ID   SDH1_YEASX              Reviewed;         338 AA.
AC   P0CF23; P17324; P40443; P40444; Q6Q579;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=L-serine dehydratase;
DE            EC=4.3.1.17;
DE   AltName: Full=L-serine deaminase;
GN   Name=SDL1; Synonyms=SDH1;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2194168; DOI=10.1093/nar/18.12.3653;
RA   Seufert W.;
RT   "Nucleotide sequence of the yeast SDH1 gene encoding a serine dehydratase
RT   homolog.";
RL   Nucleic Acids Res. 18:3653-3653(1990).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:19169,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X52657; CAA36883.1; -; Genomic_DNA.
DR   PIR; S12731; S12731.
DR   AlphaFoldDB; P0CF23; -.
DR   SMR; P0CF23; -.
DR   IntAct; P0CF23; 2.
DR   VEuPathDB; FungiDB:YCL064C; -.
DR   UniPathway; UPA00138; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003941; F:L-serine ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Gluconeogenesis; Lyase; Pyridoxal phosphate.
FT   CHAIN           1..338
FT                   /note="L-serine dehydratase"
FT                   /id="PRO_0000185597"
FT   MOD_RES         39
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   338 AA;  36824 MW;  D8D1EFFB9AD858E1 CRC64;
     MEMTHYEKTP LIRQVFNNGK TNSWFYVKHE ILQPGGSFKS RGIGHLIRKS NQQPLSEGSG
     KLAVFSSSGG NAGLAAATAC RSMALNCSVV VPKTTKPRMV KKIQSAGAKV IIHGDHWGEA
     DEYLRHKLMA QESQHGSKTL YVHPFDNETI WEGHSTIVDE IIEQLKENDI SLPRVKALVC
     SVGGGGLFSG IIKGLDRNHL AEKIPVVAVE TAGCDVLNKS LKKGSPVTLE KLTSVATSLA
     SPYIASFAFE SFNKYGCKSV VLSDQDVLAT CLRYADDYNF IVEPACGASL HLCYHPEILE
     DILEQKIYED DIVIIIACGG SCMTYEDLVK ASSTLNVS