ID   SDHL_BOVIN              Reviewed;         327 AA.
AC   Q0VCW4;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=L-serine dehydratase/L-threonine deaminase;
DE            Short=SDH;
DE            EC=4.3.1.17;
DE   AltName: Full=L-serine deaminase;
DE   AltName: Full=L-threonine dehydratase;
DE            Short=TDH;
DE            EC=4.3.1.19;
GN   Name=SDS; Synonyms=SDH;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108,
CC         ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       {ECO:0000305}.
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DR   EMBL; BC119966; AAI19967.1; -; mRNA.
DR   RefSeq; NP_001069130.1; NM_001075662.1.
DR   AlphaFoldDB; Q0VCW4; -.
DR   SMR; Q0VCW4; -.
DR   STRING; 9913.ENSBTAP00000042524; -.
DR   PaxDb; Q0VCW4; -.
DR   PeptideAtlas; Q0VCW4; -.
DR   PRIDE; Q0VCW4; -.
DR   GeneID; 514346; -.
DR   KEGG; bta:514346; -.
DR   CTD; 10993; -.
DR   eggNOG; KOG1250; Eukaryota.
DR   InParanoid; Q0VCW4; -.
DR   OrthoDB; 1199679at2759; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003941; F:L-serine ammonia-lyase activity; ISS:UniProtKB.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006565; P:L-serine catabolic process; ISS:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0042866; P:pyruvate biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cytoplasm; Gluconeogenesis; Lipid metabolism; Lyase; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN           1..327
FT                   /note="L-serine dehydratase/L-threonine deaminase"
FT                   /id="PRO_0000264629"
FT   MOD_RES         41
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   327 AA;  34441 MW;  214129C45F9CF9CE CRC64;
     MMSGRPLHME TPVRDSMTLS KVAGTTAYLK LDSAQPSGSF KIRGIGHLCK MWAERGCEHF
     VCSSAGNAGM AAAYAARKLG IPSTIVVPST TPALTIQRLK NEGATVKVVG ETLDEAIRVA
     KDLEKNNSGW VYVPPFDDPL IWEGHSSIVK ELKETMTEKP GAIVLAVGGG GLLCGVVQGL
     AEVGWRDVPV ITMETIGAES FHASTKAGKL VTLPCITSVA KALGVTTVAA QAMKVYREHP
     IFSEVVSDQE AVAALEKFVD DEKILVEPAC GAALAAVYSN VIQKLQGEGK LRTPLSSLVV
     IVCGGSNISL AQLVALKKQL GMDGLSQ