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Database: UniProt
Entry: A0A072NUN7_9EURO
LinkDB: A0A072NUN7_9EURO
Original site: A0A072NUN7_9EURO 
ID   A0A072NUN7_9EURO        Unreviewed;       397 AA.
AC   A0A072NUN7;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=A1O9_12656 {ECO:0000313|EMBL:KEF51306.1};
OS   Exophiala aquamarina CBS 119918.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF51306.1, ECO:0000313|Proteomes:UP000027920};
RN   [1] {ECO:0000313|EMBL:KEF51306.1, ECO:0000313|Proteomes:UP000027920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF51306.1,
RC   ECO:0000313|Proteomes:UP000027920};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL   Submitted (MAR-2013) 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:KEF51306.1}.
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DR   EMBL; AMGV01000025; KEF51306.1; -; Genomic_DNA.
DR   RefSeq; XP_013253896.1; XM_013398442.1.
DR   AlphaFoldDB; A0A072NUN7; -.
DR   STRING; 1182545.A0A072NUN7; -.
DR   GeneID; 25287550; -.
DR   VEuPathDB; FungiDB:A1O9_12656; -.
DR   HOGENOM; CLU_023194_7_2_1; -.
DR   OrthoDB; 5486222at2759; -.
DR   Proteomes; UP000027920; 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:UP000027920}.
FT   DOMAIN          8..137
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
SQ   SEQUENCE   397 AA;  43495 MW;  8C2B4533337AA284 CRC64;
     MSSPKVVRWG ILATGGIART FTKDMLISPK TRNVLDIQHS VAAVASSSSL SSAEKFISEV
     VSPAQSSTAT PYASYEELVQ DPNVDIIYIA TPHSHHYQNA MLCLEHNKPV LCEKALTVNA
     AQAKILFETA KKKNIFFMEA VWTRYFPLSQ AVRKHITDGD IGEVLRVGAD MSIGADQDFD
     LSSRMINLDL AGGALLDLGI YSLTWVFQTL YHTLPAGLRS QSRPKVIGTA MTPEPRTGAD
     ESTLILLEFP KSSPTGKTKS HAVATTALRV SDDPARSQSR EVGDVEVPAA RIQGEKGEIQ
     VFGPLYRPTR YRVVKKSPQP EVIDRKFEFE GGAHGMMYEA DAAARALLSG ALESETMTWA
     ESTLIMEVMD EARKQGGLVY PDGIESTEYP VKLTEKR
//
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