ID   A0A1G9RRV8_9BACT        Unreviewed;       564 AA.
AC   A0A1G9RRV8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:SDM25961.1};
GN   ORFNames=SAMN04488090_3011 {ECO:0000313|EMBL:SDM25961.1};
OS   Siphonobacter aquaeclarae.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC   Siphonobacter.
OX   NCBI_TaxID=563176 {ECO:0000313|EMBL:SDM25961.1, ECO:0000313|Proteomes:UP000198901};
RN   [1] {ECO:0000313|EMBL:SDM25961.1, ECO:0000313|Proteomes:UP000198901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21668 {ECO:0000313|EMBL:SDM25961.1,
RC   ECO:0000313|Proteomes:UP000198901};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNGS01000005; SDM25961.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9RRV8; -.
DR   STRING; 563176.SAMN04488090_3011; -.
DR   OrthoDB; 1154541at2; -.
DR   Proteomes; UP000198901; 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:UP000198901}.
FT   DOMAIN          218..314
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;  62981 MW;  BD93C6D198B8B074 CRC64;
     MKDKNSYDAI VVGSGISGGW AAKELCDKGL KTLVLERGRS VEHVKDYPTT FMHPWQIPYR
     GHMPQAFMDE NPLITKAAGF GSDNAQFFIQ DKDHPYIQEK PFDWIRGYQV GGKSLTWGRA
     CQRWSDFEFS APDRLRYGID WPIRYNDIAP WYTHVERFIG VCGNADGIEA MPDGEFLPPF
     QLNCVEEALQ KSIRTHYPDR HLVQARWAHL TQPREIHLKQ GRGKCQARNL CMRGCPFGGY
     FSSVSSTLPW AQKTGKLTIR PHSVVHSILF DEKTGKASGV RVIDAETKEA MEFSARVIFL
     NASALNTNLI LLNSRSARFP NGLGNDSGLL GKYVGFHNYR GSLSAEMPGF ENGYYFGRNP
     TDAIIANYRN LGKQDTDYVG GFTTFLGAHR HRGNASADTP GFGESFKKKM TEPGPWHIYM
     YMQGETIPKA ENHVRLSTSE TDGFGIPKLI ASVGYDDNDE KMTADFLRES KAMLEKAGCI
     NIETHDNRQA PGLDIHEMGG VRMGKDPKTS LLNAHNQLHA VPNVFVTDGA CMTSTGNQSP
     SLLYMALTAR AVDYAAKEVK ANRL
//