SitesBLAST
Comparing WP_026127746.1 NCBI__GCF_000341125.1:WP_026127746.1 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)
P9WQ73 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
66% identity, 100% coverage: 1:373/374 of query aligns to 5:376/376 of P9WQ73
- T154 (= T150) binding pyridoxal 5'-phosphate
- D176 (= D173) binding pyridoxal 5'-phosphate
- Q199 (= Q196) binding pyridoxal 5'-phosphate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2fyfA Structure of a putative phosphoserine aminotransferase from mycobacterium tuberculosis (see paper)
66% identity, 99% coverage: 5:373/374 of query aligns to 2:368/368 of 2fyfA
- active site: F101 (= F104), D168 (= D173), K192 (= K197)
- binding tetrachloroplatinate(ii): L2 (≠ I5), I321 (≠ V326), A324 (= A329)
- binding pyridoxal-5'-phosphate: A77 (≠ T80), T78 (= T81), W81 (= W84), F101 (= F104), T147 (= T150), D168 (= D173), T170 (= T175), Q191 (= Q196), K192 (= K197), N243 (= N248), T244 (= T249)
Sites not aligning to the query:
3ffrA Crystal structure of a phosphoserine aminotransferase serc (chu_0995) from cytophaga hutchinsonii atcc 33406 at 1.75 a resolution
26% identity, 93% coverage: 18:366/374 of query aligns to 7:356/361 of 3ffrA
5yb0B Crystal structure of wild type phosphoserine aminotransferase (psat) from e. Histolytica (see paper)
23% identity, 94% coverage: 17:368/374 of query aligns to 3:347/349 of 5yb0B
Q9Y617 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Homo sapiens (Human) (see 6 papers)
23% identity, 93% coverage: 17:362/374 of query aligns to 9:357/370 of Q9Y617
- S43 (= S44) 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 (= H45) binding in other chain
- R45 (= R46) binding in other chain
- Y70 (= Y71) to N: in NLS2; uncertain significance
- G79 (≠ T80) 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 (≠ T81) binding pyridoxal 5'-phosphate
- P87 (≠ A88) 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 (= A100) to V: in NLS2; does not affect secondary structure; does not affect dimerization; increased thermal stability; dbSNP:rs587777778
- D100 (vs. gap) 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 (vs. gap) binding pyridoxal 5'-phosphate
- E155 (= E149) to Q: in NLS2; uncertain significance
- T156 (= T150) binding pyridoxal 5'-phosphate
- D176 (= D173) binding pyridoxal 5'-phosphate
- S179 (= S176) 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 (= Q196) binding pyridoxal 5'-phosphate
- K200 (= K197) modified: N6-(pyridoxal phosphate)lysine
- N241 (= N248) binding in other chain
- T242 (= T249) binding in other chain
- C245 (≠ V252) 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 (≠ Y338) binding O-phospho-L-serine
- R336 (= R339) binding O-phospho-L-serine
- R342 (= R347) 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
1bt4A Phosphoserine aminotransferase from bacillus circulans subsp. Alkalophilus
23% identity, 90% coverage: 18:354/374 of query aligns to 7:341/361 of 1bt4A
8a5vE Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
23% identity, 93% coverage: 17:362/374 of query aligns to 5:353/366 of 8a5vE
8a5wC Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
23% identity, 93% coverage: 17:362/374 of query aligns to 4:352/365 of 8a5wC
8a5wA Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
23% identity, 93% coverage: 17:362/374 of query aligns to 4:352/365 of 8a5wA
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G73 (= G79), G74 (≠ T80), C75 (≠ T81), W102 (vs. gap), T151 (= T150), D171 (= D173), S173 (≠ T175), Q194 (= Q196), K195 (= K197)
- binding phosphoserine: H39 (= H45), R40 (= R46), H330 (≠ Y338), R337 (= R347)
8a5vA Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
23% identity, 93% coverage: 17:362/374 of query aligns to 4:352/365 of 8a5vA
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
21% identity, 97% coverage: 13:374/374 of query aligns to 15:376/381 of 2dr1A
1iugA The crystal structure of aspartate aminotransferase which belongs to subgroup iv from thermus thermophilus (see paper)
26% identity, 84% coverage: 21:333/374 of query aligns to 7:307/348 of 1iugA
8a5wE Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
23% identity, 93% coverage: 17:362/374 of query aligns to 5:352/365 of 8a5wE