SitesBLAST
Comparing GFF3456 FitnessBrowser__WCS417:GFF3456 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)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
30% identity, 95% coverage: 11:455/467 of query aligns to 10:476/485 of 2f2aA
- active site: K79 (= K80), S154 (= S156), S155 (= S157), S173 (= S175), T175 (≠ A177), G176 (= G178), G177 (= G179), S178 (= S180), Q181 (≠ I183)
- binding glutamine: G130 (≠ K132), S154 (= S156), D174 (= D176), T175 (≠ A177), G176 (= G178), S178 (= S180), F206 (≠ M208), Y309 (≠ F301), Y310 (vs. gap), R358 (= R344), D425 (vs. gap)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
30% identity, 95% coverage: 11:455/467 of query aligns to 10:476/485 of 2dqnA
- active site: K79 (= K80), S154 (= S156), S155 (= S157), S173 (= S175), T175 (≠ A177), G176 (= G178), G177 (= G179), S178 (= S180), Q181 (≠ I183)
- binding asparagine: M129 (≠ W131), G130 (≠ K132), T175 (≠ A177), G176 (= G178), S178 (= S180), Y309 (≠ F301), Y310 (vs. gap), R358 (= R344), D425 (vs. gap)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
31% identity, 98% coverage: 8:463/467 of query aligns to 7:485/490 of 4yjiA
- active site: K79 (= K80), S158 (= S156), S159 (= S157), G179 (≠ A177), G180 (= G178), G181 (= G179), A182 (≠ S180)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L82), G132 (= G130), S158 (= S156), G179 (≠ A177), G180 (= G178), A182 (≠ S180)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
34% identity, 83% coverage: 70:457/467 of query aligns to 85:505/508 of 3a1iA
- active site: K95 (= K80), S170 (= S156), S171 (= S157), G189 (≠ S175), Q191 (≠ A177), G192 (= G178), G193 (= G179), A194 (≠ S180), I197 (= I183)
- binding benzamide: F145 (≠ W131), S146 (≠ K132), G147 (= G133), Q191 (≠ A177), G192 (= G178), G193 (= G179), A194 (≠ S180), W327 (≠ F308)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
28% identity, 94% coverage: 16:456/467 of query aligns to 138:592/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G130), T258 (≠ G133), S281 (= S156), G302 (≠ A177), G303 (= G178), S305 (= S180), S472 (≠ Q329), I532 (≠ L396), M539 (≠ T403)
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, 94% coverage: 16:456/467 of query aligns to 138:592/607 of Q7XJJ7
- K205 (= K80) mutation to A: Loss of activity.
- SS 281:282 (= SS 156:157) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ AGGS 177:180) binding
- S305 (= S180) mutation to A: Loss of activity.
- R307 (= R182) mutation to A: Loss of activity.
- S360 (≠ P234) mutation to A: No effect.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
26% identity, 99% coverage: 3:463/467 of query aligns to 1:455/457 of 5h6sC
- active site: K77 (= K80), S152 (= S156), S153 (= S157), L173 (≠ A177), G174 (= G178), G175 (= G179), S176 (= S180)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G130), R128 (≠ K132), W129 (≠ G133), S152 (= S156), L173 (≠ A177), G174 (= G178), S176 (= S180), W306 (≠ F308), F338 (vs. gap)
3kfuE Crystal structure of the transamidosome (see paper)
31% identity, 95% coverage: 21:463/467 of query aligns to 14:465/468 of 3kfuE
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
26% identity, 95% coverage: 11:455/467 of query aligns to 9:469/478 of 3h0mA
- active site: K72 (= K80), S147 (= S156), S148 (= S157), S166 (= S175), T168 (≠ A177), G169 (= G178), G170 (= G179), S171 (= S180), Q174 (≠ I183)
- binding glutamine: M122 (≠ W131), G123 (≠ K132), D167 (= D176), T168 (≠ A177), G169 (= G178), G170 (= G179), S171 (= S180), F199 (≠ M208), Y302 (≠ F301), R351 (= R337), D418 (≠ T403)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
26% identity, 95% coverage: 11:455/467 of query aligns to 9:469/478 of 3h0lA
- active site: K72 (= K80), S147 (= S156), S148 (= S157), S166 (= S175), T168 (≠ A177), G169 (= G178), G170 (= G179), S171 (= S180), Q174 (≠ I183)
- binding asparagine: G123 (≠ K132), S147 (= S156), G169 (= G178), G170 (= G179), S171 (= S180), Y302 (≠ F301), R351 (= R337), D418 (≠ T403)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
28% identity, 94% coverage: 17:456/467 of query aligns to 15:472/482 of 3a2qA
- active site: K69 (= K80), S147 (= S156), S148 (= S157), N166 (≠ S175), A168 (= A177), A169 (≠ G178), G170 (= G179), A171 (≠ S180), I174 (= I183)
- binding 6-aminohexanoic acid: G121 (= G130), G121 (= G130), N122 (≠ W131), S147 (= S156), A168 (= A177), A168 (= A177), A169 (≠ G178), A171 (≠ S180), C313 (≠ W312)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
30% identity, 94% coverage: 7:446/467 of query aligns to 1:442/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
26% identity, 93% coverage: 21:453/467 of query aligns to 20:477/487 of 1m21A
- active site: K81 (= K80), S160 (= S156), S161 (= S157), T179 (≠ S175), T181 (≠ A177), D182 (≠ G178), G183 (= G179), S184 (= S180), C187 (≠ I183)
- binding : A129 (≠ K132), N130 (≠ G133), F131 (≠ V134), C158 (≠ G154), G159 (= G155), S160 (= S156), S184 (= S180), C187 (≠ I183), I212 (≠ M208), R318 (≠ A283), L321 (≠ G286), L365 (vs. gap), F426 (≠ V390)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
25% identity, 95% coverage: 6:449/467 of query aligns to 27:484/507 of Q84DC4
- T31 (≠ V10) 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 (= S156) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S157) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G178) 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 (= S180) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I183) 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 (≠ L311) 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 (vs. gap) 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 (≠ T403) 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.
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
25% identity, 82% coverage: 64:445/467 of query aligns to 22:443/450 of 4n0iA
- active site: K38 (= K80), S116 (= S156), S117 (= S157), T135 (≠ S175), T137 (≠ A177), G138 (= G178), G139 (= G179), S140 (= S180), L143 (≠ I183)
- binding glutamine: G89 (vs. gap), T137 (≠ A177), G138 (= G178), S140 (= S180), Y168 (≠ M208), Y271 (≠ F308), Y272 (≠ S309), R320 (= R344), D404 (vs. gap)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
28% identity, 90% coverage: 26:444/467 of query aligns to 21:430/461 of 4gysB
- active site: K72 (= K80), S146 (= S156), S147 (= S157), T165 (≠ S175), T167 (≠ A177), A168 (≠ G178), G169 (= G179), S170 (= S180), V173 (≠ I183)
- binding malonate ion: A120 (≠ G130), G122 (≠ K132), S146 (= S156), T167 (≠ A177), A168 (≠ G178), S170 (= S180), S193 (≠ Q202), G194 (≠ W203), V195 (≠ P204), R200 (≠ T209), Y297 (≠ F308), R305 (≠ A316)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 92% coverage: 25:453/467 of query aligns to 37:462/605 of Q936X2
- K91 (= K80) mutation to A: Loss of activity.
- S165 (= S156) mutation to A: Loss of activity.
- S189 (= S180) mutation to A: Loss of activity.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
26% identity, 96% coverage: 7:455/467 of query aligns to 2:404/412 of 1o9oA
- active site: K62 (= K80), A131 (≠ S156), S132 (= S157), T150 (≠ S175), T152 (≠ A177), G153 (= G178), G154 (= G179), S155 (= S180), R158 (≠ I183)
- binding 3-amino-3-oxopropanoic acid: G130 (= G155), T152 (≠ A177), G153 (= G178), G154 (= G179), S155 (= S180), R158 (≠ I183), P359 (≠ T403)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
26% identity, 96% coverage: 7:455/467 of query aligns to 2:404/412 of 1ocmA
- active site: K62 (= K80), S131 (= S156), S132 (= S157), T152 (≠ A177), G153 (= G178), G154 (= G179), S155 (= S180)
- binding pyrophosphate 2-: R113 (≠ K132), S131 (= S156), Q151 (≠ D176), T152 (≠ A177), G153 (= G178), G154 (= G179), S155 (= S180), R158 (≠ I183), P359 (≠ T403)
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)
35% identity, 45% coverage: 11:222/467 of query aligns to 81:288/579 of Q9TUI8
- S217 (= S156) mutation to A: Loss of activity.
- S218 (= S157) mutation to A: Lowers activity by at least 98%.
- D237 (= D176) mutation D->E,N: Loss of activity.
- S241 (= S180) mutation to A: Loss of activity.
- C249 (≠ T188) mutation to A: Loss of activity.
Query Sequence
>GFF3456 FitnessBrowser__WCS417:GFF3456
MSEIGQLTAVQLLQHFRDKTLSPVDVTEDALLRIERYNPVVNAYCHVDPEGALNAARASE
QRWLNGQPCGALDGVPASIKDLTLTVGMPTRKGSRTTSAEGPWDVDAPFTAFMRKAGAVL
LGKTTTPEFGWKGVTDNPLYGITRNPWDTRTTAGGSSGGAGAAAALNLGVLHQGSDAGGS
IRIPCAFTGTFGIKPTFGYVPQWPASAMTLLSHLGPMTRKVEDSVLMLQTIAQPDARDGL
IGAPRTTPWLTPGTDLNGLRVAYSPNFGYVDVDPQVAKVVAQAVAGLVQLGAHVEQIDPG
FSDPLEVFSTLWAAGAARLTRPMNDAQKQLLDPGLLRIAQRGERLSLDDFNAALEARAAL
VARMAAFHEHYDVLVSPMMPITAFDAGHDVPPGSGLQEWTQWTPFTYPFNLTQQPAASVP
CGLATNGLPVGLHVVGARFADEQVLRVCHAYAKAFPTQHLQAPQTPT
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