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Database: UniProt
Entry: F6EUL0_SPHCR
LinkDB: F6EUL0_SPHCR
Original site: F6EUL0_SPHCR 
ID   F6EUL0_SPHCR            Unreviewed;       547 AA.
AC   F6EUL0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:AEG48728.1};
DE            EC=1.1.99.1 {ECO:0000313|EMBL:AEG48728.1};
GN   ORFNames=Sphch_1037 {ECO:0000313|EMBL:AEG48728.1};
OS   Sphingobium chlorophenolicum L-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=690566 {ECO:0000313|EMBL:AEG48728.1, ECO:0000313|Proteomes:UP000007150};
RN   [1] {ECO:0000313|EMBL:AEG48728.1, ECO:0000313|Proteomes:UP000007150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-1 {ECO:0000313|EMBL:AEG48728.1,
RC   ECO:0000313|Proteomes:UP000007150};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Daligault H., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Pagani I., Turner P., Copley S., Woyke T.;
RT   "Complete sequence of chromosome 1 of Sphingobium chlorophenolicum L-1.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; CP002798; AEG48728.1; -; Genomic_DNA.
DR   RefSeq; WP_013846991.1; NC_015593.1.
DR   AlphaFoldDB; F6EUL0; -.
DR   STRING; 690566.Sphch_1037; -.
DR   KEGG; sch:Sphch_1037; -.
DR   HOGENOM; CLU_002865_7_2_5; -.
DR   Proteomes; UP000007150; Chromosome 1.
DR   GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Oxidoreductase {ECO:0000313|EMBL:AEG48728.1}.
FT   DOMAIN          89..112
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          261..275
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         91
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         226
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   547 AA;  59494 MW;  BEC3FB779870FF6E CRC64;
     MDMAHNDVGN SYDYVVIGAG SSGCVVANRL SEDGTHSVLL IEAGGPDNLF WMRAPLGTGQ
     MLRRTDVIWP YETEGVPALN GRKLRWPRGK VVGGSSSVNG TIFIRGLREE YDRWREMGNI
     GWGYDDVLPF FKKFENFKDG DPRYRGKGGP ISVERLRLNL PVTSAFLDAC AQAGIPGNAD
     YNGASIEGAS PLQFNTRYGR RQSAAVGYLS SAAKRKNLHV LANTRVKKID VVDGAASGVV
     LQNAAGERTV RANREIIISA GAIGSPQLLE LSGIGNAFIL KNAGLSVVHH LPGVGENLID
     HLQTRISLKA QNTAGLNELV RNYLFRMKVG AEWLFLGRGL MSTPLASAHA IVRSRPDAPM
     PDLKLQLHHF SGQDRMAYSK DLGIDPHPGL TIGIVQLSPR SRGHLHISSP DANVAPLIYP
     NQFEDEEDVR VLTAGIRMAR TIAAQDALSK FVVTELRPGE AASSNDEIKE YIRQSGQTSY
     HPIGTCKMGR DDWAVVDDQL RVRGIDRLRV VDASIMPTMP SSNTNAAALM IGEKGAELIR
     QAAAQKF
//
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