ID G2WWR3_VERDV Unreviewed; 353 AA.
AC G2WWR3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=2-ketogluconate reductase {ECO:0000313|EMBL:EGY21168.1};
GN ORFNames=VDAG_02692 {ECO:0000313|EMBL:EGY21168.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY21168.1, ECO:0000313|Proteomes:UP000001611};
RN [1] {ECO:0000313|Proteomes:UP000001611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC {ECO:0000313|Proteomes:UP000001611};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
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; DS572698; EGY21168.1; -; Genomic_DNA.
DR RefSeq; XP_009651640.1; XM_009653345.1.
DR AlphaFoldDB; G2WWR3; -.
DR STRING; 498257.G2WWR3; -.
DR EnsemblFungi; EGY21168; EGY21168; VDAG_02692.
DR GeneID; 20704155; -.
DR KEGG; vda:VDAG_02692; -.
DR eggNOG; KOG0069; Eukaryota.
DR HOGENOM; CLU_019796_1_2_1; -.
DR InParanoid; G2WWR3; -.
DR OMA; RIWYANG; -.
DR OrthoDB; 1111153at2759; -.
DR Proteomes; UP000001611; Chromosome 3.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd12168; Mand_dh_like; 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:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 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:UP000001611}.
FT DOMAIN 71..331
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 128..309
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 353 AA; 38829 MW; 36222BD3836D76F9 CRC64;
MPGSKPTVLR LGEDIKYNPD YYSDTFTQRF DMVANEEPDR ASFIAALKSK KYGDFSAIFR
PHFQSGGEMG QWDDELISLL PPSVRIFASA GAGFNWANVD ALGRAKIWYA NGAGASDEAV
SDTALFFILS VFRNFWRSQR AARTCDPEQF MAMHRLVGSI SWNPRDHVLG IVGLGNISKK
VALKARTALG MKIHYFDVCR SPPEVEQELQ ATYHPTLHEL LRVSDCVTLH VPLNAHTRDL
INGDALAAMK DGSRLVNTAR GEVVHEEALI AALRSGKLSA AALDVHYHEP QVSRVLAEME
NVTLTCHNGG AAITTRLNFE LGAMKNIVKV VGTDGEFIGE PLTPVNRKAF EAS
//
