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Database: UniProt
Entry: A0A0F4GYP5_9PEZI
LinkDB: A0A0F4GYP5_9PEZI
Original site: A0A0F4GYP5_9PEZI 
ID   A0A0F4GYP5_9PEZI        Unreviewed;       307 AA.
AC   A0A0F4GYP5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=TI39_contig42g00014 {ECO:0000313|EMBL:KJY02550.1};
OS   Zymoseptoria brevis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJY02550.1, ECO:0000313|Proteomes:UP000033647};
RN   [1] {ECO:0000313|EMBL:KJY02550.1, ECO:0000313|Proteomes:UP000033647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zb18110 {ECO:0000313|EMBL:KJY02550.1,
RC   ECO:0000313|Proteomes:UP000033647};
RA   Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT   "RNA-seq based gene annotation and comparative genomics of four
RT   Zymoseptoria species reveal species-specific pathogenicity related genes
RT   and transposable element activity.";
RL   Submitted (MAR-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}.
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:KJY02550.1}.
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DR   EMBL; LAFY01000039; KJY02550.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4GYP5; -.
DR   STRING; 1047168.A0A0F4GYP5; -.
DR   OrthoDB; 2898964at2759; -.
DR   Proteomes; UP000033647; 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:UP000033647}.
FT   DOMAIN          42..111
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
SQ   SEQUENCE   307 AA;  33609 MW;  5AB68C26CADE7C89 CRC64;
     MSDSKVFRLR WGIMATGHVA GRFTRDLLTD PSSRDVSDVH HLITAIASSS GLQRAAAFCD
     DVKAPQNVKL CASYAEMVSD PGVDIVYIAT PVSHHFQNAM MAIEAGKAVL SDCSLDINLP
     EDGGEVDAKN KLHRLLKLDL AGGAMLDLGI YSLTWIMQIM YHLQPKGHDK ERPMIVSAVN
     KYPAGIDETS SFVLQFPRQK AMGVGMTSLR IASGVDFDFT AGHPIRIQGT NGEIQVFGPA
     FKPRSIRVIT EDGNGPAQVQ TDEFPIPRDE GRENWAMDCS GKRTNVRDAS ETGSWRARFC
     RLTKVSS
//
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