SERC_YEAST
ID SERC_YEAST Reviewed; 395 AA.
AC P33330; D6W2P0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Phosphoserine aminotransferase {ECO:0000303|PubMed:8017107};
DE Short=PSAT {ECO:0000303|PubMed:8017107};
DE EC=2.6.1.52 {ECO:0000250|UniProtKB:Q96255};
DE AltName: Full=Phosphohydroxythreonine aminotransferase;
GN Name=SER1; Synonyms=SERC; OrderedLocusNames=YOR184W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8017107; DOI=10.1002/yea.320100311;
RA Belhumeur P., Fortin N., Clark M.W.;
RT "A gene from Saccharomyces cerevisiae which codes for a protein with
RT significant homology to the bacterial 3-phosphoserine aminotransferase.";
RL Yeast 10:385-389(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7553933; DOI=10.1007/bf00314439;
RA Melcher K., Rose M., Kunzler M., Braus G.H., Entian K.-D.;
RT "Molecular analysis of the yeast SER1 gene encoding 3-phosphoserine
RT aminotransferase: regulation by general control and serine repression.";
RL Curr. Genet. 27:501-508(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20 AND SER-112, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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:Q96255}.
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:0000250|UniProtKB:Q96255};
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 Evidence={ECO:0000250|UniProtKB:Q96255};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q96255};
CC Note=Binds 1 pyridoxal phosphate per subunit.
CC {ECO:0000250|UniProtKB:Q96255};
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 -!- MISCELLANEOUS: Present with 15900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily. {ECO:0000305}.
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DR EMBL; L20917; AAA20886.1; -; Genomic_DNA.
DR EMBL; U19714; AAA85703.1; -; Genomic_DNA.
DR EMBL; Z75092; CAA99393.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10956.1; -; Genomic_DNA.
DR PIR; S42680; S42680.
DR RefSeq; NP_014827.3; NM_001183603.3.
DR AlphaFoldDB; P33330; -.
DR SMR; P33330; -.
DR BioGRID; 34579; 318.
DR DIP; DIP-4686N; -.
DR IntAct; P33330; 8.
DR MINT; P33330; -.
DR STRING; 4932.YOR184W; -.
DR iPTMnet; P33330; -.
DR SWISS-2DPAGE; P33330; -.
DR MaxQB; P33330; -.
DR PaxDb; P33330; -.
DR PRIDE; P33330; -.
DR EnsemblFungi; YOR184W_mRNA; YOR184W; YOR184W.
DR GeneID; 854356; -.
DR KEGG; sce:YOR184W; -.
DR SGD; S000005710; SER1.
DR VEuPathDB; FungiDB:YOR184W; -.
DR eggNOG; KOG2790; Eukaryota.
DR GeneTree; ENSGT00940000153241; -.
DR HOGENOM; CLU_034866_0_0_1; -.
DR InParanoid; P33330; -.
DR OMA; GYRASMY; -.
DR BioCyc; YEAST:YOR184W-MON; -.
DR Reactome; R-SCE-977347; Serine biosynthesis.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
DR PRO; PR:P33330; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P33330; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IMP:SGD.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0006564; P:L-serine biosynthetic process; IMP:SGD.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IMP:SGD.
DR GO; GO:0009070; P:serine family amino acid biosynthetic process; IMP:SGD.
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 Amino-acid biosynthesis; Aminotransferase; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome; Serine biosynthesis; Transferase.
FT CHAIN 1..395
FT /note="Phosphoserine aminotransferase"
FT /id="PRO_0000150141"
FT BINDING 80..81
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q96255"
FT BINDING 113
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q96255"
FT BINDING 170
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q96255"
FT BINDING 194
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q96255"
FT BINDING 217
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q96255"
FT BINDING 271..272
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q96255"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 218
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q96255"
FT CONFLICT 258..259
FT /note="FD -> LH (in Ref. 2; AAA85703)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 43416 MW; A22F020CC969B4BC CRC64;
MSLEREEPQH FGAGPAQMPT PVLQQAAKDL INFNDIGLGI GEISHRSKDA TKVIEDSKKH
LIELLNIPDT HEVFYLQGGG TTGFSSVATN LAAAYVGKHG KIAPAGYLVT GSWSQKSFEE
AKRLHVPAEV IFNAKDYNNG KFGKIPDESL WEDKIKGKAF SYVYLCENET VHGVEWPELP
KCLVNDPNIE IVADLSSDIL SRKIDVSQYG VIMAGAQKNI GLAGLTLYII KKSILKNISG
ASDETLHELG VPITPIAFDY PTVVKNNSAY NTIPIFTLHV MDLVFQHILK KGGVEAQQAE
NEEKAKILYE ALDANSDFYN VPVDPKCRSK MNVVFTLKKD GLDDQFLKEA AARHLTGLKG
HRSVGGFRAS IYNALSVKAV QNLVDFIKEF AEKNA
