ID B2WME1_PYRTR Unreviewed; 312 AA.
AC B2WME1;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=6-phosphogluconate dehydrogenase 2 {ECO:0000313|EMBL:EDU44201.1};
GN ORFNames=PTRG_11151 {ECO:0000313|EMBL:EDU44201.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU44201.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
CC -!- SIMILARITY: Belongs to the HIBADH-related family. NP60 subfamily.
CC {ECO:0000256|ARBA:ARBA00007598}.
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DR EMBL; DS231630; EDU44201.1; -; Genomic_DNA.
DR RefSeq; XP_001941482.1; XM_001941447.1.
DR AlphaFoldDB; B2WME1; -.
DR STRING; 426418.B2WME1; -.
DR EnsemblFungi; EDU44201; EDU44201; PTRG_11151.
DR GeneID; 6349463; -.
DR eggNOG; KOG0409; Eukaryota.
DR HOGENOM; CLU_035117_5_1_1; -.
DR InParanoid; B2WME1; -.
DR OMA; AWVQSTT; -.
DR OrthoDB; 2715114at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR029154; HIBADH-like_NADP-bd.
DR InterPro; IPR015815; HIBADH-related.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43580:SF3; 6-PHOSPHOGLUCONATE DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_2G11600); 1.
DR PANTHER; PTHR43580; OXIDOREDUCTASE GLYR1-RELATED; 1.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000103; HIBADH; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000001471}.
FT DOMAIN 5..158
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 176..297
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT ACT_SITE 182
FT /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ SEQUENCE 312 AA; 33439 MW; 12A1DFE3D024346C CRC64;
MAPQLAWIGL GNMGRASTPH HQNLVEKGQL DKPLIIYNRT KSRAEDLSSK LGTSKTKVVD
TVNDAVKAAG IIFMCLGDDA AVNSAVDAML QEDVNGKLIV DCSTVHPDTT NALDKRITDK
GAGFVGMPVF GAPAMADNGQ LVCVTAGQKA SCDRVVPYTT GVMGRANIDY SGQPAGNATL
MKVIGNTFIL NMVSQLSEGH VLAEKSGLGV DNLHTFISTM FPGPYTAYSQ RMLDGDYYKR
EEPLFHVDLA RKDARHAMSL AESNGAKESM KMLGLAQKRL DGVKSELGDR GDIPSVYGVV
RKESGLEFKN KG
//
