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Database: UniProt
Entry: A0A0S8EKM7_9BACT
LinkDB: A0A0S8EKM7_9BACT
Original site: A0A0S8EKM7_9BACT 
ID   A0A0S8EKM7_9BACT        Unreviewed;       417 AA.
AC   A0A0S8EKM7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AMK72_05835 {ECO:0000313|EMBL:KPK48887.1};
OS   Planctomycetes bacterium SM23_25.
OC   Bacteria; Planctomycetota.
OX   NCBI_TaxID=1704028 {ECO:0000313|EMBL:KPK48887.1, ECO:0000313|Proteomes:UP000052058};
RN   [1] {ECO:0000313|EMBL:KPK48887.1, ECO:0000313|Proteomes:UP000052058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_25 {ECO:0000313|EMBL:KPK48887.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPK48887.1}.
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DR   EMBL; LJTY01000095; KPK48887.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8EKM7; -.
DR   Proteomes; UP000052058; 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; 3.30.410.40; -; 1.
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; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          66..207
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          342..392
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   417 AA;  45753 MW;  F46BB88E4C8269D9 CRC64;
     MGRDYRNEFY YGTHLGAMIY GDNHGLLFTE EGLNIIRPIM TGGATNLFTG SAARPPAWLK
     ERYKIDIDDY VEETINELDI RPLPDELLGE ASKRIMEAGI SLGYKWEPLM KFIRPARAAR
     FDCGAKCMLG CRCGAKWTAN EYVDDAVAAG CELITQAKVD RLIIEDKQVG GVRGKINKRI
     PFEVRAGVVV LAAGGIGTPL IMQNSGFFDA GNGLAVDTTA LVYGVSKYKG TSSEPPMTVA
     YTDDENGYML STIIDPWLSY PLIMFAKGIR YPLTWVNYTR TIGVMIKVKD EVSGGITVEG
     KISKPTTAQD RYKLNHASIV SRKILVEAGC DPDSVFVGPL RGTHPCATVK IGEMLDANLQ
     TEVKNLYVCD ASTFPEALDR PPVLTIIALA KKLSDHLLKT VFRRKAAQRV PAEPAEG
//
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