SERA_PIG
ID SERA_PIG Reviewed; 533 AA.
AC A5GFY8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Porcine genome sequencing project;
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-glycerate
CC to 3-phosphonooxypyruvate, the first step of the phosphorylated L-
CC serine biosynthesis pathway. Also catalyzes the reversible oxidation of
CC 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of
CC (S)-malate to oxaloacetate. {ECO:0000250|UniProtKB:O43175}.
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:0000250|UniProtKB:O43175};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) +
CC NADH; Xref=Rhea:RHEA:49612, ChEBI:CHEBI:15378, ChEBI:CHEBI:15801,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.399; 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; EC=1.1.1.37;
CC Evidence={ECO:0000250|UniProtKB:O43175};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 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}.
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DR EMBL; CR956647; CAN13230.1; -; Genomic_DNA.
DR RefSeq; NP_001116634.1; NM_001123162.1.
DR AlphaFoldDB; A5GFY8; -.
DR SMR; A5GFY8; -.
DR STRING; 9823.ENSSSCP00000007163; -.
DR PaxDb; A5GFY8; -.
DR PeptideAtlas; A5GFY8; -.
DR PRIDE; A5GFY8; -.
DR Ensembl; ENSSSCT00000007358; ENSSSCP00000007163; ENSSSCG00000006717.
DR GeneID; 100144529; -.
DR KEGG; ssc:100144529; -.
DR CTD; 26227; -.
DR VGNC; VGNC:98184; PHGDH.
DR eggNOG; KOG0068; Eukaryota.
DR GeneTree; ENSGT00940000155863; -.
DR HOGENOM; CLU_019796_8_1_1; -.
DR InParanoid; A5GFY8; -.
DR OMA; NIAGMQV; -.
DR OrthoDB; 911009at2759; -.
DR TreeFam; TF314548; -.
DR Reactome; R-SSC-977347; Serine biosynthesis.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000008227; Chromosome 4.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000006717; Expressed in uterus and 43 other tissues.
DR ExpressionAtlas; A5GFY8; baseline and differential.
DR Genevisible; A5GFY8; SS.
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: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 InterPro; IPR045626; PGDH_ASB_dom.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR Pfam; PF19304; PGDH_inter; 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 3: Inferred from homology;
KW Acetylation; Amino-acid biosynthesis; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Serine biosynthesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43175"
FT CHAIN 2..533
FT /note="D-3-phosphoglycerate dehydrogenase"
FT /id="PRO_0000318300"
FT ACT_SITE 236
FT /evidence="ECO:0000250"
FT ACT_SITE 265
FT /evidence="ECO:0000250"
FT ACT_SITE 283
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O43175"
FT BINDING 155..156
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O43175"
FT BINDING 175
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O43175"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O43175"
FT BINDING 234..236
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O43175"
FT BINDING 260
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O43175"
FT BINDING 283..286
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O43175"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O43175"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43175"
FT MOD_RES 58
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61753"
FT MOD_RES 78
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43175"
SQ SEQUENCE 533 AA; 56810 MW; 2D80F1809E1579BE CRC64;
MAFANLRKVL ISDSLDPCCR EILQDGGLQV VEKQNLSKEE LIAELQDCEG LIVRSATKVT
SDVINAAKKL QVVGRAGTGV DNVDLEAATR KGILVMNTPN GNSLSAAELT CGMILCLARQ
IPQATASMKD GKWERKKFMG TELNGKVLGI LGLGRIGREV ATRMQSFGMK TIGYDPIIAP
EVSASFGVQQ LPLEEIWPLC DFITVHTPLL PSTTGLLNDS TFALCKKGVR VVNCARGGIV
DEGALLRALQ SGQCAGAALD VFTEEPPRDR ALVDHEKVIS CPHLGASTRE AQSRCGEEIA
IQFVDMVKGR SLAGVVNAQA LTSAFSPHTK PWIGLAEALG ALMQAWAGSP KGTIQVVTQG
TSLKNSGTCL SPAVIVGLLK EASHRADVNL VNAKLLEKEA GLHVTTSHNP AAPEEQGGAE
CFLTVALAGA PYQAVGLVQG TAPMLHALNG AVFRPEVPLR RGLPLLLFRA QPSNPTMLPT
MIGLLAEARV QLLSYQTSVV SDGETWHVMA ISSLLPSLEP WKQHVTEAFQ FHF
