SitesBLAST
Comparing WP_012283093.1 NCBI__GCF_000019165.1:WP_012283093.1 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)
1bt4A Phosphoserine aminotransferase from bacillus circulans subsp. Alkalophilus
62% identity, 100% coverage: 2:361/361 of query aligns to 2:361/361 of 1bt4A
4azjA Structural basis of l-phosphoserine binding to bacillus alcalophilus phosphoserine aminotransferase (see paper)
57% identity, 99% coverage: 1:356/361 of query aligns to 1:356/360 of 4azjA
- active site: W102 (= W102), D172 (= D172), K196 (= K196)
- binding pyridoxal-5'-phosphate: A76 (= A76), S77 (= S77), W102 (= W102), T152 (= T152), D172 (= D172), S174 (= S174), Q195 (= Q195), K196 (= K196), N237 (= N237), T238 (= T238)
- binding phosphoserine: H41 (= H41), R42 (= R42), W102 (= W102), T152 (= T152), K196 (= K196), H327 (= H327), R328 (= R328), R334 (= R334)
1w23B Crystal structure of phosphoserine aminotransferase from bacillus alcalophilus (see paper)
57% identity, 99% coverage: 1:356/361 of query aligns to 1:353/357 of 1w23B
- active site: W102 (= W102), D172 (= D172), K196 (= K196)
- binding magnesium ion: Y127 (= Y127), Y154 (≠ F154), H285 (= H288), A286 (= A289)
- binding pyridoxal-5'-phosphate: A76 (= A76), S77 (= S77), W102 (= W102), T152 (= T152), D172 (= D172), S174 (= S174), Q195 (= Q195), K196 (= K196), N234 (= N237), T235 (= T238)
Q96255 Phosphoserine aminotransferase 1, chloroplastic; AtPSAT1; Phosphohydroxythreonine aminotransferase; EC 2.6.1.52 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
50% identity, 100% coverage: 2:361/361 of query aligns to 71:430/430 of Q96255
- AT 145:146 (≠ AS 76:77) binding pyridoxal 5'-phosphate
- W171 (= W102) binding pyridoxal 5'-phosphate
- T221 (= T152) binding pyridoxal 5'-phosphate
- D241 (= D172) binding pyridoxal 5'-phosphate
- Q264 (= Q195) binding pyridoxal 5'-phosphate
- K265 (= K196) modified: N6-(pyridoxal phosphate)lysine
- NT 306:307 (= NT 237:238) binding pyridoxal 5'-phosphate
6czzA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with plp- phosphoserine geminal diamine intermediate (see paper)
50% identity, 99% coverage: 3:360/361 of query aligns to 2:359/360 of 6czzA
- binding pyridoxal-5'-phosphate: G74 (= G75), A75 (= A76), T76 (≠ S77), W101 (= W102), T151 (= T152), D171 (= D172), S173 (= S174), Q194 (= Q195), K195 (= K196), N236 (= N237), T237 (= T238)
- binding phosphoserine: W101 (= W102), T151 (= T152), K195 (= K196), H326 (= H327), R327 (= R328), R333 (= R334)
6czyA Crystal structure of arabidopsis thaliana phosphoserine aminotransferase isoform 1 (atpsat1) in complex with pyridoxamine-5'- phosphate (pmp) (see paper)
50% identity, 99% coverage: 3:360/361 of query aligns to 4:361/362 of 6czyA
3qboB Crystal structure of phosphoserine aminotransferase from yersinia pestis co92
49% identity, 99% coverage: 3:361/361 of query aligns to 1:359/359 of 3qboB
6xdkD Crystal structure of phosphoserine aminotransferase (serc) from stenotrophomonas maltophilia k279a
46% identity, 99% coverage: 3:361/361 of query aligns to 1:359/359 of 6xdkD
1bjoA The structure of phosphoserine aminotransferase from e. Coli in complex with alpha-methyl-l-glutamate (see paper)
50% identity, 99% coverage: 3:361/361 of query aligns to 1:360/360 of 1bjoA
- active site: W100 (= W102), D172 (= D172), K196 (= K196)
- binding alpha-methyl-l-glutamic acid: S7 (≠ A9), W100 (= W102), T151 (= T152), K196 (= K196)
- binding pyridoxal-5'-phosphate: G74 (≠ A76), R75 (≠ S77), W100 (= W102), T151 (= T152), D172 (= D172), S174 (= S174), Q195 (= Q195), K196 (= K196)
6xdkB Crystal structure of phosphoserine aminotransferase (serc) from stenotrophomonas maltophilia k279a
45% identity, 99% coverage: 3:361/361 of query aligns to 1:355/355 of 6xdkB
8a5vE Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
48% identity, 99% coverage: 2:358/361 of query aligns to 1:362/366 of 8a5vE
Q9Y617 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Homo sapiens (Human) (see 6 papers)
48% identity, 99% coverage: 2:358/361 of query aligns to 5:366/370 of Q9Y617
- S43 (= S40) 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
- H44 (= H41) binding in other chain
- R45 (= R42) binding in other chain
- Y70 (= Y67) to N: in NLS2; uncertain significance
- G79 (≠ A76) 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 (≠ S77) binding pyridoxal 5'-phosphate
- P87 (= P84) 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 (= A94) to V: in NLS2; does not affect secondary structure; does not affect dimerization; increased thermal stability; dbSNP:rs587777778
- D100 (= D95) 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 (= W102) binding pyridoxal 5'-phosphate
- E155 (≠ N151) to Q: in NLS2; uncertain significance
- T156 (= T152) binding pyridoxal 5'-phosphate
- D176 (= D172) binding pyridoxal 5'-phosphate
- S179 (= S175) 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 (= Q195) binding pyridoxal 5'-phosphate
- K200 (= K196) modified: N6-(pyridoxal phosphate)lysine
- N241 (= N237) binding in other chain
- T242 (= T238) binding in other chain
- C245 (≠ S241) 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
- H335 (= H327) binding O-phospho-L-serine
- R336 (= R328) binding O-phospho-L-serine
- R342 (= R334) 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
8a5wC Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
48% identity, 99% coverage: 3:358/361 of query aligns to 1:361/365 of 8a5wC