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Database: UniProt
Entry: A0A074WHE8_9PEZI
LinkDB: A0A074WHE8_9PEZI
Original site: A0A074WHE8_9PEZI 
ID   A0A074WHE8_9PEZI        Unreviewed;       327 AA.
AC   A0A074WHE8;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Glycerate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=M436DRAFT_48274 {ECO:0000313|EMBL:KEQ72520.1};
OS   Aureobasidium namibiae CBS 147.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ72520.1, ECO:0000313|Proteomes:UP000027730};
RN   [1] {ECO:0000313|EMBL:KEQ72520.1, ECO:0000313|Proteomes:UP000027730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ72520.1,
RC   ECO:0000313|Proteomes:UP000027730};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA   Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA   Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; KL584711; KEQ72520.1; -; Genomic_DNA.
DR   RefSeq; XP_013426559.1; XM_013571105.1.
DR   AlphaFoldDB; A0A074WHE8; -.
DR   STRING; 1043004.A0A074WHE8; -.
DR   GeneID; 25410848; -.
DR   HOGENOM; CLU_019796_1_3_1; -.
DR   OrthoDB; 1462550at2759; -.
DR   Proteomes; UP000027730; 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; cd05198; formate_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; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027730}.
FT   DOMAIN          34..322
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          110..292
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   327 AA;  35592 MW;  8518B36B403A530C CRC64;
     MSTSEEFKHH VVQLDGHVNL PELRFPHTFE KYLHTSSSEL PSRIASATIA IATTTTFAKE
     NFACAPSLQL ISCLGAGCDK FDLHAAKESG VTITNTPAQN TSTVAEHAIS LYFAVKRRIA
     DLDRVTKEGE MWKSQGMCMG VFKGVMPRIC EEEVVGIIGY GALGKRVEKM CKALDMRVLV
     AERKGSTDIR PSRTSFEDVL KQCTTLILTC PLDPSTRNMV SHHELSLLSP TSILINVGRG
     GIVNEAALAT ALKEGKLLGA GMDVFEHEPA TKQNCPLLAD DVPGLVATPH LAWYSDRTIV
     GTKETVRNTI EAFVKGEPEN VVVDGRK
//
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