SDHL_MOUSE
ID SDHL_MOUSE Reviewed; 327 AA.
AC Q8VBT2;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 144.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 [2]
RP PROTEIN SEQUENCE OF 2-10 AND 235-257, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Bienvenut W.V.;
RL Submitted (JUL-2005) to UniProtKB.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; BC021605; AAH21605.1; -; mRNA.
DR EMBL; BC021950; AAH21950.1; -; mRNA.
DR CCDS; CCDS19619.1; -.
DR RefSeq; NP_663540.1; NM_145565.1.
DR AlphaFoldDB; Q8VBT2; -.
DR SMR; Q8VBT2; -.
DR STRING; 10090.ENSMUSP00000064849; -.
DR iPTMnet; Q8VBT2; -.
DR PhosphoSitePlus; Q8VBT2; -.
DR SwissPalm; Q8VBT2; -.
DR jPOST; Q8VBT2; -.
DR MaxQB; Q8VBT2; -.
DR PaxDb; Q8VBT2; -.
DR PRIDE; Q8VBT2; -.
DR ProteomicsDB; 253433; -.
DR Antibodypedia; 31269; 264 antibodies from 18 providers.
DR DNASU; 231691; -.
DR Ensembl; ENSMUST00000066540; ENSMUSP00000064849; ENSMUSG00000029597.
DR Ensembl; ENSMUST00000201684; ENSMUSP00000143838; ENSMUSG00000029597.
DR GeneID; 231691; -.
DR KEGG; mmu:231691; -.
DR UCSC; uc008zhg.1; mouse.
DR CTD; 10993; -.
DR MGI; MGI:98270; Sds.
DR VEuPathDB; HostDB:ENSMUSG00000029597; -.
DR eggNOG; KOG1250; Eukaryota.
DR GeneTree; ENSGT00940000160172; -.
DR InParanoid; Q8VBT2; -.
DR OMA; AEQGCEH; -.
DR OrthoDB; 1199679at2759; -.
DR PhylomeDB; Q8VBT2; -.
DR TreeFam; TF329014; -.
DR Reactome; R-MMU-8849175; Threonine catabolism.
DR UniPathway; UPA00138; -.
DR BioGRID-ORCS; 231691; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Sbds; mouse.
DR PRO; PR:Q8VBT2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8VBT2; protein.
DR Bgee; ENSMUSG00000029597; Expressed in left lobe of liver and 43 other tissues.
DR ExpressionAtlas; Q8VBT2; baseline and differential.
DR Genevisible; Q8VBT2; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; ISO:MGI.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0042866; P:pyruvate biosynthetic process; ISO:MGI.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Gluconeogenesis;
KW Lipid metabolism; Lyase; Pyridoxal phosphate; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..327
FT /note="L-serine dehydratase/L-threonine deaminase"
FT /id="PRO_0000185595"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.2"
FT MOD_RES 41
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 327 AA; 34593 MW; E4BBA96CE7147237 CRC64;
MAAQESLHVK TPLRDSMALS KLAGTSVFLK MDSSQPSGSF KIRGIGHLCK MKAKQGCRHF
VCSSAGNAGM ATAYAARRLG IPATIVVPNT TPALTIERLK NEGATVEVVG EMLDEAIQVA
KALEKNNPGW VYISPFDDPL IWEGHTSLVK ELKETLSAKP GAIVLSVGGG GLLCGVVQGL
REVGWEDVPI IAMETFGAHS FHAAIKEGKL VTLPKITSVA KALGVNTVGA QTLKLFYEHP
IFSEVISDQE AVSALEKFVD DEKILVEPAC GAALAAVYSR VVCRLQDEGR LQTPLASLVV
IVCGGSNISL AQLQALKVQL GLNGLPE
