SitesBLAST
Comparing BPHYT_RS00720 FitnessBrowser__BFirm:BPHYT_RS00720 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)
31% identity, 94% coverage: 8:452/475 of query aligns to 7:473/485 of 2f2aA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (≠ T174), T175 (≠ G176), G176 (= G177), G177 (= G178), S178 (= S179), Q181 (≠ I182)
- binding glutamine: G130 (≠ K131), S154 (= S155), D174 (= D175), T175 (≠ G176), G176 (= G177), S178 (= S179), F206 (≠ S206), Y309 (= Y308), Y310 (= Y309), R358 (= R351), D425 (≠ N402)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
31% identity, 94% coverage: 8:452/475 of query aligns to 7:473/485 of 2dqnA
- active site: K79 (= K80), S154 (= S155), S155 (= S156), S173 (≠ T174), T175 (≠ G176), G176 (= G177), G177 (= G178), S178 (= S179), Q181 (≠ I182)
- binding asparagine: M129 (≠ N130), G130 (≠ K131), T175 (≠ G176), G176 (= G177), S178 (= S179), Y309 (= Y308), Y310 (= Y309), R358 (= R351), D425 (≠ N402)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
33% identity, 94% coverage: 8:454/475 of query aligns to 7:475/490 of 4yjiA
- active site: K79 (= K80), S158 (= S155), S159 (= S156), G179 (= G176), G180 (= G177), G181 (= G178), A182 (≠ S179)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (= L82), G132 (= G129), S158 (= S155), G179 (= G176), G180 (= G177), A182 (≠ S179)
3kfuE Crystal structure of the transamidosome (see paper)
33% identity, 96% coverage: 9:464/475 of query aligns to 2:468/468 of 3kfuE
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
34% identity, 83% coverage: 70:461/475 of query aligns to 85:506/508 of 3a1iA
- active site: K95 (= K80), S170 (= S155), S171 (= S156), G189 (≠ T174), Q191 (≠ G176), G192 (= G177), G193 (= G178), A194 (≠ S179), I197 (= I182)
- binding benzamide: F145 (≠ N130), S146 (≠ K131), G147 (≠ I132), Q191 (≠ G176), G192 (= G177), G193 (= G178), A194 (≠ S179), W327 (≠ G312)
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
27% identity, 95% coverage: 3:452/475 of query aligns to 1:444/457 of 5h6sC
- active site: K77 (= K80), S152 (= S155), S153 (= S156), L173 (≠ G176), G174 (= G177), G175 (= G178), S176 (= S179)
- binding 4-oxidanylbenzohydrazide: C126 (≠ G129), R128 (≠ K131), W129 (≠ I132), S152 (= S155), L173 (≠ G176), G174 (= G177), S176 (= S179), W306 (vs. gap), F338 (≠ T343)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
27% identity, 92% coverage: 16:452/475 of query aligns to 138:588/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (= G129), T258 (≠ I132), S281 (= S155), G302 (= G176), G303 (= G177), S305 (= S179), S472 (≠ L345), I532 (vs. gap), M539 (vs. gap)
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)
27% identity, 92% coverage: 16:452/475 of query aligns to 138:588/607 of Q7XJJ7
- K205 (= K80) mutation to A: Loss of activity.
- SS 281:282 (= SS 155:156) mutation to AA: Loss of activity.
- GGGS 302:305 (= GGGS 176:179) binding
- S305 (= S179) mutation to A: Loss of activity.
- R307 (= R181) mutation to A: Loss of activity.
- S360 (≠ T233) mutation to A: No effect.
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 94% coverage: 8:452/475 of query aligns to 6:466/478 of 3h0mA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (≠ T174), T168 (≠ G176), G169 (= G177), G170 (= G178), S171 (= S179), Q174 (≠ I182)
- binding glutamine: M122 (≠ N130), G123 (≠ K131), D167 (= D175), T168 (≠ G176), G169 (= G177), G170 (= G178), S171 (= S179), F199 (≠ S206), Y302 (= Y308), R351 (≠ L345), D418 (vs. gap)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
27% identity, 94% coverage: 8:452/475 of query aligns to 6:466/478 of 3h0lA
- active site: K72 (= K80), S147 (= S155), S148 (= S156), S166 (≠ T174), T168 (≠ G176), G169 (= G177), G170 (= G178), S171 (= S179), Q174 (≠ I182)
- binding asparagine: G123 (≠ K131), S147 (= S155), G169 (= G177), G170 (= G178), S171 (= S179), Y302 (= Y308), R351 (≠ L345), D418 (vs. gap)
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
31% identity, 93% coverage: 10:452/475 of query aligns to 9:476/487 of 1m21A
- active site: K81 (= K80), S160 (= S155), S161 (= S156), T179 (= T174), T181 (≠ G176), D182 (≠ G177), G183 (= G178), S184 (= S179), C187 (≠ I182)
- binding : A129 (≠ G129), N130 (= N130), F131 (≠ K131), C158 (≠ G153), G159 (= G154), S160 (= S155), S184 (= S179), C187 (≠ I182), I212 (≠ S206), R318 (vs. gap), L321 (vs. gap), L365 (≠ V327), F426 (≠ L396)
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: 7:452/475 of query aligns to 1:448/457 of 6c6gA
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
30% identity, 93% coverage: 6:448/475 of query aligns to 1:403/412 of 1o9oA
- active site: K62 (= K80), A131 (≠ S155), S132 (= S156), T150 (= T174), T152 (≠ G176), G153 (= G177), G154 (= G178), S155 (= S179), R158 (≠ I182)
- binding 3-amino-3-oxopropanoic acid: G130 (= G154), T152 (≠ G176), G153 (= G177), G154 (= G178), S155 (= S179), R158 (≠ I182), P359 (= P404)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
30% identity, 93% coverage: 6:448/475 of query aligns to 1:403/412 of 1ocmA
- active site: K62 (= K80), S131 (= S155), S132 (= S156), T152 (≠ G176), G153 (= G177), G154 (= G178), S155 (= S179)
- binding pyrophosphate 2-: R113 (≠ K131), S131 (= S155), Q151 (≠ D175), T152 (≠ G176), G153 (= G177), G154 (= G178), S155 (= S179), R158 (≠ I182), P359 (= P404)
3a2qA Structure of 6-aminohexanoate cyclic dimer hydrolase complexed with substrate (see paper)
30% identity, 94% coverage: 8:452/475 of query aligns to 9:468/482 of 3a2qA
- active site: K69 (= K80), S147 (= S155), S148 (= S156), N166 (≠ T174), A168 (≠ G176), A169 (≠ G177), G170 (= G178), A171 (≠ S179), I174 (= I182)
- binding 6-aminohexanoic acid: G121 (= G129), G121 (= G129), N122 (= N130), S147 (= S155), A168 (≠ G176), A168 (≠ G176), A169 (≠ G177), A171 (≠ S179), C313 (≠ W319)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
27% identity, 97% coverage: 3:461/475 of query aligns to 27:496/507 of Q84DC4
- T31 (≠ L7) 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 (= S155) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S156) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G177) 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 (= S179) mutation to A: Abolishes activity on mandelamide.
- Q207 (≠ I182) 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 (≠ P270) 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 (≠ D339) 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 (vs. gap) 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.
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 93% coverage: 25:468/475 of query aligns to 20:455/461 of 4gysB
- active site: K72 (= K80), S146 (= S155), S147 (= S156), T165 (= T174), T167 (≠ G176), A168 (≠ G177), G169 (= G178), S170 (= S179), V173 (≠ I182)
- binding malonate ion: A120 (≠ G129), G122 (≠ K131), S146 (= S155), T167 (≠ G176), A168 (≠ G177), S170 (= S179), S193 (≠ A201), G194 (= G202), V195 (≠ S203), R200 (≠ T208), Y297 (≠ H315), R305 (= R326)
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
29% identity, 86% coverage: 50:457/475 of query aligns to 62:469/605 of Q936X2
- K91 (= K80) mutation to A: Loss of activity.
- S165 (= S155) mutation to A: Loss of activity.
- S189 (= S179) 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)
32% identity, 46% coverage: 2:221/475 of query aligns to 71:288/579 of Q9TUI8
- S217 (= S155) mutation to A: Loss of activity.
- S218 (= S156) mutation to A: Lowers activity by at least 98%.
- D237 (= D175) mutation D->E,N: Loss of activity.
- S241 (= S179) mutation to A: Loss of activity.
- C249 (≠ S187) mutation to A: Loss of activity.
1mt5A Crystal structure of fatty acid amide hydrolase (see paper)
37% identity, 32% coverage: 70:221/475 of query aligns to 96:252/537 of 1mt5A
- active site: K106 (= K80), S181 (= S155), S182 (= S156), T200 (= T174), I202 (≠ G176), G203 (= G177), G204 (= G178), S205 (= S179), F208 (≠ I182)
- binding methyl arachidonyl fluorophosphonate: M155 (≠ K131), L156 (≠ I132), S157 (≠ V133), S181 (= S155), D201 (= D175), I202 (≠ G176), G203 (= G177), S205 (= S179)
Sites not aligning to the query:
Query Sequence
>BPHYT_RS00720 FitnessBrowser__BFirm:BPHYT_RS00720
MSEIVMLSAAQLVAGFRQCTLSPVEVMCEVLDRITKLDPVVNAFCALDEEEAMSAASEAE
RRWMRGEPCGPLDGVPVSVKDLVAVAGLPTRQGSWTASPDRESVDAPAVARLRRAGAIPF
GKTTTSEFGNKIVTDCPMTGATRNPWDTRLSPGGSSGGSAVAVALGLGPLSLATDGGGSI
RIPACWSGVVGFKPTFALVPAGSAASWTALSTLGPITRTVRDAALMLDAMTGTNTCANSD
GPPGTGRTSAYSAGLDDGVAGLRIAWCAAPAGVSVAPDIAECVGRAVDAFGTLGATVIPT
DVAPIVDYYGDGRIHSVQWSVFFAQRVRHMEAADRTLLDPDLTALADAGARIDTATFVDA
LLARHALGASMETFFKHYDLLVTPTFHCGPPPVPSLPGHLRNAPLLTAWCNQAGVPAISV
PCGFAGDMPTGLQIIGRRGSDALVLRAARAYELARGDFPAPEGDLPLPGDTEIAP
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