BETA2_CHRSD
ID BETA2_CHRSD Reviewed; 558 AA.
AC Q9L4K0;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 81.
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};
GN Name=betA {ECO:0000255|HAMAP-Rule:MF_00750};
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=10708384; DOI=10.1099/00221287-146-2-455;
RA Canovas D., Vargas C., Kneip S., Moron M.J., Ventosa A., Bremer E.,
RA Nieto J.J.;
RT "Genes for the synthesis of the osmoprotectant glycine betaine from choline
RT in the moderately halophilic bacterium Halomonas elongata DSM 3043.";
RL Microbiology 146:455-463(2000).
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, ECO:0000269|PubMed:10708384}.
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; Evidence={ECO:0000255|HAMAP-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; AJ238780; CAB77176.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9L4K0; -.
DR SMR; Q9L4K0; -.
DR UniPathway; UPA00529; UER00385.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:RHEA.
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.
FT CHAIN 1..558
FT /note="Oxygen-dependent choline dehydrogenase"
FT /id="PRO_0000205589"
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 558 AA; 62083 MW; DE85CD0E7FEF2F14 CRC64;
MSQATEFDYI IIGAGSAGNV LATRLTEDSD VSVLLLEAGG PDYRFDFRTQ MPAALAYPLQ
GKRYNWAFET DPEPHMDNRR MECGRGKGLG GSSLINGMCY IRGNALDYDH WAKQPGLEEW
DYLSCLPYFK KSETRDIGPN DYHGGDGPVS VTTPKAGNNP LYRTFIEAGK QAGYPETEDV
NGYQQEGFGP MDRFVTPKGR RASTARGYLD TAKQRSNLTI ETRAVTDVIE FEGKRAVGVR
YEQKGQPKQA RARREVLLCG GAIASPQILQ RSGVGNPEWL KELGIPVVHE LPGVGENLQD
HLEMYIQYEC KEPISLYPAL KWYNQPKIGA EWLFKGTGVG ASNQFESCGF IRSRDDEEWP
NLQYHFLPIA ISYNGKSAVQ AHGFQAHVGS MRSESRGRIR LTSKDPHAAP SILFNYMAKE
KDWEEFRDAI RLTREIIAQP AFDRYRGREI SPGPDVQSDE ELDNFVKQHA ETAYHPCGSC
RMGEGDMAVT DAQGRVHGLE GLRVVDASLF PVIPTGNLNA PTIMLAEKIA DRIRGREPLP
RASVDYYVAN GAPAKQAS