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Database: UniProt
Entry: A0A1G7TFW6_9SPHI
LinkDB: A0A1G7TFW6_9SPHI
Original site: A0A1G7TFW6_9SPHI 
ID   A0A1G7TFW6_9SPHI        Unreviewed;       569 AA.
AC   A0A1G7TFW6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:SDG34257.1};
GN   ORFNames=SAMN05192573_103151 {ECO:0000313|EMBL:SDG34257.1};
OS   Mucilaginibacter gossypii.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=551996 {ECO:0000313|EMBL:SDG34257.1, ECO:0000313|Proteomes:UP000199705};
RN   [1] {ECO:0000313|EMBL:SDG34257.1, ECO:0000313|Proteomes:UP000199705}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gh-67 {ECO:0000313|EMBL:SDG34257.1,
RC   ECO:0000313|Proteomes:UP000199705};
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; FNCG01000003; SDG34257.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7TFW6; -.
DR   STRING; 551996.SAMN05192573_103151; -.
DR   Proteomes; UP000199705; 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          152..342
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          433..556
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   REGION          61..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   569 AA;  63731 MW;  AF4E51137A451A21 CRC64;
     MPLSNINGKA KANNTYDAIV IGSGISGGWA AKELSELGLK TIMLERGRNF EHIKDYKTAN
     QDPWDRHHAG KPTQAQRKQR PVISRNWGAS EPIMDYWTDE QAAPYTEIKP FNWWRSYQLG
     GRSILWGRQS YRWSDFDFEA NVKDGWAIDW PIRYKDLAPW YDHVEKFAGI SGSLEGLPQL
     PDGHYLPPMD MNVVEKDVAA RIKKNYNGTR HMIIGRTANL TAAIPGRTAC QFRNRCWEGC
     PFGGYFSTQS STLPAALATG NLTVRPYSIV TKILYDKDTK KAKGVEVLDA ETNQTYEYYS
     KIVFVNASAL NSAWVLMNSA TDIWPDGLGS SSGELGHNIM DHHYNLGASG LVEGFEDKYY
     YGRRANGIYI PRFTNLFGDK RDYLRGFGYQ GAASRMGWSR EIAEYNIGAQ YKDALTEPGP
     WTIGIGGFGE LLPYHENKIT LDKTRKDKWG LPILAMDAEI KENEKKMRID IVKEAKAMLE
     SAGVKNVETH DRGHNVGDGI HEMGTARMGR DPKTSVLNGN NQVWDAKNVF VTDGAAMTSA
     ACQNPSLTYM AMTARAAHFA VDELKKGNL
//
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