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Database: UniProt
Entry: A0A2V1DG60_9PLEO
LinkDB: A0A2V1DG60_9PLEO
Original site: A0A2V1DG60_9PLEO 
ID   A0A2V1DG60_9PLEO        Unreviewed;       400 AA.
AC   A0A2V1DG60;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 11.
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=DM02DRAFT_616696 {ECO:0000313|EMBL:PVH97146.1};
OS   Periconia macrospinosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Periconiaceae; Periconia.
OX   NCBI_TaxID=97972 {ECO:0000313|EMBL:PVH97146.1, ECO:0000313|Proteomes:UP000244855};
RN   [1] {ECO:0000313|EMBL:PVH97146.1, ECO:0000313|Proteomes:UP000244855}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSE2036 {ECO:0000313|EMBL:PVH97146.1,
RC   ECO:0000313|Proteomes:UP000244855};
RX   PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA   Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA   Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA   Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT   "Comparative genomics provides insights into the lifestyle and reveals
RT   functional heterogeneity of dark septate endophytic fungi.";
RL   Sci. Rep. 8:6321-6321(2018).
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; KZ805444; PVH97146.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1DG60; -.
DR   STRING; 97972.A0A2V1DG60; -.
DR   Proteomes; UP000244855; 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:UP000244855}.
FT   DOMAIN          8..135
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
SQ   SEQUENCE   400 AA;  43500 MW;  B4AB3EE93E72A323 CRC64;
     MSSPKTIRWG ILATGGIAQT FTKDLLVDPT TRGVTHIKHT VVAAASSSSQ DRAQKFLKDV
     GAPSDAKAYG SYEDFVKQPD IDIVYIATPH SHHYQNAMLC LEAGKNVLCE KAFTVNAAQA
     RALADKAKEK NLFLMEAVWT RYFPLSIYVR EQITSGRIGP IARVFADNSM ATNPEQTWSD
     GKNRMVNPDL AGGALLDLGI YSLTWVFQTL YHTQPEKDRQ PPKVLAALKT YEATGAADES
     TTIILNFPRS KEAGGDAHAI ATTSLRVATT PGGNTDVPGI RIQGPGGEIQ VFPPAFRPTR
     TRIVLKDGTI EDKDWPQPGP GEGSGWYNGF GGGTNPEGVG HGMFWEADEA ASALVEGRKE
     GKYESLAESI LIMEVMDEVR KQGNLTYPEK IETTKFPTPL
//
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