ID   A8FSA7_SHESH            Unreviewed;       564 AA.
AC   A8FSA7;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   18-JUN-2025, entry version 111.
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=Ssed_1119 {ECO:0000313|EMBL:ABV35730.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV35730.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV35730.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV35730.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-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; CP000821; ABV35730.1; -; Genomic_DNA.
DR   RefSeq; WP_012141466.1; NC_009831.1.
DR   AlphaFoldDB; A8FSA7; -.
DR   STRING; 425104.Ssed_1119; -.
DR   KEGG; sse:Ssed_1119; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_002865_7_1_6; -.
DR   OrthoDB; 9785276at2; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:TreeGrafter.
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   ECO:0000313|EMBL:ABV35730.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002015}.
FT   DOMAIN          86..109
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          259..273
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         88
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         96..99
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         224
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   564 AA;  62246 MW;  7EDB4A827CC1C12D CRC64;
     MTQSTTEKYD YIIVGAGSAG CVLANRLSAD ANNSVLLIET GGSDRSIFIQ MPTALSIPMN
     TPKYAWQFET EAEPHLDNRR MHCPRGKVLG GSSSINGMVY VRGHARDFDE WQQEGAKDWD
     YAHCLPYFKK AESWAFGEDD YRGVDGPLAV NNGNEMKNPL YQAFVDAGVD AGYMATSDYN
     GAQQEGFGPM HMTIKNGVRW STSNAYLRPA MKRENLTVIT HAQVHKVLFE GKQTVGVRFE
     RKGKMTDVHC SKEVVLSAGS IGSPHILQLS GIGAAETLAK AGIEQVHELP GVGENLQDHL
     EFYFQFKCLK PISLNGKIDP LNKLFIGTRW ILNRTGLGAT NHFESCGFIR SKAGLEWPDL
     QYHFLPAAMR YDGKEAFAGH GFQVHIGHNK PKSRGAVKVV SSDARVAPSI QFNYLSHKDD
     IEGFRACVRL TREIINQPAL DEYRGEEIQP GTSVQTDEEI DTFVRSSVES AYHPSCSCKM
     GEDAMAVVDS ETKVHGIQGL RVVDSSIFPT IPNGNLNSPT IMVAERAADI ILGMTPLPAS
     SATVTFAQQW QQKQRLRAPK RQLA
//