ID Q0UH86_PHANO Unreviewed; 339 AA.
AC Q0UH86;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Glyoxylate reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SNOG_08878 {ECO:0000313|EMBL:EAT84046.1};
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:EAT84046.1, 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 -!- 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; CH445337; EAT84046.1; -; Genomic_DNA.
DR RefSeq; XP_001799182.1; XM_001799130.1.
DR AlphaFoldDB; Q0UH86; -.
DR STRING; 321614.Q0UH86; -.
DR EnsemblFungi; SNOT_08878; SNOT_08878; SNOG_08878.
DR GeneID; 5976081; -.
DR KEGG; pno:SNOG_08878; -.
DR VEuPathDB; FungiDB:JI435_088780; -.
DR eggNOG; KOG0069; Eukaryota.
DR HOGENOM; CLU_019796_1_2_1; -.
DR InParanoid; Q0UH86; -.
DR OMA; MNVLYYN; -.
DR OrthoDB; 1462550at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IBA:GO_Central.
DR GO; GO:0016618; F:hydroxypyruvate reductase activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd05301; GDH; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR10996:SF257; GLYCERATE DEHYDROGENASE HPR, PEROXISOMAL; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000001055}.
FT DOMAIN 6..337
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 114..306
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 339 AA; 36889 MW; 097983D2657E6FBD CRC64;
MAKPKVVVTR QLIDEAQTIL DGKKEDLEIV QWSSEKPCPR SWLLENAQGA TGILVMLSDQ
VNEELVQAAG HQLKAIASFS VGTDHVDREA LKKRNIRLGY TPTCLTDAVA DLTVMLILMA
QRRGGEAISK VTKGEWPQMP WHPLLMTGPQ IRGATVGFLG FGRIAQASLV RLMGFGIKKA
IYLTSKPGKS VKEDHFGLLK EGKIPIEPAQ SADQLASESD VVVVGCALTP STKHMISTDF
FSKMKKLAVI VNIARGPVID TDALVKALDE QQIFGAGLDV IENEPNIQAD HPILKQERCV
LVPHIGSATI ETREQMATES VKNLLAGIEG SEMVNEVEL
//
