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Database: UniProt
Entry: A0A0S7DHT9_9EURO
LinkDB: A0A0S7DHT9_9EURO
Original site: A0A0S7DHT9_9EURO 
ID   A0A0S7DHT9_9EURO        Unreviewed;       309 AA.
AC   A0A0S7DHT9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:GIM36555.1};
GN   ORFNames=ALT_004440 {ECO:0000313|EMBL:GIM36555.1};
OS   Aspergillus lentulus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM36555.1};
RN   [1] {ECO:0000313|EMBL:GIM36555.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM36555.1};
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).
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC       {ECO:0000256|RuleBase:RU003369}.
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:GIM36555.1}.
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DR   EMBL; BCLY01000004; GIM36555.1; -; Genomic_DNA.
DR   STRING; 293939.A0A0S7DHT9; -.
DR   VEuPathDB; FungiDB:TMP_alenIFM54703_2324; -.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   CDD; cd00300; LDH_like; 1.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF16; L-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
DR   SUPFAM; SSF56327; LDH C-terminal 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|RuleBase:RU003369}.
SQ   SEQUENCE   309 AA;  32637 MW;  D47C07D5793E36BA CRC64;
     MLSSTGPRIG IVGVGQVGAA AANALIVNSV VRELVLVDIK PELRNAQVQE LSDVSRVSGR
     AETRVRAGTY QEAGQCDIVL ITAGSKFSVG ETSVQHMYRN LGIVRSVIQA MRPFRSDAIL
     LVVSNPVDLL TTIAQQLSGL PPSQVLGSGT LLDSVRLRGL LANKAGVAAD AIDIHVLGVQ
     GLEEVVAWST ATLGGLPLAS VVPPDTFDPG QLTNECKQIS QAIIKTKGAM PLGIGAIISR
     ICSSILNDQR DILPISHFQK EFGCCFSLPV VLGRKGIIRT ILVPADEEEQ GEIAKSAETL
     NEIIAHVNE
//
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