SDHL_RAT
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 03-AUG-2022, entry version 173.
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 PaxDb; P09367; -.
DR Ensembl; ENSRNOT00000001875; ENSRNOP00000001875; ENSRNOG00000001388. [P09367-2]
DR GeneID; 25044; -.
DR KEGG; rno:25044; -.
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; 1199679at2759; -.
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 tissues.
DR ExpressionAtlas; P09367; baseline and differential.
DR Genevisible; P09367; RN.
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 Gene3D; 3.40.50.1100; -; 4.
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 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
