ID   BETA_PSESM              Reviewed;         568 AA.
AC   Q88AE7;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 123.
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=PSPTO_0443;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016853; AAO53987.1; -; Genomic_DNA.
DR   RefSeq; NP_790292.1; NC_004578.1.
DR   RefSeq; WP_005763658.1; NC_004578.1.
DR   AlphaFoldDB; Q88AE7; -.
DR   SMR; Q88AE7; -.
DR   STRING; 223283.PSPTO_0443; -.
DR   GeneID; 1182052; -.
DR   KEGG; pst:PSPTO_0443; -.
DR   PATRIC; fig|223283.9.peg.462; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_002865_7_1_6; -.
DR   OrthoDB; 9785276at2; -.
DR   PhylomeDB; Q88AE7; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000002515; Chromosome.
DR   GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008812; F:choline dehydrogenase activity; ISS:JCVI.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0006113; P:fermentation; ISS:JCVI.
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; Reference proteome.
FT   CHAIN           1..568
FT                   /note="Oxygen-dependent choline dehydrogenase"
FT                   /id="PRO_0000205592"
FT   ACT_SITE        477
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00750"
FT   BINDING         8..37
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00750"
SQ   SEQUENCE   568 AA;  62788 MW;  147045C3DDCC9005 CRC64;
     MTTQSEYDYI IIGAGSAGNT LAARLTEDAG VTVLLLEAGG PDYRLDFRTQ MPAALAFPLQ
     GRRYNWAYET EPEPHMDNRR MECGRGKGLG GSSLINGMCY IRGNAMDYDG WAKEPGLEDW
     SYLDCLPYFR KAETRDIGPN DYHGGEGPVS VTTPKAGNNP LFHAMVEAGV QAGFPRTDDL
     NGYQQEGFGP MDRTVTPKGR RASTARGYLD EAKKRDTLSI VTHALTDRIL FEGKRAVGVA
     YLVGDSDTRI EVRARKEVLL CGGAIASPQI LQRSGVGPAE VLNKLDIPVV HDLPGVGQNL
     QDHLEMYLQY ACTQPVSLYP SLKWWNQPAI GAEWMFLGTG IGASNQFEAG GFIRSSEAFE
     WPNIQYHFLP VAINYNGTKG VQEHGFQAHV GSMRSPSRGR VHVKSKDPRE YPSILFNYMA
     SDQDWQEFRD GIRLTREIMQ QPALDPYRGR EISPGIDVQS DEALDQFVRE HAETAYHPSC
     SCKMGTDEMA VVDGQGRVHG MQNLRVVDAS IMPIITTGNL NAPTIMIAEK IADKIRGRQP
     LPRSTADYFV AGDKPARGKP LREISHQA
//