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Q8FKI8 (BETB_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:c0432
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length490 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the reversible oxidation of betaine aldehyde to the corresponding acid By similarity. HAMAP-Rule MF_00804

Catalytic activity

Betaine aldehyde + NAD+ + H2O = betaine + NADH. HAMAP-Rule MF_00804

Cofactor

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

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 By similarity. HAMAP-Rule MF_00804

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Sequence caution

The sequence AAN78913.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   LigandMetal-binding
NAD
NADP
Potassium
   Molecular functionOxidoreductase
   PTMOxidation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycine betaine biosynthetic process from choline

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionbetaine-aldehyde dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 490489NAD/NADP-dependent betaine aldehyde dehydrogenase HAMAP-Rule MF_00804
PRO_0000056543

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

Sequences

Sequence LengthMass (Da)Tools
Q8FKI8 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A88D39DFB2F296A7

FASTA49052,908
        10         20         30         40         50         60 
MSRMAEQQLY IHGGYTSATS GRTFETINPA NGNVLATVQA AGREDVDRAV KSAQQGQKIW 

        70         80         90        100        110        120 
AAMTAMERSR 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 ETGQYLTDHP GIAKVSFTGG VASGKKVMAN 

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

       310        320        330        340        350        360 
AFEQKVLARV ERIRAGDVFD PQTNFGPLVS FPHRDNVLRY IAKGKEEGAR VLCGGNVLKG 

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

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

       490 
VEMAKFQSIF 

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN78913.1. Different initiation.
RefSeqNP_752369.1. NC_004431.1.

3D structure databases

ProteinModelPortalQ8FKI8.
SMRQ8FKI8. Positions 2-490.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c0432.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN78913; AAN78913; c0432.
GeneID1036263.
KEGGecc:c0432.
PATRIC18278918. VBIEscCol75197_0405.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000271505.
KOK00130.
OMAHIMKQAA.
OrthoDBEOG6BS8QW.
ProtClustDBPRK13252.

Enzyme and pathway databases

UniPathwayUPA00529; UER00386.

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.
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...

Entry information

Entry nameBETB_ECOL6
AccessionPrimary (citable) accession number: Q8FKI8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 76 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