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Database: UniProt
Entry: A0A1H7IIB5_9SPHI
LinkDB: A0A1H7IIB5_9SPHI
Original site: A0A1H7IIB5_9SPHI 
ID   A0A1H7IIB5_9SPHI        Unreviewed;       557 AA.
AC   A0A1H7IIB5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:SEK62054.1};
GN   ORFNames=SAMN05421740_102246 {ECO:0000313|EMBL:SEK62054.1};
OS   Parapedobacter koreensis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Parapedobacter.
OX   NCBI_TaxID=332977 {ECO:0000313|EMBL:SEK62054.1, ECO:0000313|Proteomes:UP000198916};
RN   [1] {ECO:0000313|EMBL:SEK62054.1, ECO:0000313|Proteomes:UP000198916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Jip14 {ECO:0000313|EMBL:SEK62054.1,
RC   ECO:0000313|Proteomes:UP000198916};
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; FNZR01000002; SEK62054.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7IIB5; -.
DR   STRING; 332977.SAMN05421740_102246; -.
DR   OrthoDB; 9787779at2; -.
DR   Proteomes; UP000198916; 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;
FT   DOMAIN          8..329
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          421..544
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   557 AA;  62307 MW;  B5EBA7A72551AC27 CRC64;
     MSNTYDAIVV GSGISGGWAA RELCLKGLKT LLLERGRNVE HIKDYPTALL NPWDFKLRGN
     VPLAYKQNNP VQTNVSDDTD MLFFANDQDH PYIQKKPFMW FRGYQVGGRS LTWGRQCYRL
     SDLDFEANEK DGTAVDWPIR YRDIAPWYDY VESYIGVSGK NEGLPHLPDG NFLPPMELNC
     IEKHLAQSIK NNHEHRLLTI ARVANLTRGW DGRGPCLNRN LCSRGCPYGG YFSSNSATIP
     AAMATGNLTL RPFSIVAEVL HDEQADRATG VRVIDALTHE VTEFYANVIF INASTIGTAA
     ILLQSRTDRF PNGLGNDSGQ VGHNLMDHHS SAGAFGIHDG FEDRYYKGRR PCGFLIPRYR
     NLSATEKNGF IRGYAVQGRG ERQGWKSTSP NIKGFGSEFK EKLTKPGPWT VWMAGWGECL
     PYYDNEVQLS TTRKDKWGLP LVEVNFSFKE NEYRMMDDIK ETCAGMLEEA GFQQVNAFNY
     EKPGGATVHE MGTARMGKDP KTSVLNGYNQ MHAVKNVFIT DGSCMTSSAN QNPSLTYMAL
     TARACSFAVN QLKKGNL
//
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