ID A0A1G4JLV6_9SACH Unreviewed; 470 AA.
AC A0A1G4JLV6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=phosphoglycerate dehydrogenase {ECO:0000256|ARBA:ARBA00013143};
DE EC=1.1.1.95 {ECO:0000256|ARBA:ARBA00013143};
GN ORFNames=LADA_0F10748G {ECO:0000313|EMBL:SCU91570.1};
OS Lachancea dasiensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1072105 {ECO:0000313|EMBL:SCU91570.1, ECO:0000313|Proteomes:UP000190274};
RN [1] {ECO:0000313|EMBL:SCU91570.1, ECO:0000313|Proteomes:UP000190274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10888 {ECO:0000313|EMBL:SCU91570.1};
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 1/3. {ECO:0000256|ARBA:ARBA00005216}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; LT598458; SCU91570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4JLV6; -.
DR STRING; 1266660.A0A1G4JLV6; -.
DR OrthoDB; 6392at2759; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000190274; Chromosome F.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd04901; ACT_3PGDH; 1.
DR CDD; cd12176; PGDH_3; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
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 PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023299};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000190274};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT DOMAIN 400..470
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 20..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 470 AA; 50975 MW; 37056B0FC022E59A CRC64;
MASPQQINSL QNSFQRAVNL SGSPGQVSTS PTQSFMSSIP RRMSVSKQTK ALKPFSTGDI
KILLLENVNQ TAVEIFNGQG YQVEYYKASL PEDELIEKIR DVHAIGIRSK TKLSERVLKH
AKSLVVIGCF CIGTNQVDLD FAAKMGVAVF NSPFSNSRSV AELVIAEIVT LARQLGDRSI
EMHTGTWNKV SNKCWEVRGK TLGIIGYGHI GAQLSVLAEA FGMHVLYYDV VTIMALGTAK
QVSTLDELLG KSDFVTCHVP ATAETKNLLS APQFAAMKDG SYVINASRGT VIDIPALVQA
IKVGKIAGTA LDVYPHEPAK NGAGAFNDDL NDWVSELTSL PNVILTPHIG GSTEEAQSAI
GIEVATGLTK YINEGCSVGS VNFPEVSLRG LDLDQENVVR VLYIHHNVPG VLRTVNNILS
NHNIEKQFSD SQGDIAYLMA DISSVDQSGI KEIYDQLNAT EYKISIRLLY
//
