SERC_MOUSE
ID SERC_MOUSE Reviewed; 370 AA.
AC Q99K85;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 168.
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, Psat;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Sato M., Oguma T., Tsujimoto K., Tadakuma T.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 17-27; 52-94; 191-200; 223-231 AND 343-356, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-127, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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; AF259674; AAK69389.1; -; mRNA.
DR EMBL; BC004827; AAH04827.1; -; mRNA.
DR CCDS; CCDS29681.1; -.
DR RefSeq; NP_803155.1; NM_177420.2.
DR AlphaFoldDB; Q99K85; -.
DR SMR; Q99K85; -.
DR BioGRID; 223231; 12.
DR IntAct; Q99K85; 2.
DR STRING; 10090.ENSMUSP00000025542; -.
DR iPTMnet; Q99K85; -.
DR PhosphoSitePlus; Q99K85; -.
DR SwissPalm; Q99K85; -.
DR EPD; Q99K85; -.
DR jPOST; Q99K85; -.
DR MaxQB; Q99K85; -.
DR PaxDb; Q99K85; -.
DR PRIDE; Q99K85; -.
DR ProteomicsDB; 255390; -.
DR Antibodypedia; 27405; 257 antibodies from 31 providers.
DR DNASU; 107272; -.
DR Ensembl; ENSMUST00000025542; ENSMUSP00000025542; ENSMUSG00000024640.
DR GeneID; 107272; -.
DR KEGG; mmu:107272; -.
DR UCSC; uc008gwp.2; mouse.
DR CTD; 29968; -.
DR MGI; MGI:2183441; Psat1.
DR VEuPathDB; HostDB:ENSMUSG00000024640; -.
DR eggNOG; KOG2790; Eukaryota.
DR GeneTree; ENSGT00940000153241; -.
DR HOGENOM; CLU_034866_0_1_1; -.
DR InParanoid; Q99K85; -.
DR OMA; GYRASMY; -.
DR OrthoDB; 1357311at2759; -.
DR PhylomeDB; Q99K85; -.
DR TreeFam; TF312975; -.
DR Reactome; R-MMU-977347; Serine biosynthesis.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
DR BioGRID-ORCS; 107272; 6 hits in 77 CRISPR screens.
DR ChiTaRS; Psat1; mouse.
DR PRO; PR:Q99K85; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q99K85; protein.
DR Bgee; ENSMUSG00000024640; Expressed in vestibular epithelium and 274 other tissues.
DR ExpressionAtlas; Q99K85; baseline and differential.
DR Genevisible; Q99K85; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis; Aminotransferase;
KW Direct protein sequencing; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome; Serine biosynthesis; Transferase.
FT CHAIN 1..370
FT /note="Phosphoserine aminotransferase"
FT /id="PRO_0000150136"
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:0007744|PubMed:23806337"
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; 40473 MW; 6CF6B80CFDA1974B CRC64;
MEATKQVVNF GPGPAKLPHS VLLEIQKQLL DYRGLGISVL EMSHRSSDFA KIIGNTENLV
RELLAVPNNY KVIFVQGGGS GQFSAVPLNL IGLKAGRSAD YVVTGAWSAK AAEEAKKFGT
VNIVHPKLGS YTKIPDPSTW NLNPDASYVY FCANETVHGV EFDFVPDVKG AVLVCDMSSN
FLSRPVDVSK FGVIFAGAQK NVGSAGVTVV IVRDDLLGFS LRECPSVLDY KVQAGNNSLY
NTPPCFSIYV MGMVLEWIKN NGGAAAMEKL SSIKSQMIYE IIDNSQGFYV CPVERQNRSR
MNIPFRIGNA KGDEALEKRF LDKAVELNMI SLKGHRSVGG IRASLYNAVT TEDVEKLAAF
MKNFLEMHQL
