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Database: UniProt
Entry: B8NTY5_ASPFN
LinkDB: B8NTY5_ASPFN
Original site: B8NTY5_ASPFN 
ID   B8NTY5_ASPFN            Unreviewed;       349 AA.
AC   B8NTY5;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=D-xylose 1-dehydrogenase (NADP(+), D-xylono-1,5-lactone-forming) {ECO:0000256|ARBA:ARBA00038984};
DE            EC=1.1.1.179 {ECO:0000256|ARBA:ARBA00038984};
DE   AltName: Full=D-xylose-NADP dehydrogenase {ECO:0000256|ARBA:ARBA00042988};
GN   ORFNames=AFLA_101560 {ECO:0000313|EMBL:EED46492.1};
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952 {ECO:0000313|EMBL:EED46492.1, ECO:0000313|Proteomes:UP000001875};
RN   [1] {ECO:0000313|EMBL:EED46492.1, ECO:0000313|Proteomes:UP000001875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC   SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX   PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-xylose + NADP(+) = D-xylono-1,5-lactone + H(+) + NADPH;
CC         Xref=Rhea:RHEA:22000, ChEBI:CHEBI:15378, ChEBI:CHEBI:15867,
CC         ChEBI:CHEBI:53455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.179; Evidence={ECO:0000256|ARBA:ARBA00036678};
CC   -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family.
CC       {ECO:0000256|ARBA:ARBA00010928}.
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DR   EMBL; EQ963484; EED46492.1; -; Genomic_DNA.
DR   RefSeq; XP_002384028.1; XM_002383987.1.
DR   AlphaFoldDB; B8NTY5; -.
DR   STRING; 332952.B8NTY5; -.
DR   EnsemblFungi; EED46492; EED46492; AFLA_101560.
DR   VEuPathDB; FungiDB:AFLA_010407; -.
DR   eggNOG; KOG2741; Eukaryota.
DR   HOGENOM; CLU_023194_7_2_1; -.
DR   OMA; YISTPHS; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   PANTHER; PTHR22604:SF115; DIHYDRODIOL DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G07520)-RELATED; 1.
DR   PANTHER; PTHR22604; OXIDOREDUCTASES; 1.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
FT   DOMAIN          30..133
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
SQ   SEQUENCE   349 AA;  37773 MW;  50740416C8EE4CA1 CRC64;
     MSKMVNWGIL STGDNATKFA KDLLIDPSTR GAHDVTHNLV AVASSTSLQK AQDFLSAVNA
     PPSTAAYGSY ESLLADPTVE IVYISTPHSH HYQNARAALL TGKHVLLEKV FTINAAQARI
     LVQLAREKKL FLMEAMWTRF FPLTLYVRQL IKDGAIGTVQ RVVSDRNLGR DIETLYGTEH
     RLVNPALAGG ALLDSSGTSK SAPHVSGSLV KYAPTGVDET ATVIVTFPES KTQGVATASL
     RVASDPTDPG VRIFGDKGQI QIFGPAARPL SIAVVTYGEG GPEVVERKDF EIPVGHGLFW
     EADACARYLA KGETESDVMP LDETLLIMDV MDRVREENSL RYPAEVEGH
//
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