ID A0A2Y9P0A9_DELLE Unreviewed; 533 AA.
AC A0A2Y9P0A9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|ARBA:ARBA00021582, ECO:0000256|RuleBase:RU363003};
DE EC=1.1.1.95 {ECO:0000256|ARBA:ARBA00013143, ECO:0000256|RuleBase:RU363003};
GN Name=PHGDH {ECO:0000313|RefSeq:XP_022439645.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022439645.1};
RN [1] {ECO:0000313|RefSeq:XP_022439645.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022439645.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001878,
CC ECO:0000256|RuleBase:RU363003};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 1/3. {ECO:0000256|ARBA:ARBA00005216,
CC ECO:0000256|RuleBase:RU363003}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU363003}.
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DR RefSeq; XP_022439645.1; XM_022583937.2.
DR AlphaFoldDB; A0A2Y9P0A9; -.
DR STRING; 9749.A0A2Y9P0A9; -.
DR Ensembl; ENSDLET00000012933; ENSDLEP00000011724; ENSDLEG00000008553.
DR KEGG; dle:111179962; -.
DR InParanoid; A0A2Y9P0A9; -.
DR OrthoDB; 6392at2759; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0070314; P:G1 to G0 transition; IEA:Ensembl.
DR GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:Ensembl.
DR GO; GO:0021782; P:glial cell development; IEA:Ensembl.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:Ensembl.
DR GO; GO:0006544; P:glycine metabolic process; IEA:Ensembl.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0021915; P:neural tube development; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR GO; GO:0019530; P:taurine metabolic process; IEA:Ensembl.
DR GO; GO:0006566; P:threonine metabolic process; IEA:Ensembl.
DR CDD; cd12173; PGDH_4; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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 NCBIfam; TIGR01327; PGDH; 1.
DR PANTHER; PTHR42938:SF22; D-3-PHOSPHOGLYCERATE DEHYDROGENASE; 1.
DR PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR Pfam; PF19304; PGDH_inter; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF143548; Serine metabolism enzymes domain; 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU363003}; NAD {ECO:0000256|RuleBase:RU363003};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU363003};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299,
KW ECO:0000256|RuleBase:RU363003}.
FT DOMAIN 9..317
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..285
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT DOMAIN 330..409
FT /note="D-3-phosphoglycerate dehydrogenase ASB"
FT /evidence="ECO:0000259|Pfam:PF19304"
SQ SEQUENCE 533 AA; 56759 MW; 9E3210577D0D5892 CRC64;
MAFANLRKVL LSDSLDPCCR KILQDGGLQV VEKQNLSQEE LIAELQDCEG LIVRSATKVT
SDVINATKKL QVVGRAGTGV DNVDLEAATR KGILVMNTPS GNSLSAAELT CGMIMCLARQ
IPQATASMKD GKWERKKFMG TELNGKILGI LGLGRIGREV ATRMQSFGMK TIGYDPIISP
EVSASFGVQQ VPLEEIWPLC DFITVHTPLL PSTTGLLNDS TFAQCKKGVR VVNCARGGIV
DEGALLRALQ SGQCAGAALD VFTEEPPRDR ALVDHENVIS CPHLGASTQE AQSRCGKEIA
IQFVDMVKGK SLAGVVNAQA LTSAFSPHTK PWIGLAEALG ALMQAWAGSP KGTIQVVTQG
LSLKNSGNCL TPAVIVGLLK DASRQVEVNL VNAKLLVKES GLDVTTSHSP AAPGEQGCGK
CLLTVALAGA PYQAVGWVQG TTPVLQALNG AVFRPEVPLH RGLPLLMFRT HPSNPAMLPT
MIGLLAESEV QLLSYQTSMV SDGETWHVMG ISSLLPSLEP WKQHATEAFQ FHF
//
