BETB_ECOLI
ID BETB_ECOLI Reviewed; 490 AA.
AC P17445; Q2MCB1;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Betaine aldehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00804};
DE Short=BADH {ECO:0000255|HAMAP-Rule:MF_00804};
DE EC=1.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00804};
GN Name=betB {ECO:0000255|HAMAP-Rule:MF_00804};
GN OrderedLocusNames=b0312, JW0304;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-29.
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, AND INDUCTION.
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, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=2194570; DOI=10.1016/0304-4165(90)90046-y;
RA Falkenberg P., Strom A.R.;
RT "Purification and characterization of osmoregulatory betaine aldehyde
RT dehydrogenase of Escherichia coli.";
RL Biochim. Biophys. Acta 1034:253-259(1990).
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 irreversible oxidation of betaine aldehyde to
CC the corresponding acid. It is highly specific for betaine and has a
CC significantly higher affinity for NAD than for NADP.
CC {ECO:0000255|HAMAP-Rule:MF_00804, ECO:0000269|PubMed:2194570,
CC 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_00804, ECO:0000269|PubMed:2194570,
CC ECO:0000269|PubMed:3512525};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306;
CC Evidence={ECO:0000269|PubMed:2194570};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=betaine aldehyde + H2O + NADP(+) = glycine betaine + 2 H(+) +
CC NADPH; Xref=Rhea:RHEA:30067, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:2194570,
CC ECO:0000269|PubMed:3512525};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30068;
CC Evidence={ECO:0000305|PubMed:2194570};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00804};
CC Note=Binds 2 potassium ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00804};
CC -!- ACTIVITY REGULATION: Aldehydes with apolar groups are the most
CC effective inhibitors. N-Methylated compounds are also inhibitory, but
CC to a much lesser degree than the aldehydes. The alcohols are more
CC inhibitory than the corresponding acids, and the inhibitory effect
CC increases with the degree of methylation from ethanolamine to choline.
CC {ECO:0000269|PubMed:2194570}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=99 uM for NAD (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:2194570};
CC KM=160 uM for betaine aldehyde (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:2194570};
CC KM=400 uM for NADP (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:2194570};
CC KM=60 uM for NAD (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:3512525};
CC KM=130 uM for betaine aldehyde (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:3512525};
CC KM=500 uM for NADP (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:3512525};
CC Vmax=66 umol/min/mg enzyme for the NAD-dependent oxidation of betaine
CC aldehyde (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:2194570};
CC Vmax=30 umol/min/mg enzyme for the NADP-dependent oxidation of
CC betaine aldehyde (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:2194570};
CC pH dependence:
CC Optimum pH is between 7.5 and 9.5. {ECO:0000269|PubMed:2194570,
CC ECO:0000269|PubMed:3512525};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine from betaine aldehyde: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00804}.
CC -!- SUBUNIT: Dimer of dimers. {ECO:0000305|PubMed:2194570}.
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 -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00804}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23505.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB18038.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X52905; CAA37092.1; -; Genomic_DNA.
DR EMBL; M77739; AAA23506.1; -; Genomic_DNA.
DR EMBL; M77739; AAA23505.1; ALT_INIT; Genomic_DNA.
DR EMBL; U73857; AAB18038.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73415.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76095.1; -; Genomic_DNA.
DR PIR; S15181; S15181.
DR RefSeq; NP_414846.1; NC_000913.3.
DR RefSeq; WP_000089110.1; NZ_SSZK01000067.1.
DR AlphaFoldDB; P17445; -.
DR SMR; P17445; -.
DR BioGRID; 4262801; 8.
DR DIP; DIP-9208N; -.
DR IntAct; P17445; 7.
DR STRING; 511145.b0312; -.
DR jPOST; P17445; -.
DR PaxDb; P17445; -.
DR PRIDE; P17445; -.
DR EnsemblBacteria; AAC73415; AAC73415; b0312.
DR EnsemblBacteria; BAE76095; BAE76095; BAE76095.
DR GeneID; 947376; -.
DR KEGG; ecj:JW0304; -.
DR KEGG; eco:b0312; -.
DR PATRIC; fig|1411691.4.peg.1965; -.
DR EchoBASE; EB0108; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_0_6; -.
DR InParanoid; P17445; -.
DR OMA; GMKYVTM; -.
DR PhylomeDB; P17445; -.
DR BioCyc; EcoCyc:BADH-MON; -.
DR BioCyc; MetaCyc:BADH-MON; -.
DR UniPathway; UPA00529; UER00386.
DR PRO; PR:P17445; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IDA:EcoCyc.
DR GO; GO:0006970; P:response to osmotic stress; IEP:EcoCyc.
DR GO; GO:0010165; P:response to X-ray; IMP:EcoCyc.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR HAMAP; MF_00804; BADH; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR011264; BADH.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01804; BADH; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Metal-binding; NAD; NADP; Oxidation;
KW Oxidoreductase; Potassium; Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1956285"
FT CHAIN 2..490
FT /note="Betaine aldehyde dehydrogenase"
FT /id="PRO_0000056541"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT ACT_SITE 252
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT ACT_SITE 286
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT ACT_SITE 464
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 26
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 27
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 93
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 150..152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 176..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 180
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 230..233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 246
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 254
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 286
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 387
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 457
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 460
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT SITE 248
FT /note="Seems to be a necessary countercharge to the
FT potassium cations"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT MOD_RES 286
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT CONFLICT 232
FT /note="A -> R (in Ref. 2; AAA23506/AAA23505)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="R -> P (in Ref. 2; AAA23506/AAA23505)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 52911 MW; 747F822DA1233808 CRC64;
MSRMAEQQLY IHGGYTSATS GRTFETINPA NGNVLATVQA AGREDVDRAV KSAQQGQKIW
ASMTAMERSR ILRRAVDILR ERNDELAKLE TLDTGKAYSE TSTVDIVTGA DVLEYYAGLI
PALEGSQIPL RETSFVYTRR EPLGVVAGIG AWNYPIQIAL WKSAPALAAG NAMIFKPSEV
TPLTALKLAE IYSEAGLPDG VFNVLPGVGA ETGQYLTEHP GIAKVSFTGG VASGKKVMAN
SAASSLKEVT MELGGKSPLI VFDDADLDLA ADIAMMANFF SSGQVCTNGT RVFVPAKCKA
AFEQKILARV ERIRAGDVFD PQTNFGPLVS FPHRDNVLRY IAKGKEEGAR VLCGGDVLKG
DGFDNGAWVA PTVFTDCSDD MTIVREEIFG PVMSILTYES EDEVIRRAND TDYGLAAGIV
TADLNRAHRV IHQLEAGICW INTWGESPAE MPVGGYKHSG IGRENGVMTL QSYTQVKSIQ
VEMAKFQSIF
