SERA_MACFA
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 03-AUG-2022, entry version 101.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC 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 disease
RT 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-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; AB125190; BAD51978.1; -; mRNA.
DR EMBL; AB169812; BAE01893.1; -; mRNA.
DR RefSeq; XP_005542202.1; XM_005542145.2.
DR AlphaFoldDB; Q60HD7; -.
DR SMR; Q60HD7; -.
DR STRING; 9541.XP_005542202.1; -.
DR GeneID; 102128351; -.
DR KEGG; mcf:102128351; -.
DR CTD; 26227; -.
DR VEuPathDB; HostDB:ENSMFAG00000032226; -.
DR eggNOG; KOG0068; Eukaryota.
DR OrthoDB; 911009at2759; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000233100; Chromosome 1.
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 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; 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; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Serine biosynthesis; Ubl conjugation.
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_0000076013"
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 21
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q61753"
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"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:O43175"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O43175"
FT CONFLICT 95
FT /note="V -> G (in Ref. 2; BAE01893)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="I -> V (in Ref. 2; BAE01893)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="T -> K (in Ref. 1; BAD51978)"
FT /evidence="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
