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Database: UniProt
Entry: A0A0E0LE72_ORYPU
LinkDB: A0A0E0LE72_ORYPU
Original site: A0A0E0LE72_ORYPU 
ID   A0A0E0LE72_ORYPU        Unreviewed;       580 AA.
AC   A0A0E0LE72;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=phosphoglycerate dehydrogenase {ECO:0000256|ARBA:ARBA00013143};
DE            EC=1.1.1.95 {ECO:0000256|ARBA:ARBA00013143};
OS   Oryza punctata (Red rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC06G21050.1};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC06G21050.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OPUNC06G21050.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+)
CC         + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378, ChEBI:CHEBI:18110,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58272; EC=1.1.1.95;
CC         Evidence={ECO:0000256|ARBA:ARBA00001878};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC       3-phospho-D-glycerate: step 1/3. {ECO:0000256|ARBA:ARBA00005216}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854}.
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DR   AlphaFoldDB; A0A0E0LE72; -.
DR   STRING; 4537.A0A0E0LE72; -.
DR   EnsemblPlants; OPUNC06G21050.1; OPUNC06G21050.1; OPUNC06G21050.
DR   Gramene; OPUNC06G21050.1; OPUNC06G21050.1; OPUNC06G21050.
DR   eggNOG; KOG0068; Eukaryota.
DR   HOGENOM; CLU_019796_8_1_1; -.
DR   OMA; ERIFHDD; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000026962; Chromosome 6.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR   CDD; cd04902; ACT_3PGDH-xct; 1.
DR   CDD; cd12173; PGDH_4; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
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; IPR045626; PGDH_ASB_dom.
DR   PANTHER; PTHR42938:SF49; D-3-PHOSPHOGLYCERATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF19304; PGDH_inter; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF143548; Serine metabolism enzymes domain; 1.
DR   PROSITE; PS51671; ACT; 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   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026962}.
FT   DOMAIN          508..580
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   580 AA;  60704 MW;  147689A72C0614C0 CRC64;
     MALAAPLCHL LAAPAPPSTS HAADAAHDPA HHRASPLRRR GRGRLFLACR IPAAAPSARG
     AAAGVAAAAA TAAGRPTVLV TEKLGDAGLE LLRRFANVDC AYELTAEELR AKVSLVDALV
     VRSATRVTRE VFEAARGRLR VVGRAGVGID NVDLQAATEA GCLVVNAPTA NTVAAAEHAI
     ALLAAMARNV AQADASLKAG KWQRNKYVGV SLVGKTLAIM GFGKVGSEVA RRAKGLGMDI
     IAHDPYAPVD RARAIGVDLV SFDEAISTAD FISLHMPLTP STAKLFDEET FANMKKGVRI
     INVARGGVVD EDALLRALDN GTVSQEGVAL EIAEAVLGAL KGELAATAVN APMVPAEVLS
     ELSPYVVLAE KLGRLVVQLV AGGSGIKGVK IVYSSSRDPD DLDTRVLRAM VTKGIIEPIS
     SAFVNIVNAD YVAKQRGLRI SEERILLDGS PEVPIDSIQV HLANVESKFA GALSDEGDIR
     VEGEVKDGKP HLTLVGPFSV DVSLEGNLIL CRQVDQPGII GKVGSILGKM NVNVNFMSVG
     RTAPGKQAIM AIGVDEEPEK EALKLIGDIP SVEEFVFIKL
//
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