ID G0LBD3_ZOBGA Unreviewed; 567 AA.
AC G0LBD3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=FAD-dependent oxidoreductase, GMC oxidoreductase family {ECO:0000313|EMBL:CAZ95975.1};
DE EC=1.1.99.- {ECO:0000313|EMBL:CAZ95975.1};
GN OrderedLocusNames=zobellia_1922 {ECO:0000313|EMBL:CAZ95975.1};
OS Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 /
OS NCIMB 13871 / Dsij).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zobellia.
OX NCBI_TaxID=63186 {ECO:0000313|EMBL:CAZ95975.1, ECO:0000313|Proteomes:UP000008898};
RN [1] {ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RG Genoscope - CEA;
RT "Complete genome sequence of Zobellia galactanivorans Dsij.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAZ95975.1, ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RX PubMed=22513138; DOI=10.1111/j.1462-2920.2012.02751.x;
RA Thomas F., Barbeyron T., Tonon T., Genicot S., Czjzek M., Michel G.;
RT "Characterization of the first alginolytic operons in a marine bacterium:
RT from their emergence in marine Flavobacteriia to their independent
RT transfers to marine Proteobacteria and human gut Bacteroides.";
RL Environ. Microbiol. 14:2379-2394(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; FP476056; CAZ95975.1; -; Genomic_DNA.
DR RefSeq; WP_013993283.1; NC_015844.1.
DR AlphaFoldDB; G0LBD3; -.
DR STRING; 63186.ZOBELLIA_1922; -.
DR KEGG; zga:ZOBELLIA_1922; -.
DR PATRIC; fig|63186.3.peg.1895; -.
DR HOGENOM; CLU_008878_4_0_10; -.
DR OrthoDB; 9787779at2; -.
DR Proteomes; UP000008898; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
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; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR PANTHER; PTHR42784:SF1; PYRANOSE 2-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:CAZ95975.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008898}.
FT DOMAIN 99..337
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 430..553
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 567 AA; 63686 MW; 6E8F68B507B1E745 CRC64;
MNKEEIFDAI VVGTGISGGW AAKELCENGL KTLVLERGPM VRHIEDYPTM NDDPWDYPLK
GELSKADKEK YHIQSRVGWA PKEDVKHFFV NDLDHPYVET KRFDWIRGYQ VGGRSLTWGK
QSYRWSDLDF EANKKEGIGV DWPVRYKDIS PWYDKVEAYI GVSGENLGLP HLPDGIFQPK
MDLNCVEEEF KASVAEKFDD GRLITIGRAA HITDPDADFE GRGTCQNRNR CWRGCPFGGY
FSSNSSTLPA AERTGNMTLR PNSIVYEVVY DDTTKKATGV KIIDAETNEK IEFKAKVIFL
CASSMASVGI LLQSKSERFP NGLGNDSDAL GRGIMDHHYK LGASAKVDGY LDKYYKGRRP
NGFYIPRFVN LNDETKREGY LRGFGYQGSA SRQDWSASIG EMGYGKDLKE SILKPGHWQI
GVTGFGEFLP YDDNRVTLSR SKKDKWGLPQ LDFDVEFKEN EYNMREDIKK EIVAMFKAAG
FKDVQPYDEV TGPGLGIHEM GGARMGHSPK TSIVNKHNQL HTVPNVYVTD GAFMSSSSCV
NPSLTYMAFT ARAANHAAEQ LKSGKLS
//
