SitesBLAST
Comparing 3610038 FitnessBrowser__Dino:3610038 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)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
41% identity, 98% coverage: 10:440/441 of query aligns to 2:412/412 of 1o9oA
- active site: K62 (= K83), A131 (≠ S152), S132 (= S153), T150 (= T171), T152 (= T173), G153 (= G174), G154 (= G175), S155 (= S176), R158 (= R179)
- binding 3-amino-3-oxopropanoic acid: G130 (= G151), T152 (= T173), G153 (= G174), G154 (= G175), S155 (= S176), R158 (= R179), P359 (≠ A386)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
41% identity, 98% coverage: 10:440/441 of query aligns to 2:412/412 of 1ocmA
- active site: K62 (= K83), S131 (= S152), S132 (= S153), T152 (= T173), G153 (= G174), G154 (= G175), S155 (= S176)
- binding pyrophosphate 2-: R113 (≠ L134), S131 (= S152), Q151 (= Q172), T152 (= T173), G153 (= G174), G154 (= G175), S155 (= S176), R158 (= R179), P359 (≠ A386)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
41% identity, 51% coverage: 15:238/441 of query aligns to 11:246/487 of 1m21A
- active site: K81 (= K83), S160 (= S152), S161 (= S153), T179 (= T171), T181 (= T173), D182 (≠ G174), G183 (= G175), S184 (= S176), C187 (≠ R179)
- binding : A129 (= A132), N130 (≠ F133), F131 (≠ L134), C158 (≠ G150), G159 (= G151), S160 (= S152), S184 (= S176), C187 (≠ R179), I212 (≠ Q204)
Sites not aligning to the query:
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
27% identity, 96% coverage: 11:435/441 of query aligns to 7:473/485 of 2f2aA
- active site: K79 (= K83), S154 (= S152), S155 (= S153), S173 (≠ T171), T175 (= T173), G176 (= G174), G177 (= G175), S178 (= S176), Q181 (≠ R179)
- binding glutamine: G130 (≠ L134), S154 (= S152), D174 (≠ Q172), T175 (= T173), G176 (= G174), S178 (= S176), F206 (≠ Q204), Y309 (≠ F294), Y310 (≠ E295), R358 (≠ A331), D425 (≠ A386)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
27% identity, 96% coverage: 11:435/441 of query aligns to 7:473/485 of 2dqnA
- active site: K79 (= K83), S154 (= S152), S155 (= S153), S173 (≠ T171), T175 (= T173), G176 (= G174), G177 (= G175), S178 (= S176), Q181 (≠ R179)
- binding asparagine: M129 (≠ F133), G130 (≠ L134), T175 (= T173), G176 (= G174), S178 (= S176), Y309 (≠ F294), Y310 (≠ E295), R358 (≠ A331), D425 (≠ A386)
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
29% identity, 84% coverage: 50:420/441 of query aligns to 172:573/607 of Q7XJJ7
- K205 (= K83) mutation to A: Loss of activity.
- SS 281:282 (= SS 152:153) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 173:176) binding
- S305 (= S176) mutation to A: Loss of activity.
- R307 (≠ I178) mutation to A: Loss of activity.
- S360 (≠ T231) mutation to A: No effect.
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
29% identity, 84% coverage: 50:420/441 of query aligns to 172:573/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A132), T258 (vs. gap), S281 (= S152), G302 (≠ T173), G303 (= G174), S305 (= S176), S472 (≠ A331), I532 (≠ L380), M539 (≠ I387)
Sites not aligning to the query:
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 96% coverage: 11:435/441 of query aligns to 6:467/478 of 3h0mA
- active site: K72 (= K83), S147 (= S152), S148 (= S153), S166 (≠ T171), T168 (= T173), G169 (= G174), G170 (= G175), S171 (= S176), Q174 (≠ R179)
- binding glutamine: M122 (≠ F133), G123 (≠ L134), D167 (≠ Q172), T168 (= T173), G169 (= G174), G170 (= G175), S171 (= S176), F199 (≠ Q204), Y302 (≠ F294), R351 (vs. gap), D418 (vs. gap)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
29% identity, 96% coverage: 11:435/441 of query aligns to 6:467/478 of 3h0lA
- active site: K72 (= K83), S147 (= S152), S148 (= S153), S166 (≠ T171), T168 (= T173), G169 (= G174), G170 (= G175), S171 (= S176), Q174 (≠ R179)
- binding asparagine: G123 (≠ L134), S147 (= S152), G169 (= G174), G170 (= G175), S171 (= S176), Y302 (≠ F294), R351 (vs. gap), D418 (vs. gap)
3kfuE Crystal structure of the transamidosome (see paper)
31% identity, 96% coverage: 13:435/441 of query aligns to 3:454/468 of 3kfuE
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
30% identity, 92% coverage: 14:418/441 of query aligns to 5:431/457 of 6c6gA
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 98% coverage: 9:440/441 of query aligns to 27:492/507 of Q84DC4
- T31 (≠ Q13) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K83) mutation to A: Abolishes activity on mandelamide.
- S180 (vs. gap) mutation to A: Significantly decreases activity on mandelamide.
- S181 (vs. gap) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G174) 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 (= S176) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ R179) 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 (≠ V297) 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 (= I387) 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)
31% identity, 96% coverage: 7:429/441 of query aligns to 19:455/605 of Q936X2
- K91 (= K83) mutation to A: Loss of activity.
- S165 (= S152) mutation to A: Loss of activity.
- S189 (= S176) mutation to A: Loss of activity.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 93% coverage: 10:419/441 of query aligns to 3:422/461 of 4gysB
- active site: K72 (= K83), S146 (= S152), S147 (= S153), T165 (= T171), T167 (= T173), A168 (≠ G174), G169 (= G175), S170 (= S176), V173 (≠ R179)
- binding malonate ion: A120 (= A132), G122 (≠ N135), S146 (= S152), T167 (= T173), A168 (≠ G174), S170 (= S176), S193 (≠ Q199), G194 (= G200), V195 (= V201), R200 (≠ H206), Y297 (vs. gap), R305 (= R315)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
27% identity, 95% coverage: 10:429/441 of query aligns to 5:438/457 of 5h6sC
- active site: K77 (= K83), S152 (= S152), S153 (= S153), L173 (≠ T173), G174 (= G174), G175 (= G175), S176 (= S176)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A132), R128 (≠ L134), W129 (vs. gap), S152 (= S152), L173 (≠ T173), G174 (= G174), S176 (= S176), W306 (= W311), F338 (vs. gap)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
41% identity, 37% coverage: 73:236/441 of query aligns to 85:254/508 of 3a1iA
- active site: K95 (= K83), S170 (= S152), S171 (= S153), G189 (≠ T171), Q191 (≠ T173), G192 (= G174), G193 (= G175), A194 (≠ S176), I197 (≠ R179)
- binding benzamide: F145 (= F133), S146 (≠ L134), G147 (≠ N135), Q191 (≠ T173), G192 (= G174), G193 (= G175), A194 (≠ S176)
Sites not aligning to the query:
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
27% identity, 94% coverage: 11:424/441 of query aligns to 7:462/490 of 4yjiA
- active site: K79 (= K83), S158 (= S152), S159 (= S153), G179 (≠ T173), G180 (= G174), G181 (= G175), A182 (≠ S176)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ V85), G132 (vs. gap), S158 (= S152), G179 (≠ T173), G180 (= G174), A182 (≠ S176)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
27% identity, 95% coverage: 19:438/441 of query aligns to 14:471/482 of 3a2qA
- active site: K69 (= K83), S147 (= S152), S148 (= S153), N166 (≠ T171), A168 (≠ T173), A169 (≠ G174), G170 (= G175), A171 (≠ S176), I174 (≠ R179)
- binding 6-aminohexanoic acid: G121 (≠ A132), G121 (≠ A132), N122 (≠ F133), S147 (= S152), A168 (≠ T173), A168 (≠ T173), A169 (≠ G174), A171 (≠ S176), C313 (≠ I286)
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)
30% identity, 67% coverage: 3:298/441 of query aligns to 70:376/579 of Q9TUI8
- S217 (= S152) mutation to A: Loss of activity.
- S218 (= S153) mutation to A: Lowers activity by at least 98%.
- D237 (≠ Q172) mutation D->E,N: Loss of activity.
- S241 (= S176) mutation to A: Loss of activity.
- C249 (= C184) mutation to A: Loss of activity.
2wapA 3d-crystal structure of humanized-rat fatty acid amide hydrolase (faah) conjugated with the drug-like urea inhibitor pf-3845 (see paper)
31% identity, 51% coverage: 73:295/441 of query aligns to 100:341/541 of 2wapA
- active site: K110 (= K83), S185 (= S152), S186 (= S153), T204 (= T171), I206 (≠ T173), G207 (= G174), G208 (= G175), S209 (= S176), F212 (≠ R179)
- binding 4-(3-{[5-(trifluoromethyl)pyridin-2-yl]oxy}benzyl)piperidine-1-carboxylic acid: F160 (= F133), S161 (≠ L134), I206 (≠ T173), G207 (= G174), S209 (= S176), Y303 (vs. gap), L340 (≠ F294)
Sites not aligning to the query:
Query Sequence
>3610038 FitnessBrowser__Dino:3610038
MSDRSDLPDLSLQQMSAALRTGEVTALALLDAHLDRIAARDPSVKAWAWLDPDQARAQAI
ALDAAQAEGKALGPLHGIPVGLKDVIDTADMPTENGTPPDAGRQPDQDAWITARLRAVGA
VIVGKTTTTELAFLNPTETLNPHNPNHTPGGSSAGSAASVAAGMVPLAVGTQTGGSVIRP
AAFCGVVGVKPTFGAIPRQGVTMQSHTLDTLGVFTRDAEDAAFALTCMMDTEDSDPATLP
PQDAHPAIAGATRPPVFGFVRPPEWDRASAETKAALEKLAQALGAIPLSLPESFEQVADL
RARINFAEMAWHYSRYRTAGWDALSAATRDAMEAGAACAAVDYLAALMQREPLYASLDPL
FSQVDCLLCPSALGAAPEGLSSTGDAIFNGLWTFMGTPCVTLPLPETEKGLPIGVQLVGR
RGEDRALLSKAIWLQGHMGKN
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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