ID   BETA_ACIB3              Reviewed;         552 AA.
AC   B7GYG5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 85.
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=ABBFA_002684;
OS   Acinetobacter baumannii (strain AB307-0294).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=557600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB307-0294;
RX   PubMed=18931120; DOI=10.1128/jb.00834-08;
RA   Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA   MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA   Bonomo R.A., Gill S.R.;
RT   "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT   baumannii.";
RL   J. Bacteriol. 190:8053-8064(2008).
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; CP001172; ACJ57826.1; -; Genomic_DNA.
DR   RefSeq; WP_001021934.1; NZ_CP001172.1.
DR   AlphaFoldDB; B7GYG5; -.
DR   SMR; B7GYG5; -.
DR   CAZy; AA3; Auxiliary Activities 3.
DR   GeneID; 66398119; -.
DR   HOGENOM; CLU_002865_7_1_6; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000006924; Chromosome.
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.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; NAD; Oxidoreductase.
FT   CHAIN           1..552
FT                   /note="Oxygen-dependent choline dehydrogenase"
FT                   /id="PRO_1000133315"
FT   ACT_SITE        477
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00750"
FT   BINDING         7..36
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00750"
SQ   SEQUENCE   552 AA;  61302 MW;  B1B3FF7E0172F7FD CRC64;
     MNIKEYDYII IGAGSAGNVL AARLTEDKDT TVLLLEAGGP DYRLDFRTQM PAALAYPLQG
     RRYNWAYLTD PEPHMNNRRM ECGRGKGLGG SSLINGMCYI RGNAMDLEQW ATHKGLENWT
     YADCLPYYKK AETRDIGGND YHGDSGPVSV ATPKNGNNVL FHAMVEAGVQ AGYPRTDDLN
     GYQQEGFGPM DRTVTPKGRR SSTARGYLDM AKGRPNLTIL THATTNKILF NQKQAIGVEY
     IIGADQNNLQ RALVKREVLL CAGAIASPQI LQRSGVGQST FLKSMDIDVV HDLPGVGENL
     QDHLEMYLQY KCKQPVSLYP ALKWYNQPAI GAEWLFNGTG IGASNQFEAG GFIRSSDEFK
     WPNIQYHFLP VAINYNGSNA VKEHGFQAHV GSMRSPSRGR IKLKSKDPFA HPSILFNYMS
     TEQDWREFRD AIRITREIMH QPALDPYRGD EISPGKHLQT DAELDDFVRN HAETAYHPSC
     SCKMGEDEMA VVDGQGRVHG MNGLRVVDAS IMPLIITGNL NATTIMIAEK IADQIRGREA
     LPRSTAPFYV AS
//