SERC_CAEEL
ID SERC_CAEEL Reviewed; 370 AA.
AC P91856;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Probable phosphoserine aminotransferase;
DE Short=PSAT;
DE EC=2.6.1.52;
DE AltName: Full=Phosphohydroxythreonine aminotransferase;
GN ORFNames=F26H9.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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:P10658}.
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 -!- 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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 2/3.
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily. {ECO:0000305}.
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DR EMBL; Z81516; CAB04204.1; -; Genomic_DNA.
DR PIR; T21441; T21441.
DR RefSeq; NP_492483.1; NM_060082.4.
DR AlphaFoldDB; P91856; -.
DR SMR; P91856; -.
DR BioGRID; 38187; 9.
DR STRING; 6239.F26H9.5; -.
DR EPD; P91856; -.
DR PaxDb; P91856; -.
DR PeptideAtlas; P91856; -.
DR EnsemblMetazoa; F26H9.5.1; F26H9.5.1; WBGene00009177.
DR EnsemblMetazoa; F26H9.5.2; F26H9.5.2; WBGene00009177.
DR GeneID; 172756; -.
DR KEGG; cel:CELE_F26H9.5; -.
DR UCSC; F26H9.5; c. elegans.
DR CTD; 172756; -.
DR WormBase; F26H9.5; CE09710; WBGene00009177; -.
DR eggNOG; KOG2790; Eukaryota.
DR GeneTree; ENSGT00940000153241; -.
DR HOGENOM; CLU_034866_0_1_1; -.
DR InParanoid; P91856; -.
DR OMA; GYRASMY; -.
DR OrthoDB; 1357311at2759; -.
DR PhylomeDB; P91856; -.
DR Reactome; R-CEL-977347; Serine biosynthesis.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
DR PRO; PR:P91856; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00009177; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0006564; P:L-serine biosynthetic process; IBA:GO_Central.
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 PIRSF; PIRSF000525; SerC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01364; serC_1; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Pyridoxal phosphate;
KW Reference proteome; Serine biosynthesis; Transferase.
FT CHAIN 1..370
FT /note="Probable phosphoserine aminotransferase"
FT /id="PRO_0000150138"
FT BINDING 45
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 79..80
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 240..241
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 199
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 370 AA; 41002 MW; 676735A56AEEAFC1 CRC64;
MAAPGRKINF AAGPAKLPEE VLLKMQEEQL NFNNLGVSVI EMSHRSKEFG ALLNETISLI
RELMNVPDNF EILFMQGGGT GQFAAIPLNL KGDHEHADYI VTGAWSSKAA DEAGKYINVK
KVFQPSKPYV TVPDQENWVH DEKAAYLYYC ANETVHGIEF TPTAPESHNV PLVADVSSNF
MARPFDFKDH GVVFGGAQKN LGAAGLTIVI VRKDLIGKQQ AITPSVFSYK EMIANNSLYN
TPPTGGIYTT NLVLKWIKSK GGLQAIYELN LQKSGMIYDI IDNSNGFYHC AVDKRYRSIM
NVCFRIGGPS GNDELEEKFL KGSIERNMIS LKGHRSVGGI RASLYNAISV EETQVLATWM
NEFQKLHNTN
