ID A0A0N0NL81_9EURO Unreviewed; 383 AA.
AC A0A0N0NL81;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Putative 2-hydroxyacid dehydrogenase UNK4.10 {ECO:0000313|EMBL:KPI38729.1};
GN ORFNames=AB675_5946 {ECO:0000313|EMBL:KPI38729.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI38729.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI38729.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI38729.1,
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|ARBA:ARBA00005854,
CC 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:KPI38729.1}.
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DR EMBL; LFJN01000017; KPI38729.1; -; Genomic_DNA.
DR RefSeq; XP_017998692.1; XM_018146197.1.
DR AlphaFoldDB; A0A0N0NL81; -.
DR STRING; 1664694.A0A0N0NL81; -.
DR GeneID; 28738077; -.
DR OrthoDB; 1111153at2759; -.
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; 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; IPR029752; D-isomer_DH_CS1.
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:SF284; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G14400)-RELATED; 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; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000038010}.
FT DOMAIN 111..369
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 168..341
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 383 AA; 41549 MW; C37A01C73F5781AD CRC64;
MKSGRGGVKT SNADRHTDGT STEYNANLGT LFPSILFESG RRYIHIHHAK PSVLLIGSLA
HTTAEWSALS TKYTLHEFRT GTRSQFLSRL KSNDFASVTA LYRSNASATL TGPFDREICA
ALPSSLKYIC HNGAGYDNID VDAFTERGVL ISSTPIAVDN ATADTGIFLM LGALRYAVAP
LEAIRRGEWR GKGTRVGHDP TGKVLGILGM GGIGRAMASR ARAFGMKIIY HNRSRLPAEL
EGDAKYVTFE ELLAQSDVLS LNLALNAKTR HIISAREFAK MKDGVVIVNT ARGGLIKEAD
LVEALDSGKV SAVGLDVFEE EPKVHEGLLR NDRAFIVPHI GTNTYETQRE MELLVLRNLE
SAVDGNGLLT PIPEQKSKAN GNL
//
