SitesBLAST
Comparing PfGW456L13_3652 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3652 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)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
34% identity, 97% coverage: 11:476/482 of query aligns to 22:491/507 of Q84DC4
- T31 (≠ A20) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K88) 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 (≠ V185) 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 (≠ V190) 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 (≠ T304) 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 (≠ E363) 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 (≠ A423) 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.
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 92% coverage: 26:468/482 of query aligns to 14:462/478 of 3h0mA
- active site: K72 (= K88), S147 (= S163), S148 (= S164), S166 (≠ G182), T168 (= T184), G169 (≠ V185), G170 (= G186), S171 (= S187), Q174 (≠ V190)
- binding glutamine: M122 (≠ Y138), G123 (= G139), D167 (= D183), T168 (= T184), G169 (≠ V185), G170 (= G186), S171 (= S187), F199 (≠ I215), Y302 (≠ T308), R351 (vs. gap), D418 (= D418)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
31% identity, 92% coverage: 26:468/482 of query aligns to 14:462/478 of 3h0lA
- active site: K72 (= K88), S147 (= S163), S148 (= S164), S166 (≠ G182), T168 (= T184), G169 (≠ V185), G170 (= G186), S171 (= S187), Q174 (≠ V190)
- binding asparagine: G123 (= G139), S147 (= S163), G169 (≠ V185), G170 (= G186), S171 (= S187), Y302 (≠ T308), R351 (vs. gap), D418 (= D418)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
30% identity, 93% coverage: 26:472/482 of query aligns to 20:473/485 of 2f2aA
- active site: K79 (= K88), S154 (= S163), S155 (= S164), S173 (≠ G182), T175 (= T184), G176 (≠ V185), G177 (= G186), S178 (= S187), Q181 (≠ V190)
- binding glutamine: G130 (= G139), S154 (= S163), D174 (= D183), T175 (= T184), G176 (≠ V185), S178 (= S187), F206 (≠ I215), Y309 (≠ T308), Y310 (≠ W309), R358 (≠ G343), D425 (vs. gap)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
30% identity, 93% coverage: 26:472/482 of query aligns to 20:473/485 of 2dqnA
- active site: K79 (= K88), S154 (= S163), S155 (= S164), S173 (≠ G182), T175 (= T184), G176 (≠ V185), G177 (= G186), S178 (= S187), Q181 (≠ V190)
- binding asparagine: M129 (≠ Y138), G130 (= G139), T175 (= T184), G176 (≠ V185), S178 (= S187), Y309 (≠ T308), Y310 (≠ W309), R358 (≠ G343), D425 (vs. gap)
3kfuE Crystal structure of the transamidosome (see paper)
33% identity, 94% coverage: 24:474/482 of query aligns to 7:456/468 of 3kfuE
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
30% identity, 95% coverage: 14:472/482 of query aligns to 3:476/487 of 1m21A
- active site: K81 (= K88), S160 (= S163), S161 (= S164), T179 (≠ G182), T181 (= T184), D182 (≠ V185), G183 (= G186), S184 (= S187), C187 (≠ V190)
- binding : A129 (≠ S137), N130 (≠ Y138), F131 (vs. gap), C158 (≠ G161), G159 (= G162), S160 (= S163), S184 (= S187), C187 (≠ V190), I212 (= I215), R318 (= R306), L321 (≠ F312), L365 (≠ V352), F426 (≠ L420)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
29% identity, 94% coverage: 24:478/482 of query aligns to 12:457/457 of 5h6sC
- active site: K77 (= K88), S152 (= S163), S153 (= S164), L173 (≠ T184), G174 (≠ V185), G175 (= G186), S176 (= S187)
- binding 4-oxidanylbenzohydrazide: C126 (≠ S137), R128 (≠ G139), W129 (≠ L140), S152 (= S163), L173 (≠ T184), G174 (≠ V185), S176 (= S187), W306 (= W309), F338 (≠ W348)
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)
28% identity, 82% coverage: 80:475/482 of query aligns to 28:425/425 of Q9FR37
- K36 (= K88) 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.
- S214 (≠ Y260) mutation to T: Slightly reduces catalytic activity.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
26% identity, 87% coverage: 53:472/482 of query aligns to 169:588/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ S137), T258 (≠ L140), S281 (= S163), G302 (≠ T184), G303 (≠ V185), S305 (= S187), S472 (≠ A347), I532 (≠ E416), M539 (≠ A423)
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)
26% identity, 87% coverage: 53:472/482 of query aligns to 169:588/607 of Q7XJJ7
- K205 (= K88) mutation to A: Loss of activity.
- SS 281:282 (= SS 163:164) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TVGS 184:187) binding
- S305 (= S187) mutation to A: Loss of activity.
- R307 (= R189) mutation to A: Loss of activity.
- S360 (≠ T242) mutation to A: No effect.
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
45% identity, 36% coverage: 63:234/482 of query aligns to 48:221/457 of 6c6gA
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 86% coverage: 61:476/482 of query aligns to 47:446/461 of 4gysB
- active site: K72 (= K88), S146 (= S163), S147 (= S164), T165 (≠ G182), T167 (= T184), A168 (≠ V185), G169 (= G186), S170 (= S187), V173 (= V190)
- binding malonate ion: A120 (≠ S137), G122 (= G139), S146 (= S163), T167 (= T184), A168 (≠ V185), S170 (= S187), S193 (≠ D210), G194 (= G211), V195 (≠ I212), R200 (≠ H217), Y297 (≠ E305), R305 (≠ T316)
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
28% identity, 81% coverage: 80:471/482 of query aligns to 30:449/450 of 4n0iA
- active site: K38 (= K88), S116 (= S163), S117 (= S164), T135 (≠ G182), T137 (= T184), G138 (≠ V185), G139 (= G186), S140 (= S187), L143 (≠ V190)
- binding glutamine: G89 (= G139), T137 (= T184), G138 (≠ V185), S140 (= S187), Y168 (≠ I215), Y271 (≠ F312), Y272 (≠ F313), R320 (vs. gap), D404 (= D419)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
29% identity, 83% coverage: 80:477/482 of query aligns to 87:502/508 of 3a1iA
- active site: K95 (= K88), S170 (= S163), S171 (= S164), G189 (= G182), Q191 (≠ T184), G192 (≠ V185), G193 (= G186), A194 (≠ S187), I197 (≠ V190)
- binding benzamide: F145 (≠ Y138), S146 (≠ G139), G147 (≠ L140), Q191 (≠ T184), G192 (≠ V185), G193 (= G186), A194 (≠ S187), W327 (= W309)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
26% identity, 96% coverage: 9:469/482 of query aligns to 14:458/605 of Q936X2
- K91 (= K88) mutation to A: Loss of activity.
- S165 (= S163) mutation to A: Loss of activity.
- S189 (= S187) 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)
32% identity, 49% coverage: 15:249/482 of query aligns to 3:246/564 of 6te4A
Sites not aligning to the query:
Q9MUK5 Translocon at the outer membrane of chloroplasts 64 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see paper)
28% identity, 72% coverage: 122:466/482 of query aligns to 105:445/593 of Q9MUK5
Sites not aligning to the query:
- 516 N→A: Loss of HSP90 binding, but no effect on HSP70 binding.
- 550 R→A: 80% decrease of HSP70 and HSP90 binding.
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
28% identity, 88% coverage: 52:475/482 of query aligns to 27:410/412 of 1ocmA
- active site: K62 (= K88), S131 (= S163), S132 (= S164), T152 (= T184), G153 (≠ V185), G154 (= G186), S155 (= S187)
- binding pyrophosphate 2-: R113 (≠ S145), S131 (= S163), Q151 (≠ D183), T152 (= T184), G153 (≠ V185), G154 (= G186), S155 (= S187), R158 (≠ V190), P359 (≠ A423)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
27% identity, 88% coverage: 52:475/482 of query aligns to 27:410/412 of 1o9oA
- active site: K62 (= K88), A131 (≠ S163), S132 (= S164), T150 (≠ G182), T152 (= T184), G153 (≠ V185), G154 (= G186), S155 (= S187), R158 (≠ V190)
- binding 3-amino-3-oxopropanoic acid: G130 (= G162), T152 (= T184), G153 (≠ V185), G154 (= G186), S155 (= S187), R158 (≠ V190), P359 (≠ A423)
Query Sequence
>PfGW456L13_3652 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3652
MLKGDDTGISPDRFSELGVAAAAAAIRRGDISSESYTAALLRRAHTFSDLGAFITIDEAA
VLAAARACDTARATGSTAPLLGVPVAVKDSYLTQGLRTTLGIRSLENFVPARDAEVVRAI
KDAGGIVFGKNNLVEMSYGLTGHNSHFGQAKNPHNPEHVTGGSSSGAGASVGAQIVPAAL
GGDTVGSIRVPASFCGVVGFKPSPGRWSGDGIAPISHTLDTAGVFARTVEDCALIDQVVT
KTTSTVHGDWTGLRGIRLAYAPRQHLERINHEVEEHFKETIRRLCDAGAEVVEVDLGEDF
FAMTERSTWSIFFHETMESVAGFLRKNRIPSSFEDIYNELKPGLKDAWGHLVLPSGAGFI
SHETYQTALDHDRPEIQRRFNMAFSSSGAQALIMPTTPCPAPTIEQQTKFTIAGQEVDDL
ALARHTVAGSIAGLPGISIPMGMSSNGLPIGLEIDGKNGDDRKLLELARRVEAAVGAVAR
SV
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