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Database: UniProt
Entry: V5ERZ8_KALBG
LinkDB: V5ERZ8_KALBG
Original site: V5ERZ8_KALBG 
ID   V5ERZ8_KALBG            Unreviewed;       355 AA.
AC   V5ERZ8;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Glyoxylate/hydroxypyruvate reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PSEUBRA_SCAF9g01390 {ECO:0000313|EMBL:EST04639.1};
OS   Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX   NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST04639.1, ECO:0000313|Proteomes:UP000019377};
RN   [1] {ECO:0000313|Proteomes:UP000019377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX   PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA   Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA   Goldman G.H.;
RT   "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT   high producer of endo-1,4-xylanase isolated from an insect pest of
RT   sugarcane.";
RL   Genome Announc. 1:E0092013-E0092013(2013).
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; KI545895; EST04639.1; -; Genomic_DNA.
DR   RefSeq; XP_016289628.1; XM_016439694.1.
DR   AlphaFoldDB; V5ERZ8; -.
DR   STRING; 1365824.V5ERZ8; -.
DR   GeneID; 27422411; -.
DR   eggNOG; KOG0069; Eukaryota.
DR   HOGENOM; CLU_019796_1_2_1; -.
DR   OMA; GHTPKHW; -.
DR   OrthoDB; 1462550at2759; -.
DR   Proteomes; UP000019377; 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; cd05301; GDH; 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; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR10996:SF257; GLYCERATE DEHYDROGENASE HPR, PEROXISOMAL; 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:UP000019377}.
FT   DOMAIN          6..339
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          117..317
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   355 AA;  38372 MW;  61915BA7E0432478 CRC64;
     MTVPKILVCR RMPTEVLKRA EAAGKVELIT QPESDGERAP SRSWVLSNLP GCAGAVICLS
     EKVDASFLDA AGPSLKVIST MSVGYDHIDL PLVKSRGICV GNTPRVLDDA VAEVCLLLAL
     MVTRQVPVAT RTVREGEWPN FPWTPTCFMG PSIAGKTVGL LGFGNISQSL CKLLVPFKPK
     RILYTTSRER KFDREDKYFA SLMRDGFPVD RIGVENEPEP IELAKKADLV FVLVDLNAST
     KHIVGKKFLE AMKPSAYIIN ASRGGTVDTA ALVEALRNNQ IAGAGLDVVE GEPGIHADHP
     LLSADVRDKV ALLPHIGSGT TETRQAMADM TMNNLLGALG LREEQGKEAE MDAEL
//
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