ID   A0A1H2A7M1_9ACTN        Unreviewed;       602 AA.
AC   A0A1H2A7M1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:SDT41874.1};
GN   ORFNames=SAMN04488543_4273 {ECO:0000313|EMBL:SDT41874.1};
OS   Friedmanniella luteola.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Friedmanniella.
OX   NCBI_TaxID=546871 {ECO:0000313|EMBL:SDT41874.1, ECO:0000313|Proteomes:UP000199092};
RN   [1] {ECO:0000313|EMBL:SDT41874.1, ECO:0000313|Proteomes:UP000199092}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21741 {ECO:0000313|EMBL:SDT41874.1,
RC   ECO:0000313|Proteomes:UP000199092};
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; LT629749; SDT41874.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2A7M1; -.
DR   STRING; 546871.SAMN04488543_4273; -.
DR   OrthoDB; 9798604at2; -.
DR   Proteomes; UP000199092; Chromosome i.
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; IPR006076; FAD-dep_OxRdtase.
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; PF01266; DAO; 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:UP000199092}.
FT   DOMAIN          15..49
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          246..363
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          458..593
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   602 AA;  64768 MW;  6C766363B2EFA90B CRC64;
     MSAASTDAAG EVTHDVVVVG AGVAGALVAK RLTRSGLRVL LLEAGPATAS TFDGYLRHLE
     TFFETSNKGP ESPWPTALGA PQPDTHDVRS GDGYFVQQGP HPYGSTYTRL QGGSTLHWLG
     VALRMLPEDF AMRTRYGVGR DWPLDYATLE PYYRQAENEL GVAADVADQA HLGVEFADGY
     DYPMERVPPS YSDQMWAGAV DGMEVTVGDS AIPLKIRSYP AARNSVPRGD YEPVGAVDER
     ADGQALARDL GQRCAGNTAC TPICPIQAKY NANKSLAQAD RDHLEIRAQA VASKILVDPV
     TGAVTGVEYQ RYDDPSSARH QVQVARGRSY VLAAHAIENA KLLLASGLAG RSGMLGRNLM
     DHPSIYGWGL APQPIGSFRG PLSTSGIDDL RGGPFRARQA AFRVDVGNDG WRATTGAPDT
     TVAEAVTHGK LHGAALREHL TSVLRRQVRF SLNVEQLPSP SNRITVDPAH VDGFGNPRPV
     ISYDIDEYTL AGMAAAHRTY QAVFERAGIE DCSDPETGVW FPSVAYEGQE FRYHGMGHFA
     GTHVMGDDPT NSVVDADQRS WEHPNLFVLG SGSFPTMGTS NPTLTLAALA LRAADRLTTE
     LR
//