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
//