ID   BETA1_CHRSD             Reviewed;         560 AA.
AC   Q1QXE1;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=Oxygen-dependent choline dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_00750};
DE            Short=CDH 1 {ECO:0000255|HAMAP-Rule:MF_00750};
DE            Short=CHD 1 {ECO:0000255|HAMAP-Rule:MF_00750};
DE            EC=1.1.99.1 {ECO:0000255|HAMAP-Rule:MF_00750};
DE   AltName: Full=Betaine aldehyde dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_00750};
DE            Short=BADH 1 {ECO:0000255|HAMAP-Rule:MF_00750};
DE            EC=1.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00750};
GN   Name=betA1 {ECO:0000255|HAMAP-Rule:MF_00750}; Synonyms=betA;
GN   OrderedLocusNames=Csal_1514;
OS   Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS   NCIMB 13768 / 1H11).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX   PubMed=22675587; DOI=10.4056/sigs.2285059;
RA   Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA   Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA   Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA   Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA   Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT   "Complete genome sequence of the halophilic and highly halotolerant
RT   Chromohalobacter salexigens type strain (1H11(T)).";
RL   Stand. Genomic Sci. 5:379-388(2011).
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; CP000285; ABE58867.1; -; Genomic_DNA.
DR   RefSeq; WP_011506813.1; NC_007963.1.
DR   AlphaFoldDB; Q1QXE1; -.
DR   SMR; Q1QXE1; -.
DR   STRING; 290398.Csal_1514; -.
DR   KEGG; csa:Csal_1514; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_002865_7_1_6; -.
DR   OrthoDB; 9785276at2; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000000239; 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; Reference proteome.
FT   CHAIN           1..560
FT                   /note="Oxygen-dependent choline dehydrogenase 1"
FT                   /id="PRO_0000245316"
FT   ACT_SITE        475
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   560 AA;  62246 MW;  8C6D127276CBC454 CRC64;
     MTQAREYDYI IIGAGSAGNV LATRLTEDPD VQVLLLEAGG PDYRFDFRTQ MPAALAYPLQ
     GKRYNWAFET DPEPYMNNRR MECGRGKGLG GSSLINGMCY LRGNALDYDN WAKIPGLEDW
     NYLQCLPYFK RAETRDIGPN DYHGGDGPVS VATPKEGNNE LYGAFIRAGI EAGYPATEDV
     NGYQQEGFGP MDRTTTPNGR RASTARGYLD IAKQRPNLTI ETHATTDVIE FEGKRAVGVS
     YERKGQAQRV RARREVLLCA GAIASPQILQ RSGVGNPEHL EEFDIPVVHE LPGVGENLQD
     HLEMYIQYEC KKPISLYPAL KWYNQPKIGA EWLFFGKGIG ASNQFEAAGF IRTNDQEEWP
     NLQYHFLPIA ISYNGKSAVQ AHGFQAHVGS MRSMSRGRIR LTSRDPKAAP SILFNYMSHD
     KDWQEFRDAI RITREIIEQP TMDEYRGREI SPGPNVQSDA ELDEFVRQHA ETAYHPAGSC
     KMGSADDAMA VVDGAGRVHG LEGLRVIDAS IMPVIATGNL NAPTIMIAEK MADKVRGRDP
     LPPAKVDYYV ANGAPARRRA
//