ID   A0A1T4T8F2_9BACT        Unreviewed;       566 AA.
AC   A0A1T4T8F2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:SKA36428.1};
GN   ORFNames=SAMN04488128_104104 {ECO:0000313|EMBL:SKA36428.1};
OS   Chitinophaga eiseniae.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=634771 {ECO:0000313|EMBL:SKA36428.1, ECO:0000313|Proteomes:UP000190367};
RN   [1] {ECO:0000313|EMBL:SKA36428.1, ECO:0000313|Proteomes:UP000190367}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22224 {ECO:0000313|EMBL:SKA36428.1,
RC   ECO:0000313|Proteomes:UP000190367};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FUWZ01000004; SKA36428.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4T8F2; -.
DR   STRING; 634771.SAMN04488128_104104; -.
DR   OrthoDB; 9787779at2; -.
DR   Proteomes; UP000190367; 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          16..339
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   566 AA;  62868 MW;  139A0FAA41FF8968 CRC64;
     MINLNLKAEA ANTYDAIVVG SGITGGWAAK ELCEKGLKVL MIERGRQLEH VKDYETATAA
     PWEVPHRGVL TNELKKGHQF LVREKVYTEF NHSYWMKDGD SPYTEEKRFD WQRADIVGGR
     SIMWGRGSLR LSDLDFEANA KEGIGIDWPI RYKDLAPWYS HVEAFAGISG QAEGLPHLPD
     GVFQPPMEMN CFEKHVKGKL EAAFPERRMT IFRTANLTQA IGDRNKCQYR DRCSRGCPFG
     AYFSTQASTL PAAVKTGNLT LLTDSLVNSI IYDDNKGKAT GVRVIDKHTK EMTEYHARII
     FLNASALAST FVLLNSTSAR FPQGLGNDSG VLGHYLMDHH FHAGASGSSE EFADKYYHGQ
     RPAGFYIPRF ANVGNDKRGY LRGFGYTGYS SRTGWARGIA ELGVGGAFKD YISEPGPWQM
     GLMGFGECLP YKENMVSLDT SVKDAWGQPV LKMNCEFKEN EMKMRKDMAA EAAAMLEAAG
     LKNVQAFDRA SYPGMAIHEM GTARMGRDPK TSVLNEWNQV HAVKNVFVTD GACMTSSACQ
     NPSLTYMALT ARAANHAVEE LKRQSL
//