SERC_SPIOL
ID SERC_SPIOL Reviewed; 430 AA.
AC P52877; A0A0K9RWV5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Phosphoserine aminotransferase, chloroplastic {ECO:0000303|PubMed:9037153};
DE Short=PSAT {ECO:0000303|PubMed:9037153};
DE EC=2.6.1.52 {ECO:0000269|PubMed:9037153};
DE AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000303|PubMed:9037153};
DE Flags: Precursor;
GN Name=PSA {ECO:0000303|PubMed:9037153};
GN ORFNames=SOVF_019970 {ECO:0000312|EMBL:KNA24015.1};
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=cv. Parade; TISSUE=Leaf;
RX PubMed=9037153; DOI=10.1023/a:1005730725764;
RA Saito K., Takagi Y., Ling H.C., Takahashi H., Noji M.;
RT "Molecular cloning, characterization and expression of cDNA encoding
RT phosphoserine aminotransferase involved in phosphorylated pathway of serine
RT biosynthesis from spinach.";
RL Plant Mol. Biol. 33:359-366(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Viroflay; TISSUE=Leaf;
RX PubMed=24352233; DOI=10.1038/nature12817;
RA Dohm J.C., Minoche A.E., Holtgraewe D., Capella-Gutierrez S.,
RA Zakrzewski F., Tafer H., Rupp O., Soerensen T.R., Stracke R., Reinhardt R.,
RA Goesmann A., Kraft T., Schulz B., Stadler P.F., Schmidt T., Gabaldon T.,
RA Lehrach H., Weisshaar B., Himmelbauer H.;
RT "The genome of the recently domesticated crop plant sugar beet (Beta
RT vulgaris).";
RL Nature 505:546-549(2014).
CC -!- FUNCTION: Catalyzes the reversible conversion of 3-
CC phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-
CC phosphonooxybutanoate to phosphohydroxythreonine.
CC {ECO:0000250|UniProtKB:Q96255}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate +
CC L-glutamate; Xref=Rhea:RHEA:14329, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:18110, ChEBI:CHEBI:29985, ChEBI:CHEBI:57524; EC=2.6.1.52;
CC Evidence={ECO:0000269|PubMed:9037153};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-hydroxy-2-
CC oxo-4-phosphooxybutanoate + L-glutamate; Xref=Rhea:RHEA:16573,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58452,
CC ChEBI:CHEBI:58538; EC=2.6.1.52;
CC Evidence={ECO:0000269|PubMed:9037153};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q96255};
CC Note=Binds 1 pyridoxal phosphate per subunit.
CC {ECO:0000250|UniProtKB:Q96255};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 2/3. {ECO:0000269|PubMed:9037153}.
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5.
CC {ECO:0000269|PubMed:9037153}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96255}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000250|UniProtKB:Q96255}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily. {ECO:0000305}.
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DR EMBL; D84061; BAA12206.1; -; mRNA.
DR EMBL; KQ133566; KNA24015.1; -; Genomic_DNA.
DR PIR; T09156; T09156.
DR AlphaFoldDB; P52877; -.
DR SMR; P52877; -.
DR STRING; 3562.P52877; -.
DR OrthoDB; 1357311at2759; -.
DR SABIO-RK; P52877; -.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
DR Proteomes; UP000054095; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IDA:UniProtKB.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006563; P:L-serine metabolic process; IGI:UniProtKB.
DR CDD; cd00611; PSAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00160; SerC_aminotrans_5; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR022278; Pser_aminoTfrase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43247; PTHR43247; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01364; serC_1; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aminotransferase; Chloroplast; Plastid;
KW Pyridoxal phosphate; Reference proteome; Serine biosynthesis; Transferase;
KW Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 52..430
FT /note="Phosphoserine aminotransferase, chloroplastic"
FT /id="PRO_0000001283"
FT BINDING 107
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P23721"
FT BINDING 141..142
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q96255"
FT BINDING 167
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q96255"
FT BINDING 219
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q96255"
FT BINDING 241
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q96255"
FT BINDING 264
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q96255"
FT BINDING 306..307
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q96255"
FT MOD_RES 265
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q96255"
SQ SEQUENCE 430 AA; 47177 MW; E1901768E8345BE8 CRC64;
MAMAATSSTQ TNLFLKAPFN PQQNCQQTHF LPLNFKIRNP ISRITCSATP TATAVSTTTK
IDQRSEERVF NFAAGPAVLP ENVLQKAQSE LLNWRGSGMS VMEMSHRGKE FTSIIDKAEA
DLRTLLNIPS DYTVLFLQGG ASTQFSAIPL NLCTPDSAVD YIVTGSWGDK AAKEAAKYAA
VSSIWSGKSD NYVRIPNFDG SEFVQNSQAR YLHICANETI YGVEFKKYPV PANPDGFLVA
DMSSNFCSKP VDVTKFGLIY AGAQKNVGPS GVTIVIVRND LIGNAQKMTP VMLDYKIHAD
NKSLYNTPPC YGIYMCGLVF EDLLNQGGLV EVEKKNKAKA QVLYDAIDES NGFYKCPVEK
SVRSLMNVPF TLEKSELEGD FIKEAAKEKM VALKGHRSVG GMRASIYNAM PLAGVEKLVA
FMKEFQAKHA
