ID A0A1B9FVF8_9TREE Unreviewed; 359 AA.
AC A0A1B9FVF8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:OCF22752.1};
GN ORFNames=I302_07093 {ECO:0000313|EMBL:OCF22752.1};
OS Kwoniella bestiolae CBS 10118.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296100 {ECO:0000313|EMBL:OCF22752.1, ECO:0000313|Proteomes:UP000092730};
RN [1] {ECO:0000313|EMBL:OCF22752.1, ECO:0000313|Proteomes:UP000092730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10118 {ECO:0000313|EMBL:OCF22752.1,
RC ECO:0000313|Proteomes:UP000092730};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus bestiolae CBS10118.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10118 {ECO:0000313|Proteomes:UP000092730};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KI894024; OCF22752.1; -; Genomic_DNA.
DR RefSeq; XP_019043822.1; XM_019193699.1.
DR AlphaFoldDB; A0A1B9FVF8; -.
DR STRING; 1296100.A0A1B9FVF8; -.
DR GeneID; 30211492; -.
DR VEuPathDB; FungiDB:I302_07093; -.
DR OrthoDB; 1775226at2759; -.
DR Proteomes; UP000092730; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000092730}.
FT DOMAIN 156..321
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 359 AA; 39328 MW; B3E9FD73527ABA08 CRC64;
MSATYDNAVI TVEVSESKLE EVKRVYKNVY YHPDENVPEE ELKVADIWFA TWTGLPTCVK
SLDQIPNMKV LQLSSAGANK ALYSPIMSSD KARKQIKVCS SSGMHTLSIP QYIIGNVINL
YMKLHIQLYI ARSQSVWPDR DEIVRLCGMS GQAFPGNRSV SGKTVGLLGY GHIARETARL
FKAFNCSIIA ANSRGNRRPE EGYRIPGTGD ADGSIPEDYY STNDEQSFSS FLSRCDILVA
SLPSTPQTIN MLSQKHLELL PHGSVLVNVG RGDLVKSESI LGALDAPKGL WGAVLDVTDP
EPLTHGHPLY THPNVIVTPH TSGIIEGYFD VGADILIAQA AKLKQNEEPL NVVDPVKGY
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