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Database: UniProt
Entry: A0A1I1SZF0_9BACT
LinkDB: A0A1I1SZF0_9BACT
Original site: A0A1I1SZF0_9BACT 
ID   A0A1I1SZF0_9BACT        Unreviewed;       565 AA.
AC   A0A1I1SZF0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:SFD51701.1};
GN   ORFNames=SAMN05518672_102264 {ECO:0000313|EMBL:SFD51701.1};
OS   Chitinophaga sp. CF118.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=1884367 {ECO:0000313|EMBL:SFD51701.1, ECO:0000313|Proteomes:UP000199596};
RN   [1] {ECO:0000313|EMBL:SFD51701.1, ECO:0000313|Proteomes:UP000199596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF118 {ECO:0000313|EMBL:SFD51701.1,
RC   ECO:0000313|Proteomes:UP000199596};
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; FOMK01000002; SFD51701.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1SZF0; -.
DR   STRING; 1884367.SAMN05518672_102264; -.
DR   OrthoDB; 9787779at2; -.
DR   Proteomes; UP000199596; 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; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL 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          106..338
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          429..552
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   565 AA;  63462 MW;  621445E595AD3151 CRC64;
     MNLNMKAQEQ NTYDVIVIGS GVSGGWAAKE FTEKGLKVLM LDRGKPLEHV KDYDTATKDP
     WEFKHAGRIT TEQRETHPKL SRDYPYSEHN EKYWINDSTS PYNEVKRFDW YRPDIVGGKS
     IMWGRQSYRW SDIDFEANLK DGIAVDWPIR YKDLAPWYDY VEKFAGISGT AEGLPQLPDG
     QFMPAMEMNC VEKDVKKRIE SQFKGRIMTM GRVANITQPL PGRTNCQYRN LCSRGCPFGA
     YFSTQSSTLP AAVATGNLTL RPDSIVNSII YDEQKGKATG VRVIDKHTKQ MTEFYAKIVF
     VNGSTLGTTF VLMNSISHRF PNGLGNDSGV LGKYLMDHHF RNGASGKAEG FDDKYFFGRR
     ANGIYIPRYR NIGSDKRDYL RGFGYQGGAS RGSWARGIAE MGVGKDFKDM LTEPGDWSMG
     LGGFGECLPY EDNKVTLDTS VKDDWGQPVL KFDAEFKENE KKMRVDMMND AAEMLEAAGL
     KDVKTYDAGS YPGMAIHEMG TARMGRDPKT SMLNSWNQLH AVKNVFVTDG ASMTSAACVN
     PSLTYMAMTA RAVDYAVKEM KKGNI
//
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