BETA1_CHRSD
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 03-AUG-2022, entry version 113.
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; Proteobacteria; 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;
CC Evidence={ECO:0000255|HAMAP-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 PRIDE; Q1QXE1; -.
DR EnsemblBacteria; ABE58867; ABE58867; Csal_1514.
DR KEGG; csa:Csal_1514; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_002865_7_1_6; -.
DR OMA; NHFESCA; -.
DR OrthoDB; 543793at2; -.
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; -; 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 PANTHER; PTHR11552; PTHR11552; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR01810; betA; 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
