ID A0A0F4GPE3_9PEZI Unreviewed; 474 AA.
AC A0A0F4GPE3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=phosphoglycerate dehydrogenase {ECO:0000256|ARBA:ARBA00013143};
DE EC=1.1.1.95 {ECO:0000256|ARBA:ARBA00013143};
GN ORFNames=TI39_contig440g00012 {ECO:0000313|EMBL:KJX98065.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX98065.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX98065.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX98065.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJX98065.1}.
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DR EMBL; LAFY01000432; KJX98065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4GPE3; -.
DR STRING; 1047168.A0A0F4GPE3; -.
DR OrthoDB; 6392at2759; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000033647; 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; 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:UP000033647};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT DOMAIN 404..474
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 474 AA; 51391 MW; AF09C34537A35519 CRC64;
MPTAARDIPE RNGMDADSLA RTVSASFSNS YSTSPTLNYH SPNASYGGAP KASYKQLKPF
HTQDVKVLLL ENINLTGQDI LKKQGYQVEA LKSALPEDQL IEKIQDVQVI GIRSKTQLSA
NVLKHAKNLI VIGCFCIGTN QVDLKYAAEQ GIAVFNSPFS NSRSVAELMI GEIIALARQI
GDRSNEMHQG VWNKVSAGCW EVRGKTLGII GYGHVGAQLS VLAESMGMKV IYYDVVNMMG
LGTARLVPTM DALLEASDFV TLHVPELPET KNLIGAKELA KMKNGSYLLN ASRGTVVDIE
ALIGAMKSGK IAGAALDVYP NEPGGNGPHF NEQLNAWGKE LCAQKNLILT PHIGGSTEEA
QAAIGSEVAE ALVNYVNFGT TNGAVNMPEV ALRSLTINES NHLRVIYIHK NVPGVLRRVN
EILGDHNVDK QMTDSRGDVA YLMADISNVN VSEIKTLYQN LEDLGSRIRT RVLY
//
