ID K6XVQ1_9ALTE Unreviewed; 561 AA.
AC K6XVQ1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Glucoside 3-dehydrogenase {ECO:0000313|EMBL:GAC24694.1};
GN ORFNames=GMES_2399 {ECO:0000313|EMBL:GAC24694.1};
OS Paraglaciecola mesophila KMM 241.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1128912 {ECO:0000313|EMBL:GAC24694.1, ECO:0000313|Proteomes:UP000006263};
RN [1] {ECO:0000313|EMBL:GAC24694.1, ECO:0000313|Proteomes:UP000006263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMM 241 {ECO:0000313|EMBL:GAC24694.1,
RC ECO:0000313|Proteomes:UP000006263};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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}.
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:GAC24694.1}.
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DR EMBL; BAEP01000049; GAC24694.1; -; Genomic_DNA.
DR RefSeq; WP_006992845.1; NZ_BAEP01000049.1.
DR AlphaFoldDB; K6XVQ1; -.
DR eggNOG; COG2303; Bacteria.
DR OrthoDB; 9787779at2; -.
DR Proteomes; UP000006263; Unassembled WGS sequence.
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 Pfam; PF13450; NAD_binding_8; 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 Reference proteome {ECO:0000313|Proteomes:UP000006263}.
FT DOMAIN 62..334
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 425..548
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 561 AA; 63485 MW; 824744C03A0456D2 CRC64;
MKNNHYDAIV VGSGISGGWA AKELTEKGLK VLMLERGRNI EHVKDYTNAH KEAWDYPHRG
ERTQEMIENY PVLKRDYPLN EPTLGMWTNE KDSPYVEEKR FDWFRGYHMG GRSLTWGRQS
YRLNKEDFQA NAKEGIAVDW PIRYEDVSPW YDYVERFAGI SGSKDGLDVL PDGEYQTPMP
LNCVEKDVAA RIQKTFKGQR HLIPGRTSNM TEPKPKEGRT NCQYRNKCWL GCPFGGYFST
QSSTLPAAVK TGNLTVRPYS IVTEILYDKD KKRAKGVAVI DAETNETYEF TSKILFVNAS
SFNSTWLLMN SATDIWQGGL GSSSGELGHN VMDHHFRIGA HAMVEGYEDK YHYGRRPSGF
YVPRFRNWGD DKRDYVRGFG YQGSASRQGW GRDVAEMGIG ADLKNAISEP GSWQIGMTAF
GEMLPDHSNR IFLDKTKRDK WGLPVLAMDV EIKDNEKRMR KDMMQDAIDI FEAAGMKNVQ
GYDADYFPGQ GIHEMGTARM GRDPKTSVLN GNNQVWDALN VFVTDGACMT SASCVNPSLT
YMALTARAAD FAVEELKKGN L
//
