ID A0A0D2C6F2_9EURO Unreviewed; 388 AA.
AC A0A0D2C6F2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=PV08_03441 {ECO:0000313|EMBL:KIW19149.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW19149.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW19149.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW19149.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN847493; KIW19149.1; -; Genomic_DNA.
DR RefSeq; XP_016239365.1; XM_016377795.1.
DR AlphaFoldDB; A0A0D2C6F2; -.
DR STRING; 91928.A0A0D2C6F2; -.
DR GeneID; 27330524; -.
DR VEuPathDB; FungiDB:PV08_03441; -.
DR HOGENOM; CLU_023194_7_2_1; -.
DR OrthoDB; 2898964at2759; -.
DR Proteomes; UP000053328; 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:UP000053328}.
FT DOMAIN 6..130
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
SQ SEQUENCE 388 AA; 43089 MW; D0187E8FA7E87F2B CRC64;
MVYTVRWGIL ATGWIAEKFA GDLLKDPSTR NTRDVAHVVA AVASSSGKDR AERFCRDLGI
SEACAIYGSY RELVNDTNVD IVYVASPHSH HFQHTMLALE GGKHVVCEKP LTVNAAQAKI
LYKTARENNL FLLDAVWTRF FPLSIQIRES IQKGEIGEVL RVIADTSFGI HPDIALKETP
RKLTYELAGG ALLEIGIYSL TWVFQTLYHT LPRDQRKRPS SILSYMNKYE PTGVDQTTTL
LISFPTSTPS NLPNSSSHGV AMTAFAVATD PDQKNSAGPA IRIQGTRGEI QVYGPAFQPT
RYKVIPAKKG DLATTIRDVE LPFPANGHGM FYEADEAARC IRDGKLESET MPWDESILVM
EVMDEVRKQG ELKYPDSIES DVVQHSNK
//