ID M7SEM3_EUTLA Unreviewed; 355 AA.
AC M7SEM3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Putative d-mandelate dehydrogenase protein {ECO:0000313|EMBL:EMR64689.1};
GN ORFNames=UCREL1_8350 {ECO:0000313|EMBL:EMR64689.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR64689.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
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; KB707027; EMR64689.1; -; Genomic_DNA.
DR RefSeq; XP_007796220.1; XM_007798029.1.
DR AlphaFoldDB; M7SEM3; -.
DR STRING; 1287681.M7SEM3; -.
DR KEGG; ela:UCREL1_8350; -.
DR eggNOG; KOG0069; Eukaryota.
DR HOGENOM; CLU_019796_1_2_1; -.
DR OMA; RIWYANG; -.
DR OrthoDB; 1111153at2759; -.
DR Proteomes; UP000012174; Unassembled WGS sequence.
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; IPR029753; D-isomer_DH_CS.
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.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000012174}.
FT DOMAIN 29..124
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 125..307
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 355 AA; 38859 MW; 832E4846EECB1B8C CRC64;
MPKPIALHIG EPIKYNHAFY DNEFSKRFQV VRSEEPDRES FIEALKEKKY GDFSAIFRPH
FQTGGEMGQW DDELISLLPP SVRIFASAGA GFNWADVDVL GRRKIWYANG AGASDEAVSD
TGLYMILSVF RNFTRSQLAA RTCDPAKFTE VHKLTATISA NPRGHILGIV GLGNISKKLA
YKASTALGMK IHYYDVVRSS PEVEQELGAT FHESLHDLLA IADCVSLHTP LNKHTQDLIS
TDAFAAMKQG ARLVNTARGP VVNEDALVGA LKSGKISAAG LDVHYHEPQV SKELAQMENV
TLTTHVGGGA LDTRINFELF AMKNILSVVG EQGEFIGKPF TAVNTEAFES AFVDS
//
