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Database: UniProt
Entry: A5A6P1
LinkDB: A5A6P1
Original site: A5A6P1 
ID   SERA_PANTR              Reviewed;         533 AA.
AC   A5A6P1;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JAN-2019, entry version 76.
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   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cerebellum;
RX   PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
RA   Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
RA   Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
RT   "Mapping of chimpanzee full-length cDNAs onto the human genome unveils
RT   large potential divergence of the transcriptome.";
RL   Gene 399:1-10(2007).
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; AB222169; BAF62414.1; -; mRNA.
DR   RefSeq; NP_001092041.1; NM_001098571.1.
DR   UniGene; Ptr.3081; -.
DR   ProteinModelPortal; A5A6P1; -.
DR   SMR; A5A6P1; -.
DR   STRING; 9598.ENSPTRP00000002013; -.
DR   PaxDb; A5A6P1; -.
DR   PRIDE; A5A6P1; -.
DR   GeneID; 739534; -.
DR   KEGG; ptr:739534; -.
DR   CTD; 26227; -.
DR   eggNOG; KOG0068; Eukaryota.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000136693; -.
DR   HOVERGEN; HBG054241; -.
DR   InParanoid; A5A6P1; -.
DR   KO; K00058; -.
DR   OrthoDB; 911009at2759; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000002277; 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; IBA:GO_Central.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
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_0000297547.
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;  56663 MW;  A98EAB396EAB8770 CRC64;
     MAFANLRKVL ISDSLDPCCR KILQDGGLQV VEKQNLSKEE LIAELQDCEG LIVRSATKVT
     ADVINAAEKL QVVGRAGTGV DNVDLEAATR KGILVMNTPN GNSLSAAELT CGMIMCLARQ
     IPQATASMKD GKWERKKFMG TELNGKTLGI LGLGRIGREV ATRMQSFGMK TIGYDPIISP
     EVSASFGVQQ LPLEEIWPLC DFITVHTPLL PSTTGLLNDN TFAQCKKGVR VVNCARGGIV
     DEGALLRALQ SGQCAGAALD VFTEEPPRDR ALVDHENVIS CPHLGASTKE AQSRCGEEIA
     VQFVDMVKGK SLTGVVNAQA LTSAFSPHTK PWIGLAEALG TLMRAWAGSP KGTIQVITQG
     TSLKNAGNCL SPAVIVGLLK EASKQADVNL VNAKLLVKEA GLNVTTSHSP AAPGEQGFGE
     CLLAVALAGA PYQAVGLVQG TTPVLQGLNG AVFRPEVPLR RDLPLLLFRT QTSDPAMPPT
     MMGLLAEAGV RLLSYQTSLV SDGETWHVMG IPSLLPSLEA WKQHVTEAFQ FHF
//
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