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Database: UniProt
Entry: M7U7X1_BOTF1
LinkDB: M7U7X1_BOTF1
Original site: M7U7X1_BOTF1 
ID   M7U7X1_BOTF1            Unreviewed;       366 AA.
AC   M7U7X1;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Putative 2-hydroxyacid dehydrogenase protein {ECO:0000313|EMBL:EMR89799.1};
GN   ORFNames=BcDW1_1508 {ECO:0000313|EMBL:EMR89799.1};
OS   Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR89799.1, ECO:0000313|Proteomes:UP000012045};
RN   [1] {ECO:0000313|Proteomes:UP000012045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX   PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA   Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT   "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT   grape berries.";
RL   Genome Announc. 1:E0025213-E0025213(2013).
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DR   EMBL; KB707721; EMR89799.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7U7X1; -.
DR   STRING; 1290391.M7U7X1; -.
DR   HOGENOM; CLU_019796_1_0_1; -.
DR   Proteomes; UP000012045; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   CDD; cd12163; 2-Hacid_dh_5; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 2.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          123..196
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
FT   DOMAIN          224..329
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   366 AA;  40728 MW;  411446B3ACEFD872 CRC64;
     MGEIPQHQEH ILCLLPFPED SKILDRLRQK YNVEITYKQI FFGVGKALEL ADVPDETWHH
     ATILVTLSSF PPSAEKAKNL KLIHLFSAGT DRLSNTPIWK DTKIPITNSS GVHGPQISEW
     VIMQILSHSH KEKLLIEWQK EHVWGDYKRL GAMRDCVGQR LGVLGYGAIG RQAARISKAM
     GMDVIAYTAS PRTTPESRKD EGKYIVPNTG DPDGTLPSAW YSGLDKESLH NFLKQDIDIL
     LIAVPLTPQT HHFLSAAEFE ILGSKTNAFI INIARGGIIN QDDLITYLKK PLSEGGLRGA
     ALDVTDPEPL PQDSELWTLE NVAITPHVSG LGTTYAERSF AILDANLDNI EKGRNLINLV
     DRKKGY
//
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