ID   BETA_VIBVY              Reviewed;         560 AA.
AC   Q7MF12;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Oxygen-dependent choline dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00750};
DE            Short=CDH {ECO:0000255|HAMAP-Rule:MF_00750};
DE            Short=CHD {ECO:0000255|HAMAP-Rule:MF_00750};
DE            EC=1.1.99.1 {ECO:0000255|HAMAP-Rule:MF_00750};
DE   AltName: Full=Betaine aldehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00750};
DE            Short=BADH {ECO:0000255|HAMAP-Rule:MF_00750};
DE            EC=1.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00750};
GN   Name=betA {ECO:0000255|HAMAP-Rule:MF_00750};
GN   OrderedLocusNames=VVA0508;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
CC   -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine
CC       betaine. Catalyzes the oxidation of choline to betaine aldehyde and
CC       betaine aldehyde to glycine betaine at the same rate.
CC       {ECO:0000255|HAMAP-Rule:MF_00750}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + choline = AH2 + betaine aldehyde; Xref=Rhea:RHEA:17433,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15354, ChEBI:CHEBI:15710,
CC         ChEBI:CHEBI:17499; EC=1.1.99.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00750};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.8; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00750};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00750};
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:0000255|HAMAP-Rule:MF_00750}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00750}.
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DR   EMBL; BA000038; BAC96534.1; -; Genomic_DNA.
DR   RefSeq; WP_011151879.1; NC_005140.1.
DR   AlphaFoldDB; Q7MF12; -.
DR   SMR; Q7MF12; -.
DR   STRING; 672.VV93_v1c35150; -.
DR   KEGG; vvy:VVA0508; -.
DR   PATRIC; fig|196600.6.peg.3708; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_002865_7_1_6; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000002675; Chromosome II.
DR   GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
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   HAMAP; MF_00750; Choline_dehydrogen; 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   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.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; NAD; Oxidoreductase.
FT   CHAIN           1..560
FT                   /note="Oxygen-dependent choline dehydrogenase"
FT                   /id="PRO_0000205607"
FT   ACT_SITE        470
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00750"
FT   BINDING         6..35
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00750"
SQ   SEQUENCE   560 AA;  62359 MW;  9CCA2CBA8EEA613B CRC64;
     MQQHYDYIIV GAGSAGCVLA DRLSESGDHS VLLLEAGGSD KSIFIQMPTA LSYPMNSEKY
     AWQFETDAEA DLDGRRLHCP RGKVLGGSSS INGMVYVRGH ACDFDEWEEQ GAKGWNYQAC
     LPYFRRAENW IDGEDEYRGG DGPLSTCAGN KMTLNPLYRA FIDAGKEAGY PETSDYNGYQ
     QEGFGPMHMT VKNGVRASTS NAYLSRAKKR SNFKLIKGVV VQRILLEEKR AVGVEFELAG
     ELRTCFAKNE VISSAGSIGS VQLLQLSGIG PKTVLEKAGV TPVYHLPGVG QNLQDHLEVY
     FQYHCQKPIT LNGKLDWFSK GLIGTEWILT RKGLGATNHF ESCAFIRSRA GLKWPNIQYH
     FLPAAMRYDG QAAFDGHGFQ VHVGPNKPES RGRVEIVSAN PLDKPKIQFN YLSTERDRQD
     WRDCIRLTRE ILAQPAMDEF RGEEIQPGIN VATDAEIDQW VKENVESAYH PSCSCKMGAD
     DDPMAVLDEE CRVRGITNLR VVDSSVFPTI PNGNLNAPTI MVAERAADLI LHKQPLPPQR
     SKVWLAPSWE TQQRTGEPMR
//