ID A0A074X0F5_9PEZI Unreviewed; 350 AA.
AC A0A074X0F5;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Putative D-mandelate dehydrogenase {ECO:0000313|EMBL:KEQ77229.1};
GN ORFNames=M436DRAFT_60991 {ECO:0000313|EMBL:KEQ77229.1};
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:KEQ77229.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ77229.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ77229.1,
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|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; KL584703; KEQ77229.1; -; Genomic_DNA.
DR RefSeq; XP_013431110.1; XM_013575656.1.
DR AlphaFoldDB; A0A074X0F5; -.
DR STRING; 1043004.A0A074X0F5; -.
DR GeneID; 25413098; -.
DR HOGENOM; CLU_019796_1_2_1; -.
DR OrthoDB; 1111153at2759; -.
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; cd12168; Mand_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; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000027730}.
FT DOMAIN 72..326
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 126..307
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 350 AA; 38091 MW; 7C9545C35B62DFDE CRC64;
MSPKLSILHL GDPPRWHANL YKKLETNFTI IRPSAAERER PAFLQALREK RWGNFVAIMR
PFWNTGGEMG RTDRELISLL PDSVKVYGSA GAGFDWVDTD ILAEKGIVYC NGAAASSDSV
ADSALFLIIS TFRNLAWSQI AARSGNPDEL FDAHKNSPTT AINPAGRILG IVGLGNIGYR
IAQKAHLGLN MKIAYHDLFR KPKSVEEAVG ASFYDTLDEM LGAADCIIVA TPFSGKQLFT
AEKFKKFKRG SRLINIARGP LVNEADLVEA LKSGQLSACG LDVFENEPHV NKELCGLKQA
TLTAHTAGGT IDTHIGFEEL CYKNVLGALL EGKAITPVNL HLIKAGKSKL
//
