ID   A0A0C1KQN6_9BACT        Unreviewed;       564 AA.
AC   A0A0C1KQN6;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=GMC family oxidoreductase {ECO:0000313|EMBL:KIC89776.1};
GN   ORFNames=HY58_13940 {ECO:0000313|EMBL:KIC89776.1};
OS   Flavihumibacter sp. ZG627.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Flavihumibacter.
OX   NCBI_TaxID=1463156 {ECO:0000313|EMBL:KIC89776.1, ECO:0000313|Proteomes:UP000031400};
RN   [1] {ECO:0000313|EMBL:KIC89776.1, ECO:0000313|Proteomes:UP000031400}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZG627 {ECO:0000313|EMBL:KIC89776.1,
RC   ECO:0000313|Proteomes:UP000031400};
RA   Zhou G., Li M., Wang G.;
RT   "Genome sequence of Flavihumibacter carbonis ZG627.";
RL   Submitted (JUL-2014) 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:KIC89776.1}.
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DR   EMBL; JPHF01000007; KIC89776.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C1KQN6; -.
DR   STRING; 1463156.HY58_13940; -.
DR   Proteomes; UP000031400; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000031400}.
FT   DOMAIN          106..337
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          428..551
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   564 AA;  63286 MW;  2B3ACCDDE196E7D1 CRC64;
     MNGSAKEANT YDAIVVGSGI SGGWAAKELC EKGLKVVMLE RGRPLEHIKD YTTANNHPWE
     MAHRGKVTDL QRRDYPVIAR GWALNEPVME YWANEEENPY TEIQPFTWWR SYQMGGRSLL
     WGRQSYRLSD LDFMANAKDG HGIDWPIRYK DIAPWYDHVE RFAGISGSLE GIPHLPDGQF
     LPAMELNCVE KDVAARIKAH FRDQRRLIIG RVANLTAPIE GRSKCQFRNR CWEGCPFGGY
     FSTQSSTLPA AQKTGNLTVR PFSIVTKLVY DKNSKKATGV EVLDAENNKT YTYNSKIVFL
     CASALNSTWV LFNSATDIWP GGLGSSSGEL GHNVMDHHYN LGASGRVEGF EDKYYYGRRA
     NGFYIPRFVN INGDKRKYLR GFGYQGGASR MGWSREIAEM SVGKEFKDAL TEPGNWTIGA
     TGFGEILPYH ENRILLDKER HDKWGLPVLA MDAGLKQNEM DMREDIKNEL VAMLESAGVK
     NVRTYDTGHA MGHGIHEMGT ARMGRDPNTS VLNAFNQVWD AKNVYVTDGA AMTSSACQNP
     SLTYMALTAR AADHAVSELK KRNL
//