SERC_RABIT
ID SERC_RABIT Reviewed; 370 AA.
AC P10658;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Phosphoserine aminotransferase;
DE Short=PSAT;
DE EC=2.6.1.52;
DE AltName: Full=Endometrial progesterone-induced protein;
DE Short=EPIP;
DE AltName: Full=Phosphohydroxythreonine aminotransferase;
GN Name=PSAT1; Synonyms=PSA;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3651428; DOI=10.1021/bi00387a035;
RA Misrahi M., Atger M., Milgrom E.;
RT "A novel progesterone-induced messenger RNA in rabbit and human endometria.
RT Cloning and sequence analysis of the complementary DNA.";
RL Biochemistry 26:3975-3982(1987).
RN [2]
RP POSSIBLE FUNCTION.
RX PubMed=2682527; DOI=10.1093/nar/17.20.8379;
RA van der Zel A., Lam H.-M., Winkler M.E.;
RT "Extensive homology between the Escherichia coli K-12 SerC(PdxF)
RT aminotransferase and a protein encoded by a progesterone-induced mRNA in
RT rabbit and human endometria.";
RL Nucleic Acids Res. 17:8379-8379(1989).
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:0000269|PubMed:2682527}.
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.
CC -!- INDUCTION: By progesterone.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily. {ECO:0000305}.
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DR EMBL; M17099; AAA31245.1; -; mRNA.
DR PIR; A26998; A26998.
DR RefSeq; NP_001075740.1; NM_001082271.1.
DR AlphaFoldDB; P10658; -.
DR SMR; P10658; -.
DR STRING; 9986.ENSOCUP00000006706; -.
DR GeneID; 100009099; -.
DR KEGG; ocu:100009099; -.
DR CTD; 29968; -.
DR eggNOG; KOG2790; Eukaryota.
DR InParanoid; P10658; -.
DR OrthoDB; 1357311at2759; -.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Acetylation; Amino-acid biosynthesis; Aminotransferase; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome; Serine biosynthesis; Transferase.
FT CHAIN 1..370
FT /note="Phosphoserine aminotransferase"
FT /id="PRO_0000150137"
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 107
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 241..242
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y617"
FT MOD_RES 51
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y617"
FT MOD_RES 127
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K85"
FT MOD_RES 200
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 269
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y617"
FT MOD_RES 318
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y617"
FT MOD_RES 323
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y617"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y617"
FT MOD_RES 333
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y617"
SQ SEQUENCE 370 AA; 40621 MW; 7AB3A6E6B2D4085F CRC64;
MDSPRQIVNF GPGPAKLPHS VLLEIQKELL DYKGLGISVL EMSHRSSDFA KIVNNTENLV
RELLAVPDNY KVIFLQGGGC GQFSAVPLNL IGLKPGRCAD YVVTGAWSAK AAEEAKKFGT
VNIVHPKLGS YTKIPDPSTW NLNPDASYVY YCANETVHGV EFDFVPDVKG AILVCDMSSN
FLSRPVDVSK FGVIFAGAQK NVGAAGVTVV IVRDDLLGFA LRECPSVLEY KVQATSSSLY
NTPPCFSIYV MGLVLEWIKN NGGAAAMKKL STIKSQMIYE IIDNSQGFYV CPVEPRNRSM
MNIPFRIGNA KGDEALEKRF LDKALELHMI SLKGHRSVGG VRVSLYNAVT IEDVQKLASF
MKNFLEMHQL
