ID A0A0S7DDW1_9EURO Unreviewed; 343 AA.
AC A0A0S7DDW1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KAF4175349.1};
GN ORFNames=ALT_006880 {ECO:0000313|EMBL:GIM34620.1}, CNMCM8060_007439
GN {ECO:0000313|EMBL:KAF4175349.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:KAF4175349.1, ECO:0000313|Proteomes:UP000713487};
RN [1] {ECO:0000313|EMBL:GIM34620.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM34620.1};
RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT lentulus IFM 54703T.";
RL Genome Announc. 4:e01568-15(2016).
RN [2] {ECO:0000313|EMBL:KAF4175349.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4175349.1};
RA dos Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E.,
RA Silva L.P., Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RT "Genomic and phenotypic heterogeneity of clinical isolates of the human
RT pathogens Aspergillus fumigatus, Aspergillus lentulus and Aspergillus
RT fumigatiaffinis.";
RL bioRxiv 0:0-0(2020).
RN [3] {ECO:0000313|EMBL:KAF4175349.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4175349.1};
RA Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E., Silva L.P.,
RA Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RL Submitted (APR-2020) 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:KAF4175349.1}.
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DR EMBL; BCLY01000001; GIM34620.1; -; Genomic_DNA.
DR EMBL; JAAAPS010000059; KAF4175349.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7DDW1; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_469; -.
DR OrthoDB; 2900331at2759; -.
DR Proteomes; UP000713487; 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; cd12169; PGDH_like_1; 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; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 28..342
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 121..311
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 343 AA; 37396 MW; 51A60C1B0AE936EE CRC64;
MSRIKFAILD DYQNLSRKHF AHLTSRVDVS YFPDTLDPRD PAQQQQLIGR LRPFDAILAM
RERTPFNAAT IDALPNLKLL LTTGNRNLSL DLPALTARGI PVAGTVGRPP GVNSTVQHTW
ALILALARHV ARDDAAVKAG KWQGSLGVNL SGKTLALLGL GKLGAQVGRI AVLAFGMKVI
AWSANLTQDK ADEQATAQGL PAGSFEAVPE KGEFLRRADV LSVHYVLSER SRGIVGAKDL
AALRPEAMIV NTSRGPLIDE RALLETLNAG RIRGAALDVF DPEPLPVDSP WRTTAWGVDG
RSEVLLTPHM GYGEEELING WYKEAAENLE RWLDGKELQV RLN
//
