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Database: UniProt
Entry: Q60HD7
LinkDB: Q60HD7
Original site: Q60HD7 
ID   SERA_MACFA              Reviewed;         533 AA.
AC   Q60HD7; Q4R4T2;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 4.
DT   16-JAN-2019, entry version 86.
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; ORFNames=QccE-10982, QccE-21483;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RA   Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT   "Isolation and characterization of cDNA for macaque neurological
RT   disease genes.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) 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; AB125190; BAD51978.1; -; mRNA.
DR   EMBL; AB169812; BAE01893.1; -; mRNA.
DR   RefSeq; XP_005542202.1; XM_005542145.2.
DR   UniGene; Mfa.846; -.
DR   ProteinModelPortal; Q60HD7; -.
DR   SMR; Q60HD7; -.
DR   PRIDE; Q60HD7; -.
DR   Ensembl; ENSMFAT00000069009; ENSMFAP00000018464; ENSMFAG00000032226.
DR   GeneID; 102128351; -.
DR   KEGG; mcf:102128351; -.
DR   CTD; 26227; -.
DR   GeneTree; ENSGT00940000155863; -.
DR   HOVERGEN; HBG054241; -.
DR   KO; K00058; -.
DR   OrthoDB; 911009at2759; -.
DR   UniPathway; UPA00135; UER00196.
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; Isopeptide bond; NAD;
KW   Oxidoreductase; Phosphoprotein; 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_0000076013.
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}.
FT   CONFLICT     95     95       V -> G (in Ref. 2; BAE01893).
FT                                {ECO:0000305}.
FT   CONFLICT    178    178       I -> V (in Ref. 2; BAE01893).
FT                                {ECO:0000305}.
FT   CONFLICT    442    442       T -> K (in Ref. 1; BAD51978).
FT                                {ECO:0000305}.
SQ   SEQUENCE   533 AA;  56518 MW;  92875C1F602A0956 CRC64;
     MAFANLRKVL ISDSLDPCCR KILQDGGLQV VEKQNLSKEE LIAELQDCEG LIVRSATKVT
     ADVINAAEKL QVVGRAGTGV DNVDLEAATR KGVLVMNTPN GNSLSAAELT CGMIMCLARQ
     IPQATASMKD GKWERKKFMG TELNGKTLGI LGLGRIGREV ATRMQSFGMK TIGYDPIISP
     EVSASFGVQQ LPLEEIWPLC DFITVHTPLL PSTTGLLNDN TFAQCKKGVR VVNCARGGIV
     DEGALLRALQ SGQCAGAALD VFTEEPPRDR ALVDHENVIS CPHLGASTKE AQSRCGEEIA
     VQFVDMVKGK SLAGVVNAQA LTSAFSPHTK PWIGLAEALG TLMRAWAGSP KGTIQVITQG
     TSLKNAGNCL SPAVIVGLLK EASKQADVNL VNAKLLVKEA GLDVTTSHSP AAPGEQGFGE
     CLLAVALAGA PYQAVGLVQG TTPVLQGLNG AVFRPEVPLR RGLPLLLFRT QTSDPAMLPT
     MIGLLAEAGV RLLSYQTSLV SDGETWHVMG ISSLLPSLEA WKPHVTEAFQ FHF
//
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