GenomeNet

Database: UniProt
Entry: A0A0L1JI78_ASPNO
LinkDB: A0A0L1JI78_ASPNO
Original site: A0A0L1JI78_ASPNO 
ID   A0A0L1JI78_ASPNO        Unreviewed;       370 AA.
AC   A0A0L1JI78;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=ANOM_000021 {ECO:0000313|EMBL:KNG91451.1};
OS   Aspergillus nomiae NRRL 13137.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG91451.1, ECO:0000313|Proteomes:UP000037505};
RN   [1] {ECO:0000313|EMBL:KNG91451.1, ECO:0000313|Proteomes:UP000037505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG91451.1,
RC   ECO:0000313|Proteomes:UP000037505};
RA   Moore M.G., Shannon B.M., Brian M.M.;
RT   "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KNG91451.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JNOM01000002; KNG91451.1; -; Genomic_DNA.
DR   RefSeq; XP_015412374.1; XM_015545279.1.
DR   AlphaFoldDB; A0A0L1JI78; -.
DR   STRING; 1509407.A0A0L1JI78; -.
DR   GeneID; 26801825; -.
DR   OrthoDB; 2898964at2759; -.
DR   Proteomes; UP000037505; 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   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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000037505}.
FT   DOMAIN          46..120
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
SQ   SEQUENCE   370 AA;  41236 MW;  9EBC61F49755A9B0 CRC64;
     MGADNVTTIR WGIMATGEIA KLFVKDLLID PATQLFIQQN ITPVMSRDIS CTAYGSYEEL
     VTDANVDVLY IASPHSHHYQ NCMLALENSK AILCEKPLTV NAKQAKVLYE TAQRQNLFLM
     EAVWTRYFPL STAVRQYIRD GLIGEVLRVY VDNSTGVDIS NLSSTHRYLD KELAGGALLD
     IGIYPLIWVF QTLYHTREKH QRQKPSQVVS LLTYEKSSRT DQMASVMVEF PSSTPSGTSV
     AHGIMSTSMI LSNDADGKGS SGTAVRIQGL EGEIQILGPV HRPESVKIIR KGECRTVHFE
     IPAGGHGMYW EADEAGRCIR DGKIQSEVIP WDESVAIMEV VDEIRAQANY SYPEQIESTE
     YPLSLKKKAL
//
DBGET integrated database retrieval system