Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P17445 (BETB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NAD/NADP-dependent betaine aldehyde dehydrogenase

Short name=BADH
EC=1.2.1.8
Gene names
Name:betB
Ordered Locus Names:b0312, JW0304
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length490 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7

Catalytic activity

Betaine aldehyde + NAD+ + H2O = betaine + NADH. Ref.6 Ref.7

Cofactor

Binds 2 potassium ions per subunit By similarity. HAMAP-Rule MF_00804

Enzyme regulation

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. Ref.7

Pathway

Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. HAMAP-Rule MF_00804

Subunit structure

Dimer of dimers Probable. Ref.7

Induction

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. Ref.6 Ref.7 Ref.8

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=99 µM for NAD (at pH 7.5 and 25 degrees Celsius) Ref.6 Ref.7

KM=160 µM for betaine aldehyde (at pH 7.5 and 25 degrees Celsius)

KM=400 µM for NADP (at pH 7.5 and 25 degrees Celsius)

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

pH dependence:

Optimum pH is between 7.5 and 9.5.

Sequence caution

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 490489NAD/NADP-dependent betaine aldehyde dehydrogenase HAMAP-Rule MF_00804
PRO_0000056541

Regions

Nucleotide binding150 – 1534NAD/NADP By similarity
Nucleotide binding176 – 1794NAD/NADP By similarity
Nucleotide binding229 – 2346NAD/NADP By similarity

Sites

Active site1621Charge relay system By similarity
Active site2521Proton acceptor By similarity
Active site4641Charge relay system By similarity
Metal binding261Potassium 1 By similarity
Metal binding271Potassium 1; via carbonyl oxygen By similarity
Metal binding931Potassium 1 By similarity
Metal binding1801Potassium 1; via carbonyl oxygen By similarity
Metal binding2461Potassium 2; via carbonyl oxygen By similarity
Metal binding4571Potassium 2; via carbonyl oxygen By similarity
Metal binding4601Potassium 2; via carbonyl oxygen By similarity
Binding site2091NAD/NADP; via amide nitrogen By similarity
Binding site2861NAD/NADP By similarity
Binding site3871NAD/NADP By similarity
Site2481Seems to be a necessary countercharge to the potassium cations By similarity

Amino acid modifications

Modified residue2861Cysteine sulfenic acid (-SOH) By similarity

Experimental info

Sequence conflict2321A → R in AAA23506. Ref.2
Sequence conflict2321A → R in AAA23505. Ref.2
Sequence conflict3121R → P in AAA23506. Ref.2
Sequence conflict3121R → P in AAA23505. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P17445 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 747F822DA1233808

FASTA49052,911
        10         20         30         40         50         60 
MSRMAEQQLY IHGGYTSATS GRTFETINPA NGNVLATVQA AGREDVDRAV KSAQQGQKIW 

        70         80         90        100        110        120 
ASMTAMERSR ILRRAVDILR ERNDELAKLE TLDTGKAYSE TSTVDIVTGA DVLEYYAGLI 

       130        140        150        160        170        180 
PALEGSQIPL RETSFVYTRR EPLGVVAGIG AWNYPIQIAL WKSAPALAAG NAMIFKPSEV 

       190        200        210        220        230        240 
TPLTALKLAE IYSEAGLPDG VFNVLPGVGA ETGQYLTEHP GIAKVSFTGG VASGKKVMAN 

       250        260        270        280        290        300 
SAASSLKEVT MELGGKSPLI VFDDADLDLA ADIAMMANFF SSGQVCTNGT RVFVPAKCKA 

       310        320        330        340        350        360 
AFEQKILARV ERIRAGDVFD PQTNFGPLVS FPHRDNVLRY IAKGKEEGAR VLCGGDVLKG 

       370        380        390        400        410        420 
DGFDNGAWVA PTVFTDCSDD MTIVREEIFG PVMSILTYES EDEVIRRAND TDYGLAAGIV 

       430        440        450        460        470        480 
TADLNRAHRV IHQLEAGICW INTWGESPAE MPVGGYKHSG IGRENGVMTL QSYTQVKSIQ 

       490 
VEMAKFQSIF 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS15181.
RefSeqNP_414846.1. NC_000913.3.
YP_488607.1. NC_007779.1.

3D structure databases

ProteinModelPortalP17445.
SMRP17445. Positions 2-490.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9208N.
IntActP17445. 7 interactions.
STRING511145.b0312.

Proteomic databases

PaxDbP17445.
PRIDEP17445.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73415; AAC73415; b0312.
BAE76095; BAE76095; BAE76095.
GeneID12933807.
947376.
KEGGecj:Y75_p0302.
eco:b0312.
PATRIC32115753. VBIEscCol129921_0319.

Organism-specific databases

EchoBASEEB0108.
EcoGeneEG10110. betB.

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271505.
KOK00130.
OMACTDEMTI.
OrthoDBEOG6BS8QW.
PhylomeDBP17445.

Enzyme and pathway databases

BioCycEcoCyc:BADH-MONOMER.
ECOL316407:JW0304-MONOMER.
MetaCyc:BADH-MONOMER.
UniPathwayUPA00529; UER00386.

Gene expression databases

GenevestigatorP17445.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
HAMAPMF_00804. BADH.
InterProIPR016161. 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]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR01804. BADH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP17445.

Entry information

Entry nameBETB_ECOLI
AccessionPrimary (citable) accession number: P17445
Secondary accession number(s): Q2MCB1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene