:464/474 of query aligns to 1:475/490 of 4yjiA
- active site: K79 (= K74), S158 (= S151), S159 (= S152), G179 (≠ C172), G180 (= G173), G181 (= G174), A182 (≠ S175)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ T76), G132 (≠ A125), S158 (= S151), G179 (≠ C172), G180 (= G173), A182 (≠ S175)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
29% identity, 84% coverage: 64:463/474 of query aligns to 85:498/508 of 3a1iA
- active site: K95 (= K74), S170 (= S151), S171 (= S152), G189 (≠ T170), Q191 (≠ C172), G192 (= G173), G193 (= G174), A194 (≠ S175), I197 (≠ V178)
- binding benzamide: F145 (= F124), S146 (≠ A125), G147 (= G126), Q191 (≠ C172), G192 (= G173), G193 (= G174), A194 (≠ S175), W327 (= W298)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
30% identity, 97% coverage: 9:467/474 of query aligns to 1:453/457 of 6c6gA
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
27% identity, 84% coverage: 64:463/474 of query aligns to 67:445/457 of 5h6sC
- active site: K77 (= K74), S152 (= S151), S153 (= S152), L173 (≠ C172), G174 (= G173), G175 (= G174), S176 (= S175)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A125), R128 (≠ D127), W129 (≠ F128), S152 (= S151), L173 (≠ C172), G174 (= G173), S176 (= S175), W306 (≠ A308), F338 (≠ I339)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
27% identity, 97% coverage: 6:463/474 of query aligns to 3:477/487 of 1m21A
- active site: K81 (= K74), S160 (= S151), S161 (= S152), T179 (= T170), T181 (≠ C172), D182 (≠ G173), G183 (= G174), S184 (= S175), C187 (≠ V178)
- binding : A129 (= A125), N130 (≠ G126), F131 (vs. gap), C158 (≠ G149), G159 (= G150), S160 (= S151), S184 (= S175), C187 (≠ V178), I212 (≠ F204), R318 (≠ A309), L321 (≠ W312), L365 (≠ F343), F426 (≠ H401)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
25% identity, 95% coverage: 14:465/474 of query aligns to 7:410/412 of 1o9oA
- active site: K62 (= K74), A131 (≠ S151), S132 (= S152), T150 (= T170), T152 (≠ C172), G153 (= G173), G154 (= G174), S155 (= S175), R158 (≠ V178)
- binding 3-amino-3-oxopropanoic acid: G130 (= G150), T152 (≠ C172), G153 (= G173), G154 (= G174), S155 (= S175), R158 (≠ V178), P359 (≠ R400)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
25% identity, 95% coverage: 14:465/474 of query aligns to 7:410/412 of 1ocmA
- active site: K62 (= K74), S131 (= S151), S132 (= S152), T152 (≠ C172), G153 (= G173), G154 (= G174), S155 (= S175)
- binding pyrophosphate 2-: R113 (≠ D127), S131 (= S151), Q151 (≠ D171), T152 (≠ C172), G153 (= G173), G154 (= G174), S155 (= S175), R158 (≠ V178), P359 (≠ R400)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
29% identity, 87% coverage: 54:465/474 of query aligns to 49:441/461 of 4gysB
- active site: K72 (= K74), S146 (= S151), S147 (= S152), T165 (= T170), T167 (≠ C172), A168 (≠ G173), G169 (= G174), S170 (= S175), V173 (= V178)
- binding malonate ion: A120 (= A125), G122 (≠ D127), S146 (= S151), T167 (≠ C172), A168 (≠ G173), S170 (= S175), S193 (≠ G198), G194 (≠ H200), V195 (= V201), R200 (≠ G206), Y297 (≠ F311), R305 (vs. gap)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 85% coverage: 65:465/474 of query aligns to 91:490/507 of Q84DC4
- K100 (= K74) mutation to A: Abolishes activity on mandelamide.
- S180 (= S151) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S152) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G173) 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 (= S175) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ V178) 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 (≠ G305) 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 (≠ H357) 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 (≠ Y406) 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.
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 85% coverage: 54:457/474 of query aligns to 71:456/605 of Q936X2
- K91 (= K74) mutation to A: Loss of activity.
- S165 (= S151) mutation to A: Loss of activity.
- S189 (= S175) 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)
24% identity, 95% coverage: 14:463/474 of query aligns to 82:570/579 of Q9TUI8
- S217 (= S151) mutation to A: Loss of activity.
- S218 (= S152) mutation to A: Lowers activity by at least 98%.
- D237 (= D171) mutation D->E,N: Loss of activity.
- S241 (= S175) mutation to A: Loss of activity.
- C249 (= C183) mutation to A: Loss of activity.
1mt5A Crystal structure of fatty acid amide hydrolase (see paper)
32% identity, 38% coverage: 15:194/474 of query aligns to 47:224/537 of 1mt5A
- active site: K106 (= K74), S181 (= S151), S182 (= S152), T200 (= T170), I202 (≠ C172), G203 (= G173), G204 (= G174), S205 (= S175), F208 (≠ V178)
- binding methyl arachidonyl fluorophosphonate: M155 (≠ A125), L156 (≠ G126), S157 (≠ D127), S181 (= S151), D201 (= D171), I202 (≠ C172), G203 (= G173), S205 (= S175)
Sites not aligning to the query:
Query Sequence
>PfGW456L13_3622 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3622
MTPEEFKSLDAVGLVQRLKSGEVTPLELVNLAAREIEIQDPALGAVVAIDIEGAQRAALD
PKAGPLAGVPILIKDTNIDVKGFATRHGSRLYEDAVPAQVDSEFVSRLRNAGAIILGKTK
TPEFAGDFVTEPEWQGPCRNPRNPQYASGGSSGGSACAVGAGMVPVAHGTDCGGSIRVPA
SVCGVVGLKPSRGRTPVGPHVGEFVGGLDSEHVLTRTVRDSALLLDVLSGYEPGAPYAAP
PAPPSWLECLKTRSPRLKIAFACARPDGSSIDETIHKAILNAVDFLSKDGHELRPFNWPD
MTKAGAAAALFWQMEIEALMEHKAQTRGYPISVQDVEWITYEFYKCSTQRTALDVHHARA
TQNKVSHDMADSFTDIDVLITPTVALAPPLIGGFVATGERHLDEWYKNAYAFSPFTEVFN
LTGQPAISIPVGIMENGLPIGMQIVGKFGDEETILRLASEVERSLLATTLFAKA
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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