ID A0A0P7BM19_9HYPO Unreviewed; 474 AA.
AC A0A0P7BM19;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=phosphoglycerate dehydrogenase {ECO:0000256|ARBA:ARBA00013143};
DE EC=1.1.1.95 {ECO:0000256|ARBA:ARBA00013143};
GN ORFNames=AK830_g4942 {ECO:0000313|EMBL:KPM41658.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM41658.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM41658.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM41658.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-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:KPM41658.1}.
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DR EMBL; LKCW01000061; KPM41658.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7BM19; -.
DR STRING; 78410.A0A0P7BM19; -.
DR OrthoDB; 6392at2759; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000050424; 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; 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:UP000050424};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299}.
FT DOMAIN 404..474
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 474 AA; 51826 MW; 2880A7BEDFA29849 CRC64;
MASAQDIQSN LSASFQKTVS HSWDHNLSAS PTATFQSPPS GSWGGGALAN RSVPKTLKPF
NTQDIKILLL ENVNVGGQEI LRGQGYQVEA LKTSLPEDQL IEKIRDIHVI GIRSKTKLTE
RVLREAKNLL VVGCFCIGTN QVDLEYAASH GIAVFNSPFA NSRSVAELVI AEIITLARQL
GDRSNEMHRG TWNKVSSKCW EIRGKTLGIV GYGHIGSQLS VLAEAMGMTV IYYDVVTLMA
LGTARQVPTL EKLLEEADFV TLHVPDLPET RNLITTSHFE HMKNGSYLIN ASRGSVVDIP
ALIKASRSGK VAGAALDVFP QEPAANGDYF NSTLNTWGDD LRSLSNLILT PHIGGSTEEA
QRAIGIEVAD ALVRYINQGI TLGSVNLPEV QMRSITLDEP EHARVIYIHH NVPGVLRKVN
EILGDHNVDK QISDSRGDVA YLMADISSVK YEQIKDIQES LEALSSRILT RVLY
//
