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Database: UniProt
Entry: A0A1M5MGT6_9FLAO
LinkDB: A0A1M5MGT6_9FLAO
Original site: A0A1M5MGT6_9FLAO 
ID   A0A1M5MGT6_9FLAO        Unreviewed;       567 AA.
AC   A0A1M5MGT6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:SHG76548.1};
GN   ORFNames=SAMN04488116_2445 {ECO:0000313|EMBL:SHG76548.1};
OS   Allomuricauda flava.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Allomuricauda.
OX   NCBI_TaxID=570519 {ECO:0000313|EMBL:SHG76548.1, ECO:0000313|Proteomes:UP000184532};
RN   [1] {ECO:0000313|Proteomes:UP000184532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22638 {ECO:0000313|Proteomes:UP000184532};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-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; FQWL01000003; SHG76548.1; -; Genomic_DNA.
DR   RefSeq; WP_073179904.1; NZ_FQWL01000003.1.
DR   AlphaFoldDB; A0A1M5MGT6; -.
DR   STRING; 570519.SAMN04488116_2445; -.
DR   OrthoDB; 9787779at2; -.
DR   Proteomes; UP000184532; 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          8..337
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   567 AA;  63951 MW;  3B1933A08D2FB3C4 CRC64;
     MDENVVYDAI VVGTGITGGW AAKELCENGL KTLVLDRGPM VEHIVDYKTM NLDPWDMPNN
     GELSRIDKEK YHKQIRVGWA PKEDVKHFFV NDLEHPYQET KRFDWIRGYH VGGRSITWGK
     QSYRWSDIDF AANKKEGIAV DWPVRYNDIS PWYDKVESYI GVSGENLGLK QLPDGKFQPP
     MELNCVEKEL QQSLQKGFDD GRLLTIGRAA HITEKTTKFE GRGTCQYRNR CWRGCPFGGY
     FSSLSSTLPA AERTGNMTLR ANSVVHEVIY DEKTKKATGV KVIDAETNEK LEFKGKIVFL
     CASAMASVGI LLQSKSKSFP NGLGNNYDEV GRNIMDHHYQ LGASAKVDGH LDKYYKGRRP
     NGFYIPRFVN LDDKTKRPQF LRGFGYQGGA SRNNWSESVA EMGYGAVLKE AILKPGGWEI
     GMTGFGEMLP YHDNRVTLSK DKKDQWGLPQ LDFDVEFKEN ELKMRDAIKK EAVAMLKSAG
     FRNVTEWDRE TGPGLGIHEM GGARMGHDPK TSVLNKHNQL HDVPNVYVTD GAFMTSASCV
     NPSLTYMAFT ARAANHAAEQ FKQNKFS
//
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