ID   SDHL_RAT                Reviewed;         363 AA.
AC   P09367; Q5M8C4;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 179.
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;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=3413060; DOI=10.1073/pnas.85.16.5809;
RA   Ogawa H., Miller D.A., Dunn T., Su Y., Burcham J.M., Peraino C.,
RA   Fujioka M., Babcock K., Pitot H.C.;
RT   "Isolation and nucleotide sequence of the cDNA for rat liver serine
RT   dehydratase mRNA and structures of the 5' and 3' flanking regions of the
RT   serine dehydratase gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:5809-5813(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3205731; DOI=10.1093/nar/16.22.10921;
RA   Ogawa H., Su Y., Dunn T., Miller D.A., Matsuda Y., Fujioka M., Pitot H.C.;
RT   "Sequence of the rat serine dehydratase gene.";
RL   Nucleic Acids Res. 16:10921-10923(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Liver;
RX   PubMed=3391277; DOI=10.1016/0014-5793(88)80110-8;
RA   Noda C., Ito K., Nakamura T., Ichihara A.;
RT   "Primary structure of rat liver serine dehydratase deduced from the cDNA
RT   sequence.";
RL   FEBS Lett. 234:331-335(1988).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-363 (ISOFORM 2).
RC   STRAIN=Wistar; TISSUE=Liver;
RX   PubMed=2228554;
RA   Leoncini R., Henschen A., Krieglstein K., Calvete J.J., Pagani R.,
RA   Marinello E.;
RT   "Primary structure of rat liver L-threonine deaminase.";
RL   Ital. J. Biochem. 39:228-234(1990).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-5 AND 31-50, CLEAVAGE OF INITIATOR METHIONINE,
RP   ACETYLATION AT ALA-2, AND PYRIDOXAL PHOSPHATE AT LYS-41.
RC   TISSUE=Liver;
RX   PubMed=2660911; DOI=10.1016/0167-4838(89)90106-4;
RA   Ogawa H., Konishi K., Fujioka M.;
RT   "The peptide sequences near the bound pyridoxal phosphate are conserved in
RT   serine dehydratase from rat liver, and threonine dehydratases from yeast
RT   and Escherichia coli.";
RL   Biochim. Biophys. Acta 996:139-141(1989).
RN   [7]
RP   PYRIDOXAL PHOSPHATE AT LYS-41.
RX   PubMed=2228555;
RA   Leoncini R., Henschen A., Krieglstein K., Calvete J.J., Pagani R.,
RA   Marinello E.;
RT   "Amino acid sequence around the pyridoxal 5'-phosphate binding site of rat
RT   liver L-threonine deaminase.";
RL   Ital. J. Biochem. 39:235-241(1990).
RN   [8]
RP   CHARACTERIZATION.
RC   TISSUE=Liver;
RX   PubMed=7581747; DOI=10.1159/000474974;
RA   Pagani R., Leoncini R., Pizzichini M., Vannoni D., Tabucci A.,
RA   Marinello E.;
RT   "Properties of rat liver L-threonine deaminase.";
RL   Enzyme Protein 48:90-97(1994).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   PubMed=14596599; DOI=10.1021/bi035324p;
RA   Yamada T., Komoto J., Takata Y., Ogawa H., Pitot H.C., Takusagawa F.;
RT   "Crystal structure of serine dehydratase from rat liver.";
RL   Biochemistry 42:12854-12865(2003).
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   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P09367-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P09367-2; Sequence=VSP_024798;
CC   -!- INDUCTION: By glucocorticoids and glucagon.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       {ECO:0000305}.
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DR   EMBL; J03863; AAA42123.1; -; mRNA.
DR   EMBL; X13119; CAA31511.1; -; Genomic_DNA.
DR   EMBL; Y00752; CAA68721.1; -; mRNA.
DR   EMBL; BC088110; AAH88110.1; -; mRNA.
DR   PIR; S01009; DWRTT.
DR   PIR; S01973; S01973.
DR   RefSeq; NP_446414.3; NM_053962.3. [P09367-2]
DR   PDB; 1PWE; X-ray; 2.80 A; A/B/C/D/E/F=1-363.
DR   PDB; 1PWH; X-ray; 2.60 A; A/B/C/D=1-363.
DR   PDBsum; 1PWE; -.
DR   PDBsum; 1PWH; -.
DR   AlphaFoldDB; P09367; -.
DR   SMR; P09367; -.
DR   STRING; 10116.ENSRNOP00000001876; -.
DR   ChEMBL; CHEMBL1075240; -.
DR   iPTMnet; P09367; -.
DR   PhosphoSitePlus; P09367; -.
DR   PaxDb; 10116-ENSRNOP00000001876; -.
DR   Ensembl; ENSRNOT00000001875.5; ENSRNOP00000001875.3; ENSRNOG00000001388.7. [P09367-2]
DR   GeneID; 25044; -.
DR   KEGG; rno:25044; -.
DR   AGR; RGD:67376; -.
DR   CTD; 10993; -.
DR   RGD; 67376; Sds.
DR   VEuPathDB; HostDB:ENSRNOG00000001388; -.
DR   eggNOG; KOG1250; Eukaryota.
DR   GeneTree; ENSGT00940000160172; -.
DR   HOGENOM; CLU_021152_3_0_1; -.
DR   InParanoid; P09367; -.
DR   OrthoDB; 8406at2759; -.
DR   PhylomeDB; P09367; -.
DR   BRENDA; 4.3.1.17; 5301.
DR   Reactome; R-RNO-8849175; Threonine catabolism.
DR   SABIO-RK; P09367; -.
DR   UniPathway; UPA00138; -.
DR   EvolutionaryTrace; P09367; -.
DR   PRO; PR:P09367; -.
DR   Proteomes; UP000002494; Chromosome 12.
DR   Bgee; ENSRNOG00000001388; Expressed in Ammon's horn and 15 other cell types or tissues.
DR   ExpressionAtlas; P09367; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003941; F:L-serine ammonia-lyase activity; ISO:RGD.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; ISO:RGD.
DR   GO; GO:0006094; P:gluconeogenesis; TAS:RGD.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006565; P:L-serine catabolic process; ISO:RGD.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0065003; P:protein-containing complex assembly; IDA:RGD.
DR   GO; GO:0042866; P:pyruvate biosynthetic process; ISO:RGD.
DR   GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR   GO; GO:0033590; P:response to cobalamin; IEP:RGD.
DR   GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR   GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central.
DR   CDD; cd06448; L-Ser-dehyd; 1.
DR   Gene3D; 3.40.50.1100; -; 4.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   PANTHER; PTHR48078:SF8; L-SERINE DEHYDRATASE_L-THREONINE DEAMINASE; 1.
DR   PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00291; PALP; 2.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
DR   Genevisible; P09367; RN.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; Gluconeogenesis; Lipid metabolism; Lyase;
KW   Pyridoxal phosphate; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2660911"
FT   CHAIN           2..363
FT                   /note="L-serine dehydratase/L-threonine deaminase"
FT                   /id="PRO_0000185596"
FT   REGION          74..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:2660911"
FT   MOD_RES         41
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   VAR_SEQ         65..100
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:3391277"
FT                   /id="VSP_024798"
FT   CONFLICT        12
FT                   /note="P -> T (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        16
FT                   /note="S -> T (in Ref. 1; AAA42123)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        164
FT                   /note="P -> Q (in Ref. 1; AAA42123)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        276
FT                   /note="P -> T (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        325
FT                   /note="G -> A (in Ref. 3; CAA68721)"
FT                   /evidence="ECO:0000305"
FT   STRAND          13..15
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   HELIX           17..23
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   STRAND          27..30
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   HELIX           32..34
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   HELIX           42..54
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   STRAND          59..63
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   HELIX           103..114
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   STRAND          119..123
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   HELIX           129..137
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   STRAND          141..144
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   HELIX           149..161
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   STRAND          166..169
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   TURN            171..173
FT                   /evidence="ECO:0007829|PDB:1PWE"
FT   HELIX           175..191
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   STRAND          199..202
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   STRAND          204..206
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   HELIX           207..219
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   STRAND          226..231
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   HELIX           236..243
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   HELIX           257..259
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   HELIX           266..272
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   TURN            273..276
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   STRAND          277..282
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   HELIX           284..298
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   HELIX           304..314
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   HELIX           317..323
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   STRAND          324..327
FT                   /evidence="ECO:0007829|PDB:1PWE"
FT   STRAND          334..337
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   HELIX           346..355
FT                   /evidence="ECO:0007829|PDB:1PWH"
FT   TURN            356..359
FT                   /evidence="ECO:0007829|PDB:1PWH"
SQ   SEQUENCE   363 AA;  38433 MW;  C94FFF2EB9C6E33C CRC64;
     MAAQESLHVK TPLRDSMALS KVAGTSVFLK MDSSQPSGSF KIRGIGHLCK MKAKQGCKHF
     VCSSVVQIWG SRMRGRSHSG DEQPHVRSQA LLPDTPSPLT AGNAGMATAY AARRLGLPAT
     IVVPSTTPAL TIERLKNEGA TVEVVGEMLD EAIQLAKALE KNNPGWVYIS PFDDPLIWEG
     HTSLVKELKE TLSAKPGAIV LSVGGGGLLC GVVQGLREVG WEDVPIIAME TFGAHSFHAA
     VKEGKLVTLP KITSVAKALG VNTVGAQTLK LFYEHPIFSE VISDQEAVTA IEKFVDDEKI
     LVEPACGAAL AAVYSGVVCR LQAEGRLQTP LASLVVIVCG GSNISLAQLQ ALKAQLGLNE
     LLK
//