SitesBLAST
Comparing WP_068114277.1 NCBI__GCF_001653335.1:WP_068114277.1 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)
2fyfA Structure of a putative phosphoserine aminotransferase from mycobacterium tuberculosis (see paper)
64% identity, 99% coverage: 4:372/372 of query aligns to 2:368/368 of 2fyfA
- active site: F101 (= F103), D168 (= D172), K192 (= K196)
- binding tetrachloroplatinate(ii): L2 (= L4), I321 (≠ V325), A324 (= A328)
- binding pyridoxal-5'-phosphate: A77 (≠ S79), T78 (= T80), W81 (= W83), F101 (= F103), T147 (= T149), D168 (= D172), T170 (= T174), Q191 (= Q195), K192 (= K196), N243 (= N247), T244 (= T248)
Sites not aligning to the query:
P9WQ73 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
64% identity, 99% coverage: 4:372/372 of query aligns to 9:376/376 of P9WQ73
- T154 (= T149) binding pyridoxal 5'-phosphate
- D176 (= D172) binding pyridoxal 5'-phosphate
- Q199 (= Q195) binding pyridoxal 5'-phosphate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3ffrA Crystal structure of a phosphoserine aminotransferase serc (chu_0995) from cytophaga hutchinsonii atcc 33406 at 1.75 a resolution
25% identity, 93% coverage: 17:361/372 of query aligns to 7:352/361 of 3ffrA
5yb0B Crystal structure of wild type phosphoserine aminotransferase (psat) from e. Histolytica (see paper)
21% identity, 94% coverage: 16:365/372 of query aligns to 3:344/349 of 5yb0B
Q9Y617 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Homo sapiens (Human) (see 6 papers)
22% identity, 95% coverage: 16:370/372 of query aligns to 9:366/370 of Q9Y617
- S43 (= S43) 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 (= H44) binding in other chain
- R45 (= R45) binding in other chain
- Y70 (= Y70) to N: in NLS2; uncertain significance
- G79 (≠ S79) 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 (≠ T80) binding pyridoxal 5'-phosphate
- P87 (≠ T87) 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 (vs. gap) to V: in NLS2; does not affect secondary structure; does not affect dimerization; increased thermal stability; dbSNP:rs587777778
- D100 (≠ Q96) 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 (≠ F103) binding pyridoxal 5'-phosphate
- E155 (= E148) to Q: in NLS2; uncertain significance
- T156 (= T149) 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 (= N247) binding in other chain
- T242 (= T248) binding in other chain
- C245 (≠ I251) 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 (≠ Y337) binding O-phospho-L-serine
- R336 (= R338) binding O-phospho-L-serine
- R342 (= R346) 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)
22% identity, 95% coverage: 16:370/372 of query aligns to 5:362/366 of 8a5vE
8a5wC Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
22% identity, 95% coverage: 16:370/372 of query aligns to 4:361/365 of 8a5wC
8a5wA Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
22% identity, 95% coverage: 16:370/372 of query aligns to 4:361/365 of 8a5wA
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G73 (= G78), G74 (≠ S79), C75 (≠ T80), W102 (≠ F103), T151 (= T149), D171 (= D172), S173 (≠ T174), Q194 (= Q195), K195 (= K196)
- binding phosphoserine: H39 (= H44), R40 (= R45), H330 (≠ Y337), R337 (= R346)
8a5vA Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
22% identity, 95% coverage: 16:370/372 of query aligns to 4:361/365 of 8a5vA
8a5wE Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
21% identity, 95% coverage: 16:370/372 of query aligns to 5:361/365 of 8a5wE
- binding (2S)-2-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]-3-phosphonooxy-propanoic acid: H40 (= H44), R41 (= R45), N236 (= N247), T237 (= T248)
- binding (2~{S})-2-[[(~{R})-[[(5~{S})-5-azanyl-6-oxidanylidene-hexyl]amino]-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methyl]amino]-3-phosphonooxy-propanoic acid: G74 (= G78), G75 (≠ S79), C76 (≠ T80), W103 (≠ F103), T152 (= T149), S174 (≠ T174), A194 (≠ P194), Q195 (= Q195), N196 (≠ K196), H330 (≠ Y337), R331 (= R338), R337 (= R346), Y341 (≠ F350)
3e77A Human phosphoserine aminotransferase in complex with plp
22% identity, 91% coverage: 34:370/372 of query aligns to 27:359/363 of 3e77A
- active site: W100 (≠ F103), D169 (= D172), K193 (= K196)
- binding pyridoxal-5'-phosphate: G71 (= G78), G72 (≠ S79), C73 (≠ T80), W100 (≠ F103), T149 (= T149), D169 (= D172), S171 (≠ T174), Q192 (= Q195), K193 (= K196), N234 (= N247), T235 (= T248)
1bt4A Phosphoserine aminotransferase from bacillus circulans subsp. Alkalophilus
22% identity, 94% coverage: 17:366/372 of query aligns to 7:354/361 of 1bt4A
1w23B Crystal structure of phosphoserine aminotransferase from bacillus alcalophilus (see paper)
19% identity, 94% coverage: 16:365/372 of query aligns to 6:344/357 of 1w23B