ID   A0A1H9P988_9BACT        Unreviewed;       572 AA.
AC   A0A1H9P988;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:SER44768.1};
GN   ORFNames=SAMN05444359_14415 {ECO:0000313|EMBL:SER44768.1};
OS   Neolewinella agarilytica.
OC   Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae;
OC   Neolewinella.
OX   NCBI_TaxID=478744 {ECO:0000313|EMBL:SER44768.1, ECO:0000313|Proteomes:UP000199021};
RN   [1] {ECO:0000313|Proteomes:UP000199021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24740 {ECO:0000313|Proteomes:UP000199021};
RA   Varghese N., Submissions S.;
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; FOFB01000044; SER44768.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9P988; -.
DR   STRING; 478744.SAMN05444359_14415; -.
DR   InParanoid; A0A1H9P988; -.
DR   OrthoDB; 9787779at2; -.
DR   Proteomes; UP000199021; 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:UP000199021}.
FT   DOMAIN          81..342
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          436..559
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   572 AA;  63447 MW;  B93BC5E7683BBDF4 CRC64;
     MQGKKNNTYD AIVIGTGISG GIAAMELCRK GLKTLVLERG RNIKHGDYPT AMLESWELPH
     QGKIPEDVKK KDYEYLSRKD YIMEQGGIHH FVKDSDHPYT EKKRFDWIRA YQTGGRSLVW
     GRQCYQLSDL DFEANAKEGI AIDWPIRHKD LKPWYDYVTR FVGVSGRAEG LAHFPDGPFQ
     PPMPLNCVED HFRKGVHAKL PHIRVSEGRA AHLTAYDPAV NLGTRGNCQY RNRCRRGCPY
     GGYYSSNSGP IPVAIETGNM TLVNGAAVRE IIYDADKKRA TGVRVKLTET GQETEFFTDG
     VVFLCASALN SAAILLASKS DAQPNGLGND NDQVGRNVMD HHHSVGAGGT MEGFEDKYFK
     GRKPNGIYIP RFVNLGDQAT KRNYLRGFGY QGGASRSNWR RLVRELSVGP GSELKQAMLE
     PGEWSVGIGG FGESLPNPDN RVTLNYDKLD ADGLPTLIMD VAFGENEAAM RKDMKAYAVE
     MLEAAGVKNI KPYDRKVFPG YSIHEMGTAR MGRDPKTSVL NAHNQVWNCP NLYVTDGAAM
     TSASNVNPSL TYMALTARAV DHAVKALNRQ EL
//