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Database: UniProt
Entry: Q0UFP9_PHANO
LinkDB: Q0UFP9_PHANO
Original site: Q0UFP9_PHANO 
ID   Q0UFP9_PHANO            Unreviewed;       489 AA.
AC   Q0UFP9;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=phosphoglycerate dehydrogenase {ECO:0000256|ARBA:ARBA00013143};
DE            EC=1.1.1.95 {ECO:0000256|ARBA:ARBA00013143};
GN   ORFNames=SNOG_09415 {ECO:0000313|EMBL:EAT83607.1};
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT83607.1, ECO:0000313|Proteomes:UP000001055};
RN   [1] {ECO:0000313|Proteomes:UP000001055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC   {ECO:0000313|Proteomes:UP000001055};
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA   Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA   McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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; CH445338; EAT83607.1; -; Genomic_DNA.
DR   RefSeq; XP_001799709.1; XM_001799657.1.
DR   AlphaFoldDB; Q0UFP9; -.
DR   STRING; 321614.Q0UFP9; -.
DR   EnsemblFungi; SNOT_09415; SNOT_09415; SNOG_09415.
DR   GeneID; 5976610; -.
DR   KEGG; pno:SNOG_09415; -.
DR   VEuPathDB; FungiDB:JI435_094150; -.
DR   eggNOG; KOG0068; Eukaryota.
DR   HOGENOM; CLU_019796_9_2_1; -.
DR   InParanoid; Q0UFP9; -.
DR   OMA; SKGCWEV; -.
DR   OrthoDB; 6392at2759; -.
DR   UniPathway; UPA00135; UER00196.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
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; 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:ARBA00023299};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001055};
KW   Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT   DOMAIN          412..486
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          18..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   489 AA;  52989 MW;  A2C940FF217F27BC CRC64;
     MTPPQDIAGS LAHSVSNSLN LSTSPSLSFH SPPSTFRQPP SGSFQDGRNG SVPALSHASQ
     LAKQLKPFDT KDFKVLLLEN VNDAGVNILK GQGYQVEALK SSLSEDQLIE KIRDVHVIGI
     RSKTKLTKRV LEEAKNLIVI GCFCIGTNQV DLQTAAQKGI AVFNSPFSNS RSVAELVIAE
     IIALARQLGD RSNELHNGTW NKVSKGCWEI RGKTLGIVGY GHIGSQLSVL AESMGMSVIY
     YDVLTMMGLG TARQVTTLDE LLQQADFVSL HVPATADTKD LIGADELAKM KDGSYLINNA
     RGTVIDIPAL IEASRSGKIA GAAIDVFPNE PAGNGDYFAN DLNSWTKDLV GLKNIILTPH
     IGGSTEEAQS AIGVEVSTAL VRYVNEGTTL GAVNLPEVNL RSLTHDEPNS LRVIYIHKNV
     PGVLRQVNNV LLHHNIEKQM SDSRGEIAYL MADISDVKEE EIRDLFQSLE ELSFSECFHN
     IGSVFFNSQ
//
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