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Database: UniProt
Entry: A0A0N0NQM3_9EURO
LinkDB: A0A0N0NQM3_9EURO
Original site: A0A0N0NQM3_9EURO 
ID   A0A0N0NQM3_9EURO        Unreviewed;       355 AA.
AC   A0A0N0NQM3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Putative 2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:KPI43869.1};
GN   ORFNames=AB675_6520 {ECO:0000313|EMBL:KPI43869.1};
OS   Phialophora attinorum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI43869.1, ECO:0000313|Proteomes:UP000038010};
RN   [1] {ECO:0000313|EMBL:KPI43869.1, ECO:0000313|Proteomes:UP000038010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI43869.1,
RC   ECO:0000313|Proteomes:UP000038010};
RA   Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA   de Vries M., Cruz L.M., Souza E.M.;
RT   "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT   131958.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPI43869.1}.
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DR   EMBL; LFJN01000004; KPI43869.1; -; Genomic_DNA.
DR   RefSeq; XP_018003832.1; XM_018146819.1.
DR   AlphaFoldDB; A0A0N0NQM3; -.
DR   STRING; 1664694.A0A0N0NQM3; -.
DR   GeneID; 28738699; -.
DR   OrthoDB; 1462550at2759; -.
DR   Proteomes; UP000038010; 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; cd05198; formate_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; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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:UP000038010}.
FT   DOMAIN          28..334
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          118..310
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   355 AA;  38441 MW;  D42E05B0463BC901 CRC64;
     MATFKPPPLP TGKDKHHVVV LEAKHVPMPR FDFPHTIDLH PLTKQHEVAE RIKDATIVIA
     CVTPVTPADL DVAKHVGCLA IMAVGMAWLN KEEFAKRGVT VTNCAGANVE AVSEHFLALY
     FALRKKVVEI DRTVKETDEW RQEGTVTNHW ESRKPPPGCG QEVLGILGYG TIGKRIALLG
     KALGFAEILI ADRKGATAEA TKEGRTPFDE VVKRSSTLAV CAPLTKDTVD LISESELQSM
     RKEALVINLA RGGIVNEAAL ARALTSGQVA GAATDVLETE PGGPGSTPLL PDLSKGEPAI
     PNFVISPHIA WFTQVTIINY QQMLKEGVER WVAGSLIQDG KVIHAVCIHD GKIYR
//
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