ID   BETA_PHOPR              Reviewed;         568 AA.
AC   Q6LGH5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   18-JUN-2025, entry version 118.
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=PBPRB1745;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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=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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00750};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=betaine aldehyde + NAD(+) + H2O = glycine betaine + NADH + 2
CC         H(+); 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; CR378680; CAG23605.1; -; Genomic_DNA.
DR   RefSeq; WP_011221752.1; NC_006371.1.
DR   AlphaFoldDB; Q6LGH5; -.
DR   SMR; Q6LGH5; -.
DR   STRING; 298386.PBPRB1745; -.
DR   KEGG; ppr:PBPRB1745; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_002865_7_1_6; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000000593; Chromosome 2.
DR   GO; GO:0016020; C:membrane; IEA:TreeGrafter.
DR   GO; GO:0008802; F:betaine-aldehyde dehydrogenase (NAD+) 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   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; Flavoprotein; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..568
FT                   /note="Oxygen-dependent choline dehydrogenase"
FT                   /id="PRO_0000258927"
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   568 AA;  62698 MW;  F0017136A0C40B0C CRC64;
     MNTTYDYIIV GAGSAGCVLA DRLSASGEHY ILLLEAGGSD RSIFIQMPTA LSYPMNSEKY
     AWQFETQPEA GLDSRSLHCP RGRVLGGSSS INGMVYVRGH ACDYDEWVEQ GAEGWSYQEC
     LPYFRRAESW IHGEDTYRGG DGPVGTCNGN DMELNPLYQA FIDAGQQAGY PKTDDYNGYQ
     QEGFGPMHMT VDKGIRASTS NAYLRRAMKR SNLTVRKGVV TRKVLIKNKQ AIGVEIEVGG
     KVQSVYANTE VLLSAGSVGS PQLLQLSGIG PKAVLEQAGI AVKHDLPGVG ENLQDHLEVY
     FQYACHQPIT LNSKLGLISK GLIGTRWILQ KDGLGATNHF ESCAFIRSRA GLKWPNIQYH
     FLPAAMRYDG QAAFDGHGFQ VHVGPNKPQS RGRIWITSAD PHQKPNIEFN YISTEQDKQD
     WRDCIRLTRE ILAQPAMDDY RGEEIQPGAD ITSDEAMDAW VRQNVESAYH PSCTCKMGSD
     NDPMTVLNKD CQVRGIDSLR VIDSSVFPTI PNGNLNAPTI MVAEKAADAI LGNTPLSPSN
     APTWIAPQWE TEQRNGAAQR PMFHQQRK
//