ID   SDHL_YEAS1              Reviewed;         338 AA.
AC   B3LU13;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=L-serine dehydratase;
DE            EC=4.3.1.17;
DE   AltName: Full=L-serine deaminase;
GN   Name=SDL1; Synonyms=SDH1; ORFNames=SCRG_05338;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; CH408055; EDV09644.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LU13; -.
DR   SMR; B3LU13; -.
DR   EnsemblFungi; EDV09644; EDV09644; SCRG_05338.
DR   HOGENOM; CLU_021152_3_1_1; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000008335; 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_0000393395"
FT   MOD_RES         39
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   338 AA;  36800 MW;  CBF4CAC6DE4D58A5 CRC64;
     MEMTHYEKTP LIRQVFNNGK TNSWFYVKHE ILQPGGSFKS RGIGHLIRKS NEEALSEGSG
     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