ID A0A0D1YKL5_9EURO Unreviewed; 411 AA.
AC A0A0D1YKL5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIV81554.1};
GN ORFNames=PV11_03730 {ECO:0000313|EMBL:KIV81554.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV81554.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV81554.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV81554.1,
RC ECO:0000313|Proteomes:UP000053599};
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 Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN846952; KIV81554.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1YKL5; -.
DR STRING; 1016849.A0A0D1YKL5; -.
DR HOGENOM; CLU_019796_1_2_1; -.
DR OrthoDB; 1111153at2759; -.
DR Proteomes; UP000053599; 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; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR10996:SF178; GLYOXYLATE REDUCTASE 1; 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|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000053599}.
FT DOMAIN 135..399
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 198..369
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 411 AA; 45205 MW; D61C5B274E203105 CRC64;
MFSISSYSQK FAVRILEQPR IWRATLPSFF LSTRPYHNFP PSTGFGKGRR VRPTSTHPSS
PIYPFLHQTF TSTTLNMSKP TVLLIGGLTH AKNEWNAYGS KYNLKEFLKE DRQEFLSNLK
NGEYDNVVAL YRSNNSVAQT GPFDKELVTL LPKSLKFVCH NGAGYDNIDV DACTQKGVKI
SSTPIAVDNA TADVGIFVLL GALRQAWVPL KAIKEGKWRG SASLGHDPNG KLLGILGMGG
IGRAMAERAR AFGMKIAYHN RSRLPKELEG DATYLSFDEL LAQSDVLSLN LSLNAKTRHI
ISAPEFAKMK DGVVIVNTAR GALINEKDLV AALDSGKVAS VGLDVFENEP EIEEGLLKSD
KAFIVPHIGT MTYETQREME LLVLHNLENA VDKGSLLTPI PEQKSKANGN L
//