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Database: UniProt
Entry: Q5R7M2
LinkDB: Q5R7M2
Original site: Q5R7M2 
ID   SERA_PONAB              Reviewed;         533 AA.
AC   Q5R7M2;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   05-DEC-2018, entry version 87.
DE   RecName: Full=D-3-phosphoglycerate dehydrogenase;
DE            Short=3-PGDH;
DE            EC=1.1.1.95 {ECO:0000250|UniProtKB:O43175};
DE   AltName: Full=2-oxoglutarate reductase {ECO:0000305};
DE            EC=1.1.1.399 {ECO:0000250|UniProtKB:O43175};
DE   AltName: Full=Malate dehydrogenase {ECO:0000305};
DE            EC=1.1.1.37 {ECO:0000250|UniProtKB:O43175};
GN   Name=PHGDH;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Also catalyzes the
CC       reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and
CC       the reversible oxidation of (S)-malate to oxaloacetate.
CC       {ECO:0000250|UniProtKB:O43175}.
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:0000250|UniProtKB:O43175};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) +
CC         NADH; Xref=Rhea:RHEA:49612, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15801, ChEBI:CHEBI:16810, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.399;
CC         Evidence={ECO:0000250|UniProtKB:O43175};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC         Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.37; Evidence={ECO:0000250|UniProtKB:O43175};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine
CC       from 3-phospho-D-glycerate: step 1/3.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:O08651}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; CR860092; CAH92238.1; -; mRNA.
DR   RefSeq; NP_001126309.1; NM_001132837.1.
DR   UniGene; Pab.19861; -.
DR   ProteinModelPortal; Q5R7M2; -.
DR   SMR; Q5R7M2; -.
DR   STRING; 9601.ENSPPYP00000001120; -.
DR   PRIDE; Q5R7M2; -.
DR   GeneID; 100173288; -.
DR   CTD; 26227; -.
DR   eggNOG; KOG0068; Eukaryota.
DR   eggNOG; COG0111; LUCA.
DR   HOVERGEN; HBG054241; -.
DR   InParanoid; Q5R7M2; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
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; PS00306; CASEIN_ALPHA_BETA; 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   2: Evidence at transcript level;
KW   Acetylation; Amino-acid biosynthesis; Complete proteome;
KW   Isopeptide bond; NAD; Oxidoreductase; Phosphoprotein;
KW   Reference proteome; Serine biosynthesis; Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:O43175}.
FT   CHAIN         2    533       D-3-phosphoglycerate dehydrogenase.
FT                                /FTId=PRO_0000076015.
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;  56512 MW;  4B4F33D534767322 CRC64;
     MAFANLRKVL ISDSLDPCCR KILQDGGLQV VEKQNLSKEE LIAELQDCEG LIVRSATKVT
     ADVINAAEKL QVVGRAGTGV DNVDLEAATR KGILVMNTPN GNSLSAAELT CGMIMCLARQ
     IPQATASMKD GKWERKKFMG TELNGKTLGI LGLGRIGREV AIRMQSLGMK TIGYDPIISP
     EVSASFGVQQ LPLEEIWPLC DFITVHTPLL PSTTGLLNDN TFAQCKKGVR VVNCARGGIV
     DEGALLRALQ SGQCAGAALD VFTEEPPRGR ALVDHENVIS CPHLGASTKE AQSRCGEEIA
     VQFVDMVKGK SLTGVVNAQA LTSAFSPHTK PWIGLAEALG TLMRAWAGSP KGAIQVITQG
     TSLKNAGNCL SPAVIVGLLK EASKQADVNL VNAKLLVKEA GLNVTTSHSP AAPGEQGFGE
     CLLAVALAGA PYQAVGLVQG TTPVLQGLNG AVFRPEVPLR RDLPLLLFRT QTSDPAMLPT
     MIGLLAEAGV RLLSYQTSLV SDGETWHVMG ISSLLPSLEA WKQHATEAFQ FHF
//
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