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Database: UniProt
Entry: A0A137QXG9_9AGAR
LinkDB: A0A137QXG9_9AGAR
Original site: A0A137QXG9_9AGAR 
ID   A0A137QXG9_9AGAR        Unreviewed;       332 AA.
AC   A0A137QXG9;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=D-lactate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AN958_11022 {ECO:0000313|EMBL:KXN91962.1};
OS   Leucoagaricus sp. SymC.cos.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX   NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN91962.1, ECO:0000313|Proteomes:UP000070249};
RN   [1] {ECO:0000313|EMBL:KXN91962.1, ECO:0000313|Proteomes:UP000070249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SymC.cos {ECO:0000313|EMBL:KXN91962.1,
RC   ECO:0000313|Proteomes:UP000070249};
RA   Hu H.;
RT   "Leucoagaricus sp. SymC.cos WGS genome.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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; KQ961943; KXN91962.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137QXG9; -.
DR   STRING; 1714833.A0A137QXG9; -.
DR   OrthoDB; 4204864at2759; -.
DR   Proteomes; UP000070249; 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; 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.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070249}.
FT   DOMAIN          5..330
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          110..299
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   332 AA;  36455 MW;  6B25FA667B28BE14 CRC64;
     MKVAVYGTRK YDVDSLQPLT ADTDIKFTFI EALLDELTVQ LADGHDAVCL FVNDVCNVEV
     LKHLNVLGVK YIALRCAGFN NVDLPAADKY NIKVARVPAY SPEAVAEFTV GMIMTVVRKY
     HKAYNRVREG NFLLDGLLGF NLHTKTVGLI GTGKIGLLTG RILAKGFGCN VIAYDPFPSS
     LAQEFGITYA ENLDEFLEKS DIVSLHCPLT ESTKYIINDN TLGKMKEGVI LINTSRGGLI
     DTYALIRALK AGHVAAVGMD VYERESTYFF ADSSTKVIHD DVFARLLSFY NVFMTGHQAF
     LTEEALKNIA ETTVSNLLQL ESAGTCHNIV SG
//
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