ID   SDHL_YEAS6              Reviewed;         338 AA.
AC   B5VKE8;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=L-serine dehydratase;
DE            EC=4.3.1.17;
DE   AltName: Full=L-serine deaminase;
GN   Name=SDL1; Synonyms=SDH1; ORFNames=AWRI1631_90030;
OS   Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=545124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1631;
RX   PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA   Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT   "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL   FEMS Yeast Res. 8:1185-1195(2008).
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}.
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DR   EMBL; ABSV01001169; EDZ71597.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5VKE8; -.
DR   SMR; B5VKE8; -.
DR   TopDownProteomics; B5VKE8; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000008988; Unassembled WGS sequence.
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_0000393396"
FT   MOD_RES         39
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   338 AA;  36862 MW;  199DA2F645421F7D CRC64;
     MEMTHYEKTP LIRQVFNNGK TNSWFYVKHE ILQPGGSFKS RGIGHLIRKN NEEALSEGSG
     KLAVFSSSGG NAGLAAATAC RSMALNCSVV VPKTTKPRMV KKIQSAGAKV IIHGDHWGEA
     DEYLRHELMA QESQHGSKTL YVHPFDNETI WEGHSTIVDE IIEQLKENDI SLPRVKALVC
     SVGGGGLFSG IIKGLERNHL AEKIPVVAVE TAGCDVLNKS LKKGSPVTLE KLTSVATSLG
     SPYIASFAFE SFNKYGCKSV VLSDQDVLAT CLRYADDYNF IVEPACGASL HLCYHPEILE
     DILEQKIYED DIVIIIACGG SCMTYEDFVK ASSTLNVS