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Database: UniProt
Entry: A0A2K6CK28_MACNE
LinkDB: A0A2K6CK28_MACNE
Original site: A0A2K6CK28_MACNE 
ID   A0A2K6CK28_MACNE        Unreviewed;       324 AA.
AC   A0A2K6CK28;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=phosphoserine transaminase {ECO:0000256|ARBA:ARBA00013030};
DE            EC=2.6.1.52 {ECO:0000256|ARBA:ARBA00013030};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000024021.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000024021.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   -!- 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   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. SerC subfamily.
CC       {ECO:0000256|ARBA:ARBA00006904}.
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DR   AlphaFoldDB; A0A2K6CK28; -.
DR   Ensembl; ENSMNET00000048288.1; ENSMNEP00000024021.1; ENSMNEG00000035579.1.
DR   GeneTree; ENSGT00940000153241; -.
DR   UniPathway; UPA00135; UER00197.
DR   UniPathway; UPA00244; UER00311.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000035579; Expressed in liver and 9 other cell types or tissues.
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   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
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; 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; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43247:SF1; PHOSPHOSERINE AMINOTRANSFERASE; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000525; SerC; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW   Transferase {ECO:0000256|ARBA:ARBA00022576}.
FT   DOMAIN          8..290
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   324 AA;  35178 MW;  7921FEF69AF7BBA5 CRC64;
     MDAPRQVVNF GPGPAKLPHS VLLEMQKELL DYKGIGISVL EMSHRSSDFA KIINNTETLV
     RELLAVPDNY KVIFLQGGGS GQFGAVPLNL IGLKAGRCAD YVVTGAWSAK AAEEAKKFGT
     INIVHPKLGS YTKIPDPSTW NLNPDASYVY YCANETVHGV EFDFIPDVKG AVLVCDMSSN
     FLSKPVDVSK FGVIFAGAQK NVGSAGVTVV IVRDDLLGFA LRECPSVLEY KVQAGNSSLY
     NTPPCFSIYV MGLVLEWIKN NGGAAAMEKL SSIKSQMIYE IIDNSQGFYV SVGGIRASLY
     NAVTIEDVQK LAAFMKNFLE MHQL
//
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