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
//