SitesBLAST
Comparing AZOBR_RS22750 FitnessBrowser__azobra:AZOBR_RS22750 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)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
32% identity, 99% coverage: 6:468/470 of query aligns to 2:476/478 of 3h0mA
- active site: K72 (= K82), S147 (= S157), S148 (= S158), S166 (≠ T176), T168 (≠ F178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (≠ T184)
- binding glutamine: M122 (≠ F132), G123 (= G133), D167 (= D177), T168 (≠ F178), G169 (= G179), G170 (= G180), S171 (= S181), F199 (≠ A209), Y302 (vs. gap), R351 (≠ N341), D418 (≠ I411)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
32% identity, 99% coverage: 6:468/470 of query aligns to 2:476/478 of 3h0lA
- active site: K72 (= K82), S147 (= S157), S148 (= S158), S166 (≠ T176), T168 (≠ F178), G169 (= G179), G170 (= G180), S171 (= S181), Q174 (≠ T184)
- binding asparagine: G123 (= G133), S147 (= S157), G169 (= G179), G170 (= G180), S171 (= S181), Y302 (vs. gap), R351 (≠ N341), D418 (≠ I411)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
33% identity, 87% coverage: 52:459/470 of query aligns to 175:589/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G131), T258 (≠ A134), S281 (= S157), G302 (≠ F178), G303 (= G179), S305 (= S181), S472 (≠ N341), I532 (≠ L402), M539 (≠ L409)
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)
33% identity, 87% coverage: 52:459/470 of query aligns to 175:589/607 of Q7XJJ7
- K205 (= K82) mutation to A: Loss of activity.
- SS 281:282 (= SS 157:158) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ FGGS 178:181) binding
- S305 (= S181) mutation to A: Loss of activity.
- R307 (= R183) mutation to A: Loss of activity.
- S360 (≠ P236) mutation to A: No effect.
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
32% identity, 96% coverage: 8:459/470 of query aligns to 4:445/457 of 5h6sC
- active site: K77 (= K82), S152 (= S157), S153 (= S158), L173 (≠ F178), G174 (= G179), G175 (= G180), S176 (= S181)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G131), R128 (≠ G133), W129 (≠ A134), S152 (= S157), L173 (≠ F178), G174 (= G179), S176 (= S181), W306 (≠ F311), F338 (vs. gap)
3kfuE Crystal structure of the transamidosome (see paper)
38% identity, 95% coverage: 14:458/470 of query aligns to 1:454/468 of 3kfuE
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
30% identity, 96% coverage: 18:467/470 of query aligns to 15:482/485 of 2f2aA
- active site: K79 (= K82), S154 (= S157), S155 (= S158), S173 (≠ T176), T175 (≠ F178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (≠ T184)
- binding glutamine: G130 (= G133), S154 (= S157), D174 (= D177), T175 (≠ F178), G176 (= G179), S178 (= S181), F206 (≠ A209), Y309 (≠ D296), Y310 (≠ F297), R358 (vs. gap), D425 (= D407)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
30% identity, 96% coverage: 18:467/470 of query aligns to 15:482/485 of 2dqnA
- active site: K79 (= K82), S154 (= S157), S155 (= S158), S173 (≠ T176), T175 (≠ F178), G176 (= G179), G177 (= G180), S178 (= S181), Q181 (≠ T184)
- binding asparagine: M129 (≠ F132), G130 (= G133), T175 (≠ F178), G176 (= G179), S178 (= S181), Y309 (≠ D296), Y310 (≠ F297), R358 (vs. gap), D425 (= D407)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
35% identity, 96% coverage: 9:458/470 of query aligns to 1:448/457 of 6c6gA
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
31% identity, 92% coverage: 10:441/470 of query aligns to 7:456/490 of 4yjiA
- active site: K79 (= K82), S158 (= S157), S159 (= S158), G179 (≠ F178), G180 (= G179), G181 (= G180), A182 (≠ S181)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L84), G132 (= G131), S158 (= S157), G179 (≠ F178), G180 (= G179), A182 (≠ S181)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
30% identity, 99% coverage: 6:470/470 of query aligns to 25:496/507 of Q84DC4
- T31 (≠ A12) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K82) mutation to A: Abolishes activity on mandelamide.
- S180 (= S157) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S158) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G179) 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 (= S181) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ T184) 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 (≠ G278) 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 (≠ V338) 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 (≠ S403) 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.
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
33% identity, 99% coverage: 5:469/470 of query aligns to 2:479/482 of 3a2qA
- active site: K69 (= K82), S147 (= S157), S148 (= S158), N166 (≠ T176), A168 (≠ F178), A169 (≠ G179), G170 (= G180), A171 (≠ S181), I174 (≠ T184)
- binding 6-aminohexanoic acid: G121 (= G131), G121 (= G131), N122 (≠ F132), S147 (= S157), A168 (≠ F178), A168 (≠ F178), A169 (≠ G179), A171 (≠ S181), C313 (≠ R315)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
32% identity, 93% coverage: 28:465/470 of query aligns to 25:483/487 of 1m21A
- active site: K81 (= K82), S160 (= S157), S161 (= S158), T179 (= T176), T181 (≠ F178), D182 (≠ G179), G183 (= G180), S184 (= S181), C187 (≠ T184)
- binding : A129 (vs. gap), N130 (vs. gap), F131 (vs. gap), C158 (≠ G155), G159 (= G156), S160 (= S157), S184 (= S181), C187 (≠ T184), I212 (≠ A209), R318 (≠ A316), L321 (≠ I319), L365 (vs. gap), F426 (≠ Y408)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
31% identity, 87% coverage: 52:462/470 of query aligns to 45:442/461 of 4gysB
- active site: K72 (= K82), S146 (= S157), S147 (= S158), T165 (= T176), T167 (≠ F178), A168 (≠ G179), G169 (= G180), S170 (= S181), V173 (≠ T184)
- binding malonate ion: A120 (≠ G131), G122 (= G133), S146 (= S157), T167 (≠ F178), A168 (≠ G179), S170 (= S181), S193 (≠ P204), G194 (= G205), V195 (≠ R206), R200 (≠ D211), Y297 (≠ F311), R305 (≠ I319)
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
30% identity, 88% coverage: 49:461/470 of query aligns to 16:410/412 of 1o9oA
- active site: K62 (= K82), A131 (≠ S157), S132 (= S158), T150 (= T176), T152 (≠ F178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ T184)
- binding 3-amino-3-oxopropanoic acid: G130 (= G156), T152 (≠ F178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ T184), P359 (≠ I397)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
30% identity, 88% coverage: 49:461/470 of query aligns to 16:410/412 of 1ocmA
- active site: K62 (= K82), S131 (= S157), S132 (= S158), T152 (≠ F178), G153 (= G179), G154 (= G180), S155 (= S181)
- binding pyrophosphate 2-: R113 (≠ G133), S131 (= S157), Q151 (≠ D177), T152 (≠ F178), G153 (= G179), G154 (= G180), S155 (= S181), R158 (≠ T184), P359 (≠ I397)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
29% identity, 85% coverage: 72:470/470 of query aligns to 85:506/508 of 3a1iA
- active site: K95 (= K82), S170 (= S157), S171 (= S158), G189 (≠ T176), Q191 (≠ F178), G192 (= G179), G193 (= G180), A194 (≠ S181), I197 (≠ T184)
- binding benzamide: F145 (= F132), S146 (≠ G133), G147 (≠ A134), Q191 (≠ F178), G192 (= G179), G193 (= G180), A194 (≠ S181), W327 (≠ F320)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 93% coverage: 27:461/470 of query aligns to 37:465/605 of Q936X2
- K91 (= K82) mutation to A: Loss of activity.
- S165 (= S157) mutation to A: Loss of activity.
- S189 (= S181) 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)
33% identity, 51% coverage: 6:247/470 of query aligns to 74:313/579 of Q9TUI8
- S217 (= S157) mutation to A: Loss of activity.
- S218 (= S158) mutation to A: Lowers activity by at least 98%.
- D237 (= D177) mutation D->E,N: Loss of activity.
- S241 (= S181) mutation to A: Loss of activity.
- C249 (= C189) mutation to A: Loss of activity.
2wj1A 3d-crystal structure of humanized-rat fatty acid amide hydrolase (faah) conjugated with 7-phenyl-1-(4-(pyridin-2-yl)oxazol-2-yl) heptan- 1-one, an alpha-ketooxazole (see paper)
38% identity, 37% coverage: 72:247/470 of query aligns to 99:280/543 of 2wj1A
- active site: K109 (= K82), S184 (= S157), S185 (= S158), T203 (= T176), I205 (≠ F178), G206 (= G179), G207 (= G180), S208 (= S181), F211 (≠ T184)
- binding 7-phenyl-1-(4-pyridin-2-yl-1,3-oxazol-2-yl)heptane-1,1-diol: S157 (≠ F130), M158 (≠ G131), F159 (= F132), S184 (= S157), T203 (= T176), D204 (= D177), I205 (≠ F178), G206 (= G179), S208 (= S181), C236 (≠ L208)
Sites not aligning to the query:
Query Sequence
>AZOBR_RS22750 FitnessBrowser__azobra:AZOBR_RS22750
MSTPDLFRLSAAEMAEGVRNRRFRARDLVAASLERIAALDGGLKSFITVAPDAALAAAEA
ADRRVEAGAPLGPLHGVPVGVKDLTLTAGLRTTYGSTLYADLIPDTDDLSVARLKAAGAI
IVGKTNTPEFGFGAITGNELCGPTANPYDLDKTSGGSSGGSAAAVAAGLVPLAQGTDFGG
SVRTPASFCGVVGLRPTPGRIPSPGRALAWDGLATQGFLARDIADAALALAAVSGPDPRD
PTSLPVPEWTVPDLDALDPLSLRVAWSTDLGSALIDLGLAERFEAVMRGLEGRFGDFVEA
TPDCREAGAAFGTLRAAHIFHTYGRTLEQDGDRLSPSVAWNIARGKGLSAADYLRAEAQR
SALYRRFAAFFRDHDILMTLSASVPPFPNAQGDVTEINGFRLSTIIDYLAITYTVSLIGF
PCLSIPCGWTADGLPIGLQLIARPYEEDRLLRCARFLERELEFRHRWPSP
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