Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NAD/NADP-dependent betaine aldehyde dehydrogenase

Gene

betB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the reversible oxidation of betaine aldehyde to the corresponding acid. It is highly specific for betaine and has a significantly higher affinity for NAD than for NADP.UniRule annotation2 Publications

Catalytic activityi

Betaine aldehyde + NAD+ + H2O = betaine + NADH.UniRule annotation2 Publications

Cofactori

K(+)UniRule annotationNote: Binds 2 potassium ions per subunit.UniRule annotation

Enzyme regulationi

Aldehydes with apolar groups are the most effective inhibitors. N-Methylated compounds are also inhibitory, but to a much lesser degree than the aldehydes. The alcohols are more inhibitory than the corresponding acids, and the inhibitory effect increases with the degree of methylation from ethanolamine to choline.1 Publication

Kineticsi

  1. KM=99 µM for NAD (at pH 7.5 and 25 degrees Celsius)2 Publications
  2. KM=160 µM for betaine aldehyde (at pH 7.5 and 25 degrees Celsius)2 Publications
  3. KM=400 µM for NADP (at pH 7.5 and 25 degrees Celsius)2 Publications

Vmax=66 µmol/min/mg enzyme (at pH 7.5 and 25 degrees Celsius)2 Publications

pH dependencei

Optimum pH is between 7.5 and 9.5.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi26 – 261Potassium 1UniRule annotation
Metal bindingi27 – 271Potassium 1; via carbonyl oxygenUniRule annotation
Metal bindingi93 – 931Potassium 1UniRule annotation
Active sitei162 – 1621Charge relay systemUniRule annotation
Metal bindingi180 – 1801Potassium 1; via carbonyl oxygenUniRule annotation
Binding sitei209 – 2091NAD/NADP; via amide nitrogenUniRule annotation
Metal bindingi246 – 2461Potassium 2; via carbonyl oxygenUniRule annotation
Sitei248 – 2481Seems to be a necessary countercharge to the potassium cationsUniRule annotation
Active sitei252 – 2521Proton acceptorUniRule annotation
Binding sitei286 – 2861NAD/NADPUniRule annotation
Binding sitei387 – 3871NAD/NADPUniRule annotation
Metal bindingi457 – 4571Potassium 2; via carbonyl oxygenUniRule annotation
Metal bindingi460 – 4601Potassium 2; via carbonyl oxygenUniRule annotation
Active sitei464 – 4641Charge relay systemUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi150 – 1534NAD/NADPUniRule annotation
Nucleotide bindingi176 – 1794NAD/NADPUniRule annotation
Nucleotide bindingi229 – 2346NAD/NADPUniRule annotation

GO - Molecular functioni

  1. betaine-aldehyde dehydrogenase activity Source: EcoCyc
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. glycine betaine biosynthetic process from choline Source: EcoCyc
  2. response to osmotic stress Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Stress response

Keywords - Ligandi

Metal-binding, NAD, NADP, Potassium

Enzyme and pathway databases

BioCyciEcoCyc:BADH-MONOMER.
ECOL316407:JW0304-MONOMER.
MetaCyc:BADH-MONOMER.
UniPathwayiUPA00529; UER00386.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD/NADP-dependent betaine aldehyde dehydrogenaseUniRule annotation (EC:1.2.1.8UniRule annotation)
Short name:
BADHUniRule annotation
Gene namesi
Name:betBUniRule annotation
Ordered Locus Names:b0312, JW0304
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10110. betB.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 490489NAD/NADP-dependent betaine aldehyde dehydrogenasePRO_0000056541Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei286 – 2861Cysteine sulfenic acid (-SOH)UniRule annotation

Keywords - PTMi

Oxidation

Proteomic databases

PaxDbiP17445.
PRIDEiP17445.

Expressioni

Inductioni

By osmotic stress. Choline is required for full expression. Oxygen and choline exert their control via the transacting DNA-binding proteins ArcA and BetI, respectively.2 Publications

Gene expression databases

GenevestigatoriP17445.

Interactioni

Subunit structurei

Dimer of dimers.1 Publication

Protein-protein interaction databases

DIPiDIP-9208N.
IntActiP17445. 7 interactions.
STRINGi511145.b0312.

Structurei

3D structure databases

ProteinModelPortaliP17445.
SMRiP17445. Positions 2-490.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
InParanoidiP17445.
KOiK00130.
OMAiVGGYKES.
OrthoDBiEOG6BS8QW.
PhylomeDBiP17445.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
HAMAPiMF_00804. BADH.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR011264. BADH.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01804. BADH. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17445-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRMAEQQLY IHGGYTSATS GRTFETINPA NGNVLATVQA AGREDVDRAV
60 70 80 90 100
KSAQQGQKIW ASMTAMERSR ILRRAVDILR ERNDELAKLE TLDTGKAYSE
110 120 130 140 150
TSTVDIVTGA DVLEYYAGLI PALEGSQIPL RETSFVYTRR EPLGVVAGIG
160 170 180 190 200
AWNYPIQIAL WKSAPALAAG NAMIFKPSEV TPLTALKLAE IYSEAGLPDG
210 220 230 240 250
VFNVLPGVGA ETGQYLTEHP GIAKVSFTGG VASGKKVMAN SAASSLKEVT
260 270 280 290 300
MELGGKSPLI VFDDADLDLA ADIAMMANFF SSGQVCTNGT RVFVPAKCKA
310 320 330 340 350
AFEQKILARV ERIRAGDVFD PQTNFGPLVS FPHRDNVLRY IAKGKEEGAR
360 370 380 390 400
VLCGGDVLKG DGFDNGAWVA PTVFTDCSDD MTIVREEIFG PVMSILTYES
410 420 430 440 450
EDEVIRRAND TDYGLAAGIV TADLNRAHRV IHQLEAGICW INTWGESPAE
460 470 480 490
MPVGGYKHSG IGRENGVMTL QSYTQVKSIQ VEMAKFQSIF
Length:490
Mass (Da):52,911
Last modified:January 23, 2007 - v3
Checksum:i747F822DA1233808
GO

Sequence cautioni

The sequence AAA23505.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB18038.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti232 – 2321A → R in AAA23506 (PubMed:1879697).Curated
Sequence conflicti232 – 2321A → R in AAA23505 (PubMed:1879697).Curated
Sequence conflicti312 – 3121R → P in AAA23506 (PubMed:1879697).Curated
Sequence conflicti312 – 3121R → P in AAA23505 (PubMed:1879697).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52905 Genomic DNA. Translation: CAA37092.1.
M77739 Genomic DNA. Translation: AAA23506.1.
M77739 Genomic DNA. Translation: AAA23505.1. Different initiation.
U73857 Genomic DNA. Translation: AAB18038.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73415.1.
AP009048 Genomic DNA. Translation: BAE76095.1.
PIRiS15181.
RefSeqiNP_414846.1. NC_000913.3.
YP_488607.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73415; AAC73415; b0312.
BAE76095; BAE76095; BAE76095.
GeneIDi12933807.
947376.
KEGGiecj:Y75_p0302.
eco:b0312.
PATRICi32115753. VBIEscCol129921_0319.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52905 Genomic DNA. Translation: CAA37092.1.
M77739 Genomic DNA. Translation: AAA23506.1.
M77739 Genomic DNA. Translation: AAA23505.1. Different initiation.
U73857 Genomic DNA. Translation: AAB18038.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73415.1.
AP009048 Genomic DNA. Translation: BAE76095.1.
PIRiS15181.
RefSeqiNP_414846.1. NC_000913.3.
YP_488607.1. NC_007779.1.

3D structure databases

ProteinModelPortaliP17445.
SMRiP17445. Positions 2-490.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9208N.
IntActiP17445. 7 interactions.
STRINGi511145.b0312.

Proteomic databases

PaxDbiP17445.
PRIDEiP17445.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73415; AAC73415; b0312.
BAE76095; BAE76095; BAE76095.
GeneIDi12933807.
947376.
KEGGiecj:Y75_p0302.
eco:b0312.
PATRICi32115753. VBIEscCol129921_0319.

Organism-specific databases

EchoBASEiEB0108.
EcoGeneiEG10110. betB.

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
InParanoidiP17445.
KOiK00130.
OMAiVGGYKES.
OrthoDBiEOG6BS8QW.
PhylomeDBiP17445.

Enzyme and pathway databases

UniPathwayiUPA00529; UER00386.
BioCyciEcoCyc:BADH-MONOMER.
ECOL316407:JW0304-MONOMER.
MetaCyc:BADH-MONOMER.

Miscellaneous databases

PROiP17445.

Gene expression databases

GenevestigatoriP17445.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
HAMAPiMF_00804. BADH.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR011264. BADH.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01804. BADH. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence and analysis of the bet genes encoding the osmoregulatory choline-glycine betaine pathway of Escherichia coli."
    Lamark T., Kaasen E., Eshoo M.W., Falkenberg P., McDougall J., Strom A.R.
    Mol. Microbiol. 5:1049-1064(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-29.
    Strain: K12.
  2. "Characterization of an Escherichia coli gene encoding betaine aldehyde dehydrogenase (BADH): structural similarity to mammalian ALDHs and a plant BADH."
    Boyd L.A., Adam L., Pelcher L.E., McHughen A., Hirji R., Selvaraj G.
    Gene 103:45-52(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Choline-glycine betaine pathway confers a high level of osmotic tolerance in Escherichia coli."
    Landfald B., Strom A.R.
    J. Bacteriol. 165:849-855(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION.
  7. "Purification and characterization of osmoregulatory betaine aldehyde dehydrogenase of Escherichia coli."
    Falkenberg P., Strom A.R.
    Biochim. Biophys. Acta 1034:253-259(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBSTRATE SPECIFICITY, SUBUNIT.
  8. "The complex bet promoters of Escherichia coli: regulation by oxygen (ArcA), choline (BetI), and osmotic stress."
    Lamark T., Rokenes T.P., McDougall J., Strom A.R.
    J. Bacteriol. 178:1655-1662(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiBETB_ECOLI
AccessioniPrimary (citable) accession number: P17445
Secondary accession number(s): Q2MCB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.