ID   Q80YG1_RAT              Unreviewed;       370 AA.
AC   Q80YG1;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=Phosphoserine aminotransferase {ECO:0000256|RuleBase:RU004505};
DE            EC=2.6.1.52 {ECO:0000256|RuleBase:RU004505};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|EMBL:AAO89062.1};
RN   [1] {ECO:0000313|EMBL:AAO89062.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Baek J.Y., Jun D.Y., Kim Y.H.;
RT   "Isolation and characterization of rat phosphoserine aminotransferase.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001871,
CC         ECO:0000256|RuleBase:RU004505};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU004504};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC       3-phospho-D-glycerate: step 2/3. {ECO:0000256|ARBA:ARBA00005099,
CC       ECO:0000256|RuleBase:RU004505}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. SerC subfamily.
CC       {ECO:0000256|ARBA:ARBA00006904}.
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DR   EMBL; AY239016; AAO89062.1; -; mRNA.
DR   AlphaFoldDB; Q80YG1; -.
DR   UCSC; RGD:735170; rat.
DR   PhylomeDB; Q80YG1; -.
DR   UniPathway; UPA00135; UER00197.
DR   UniPathway; UPA00244; UER00311.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_00160; SerC_aminotrans_5; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR007110; Ig-like_dom.
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   NCBIfam; TIGR01364; serC_1; 1.
DR   PANTHER; PTHR43247; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43247:SF1; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000525; SerC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU004505};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000256|RuleBase:RU004505};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299,
KW   ECO:0000256|RuleBase:RU004505};
KW   Transferase {ECO:0000256|RuleBase:RU004505, ECO:0000313|EMBL:AAO89062.1}.
FT   DOMAIN          225..302
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
SQ   SEQUENCE   370 AA;  40589 MW;  CD7DE32BAEFB7B15 CRC64;
     MEATKQVVNF GPGPAKLPYS VLLEIQKQLL DYKGLGISVL EMSHRSPDFA KIISNTENLV
     RELLAVPNNY KVIFVQGGGT GQFSAVPLNL IGLKAGRCAD YVVTGAWSAK AAEEARKFGT
     VNIVHPKLGS YTKIPDPSTW NLNPDASYVY FCANETVHGV EFDFIPDVKG AMLVCDMSSN
     FLSRPVDVSK FGVIFAGAQK NVGSAGVTVV IVRDDLLGFA LRECPSVLDY KVQAGNNSLY
     NTPPCFSTYV MGMVLEWIKN NGGAAAMEKL SSVKSQMIYE IIDNSQGFYV CPVERQNRSR
     MNIPFRIGNS KGDEALEKRF LDKAVELNMI SLKGHRSVGG IRASLYNAVT TEDVEKLAAF
     MKNFLEMHQL
//