BETA_ECOLI
ID BETA_ECOLI Reviewed; 556 AA.
AC P17444; P77861; Q2MCB2;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 176.
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=b0311, JW0303;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1956285; DOI=10.1111/j.1365-2958.1991.tb01877.x;
RA Lamark T., Kaasen E., Eshoo M.W., Falkenberg P., McDougall J., Strom A.R.;
RT "DNA sequence and analysis of the bet genes encoding the osmoregulatory
RT choline-glycine betaine pathway of Escherichia coli.";
RL Mol. Microbiol. 5:1049-1064(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1879697; DOI=10.1016/0378-1119(91)90389-s;
RA Boyd L.A., Adam L., Pelcher L.E., McHughen A., Hirji R., Selvaraj G.;
RT "Characterization of an Escherichia coli gene encoding betaine aldehyde
RT dehydrogenase (BADH): structural similarity to mammalian ALDHs and a plant
RT BADH.";
RL Gene 103:45-52(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION,
RP ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=3512525; DOI=10.1128/jb.165.3.849-855.1986;
RA Landfald B., Strom A.R.;
RT "Choline-glycine betaine pathway confers a high level of osmotic tolerance
RT in Escherichia coli.";
RL J. Bacteriol. 165:849-855(1986).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND NOMENCLATURE.
RX PubMed=3512526; DOI=10.1128/jb.165.3.856-863.1986;
RA Styrvold O.B., Falkenberg P., Landfald B., Eshoo M.W., Bjornsen T.,
RA Strom A.R.;
RT "Selection, mapping, and characterization of osmoregulatory mutants of
RT Escherichia coli blocked in the choline-glycine betaine pathway.";
RL J. Bacteriol. 165:856-863(1986).
RN [8]
RP INDUCTION.
RX PubMed=8626294; DOI=10.1128/jb.178.6.1655-1662.1996;
RA Lamark T., Rokenes T.P., McDougall J., Strom A.R.;
RT "The complex bet promoters of Escherichia coli: regulation by oxygen
RT (ArcA), choline (BetI), and osmotic stress.";
RL J. Bacteriol. 178:1655-1662(1996).
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:3512525,
CC ECO:0000269|PubMed:3512526}.
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, ECO:0000269|PubMed:3512525};
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, ECO:0000269|PubMed:3512525};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00750};
CC -!- ACTIVITY REGULATION: Activated by high osmotic strength.
CC {ECO:0000269|PubMed:3512525}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.06 mM for NAD (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:3512525};
CC KM=0.13 mM for glycine betaine aldehyde (at pH 7.5 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:3512525};
CC KM=0.5 mM for NADP (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:3512525};
CC KM=1.5 mM for choline (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:3512525};
CC KM=1.6 mM for glycine betaine aldehyde (at pH 7.5 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:3512525};
CC pH dependence:
CC Optimum pH is 7.5 for choline dehydrogenase and is between 7.5 and
CC 9.5 for glycine betaine-aldehyde dehydrogenase.
CC {ECO:0000269|PubMed:3512525};
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:3512525};
CC Peripheral membrane protein {ECO:0000269|PubMed:3512525}.
CC -!- INDUCTION: By osmotic stress. Choline is required for full expression.
CC Oxygen and choline exert their control via the transacting DNA-binding
CC proteins ArcA and BetI, respectively. {ECO:0000269|PubMed:3512525,
CC ECO:0000269|PubMed:8626294}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not grow at high
CC osmotic strength in the presence of choline, but are able to grow when
CC the medium is supplemented with glycine betaine.
CC {ECO:0000269|PubMed:3512526}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000255|HAMAP-Rule:MF_00750}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18037.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X52905; CAA37093.1; -; Genomic_DNA.
DR EMBL; M77738; AAA23504.1; -; Genomic_DNA.
DR EMBL; U73857; AAB18037.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73414.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76094.1; -; Genomic_DNA.
DR PIR; S15182; S10901.
DR RefSeq; NP_414845.1; NC_000913.3.
DR RefSeq; WP_001159094.1; NZ_STEB01000020.1.
DR AlphaFoldDB; P17444; -.
DR SMR; P17444; -.
DR BioGRID; 4262800; 6.
DR BioGRID; 850086; 1.
DR IntAct; P17444; 8.
DR STRING; 511145.b0311; -.
DR PaxDb; P17444; -.
DR PRIDE; P17444; -.
DR EnsemblBacteria; AAC73414; AAC73414; b0311.
DR EnsemblBacteria; BAE76094; BAE76094; BAE76094.
DR GeneID; 945716; -.
DR KEGG; ecj:JW0303; -.
DR KEGG; eco:b0311; -.
DR PATRIC; fig|1411691.4.peg.1966; -.
DR EchoBASE; EB0107; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_002865_7_1_6; -.
DR InParanoid; P17444; -.
DR OMA; NHFESCA; -.
DR PhylomeDB; P17444; -.
DR BioCyc; EcoCyc:CHD-MON; -.
DR BioCyc; MetaCyc:CHD-MON; -.
DR UniPathway; UPA00529; UER00385.
DR PRO; PR:P17444; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008812; F:choline dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IMP:EcoCyc.
DR GO; GO:0006970; P:response to osmotic stress; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Cell membrane; FAD; Flavoprotein; Membrane; NAD; Oxidoreductase;
KW Reference proteome; Stress response.
FT CHAIN 1..556
FT /note="Oxygen-dependent choline dehydrogenase"
FT /id="PRO_0000205586"
FT ACT_SITE 473
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00750"
FT BINDING 4..33
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00750"
SQ SEQUENCE 556 AA; 61878 MW; E182480168C8E9FD CRC64;
MQFDYIIIGA GSAGNVLATR LTEDPNTSVL LLEAGGPDYR FDFRTQMPAA LAFPLQGKRY
NWAYETEPEP FMNNRRMECG RGKGLGGSSL INGMCYIRGN ALDLDNWAQE PGLENWSYLD
CLPYYRKAET RDMGENDYHG GDGPVSVTTS KPGVNPLFEA MIEAGVQAGY PRTDDLNGYQ
QEGFGPMDRT VTPQGRRAST ARGYLDQAKS RPNLTIRTHA MTDHIIFDGK RAVGVEWLEG
DSTIPTRATA NKEVLLCAGA IASPQILQRS GVGNAELLAE FDIPLVHELP GVGENLQDHL
EMYLQYECKE PVSLYPALQW WNQPKIGAEW LFGGTGVGAS NHFEAGGFIR SREEFAWPNI
QYHFLPVAIN YNGSNAVKEH GFQCHVGSMR SPSRGHVRIK SRDPHQHPAI LFNYMSHEQD
WQEFRDAIRI TREIMHQPAL DQYRGREISP GVECQTDEQL DEFVRNHAET AFHPCGTCKM
GYDEMSVVDG EGRVHGLEGL RVVDASIMPQ IITGNLNATT IMIGEKIADM IRGQEALPRS
TAGYFVANGM PVRAKK
