SitesBLAST
Comparing RR42_RS04455 FitnessBrowser__Cup4G11:RR42_RS04455 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)
3qboB Crystal structure of phosphoserine aminotransferase from yersinia pestis co92
54% identity, 94% coverage: 20:383/386 of query aligns to 1:356/359 of 3qboB
1bjoA The structure of phosphoserine aminotransferase from e. Coli in complex with alpha-methyl-l-glutamate (see paper)
51% identity, 94% coverage: 20:383/386 of query aligns to 1:357/360 of 1bjoA
- active site: W100 (= W123), D172 (= D198), K196 (= K222)
- binding alpha-methyl-l-glutamic acid: S7 (≠ P26), W100 (= W123), T151 (= T173), K196 (= K222)
- binding pyridoxal-5'-phosphate: G74 (≠ A93), R75 (≠ I94), W100 (= W123), T151 (= T173), D172 (= D198), S174 (= S200), Q195 (= Q221), K196 (= K222)
7t7jB Crystal structure of phosphoserine aminotransferase from klebsiella pneumoniae subsp. Pneumoniae in complex with pyridoxal phosphate
50% identity, 94% coverage: 20:383/386 of query aligns to 1:357/360 of 7t7jB
- binding pyridoxal-5'-phosphate: G73 (= G92), G74 (≠ A93), R75 (≠ I94), W100 (= W123), T151 (= T173), D172 (= D198), S174 (= S200), Q195 (= Q221), K196 (= K222), N237 (= N263), T238 (= T264)
6xdkD Crystal structure of phosphoserine aminotransferase (serc) from stenotrophomonas maltophilia k279a
51% identity, 94% coverage: 20:383/386 of query aligns to 1:356/359 of 6xdkD
Q96255 Phosphoserine aminotransferase 1, chloroplastic; AtPSAT1; Phosphohydroxythreonine aminotransferase; EC 2.6.1.52 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
46% identity, 94% coverage: 19:382/386 of query aligns to 71:426/430 of Q96255
- AT 145:146 (≠ AI 93:94) binding pyridoxal 5'-phosphate
- W171 (= W123) binding pyridoxal 5'-phosphate
- T221 (= T173) binding pyridoxal 5'-phosphate
- D241 (= D198) binding pyridoxal 5'-phosphate
- Q264 (= Q221) binding pyridoxal 5'-phosphate
- K265 (= K222) modified: N6-(pyridoxal phosphate)lysine
- NT 306:307 (= NT 263:264) binding pyridoxal 5'-phosphate
6czyA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with pyridoxamine-5'- phosphate (pmp) (see paper)
46% identity, 94% coverage: 20:382/386 of query aligns to 4:358/362 of 6czyA
6czzA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with plp- phosphoserine geminal diamine intermediate (see paper)
46% identity, 94% coverage: 20:382/386 of query aligns to 2:356/360 of 6czzA
- binding pyridoxal-5'-phosphate: G74 (= G92), A75 (= A93), T76 (≠ I94), W101 (= W123), T151 (= T173), D171 (= D198), S173 (= S200), Q194 (= Q221), K195 (= K222), N236 (= N263), T237 (= T264)
- binding phosphoserine: W101 (= W123), T151 (= T173), K195 (= K222), H326 (= H352), R327 (≠ K353), R333 (= R359)
6xdkB Crystal structure of phosphoserine aminotransferase (serc) from stenotrophomonas maltophilia k279a
50% identity, 94% coverage: 20:383/386 of query aligns to 1:352/355 of 6xdkB
8a5wC Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
47% identity, 94% coverage: 20:381/386 of query aligns to 1:359/365 of 8a5wC
8a5wA Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
47% identity, 94% coverage: 20:381/386 of query aligns to 1:359/365 of 8a5wA
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G73 (= G92), G74 (≠ A93), C75 (≠ I94), W102 (= W123), T151 (= T173), D171 (= D198), S173 (= S200), Q194 (= Q221), K195 (= K222)
- binding phosphoserine: H39 (= H58), R40 (= R59), H330 (= H352), R337 (= R359)
8a5vA Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
47% identity, 94% coverage: 20:381/386 of query aligns to 1:359/365 of 8a5vA
Q9Y617 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Homo sapiens (Human) (see 6 papers)
47% identity, 94% coverage: 20:381/386 of query aligns to 6:364/370 of Q9Y617
- S43 (= S57) to R: in PSATD; reduced O-phospho-L-serine:2-oxoglutarate aminotransferase catalytic efficiency; 3-fold increase of KM for 3-phosphohydroxypyruvate; 5-fold increase of KM for L-glutamate; decreased function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; does not affect secondary structure; does not affect dimerization; does not affect thermal stability; dbSNP:rs1828113407 and dbSNP:rs1828113460
- H44 (= H58) binding in other chain
- R45 (= R59) binding in other chain
- Y70 (≠ F84) to N: in NLS2; uncertain significance; dbSNP:rs1828155814
- G79 (≠ A93) binding pyridoxal 5'-phosphate; to W: in NLS2; loss of O-phospho-L-serine:2-oxoglutarate aminotransferase activity; loss of function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway
- C80 (≠ I94) binding pyridoxal 5'-phosphate
- P87 (= P101) to A: has no effect on O-phospho-L-serine:2-oxoglutarate aminotransferase catalytic efficiency; does not affect KM for 3-phosphohydroxypyruvate; does not affect KM for L-glutamate; no effect on function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; does not affect secondary structure; does not affect dimerization; does not affect thermal stability; dbSNP:rs11540974
- A99 (= A115) to V: in NLS2; does not affect secondary structure; does not affect dimerization; increased thermal stability; dbSNP:rs587777778
- D100 (= D116) to A: in PSATD; has no effect on O-phospho-L-serine:2-oxoglutarate aminotransferase catalytic efficiency; does not affect KM for 3-phosphohydroxypyruvate; does not affect KM for L-glutamate; does not affect secondary structure; results in increased protein aggregation as shown by dynamic light scattering; dbSNP:rs118203967
- W107 (= W123) binding pyridoxal 5'-phosphate
- E155 (= E172) to Q: in NLS2; uncertain significance; dbSNP:rs369153467
- T156 (= T173) binding pyridoxal 5'-phosphate
- D176 (= D198) binding pyridoxal 5'-phosphate
- S179 (= S201) to L: in NLS2; loss of O-phospho-L-serine:2-oxoglutarate aminotransferase activity; loss of function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; dbSNP:rs587777777
- Q199 (= Q221) binding pyridoxal 5'-phosphate
- K200 (= K222) modified: N6-(pyridoxal phosphate)lysine
- N241 (= N263) binding in other chain
- T242 (= T264) binding in other chain
- C245 (≠ T267) to R: in NLS2; reduced O-phospho-L-serine:2-oxoglutarate aminotransferase catalytic efficiency; 9-fold increase of KM for L-glutamate; does not affect KM for 3-phosphohydroxypyruvate; decreased function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; does not affect secondary structure; does not affect dimerization; dbSNP:rs1305396127
- H335 (= H352) binding O-phospho-L-serine
- R336 (≠ K353) binding O-phospho-L-serine
- R342 (= R359) binding O-phospho-L-serine; to W: in NLS2; loss of O-phospho-L-serine:2-oxoglutarate aminotransferase activity; loss of function in L-serine biosynthesis shown through in vitro reconstruction of the phosphorylated pathway; dbSNP:rs202103028
8a5vE Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
47% identity, 94% coverage: 20:381/386 of query aligns to 2:360/366 of 8a5vE