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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//