ID A0A0D2GQ94_9EURO Unreviewed; 331 AA.
AC A0A0D2GQ94;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding domain-containing protein {ECO:0000259|Pfam:PF02826};
GN ORFNames=Z517_11319 {ECO:0000313|EMBL:KIW74549.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW74549.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW74549.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW74549.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN846976; KIW74549.1; -; Genomic_DNA.
DR RefSeq; XP_013278357.1; XM_013422903.1.
DR AlphaFoldDB; A0A0D2GQ94; -.
DR STRING; 1442368.A0A0D2GQ94; -.
DR GeneID; 25310809; -.
DR VEuPathDB; FungiDB:Z517_11319; -.
DR HOGENOM; CLU_019796_1_0_1; -.
DR OrthoDB; 1327616at2759; -.
DR Proteomes; UP000053029; 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; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 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:UP000053029}.
FT DOMAIN 100..283
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT REGION 312..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 331 AA; 35928 MW; 2C3105630B710A14 CRC64;
MKLLYPTSLK LDVASLEGFG VTLHPYDVHK LIPEELVDAE ILVTWANTNL RDAAKRMSRL
RWIQSLFAGP NDELAAGFPS NVIITAGTNL HNETVAEHAL ALVLSAARRL YEMRDFQNQG
KWPGHLGGFL PDRPQGSFTS LKGANITIWG MGNIGRTLAP HLTALGANIR GVGLYEEIID
GIQVHTNAAL PSLLPQTDCL IMILPGSRAT WHSLNTERLA KLPQHAWVIN VGRGICVDED
ALAHALKKGI IGGAALDVFH KEPLPESSPL WKAPNLIISP HAAGGRPRYS ELLIAENLRR
FLAGQPLKHD VTAGGMYSTS PKNSSTLKAS L
//