ID G2WX69_VERDV Unreviewed; 361 AA.
AC G2WX69;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:EGY21324.1};
GN ORFNames=VDAG_02848 {ECO:0000313|EMBL:EGY21324.1};
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:EGY21324.1, 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; EGY21324.1; -; Genomic_DNA.
DR RefSeq; XP_009651796.1; XM_009653501.1.
DR AlphaFoldDB; G2WX69; -.
DR STRING; 498257.G2WX69; -.
DR EnsemblFungi; EGY21324; EGY21324; VDAG_02848.
DR GeneID; 20704311; -.
DR KEGG; vda:VDAG_02848; -.
DR eggNOG; KOG0068; Eukaryota.
DR HOGENOM; CLU_019796_1_1_1; -.
DR InParanoid; G2WX69; -.
DR OMA; VIVTAHQ; -.
DR OrthoDB; 4204864at2759; -.
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; cd12183; LDH_like_2; 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; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-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.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000001611}.
FT DOMAIN 3..332
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 116..301
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 361 AA; 39344 MW; 632414020F85E10C CRC64;
MKIAVFSAKP YDEKYLTAAK PPGLDVVFHD VSLTPKTTSL LTPHAGSDPY TAVCVFVNDH
LPASVLDDLH DAGIRVVLLR CAGFNNVDLP HAEKLGIAVA NVPSYSPEAV AEFAVALLQT
LNRNTHRAYN RVRENNFALN GLCGRTLHGK TVGLIGTGRI GVAFARIMKG FGCKVIAHDP
YPSEAFEQYG KYVDLHELLP LCDVVSLHCP LTEQTRHIIN DDTLGLLKKG ALLINTSRGG
LVKTKAVITA LKEHKLGGLA LDVYEGEGAL FYDDHSGDII DDDELMRLMT FPNVVICGHQ
AFFTDEALTE ISECTVRNLE DLVAGRACKN ALVQPREGVQ EDEKGLVKPL ARRESLPVRT
V
//
