ID   A3D280_SHEB5            Unreviewed;       561 AA.
AC   A3D280;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   28-JAN-2026, entry version 113.
DE   RecName: Full=Choline dehydrogenase {ECO:0000256|NCBIfam:TIGR01810, ECO:0000256|RuleBase:RU003969};
DE            EC=1.1.99.1 {ECO:0000256|NCBIfam:TIGR01810, ECO:0000256|RuleBase:RU003969};
GN   OrderedLocusNames=Sbal_1325 {ECO:0000313|EMBL:ABN60843.1};
OS   Shewanella baltica (strain OS155 / ATCC BAA-1091).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Shewanellaceae; Shewanella.
OX   NCBI_TaxID=325240 {ECO:0000313|EMBL:ABN60843.1, ECO:0000313|Proteomes:UP000001557};
RN   [1] {ECO:0000313|EMBL:ABN60843.1, ECO:0000313|Proteomes:UP000001557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS155 / ATCC BAA-1091 {ECO:0000313|Proteomes:UP000001557};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I.,
RA   Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS155.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=choline + A = betaine aldehyde + AH2; Xref=Rhea:RHEA:17433,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15354, ChEBI:CHEBI:15710,
CC         ChEBI:CHEBI:17499; EC=1.1.99.1;
CC         Evidence={ECO:0000256|RuleBase:RU003969};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC       choline pathway; betaine aldehyde from choline (cytochrome c reductase
CC       route): step 1/1. {ECO:0000256|RuleBase:RU003969}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; CP000563; ABN60843.1; -; Genomic_DNA.
DR   RefSeq; WP_011846257.1; NC_009052.1.
DR   AlphaFoldDB; A3D280; -.
DR   STRING; 325240.Sbal_1325; -.
DR   KEGG; sbl:Sbal_1325; -.
DR   HOGENOM; CLU_002865_7_1_6; -.
DR   OrthoDB; 9785276at2; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000001557; Chromosome.
DR   GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniRule.
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; IPR011533; BetA.
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   NCBIfam; TIGR01810; betA; 1.
DR   NCBIfam; NF002550; PRK02106.1; 1.
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:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001557}.
FT   DOMAIN          87..110
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          260..274
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         89
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         97..100
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         225
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   561 AA;  61680 MW;  09997D6B6E1F5636 CRC64;
     MAHSLQQKYY NYIIVGAGSA GCVLANRLSK DPKNEVLLLE TGGSDKSIFI QMPTALSIPM
     NSPKYAWQFE TQPEPHLDNR KMHCPRGKVL GGSSSINGMV YVRGHARDFD EWQAQGATNW
     DYSHCLPYFK KAETWAFGGD EYRGESGPLG VNNGNQMQNP LYQAFVDAGI AAGYLSTADY
     NAAQQEGFGP MHMTVKKGVR WSTANAYLRP AMARRNLTVL THTLVHKVLL EGQAAVGVRI
     EHKGKVEDIR CNKEVILAAG SIGSPHLLQL SGIGDPQVLA DAGVELQHEL PGVGQNLQDH
     LEFYFQFKCL KPISLNGKLD PFSKFLIGAR WILDKSGLGA TNHFESCGFI RSKAGLEWPD
     LQYHFLPAAM RYDGKEAFAG HGFQVHVGHN KPKSRGAVTL VSADPKAPPK IQFNYLQHPD
     DIEGFRACVR LTREIINQAP FDEYRGEEIQ PGTQVQTDEQ IDAFVRQSVE SAYHPSCSCK
     MGTDAMAVVD PETRVHGLQN LRVVDSSIFP TIPNGNLNAP TIMLAERAAD MILEAEMLAP
     ADSAVVVADA WQTTQRSTAT S
//