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Database: UniProt
Entry: O08651
LinkDB: O08651
Original site: O08651 
ID   SERA_RAT                Reviewed;         533 AA.
AC   O08651; Q546Q9;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   13-FEB-2019, entry version 154.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase;
DE            Short=3-PGDH;
DE            EC=1.1.1.95 {ECO:0000269|PubMed:9163325};
GN   Name=Phgdh;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, TISSUE SPECIFICITY, FUNCTION,
RP   CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=9163325; DOI=10.1042/bj3230365;
RA   Achouri Y., Rider M.H., van Schaftingen E., Robbi M.;
RT   "Cloning, sequencing and expression of rat liver 3-phosphoglycerate
RT   dehydrogenase.";
RL   Biochem. J. 323:365-370(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Robbi M., Achouri Y., Szpirer C., Van Schaftingen E.;
RT   "Structure and chromosomal localization of the rat gene encoding 3-
RT   phosphoglycerate dehydrogenase.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 34-54; 248-270; 271-289 AND 365-380, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (NOV-2006) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-
CC       glycerate to 3-phosphonooxypyruvate, the first step of the
CC       phosphorylated L-serine biosynthesis pathway. Does not catalyze
CC       the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate
CC       and the reversible oxidation of (S)-malate to oxaloacetate.
CC       {ECO:0000269|PubMed:9163325}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phospho-D-glycerate + NAD(+) = 3-phosphooxypyruvate +
CC         H(+) + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18110, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58272; EC=1.1.1.95;
CC         Evidence={ECO:0000269|PubMed:9163325};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 1/3.
CC       {ECO:0000269|PubMed:9163325}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9163325}.
CC   -!- TISSUE SPECIFICITY: Liver, kidney, brain, testis.
CC       {ECO:0000269|PubMed:9163325}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; X97772; CAA66374.1; -; mRNA.
DR   EMBL; AJ271975; CAB89828.1; -; Genomic_DNA.
DR   EMBL; BC086327; AAH86327.1; -; mRNA.
DR   RefSeq; NP_113808.1; NM_031620.1.
DR   RefSeq; XP_006233072.1; XM_006233010.1.
DR   UniGene; Rn.6872; -.
DR   ProteinModelPortal; O08651; -.
DR   SMR; O08651; -.
DR   BioGrid; 248638; 2.
DR   IntAct; O08651; 1.
DR   STRING; 10116.ENSRNOP00000053019; -.
DR   iPTMnet; O08651; -.
DR   PhosphoSitePlus; O08651; -.
DR   SwissPalm; O08651; -.
DR   World-2DPAGE; 0004:O08651; -.
DR   jPOST; O08651; -.
DR   PaxDb; O08651; -.
DR   PRIDE; O08651; -.
DR   Ensembl; ENSRNOT00000056173; ENSRNOP00000053019; ENSRNOG00000019328.
DR   GeneID; 58835; -.
DR   KEGG; rno:58835; -.
DR   UCSC; RGD:61987; rat.
DR   CTD; 26227; -.
DR   RGD; 61987; Phgdh.
DR   eggNOG; KOG0068; Eukaryota.
DR   eggNOG; COG0111; LUCA.
DR   GeneTree; ENSGT00940000155863; -.
DR   HOGENOM; HOG000136693; -.
DR   HOVERGEN; HBG054241; -.
DR   InParanoid; O08651; -.
DR   KO; K00058; -.
DR   OMA; NIAGMQV; -.
DR   OrthoDB; 911009at2759; -.
DR   PhylomeDB; O08651; -.
DR   TreeFam; TF314548; -.
DR   BioCyc; MetaCyc:MONOMER-10261; -.
DR   Reactome; R-RNO-977347; Serine biosynthesis.
DR   UniPathway; UPA00135; UER00196.
DR   PRO; PR:O08651; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000019328; Expressed in 10 organ(s), highest expression level in adult mammalian kidney.
DR   Genevisible; O08651; RN.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IDA:RGD.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR   GO; GO:0070314; P:G1 to G0 transition; IEA:Ensembl.
DR   GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:Ensembl.
DR   GO; GO:0021782; P:glial cell development; IEA:Ensembl.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:Ensembl.
DR   GO; GO:0006544; P:glycine metabolic process; IEA:Ensembl.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0021915; P:neural tube development; IEA:Ensembl.
DR   GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0009070; P:serine family amino acid biosynthetic process; TAS:RGD.
DR   GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR   GO; GO:0019530; P:taurine metabolic process; IEA:Ensembl.
DR   GO; GO:0006566; P:threonine metabolic process; IEA:Ensembl.
DR   Gene3D; 3.30.1330.90; -; 1.
DR   InterPro; IPR029009; ASB_dom_sf.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006236; PGDH.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF143548; SSF143548; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01327; PGDH; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Amino-acid biosynthesis; Complete proteome;
KW   Direct protein sequencing; Isopeptide bond; NAD; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Serine biosynthesis;
KW   Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:O43175}.
FT   CHAIN         2    533       D-3-phosphoglycerate dehydrogenase.
FT                                /FTId=PRO_0000076016.
FT   NP_BIND     155    156       NAD. {ECO:0000250|UniProtKB:O43175}.
FT   NP_BIND     234    236       NAD. {ECO:0000250|UniProtKB:O43175}.
FT   NP_BIND     283    286       NAD. {ECO:0000250|UniProtKB:O43175}.
FT   ACT_SITE    236    236       {ECO:0000250}.
FT   ACT_SITE    265    265       {ECO:0000250}.
FT   ACT_SITE    283    283       Proton donor. {ECO:0000250}.
FT   BINDING      78     78       NAD. {ECO:0000250|UniProtKB:O43175}.
FT   BINDING     175    175       NAD. {ECO:0000250|UniProtKB:O43175}.
FT   BINDING     207    207       NAD; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:O43175}.
FT   BINDING     260    260       NAD. {ECO:0000250|UniProtKB:O43175}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:O43175}.
FT   MOD_RES      14     14       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O43175}.
FT   MOD_RES      21     21       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q61753}.
FT   MOD_RES      58     58       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q61753}.
FT   MOD_RES      78     78       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O43175}.
FT   CROSSLNK     21     21       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO1);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:O43175}.
FT   CROSSLNK     21     21       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:O43175}.
SQ   SEQUENCE   533 AA;  56493 MW;  7273DAC3349E95EF CRC64;
     MAFANLRKIL ISDSLDPCCR KILQDGGLQV VEKQNLSKEE LIAELQDCEG LIVRSATKVT
     ADVINAAEKL QVVGRAGTGV DNVDLEAATR KGVLVMNTPN GNSLSAAELT CGMLMCLARQ
     IPQATASMKD GKWDRKKFMG TELNGKTLGI LGLGRIGREV AARMQAFGMK TVGYDPIISP
     EVAASFGVQQ LPLEEIWPLC DFITVHTPLL PSTTGLLNDS TFAQCKKGVR VVNCARGGIV
     DEGALLRALQ SGQCAGAALD VFTEEPPRDR ALVDHENVIS CPHLGASTKE AQSRCGEEIA
     VQFVDMVKGK SLTGVVNAQA LTSAFSPHTK PWIGLAEALG TLMHAWAGSP KGTIQVVTQG
     TSLKNAGTCL SPAVIVGLLR EASKQADVNL VNAKLLVKEA GLNVTTSHSP GVPGEQGIGE
     CLLTVALAGA PYQAVGLVQG TTPMLQMLNG AVFRPEVPLR RGQPLLLFRA QPSDPVMLPT
     MIGLLAEAGV QLLSYQTSKV SDGDTWHVMG LSSLLPSLDA WKQHVSEAFQ FCF
//
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