ID   A0A368JG44_9BACT        Unreviewed;       567 AA.
AC   A0A368JG44;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=GMC family oxidoreductase {ECO:0000313|EMBL:RCR66620.1};
GN   ORFNames=DUE52_25285 {ECO:0000313|EMBL:RCR66620.1};
OS   Larkinella punicea.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Larkinella.
OX   NCBI_TaxID=2315727 {ECO:0000313|EMBL:RCR66620.1, ECO:0000313|Proteomes:UP000253383};
RN   [1] {ECO:0000313|EMBL:RCR66620.1, ECO:0000313|Proteomes:UP000253383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=zzj9 {ECO:0000313|Proteomes:UP000253383};
RA   Zhou Z., Wang G.;
RT   "Genome analysis of Larkinella rosea.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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:RCR66620.1}.
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DR   EMBL; QOWE01000025; RCR66620.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368JG44; -.
DR   OrthoDB; 1154541at2; -.
DR   Proteomes; UP000253383; 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   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          90..340
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          431..554
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   567 AA;  63279 MW;  8C9486837248A4FD CRC64;
     MNLNIDAVKA QTYDAIVIGS GVSGGWAAKE LTEKGLRVLM LERGRPLEHV TGYTEALKAP
     WEMPEMTRLG DLALKYPQAP PDAAKTVPTY WMPGADASYR QEKPFRWLRP DIVGGKSIMW
     GRQSYRFSDI DFEANAKEGI GIDWPIRYKD IAPWYSYVEK FAGISGEKLG LPQLPDSEFI
     APMDMFLVEK EVRKSIEKNY PGRVMTIGRT ANLSEAQKVH VDNGRSPCQY RNQCIRGCPY
     GAYFSTQSCT LPPAVKTGRL TLRPHSVVTE VIYDAQKQRA SGVRVKDAQT LESQEYFAKV
     IFVCASAMAS TALLMNSVSD RFPNGLGNDS GQLGHNLMDH HFRIGANGQW EGGQDRYYYG
     RRANGIYIPR YRNIGSDKRD YLRGFGYQGG GGRQGWQHQV AELAFGASLK EELTKPGLWN
     MGLIGFGEQL PEYKNRMYLD KSKLDKWGMP MLVFDAEIGE NEKKMRVDML NDAQEMLEKA
     GLINVKTYDQ GSVLGQAVHE MGTARMGRDP KTSVLNGNNQ IHAVKNVFVT DGACMTSSAC
     VNPSLTYMAL SARAANFAVQ ELKAMRI
//