SitesBLAST
Comparing 3609935 Dshi_3317 phosphoserine aminotransferase (RefSeq) to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 9 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)
26% identity, 95% coverage: 9:374/384 of query aligns to 16:374/376 of P9WQ73
- T154 (= T145) binding
- D176 (= D168) binding
- Q199 (= Q191) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2fyfA Structure of a putative phosphoserine aminotransferase from mycobacterium tuberculosis (see paper)
25% identity, 95% coverage: 9:374/384 of query aligns to 9:366/368 of 2fyfA
- active site: F101 (vs. gap), D168 (= D168), K192 (= K192)
- binding tetrachloroplatinate(ii): I321 (≠ R329), A324 (= A332)
- binding pyridoxal-5'-phosphate: A77 (≠ D75), T78 (= T76), W81 (≠ Y79), F101 (vs. gap), T147 (= T145), D168 (= D168), T170 (= T170), Q191 (= Q191), K192 (= K192), N243 (= N245), T244 (= T246)
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
27% identity, 52% coverage: 15:212/384 of query aligns to 7:210/361 of 3ffrA
Sites not aligning to the query:
Q9Y617 Phosphoserine aminotransferase; Phosphohydroxythreonine aminotransferase; PSAT; EC 2.6.1.52 from Homo sapiens (Human) (see 6 papers)
18% identity, 95% coverage: 14:376/384 of query aligns to 9:368/370 of Q9Y617
- S43 (= S39) 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 (= H40) binding in other chain
- R45 (= R41) binding in other chain
- Y70 (= Y66) to N: in NLS2; unknown pathological significance
- G79 (≠ D75) binding ; 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 (≠ T76) binding
- P87 (≠ M83) 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 (≠ L95) to V: in NLS2; does not affect secondary structure; does not affect dimerization; increased thermal stability; dbSNP:rs587777778
- D100 (≠ A96) 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 (= W104) binding
- E155 (≠ S147) to Q: in NLS2; unknown pathological significance
- T156 (≠ G148) binding
- D176 (= D168) binding
- S179 (= S171) 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 (= Q191) binding
- K200 (= K192) modified: N6-(pyridoxal phosphate)lysine
- N241 (= N245) binding in other chain
- T242 (= T246) binding in other chain
- C245 (≠ M249) 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 (≠ Y342) binding
- R336 (= R343) binding
- R342 (= R350) binding ; 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)
18% identity, 95% coverage: 14:376/384 of query aligns to 5:364/366 of 8a5vE
8a5wC Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
18% identity, 95% coverage: 14:376/384 of query aligns to 4:363/365 of 8a5wC
8a5wA Crystal structure of the human phosphoserine aminotransferase (psat) in complex with o-phosphoserine (see paper)
18% identity, 95% coverage: 14:376/384 of query aligns to 4:363/365 of 8a5wA
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G73 (≠ S74), G74 (≠ D75), C75 (≠ T76), W102 (= W104), T151 (≠ G148), D171 (= D168), S173 (≠ T170), Q194 (= Q191), K195 (= K192)
- binding phosphoserine: H39 (= H40), R40 (= R41), H330 (≠ Y342), R337 (= R350)
8a5vA Crystal structure of the human phosposerine aminotransferase (psat) (see paper)
18% identity, 95% coverage: 14:376/384 of query aligns to 4:363/365 of 8a5vA
3e77A Human phosphoserine aminotransferase in complex with plp
18% identity, 90% coverage: 31:376/384 of query aligns to 28:361/363 of 3e77A
- active site: W100 (= W104), D169 (= D168), K193 (= K192)
- binding pyridoxal-5'-phosphate: G71 (≠ S74), G72 (≠ D75), C73 (≠ T76), W100 (= W104), T149 (≠ G148), D169 (= D168), S171 (≠ T170), Q192 (= Q191), K193 (= K192), N234 (= N245), T235 (= T246)
Query Sequence
>3609935 Dshi_3317 phosphoserine aminotransferase (RefSeq)
MALDAPVTRPANPRFSSGPCAKPPTWTLDTLGDAALGRSHRATVGKDKLKAAIETTREVL
GVPADYKIGIVPASDTGAYEMAMWSLLGERPVEMLAWESFGSGWVTDAIKQLKLDATTRT
AEYGEIVDLAAVDFDKDVCFTWNGTTSGVRVPDGDWIPADRAGLTLCDATSAAFAMDLAW
DKLDATTFSWQKVLGGEAAHGILILSPRAVARLESYTPPWPLPKIFRLTKGGKLIDGIFR
GETINTPSMLCVEDYLFALDWAKSVGGLPGLIARAEANTAAIAAFVAANDWIDFLAADPA
TRSTTSVCLKFTDDRIADGAAFAKAVAKRLEAEGIAFDIGAYRDAPPGLRIWCGGTVETS
DVEALLPWLSWAFEAEIAAQLAEA
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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