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Database: UniProt
Entry: S0E6Y6_GIBF5
LinkDB: S0E6Y6_GIBF5
Original site: S0E6Y6_GIBF5 
ID   S0E6Y6_GIBF5            Unreviewed;       419 AA.
AC   S0E6Y6;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=FFUJ_06420 {ECO:0000313|EMBL:CCT70445.1};
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT70445.1, ECO:0000313|Proteomes:UP000016800};
RN   [1] {ECO:0000313|Proteomes:UP000016800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC   {ECO:0000313|Proteomes:UP000016800};
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
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; HF679028; CCT70445.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0E6Y6; -.
DR   STRING; 1279085.S0E6Y6; -.
DR   EnsemblFungi; CCT70445; CCT70445; FFUJ_06420.
DR   VEuPathDB; FungiDB:FFUJ_06420; -.
DR   HOGENOM; CLU_023194_5_2_1; -.
DR   OrthoDB; 5486222at2759; -.
DR   Proteomes; UP000016800; Chromosome 6.
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; OXIDOREDUCTASES; 1.
DR   PANTHER; PTHR22604:SF105; TRANS-1,2-DIHYDROBENZENE-1,2-DIOL DEHYDROGENASE; 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:UP000016800}.
FT   DOMAIN          27..133
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
SQ   SEQUENCE   419 AA;  47510 MW;  FA335A0FA9BF35BB CRC64;
     MSSVSGFLRR NWQAYSPPEP PKNANAIKFG ILGAANIAAT ALITPAKSHP DIKIYAVAAR
     QKEKAEAYAK KHNIPHVFDS YQAILDDPSV DAVYIPLIVT LHCEWAIKAI AKGKHVLLEK
     PATVNAAEAE MLFRSPLLRR PDAPVLLEAM HFRFQPSWQY FLSLVDRQNI QTVDSVALLP
     SYIIPKGNAQ LEYNLGGGTM LHLGTYPMYA LRQIMGREPE ECMACRIRSV PPPGDLCDEF
     AETRFRFPNG RIGNAIINAR GSITTFPTFN ISVCHKEIKL DDMTLPKEQT KWKLRKLSVS
     NFLISSFWHR IDIVDEYTIR DDRNDTDLKK WTVKQSKKVY TFKDAGIDQP SEPFWSSYRH
     LLEQFVTRVR GKQGSGLWVG HEDSIAQARM IDMAYEKSGL PLRPTREFRL EDYSASLLG
//
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