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Database: UniProt
Entry: A0A1I0PKJ4_9FIRM
LinkDB: A0A1I0PKJ4_9FIRM
Original site: A0A1I0PKJ4_9FIRM 
ID   A0A1I0PKJ4_9FIRM        Unreviewed;       585 AA.
AC   A0A1I0PKJ4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:SEW14957.1};
GN   ORFNames=SAMN05421659_105159 {ECO:0000313|EMBL:SEW14957.1};
OS   [Clostridium] fimetarium.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=99656 {ECO:0000313|EMBL:SEW14957.1, ECO:0000313|Proteomes:UP000199701};
RN   [1] {ECO:0000313|EMBL:SEW14957.1, ECO:0000313|Proteomes:UP000199701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9179 {ECO:0000313|EMBL:SEW14957.1,
RC   ECO:0000313|Proteomes:UP000199701};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; FOJI01000005; SEW14957.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0PKJ4; -.
DR   STRING; 99656.SAMN05421659_105159; -.
DR   OrthoDB; 9787779at2; -.
DR   Proteomes; UP000199701; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD 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; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000199701}.
FT   DOMAIN          4..35
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   DOMAIN          230..348
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          460..572
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   585 AA;  64978 MW;  B359A9F1E596E3AF CRC64;
     MNNDADVIII GAGGGGAVVA KELAEKGIKV LLIEAGPWYG NKKWPNPNSE PGAVSGSSYD
     DLSIDILKKS FTDLEDDMND SMSGKFRWGP ANRELSPWPR SIAGRGFTWQ NSGVGGSTLH
     YFGNCPRAYP QAVDNIWPIP YEELIPYYEK VETTLPVWPA PATAKEDLFY YGAKKAGWKR
     LETPNVTSPG YRPQPNAILR PNPRLNDPDF DLENNKSVGC TLRGHCVNGC NMGPTIEGVA
     KRSTFVSYVP RALRSGNIEV RPNTFVTKIL TKDDEQEGDS QQNALKEINN REGLHAIGVL
     YRDTWTGETG ELRAKVVVMA AGGIETPRLW LNSQLPENEW VGKGLVNHWF DCVAGIFDEK
     QLIDILGVSD IKPYVGQNAA ARFDYPGLGV VEIFGLSPGL YSSMIYGTSD KGYNFLNKSK
     EKEPWDIEGL VVGEQLKEFM IDYPRTLSIL IFTDDEINQK NGVTLDHELK DENGFIPVIR
     CEPSDKDKEK RDKLASIASE ILRKAGAKTI IRSNWPPNIY IHIQSTMRMG YVTDTNCEAK
     QVKRLYIADN SVLYNGLGGP NPTLTTQALA TRTAEKIIEK YFGPR
//
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