GenomeNet

Database: UniProt
Entry: F9FY37_FUSOF
LinkDB: F9FY37_FUSOF
Original site: F9FY37_FUSOF 
ID   F9FY37_FUSOF            Unreviewed;       425 AA.
AC   F9FY37;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=FOXB_11319 {ECO:0000313|EMBL:EGU78169.1};
OS   Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU78169.1};
RN   [1] {ECO:0000313|EMBL:EGU78169.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU78169.1};
RX   PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA   Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT   "A highly conserved effector in Fusarium oxysporum is required for full
RT   virulence on Arabidopsis.";
RL   Mol. Plant Microbe Interact. 25:180-190(2012).
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:EGU78169.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AFQF01002872; EGU78169.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9FY37; -.
DR   STRING; 660025.F9FY37; -.
DR   PaxDb; 5507-FOXG_02907P0; -.
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;
FT   DOMAIN          27..139
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
SQ   SEQUENCE   425 AA;  47928 MW;  24963BF0E7A8C23A CRC64;
     MSSVLGFLRR NWQAYSPPEP PKNTNPIKFG ILGAANIAAN ALIAPAKSHP DVEIHAVAAR
     QKDKAKAYAK KHNIPHAFDS YQANFVYVAI LDDPSIDAVY IPLVASLHYE WAIKAIAKGK
     HVLLEKPATV NAAEAEMLFR SPLLRQPNAP VLLEAMHFRF QPSWQYFLSL VDHENIQTVD
     SVAELPSYII PKGNAQLEYN LGGGTMLHLG TYPMYALRQI MGDEPKGCIT CRIRSTPPPV
     NLSDESTEVS FRFHGGRIGN AVINARASVT TLPTFNISVC HKEIKLEDMT LPKGQTKWTR
     RKLSISNFLI SSFWHRIDIV DEYTIRDETN EKDLKKWTVK QSKKVYTFKD ANVDQPSEPF
     WSSFRHQLEQ FVNRVRGKQG SGLWVGQEDS IAQARMIDMA YEKSRLPLRP TSKFRLEIST
     GNLLG
//
DBGET integrated database retrieval system