ID   SDHL_YEAS7              Reviewed;         338 AA.
AC   A6ZVB1;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=L-serine dehydratase;
DE            EC=4.3.1.17;
DE   AltName: Full=L-serine deaminase;
GN   Name=SDL1; Synonyms=SDH1; ORFNames=SCY_2627;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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; AAFW02000124; EDN61336.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZVB1; -.
DR   SMR; A6ZVB1; -.
DR   EnsemblFungi; EDN61336; EDN61336; SCY_2627.
DR   HOGENOM; CLU_021152_3_1_1; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000007060; 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_0000393397"
FT   MOD_RES         39
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   338 AA;  36786 MW;  6BF1CAC505263513 CRC64;
     MEMTHYEKTP LIRQVFNNGK TNSWFYVKHE ILQPGGSFKS RGIGHLIRKS NEEALSEGSG
     KLAVFSSSGG NAGLAAATAC RSMALNCSVV VPKTTKPRMV KKIQSAGAKV IIHGDHWGEA
     DEYLRHKLMA QESQHGSKTL YVHPFDNETI WEGHSTIVDE IIEQLKENDI SLPRVKALVC
     SVGGGGLFSG IIKGLDRNHL AEKIPVVAVE TAGCDVLNKS LKNGSPVTLE KLTSVATSLA
     SPYIASFAFE SFNKYGCKSV VLSDQDVLAT CLRYADDYNF IVEPACGASL HLCYHPEILE
     DILEQKIYED DIVIIIACGG SCMTYEDLVK ASSTLNVS