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Database: UniProt
Entry: A0A1X6YV86_9RHOB
LinkDB: A0A1X6YV86_9RHOB
Original site: A0A1X6YV86_9RHOB 
ID   A0A1X6YV86_9RHOB        Unreviewed;       522 AA.
AC   A0A1X6YV86;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Fructose dehydrogenase large subunit {ECO:0000313|EMBL:SLN32488.1};
DE            EC=1.1.99.11 {ECO:0000313|EMBL:SLN32488.1};
GN   Name=fdhL {ECO:0000313|EMBL:SLN32488.1};
GN   ORFNames=ROJ8625_01496 {ECO:0000313|EMBL:SLN32488.1};
OS   Roseivivax jejudonensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseivivax.
OX   NCBI_TaxID=1529041 {ECO:0000313|EMBL:SLN32488.1, ECO:0000313|Proteomes:UP000193570};
RN   [1] {ECO:0000313|EMBL:SLN32488.1, ECO:0000313|Proteomes:UP000193570}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8625 {ECO:0000313|EMBL:SLN32488.1,
RC   ECO:0000313|Proteomes:UP000193570};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; FWFK01000002; SLN32488.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X6YV86; -.
DR   OrthoDB; 9798604at2; -.
DR   Proteomes; UP000193570; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0047904; F:fructose 5-dehydrogenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000313|EMBL:SLN32488.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193570}.
FT   DOMAIN          88..305
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          391..508
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   REGION          444..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   522 AA;  56824 MW;  77E495D5E0B20A96 CRC64;
     MAAPFELSDD NVVVIIGTGA GGGVLANELA QKGVSVVALE AGGRYLPEDY VNDEWDSFGQ
     LAWTDTRTTS GDWRVAKDFS NLPAWIVKAV GGTTTHWAGA SLRFQPHEWK ALTNYGAVDG
     ASLLDWPIDA EEMDPYYTRA EDKLGVTRTN DIPGLPGCNN YKVFEAGAKK LGYKEVHTGR
     MAINSQERDG RMACQQTGFC FQGCKWGAKW SAAYTDIPAG EATGNLEVRE KAHVARILHD
     DSGKVTGVEY FDEAGDLQMQ RARVVCVAGN SFESPRLLLN SHSSMFPDGL ANSSGMVGRN
     YMRHLTGSVY ATFEQPVRMW RGTTMAGIVQ DEARHDPSRG FVGGYELETL SLGLPFMAAF
     LDPGAWGREF TTALDSYENM AGMWIVGEDM PQESNRVTLS DAEDAFGLKV ANVHYSDHPN
     DTAMRDHAYK QGAAIYDAVG ATRTLPTPPY PSTHNLGTNR MSERPEDGVV NRNGRAHDVP
     NLYVSDGSQF TTGAAENPTL TIVALAIRQA EHIASEMNQG VL
//
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