ID A1DN23_NEOFI Unreviewed; 334 AA.
AC A1DN23;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Pyridine nucleotide-disulphide oxidoreductase, putative {ECO:0000313|EMBL:EAW16194.1};
GN ORFNames=NFIA_055430 {ECO:0000313|EMBL:EAW16194.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW16194.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009333}.
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DR EMBL; DS027698; EAW16194.1; -; Genomic_DNA.
DR RefSeq; XP_001258091.1; XM_001258090.1.
DR AlphaFoldDB; A1DN23; -.
DR STRING; 331117.A1DN23; -.
DR EnsemblFungi; EAW16194; EAW16194; NFIA_055430.
DR GeneID; 4584606; -.
DR KEGG; nfi:NFIA_055430; -.
DR VEuPathDB; FungiDB:NFIA_055430; -.
DR eggNOG; ENOG502QQDE; Eukaryota.
DR HOGENOM; CLU_031864_5_0_1; -.
DR OMA; QHMHNVL; -.
DR OrthoDB; 1447958at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0097237; P:cellular response to toxic substance; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR PANTHER; PTHR48105:SF28; THIOREDOXIN REDUCTASE GLIT (AFU_ORTHOLOGUE AFUA_6G09740); 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..334
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002634274"
FT DOMAIN 15..309
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 334 AA; 36021 MW; F4C3D707E667184A CRC64;
MSIGKLLSNG ALLVDVLIIG AGPAGLSAAT GLARQLHTAV VFDSGVYRNA KTQHMHNVLG
WDHRNPAELR AAGRADLTNR YSTIQFQNST IEAIRQIETH QLFEARDSEG HSWYGRKVVL
ATGVRDIPLD IEGYSECWAN GIYHCLFCDG YEERGQETAG VLALGPIANP PRALHLARMA
NRLSESVTVY TNGNEQLAKE IQQAAEESPA GASWLKFDAR PIKQFEKGDV AKTVIVHFGE
SESKTEGFLV YNPQTEVNGP FAKQLALNMT EGGDILTTPP FHETSVPGVF AVGDCATPLK
AVTPAVAMGS LAAGGLVAQL QAQSLPEFRL DQEL
//
