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Database: UniProt
Entry: A0A0D1YKL5_9EURO
LinkDB: A0A0D1YKL5_9EURO
Original site: A0A0D1YKL5_9EURO 
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
//
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