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

B0RNV0 (BETB_XANCB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 50. 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:xcc-b100_0794
OrganismXanthomonas campestris pv. campestris (strain B100) [Complete proteome] [HAMAP]
Taxonomic identifier509169 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length490 AA.
Sequence statusComplete.
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.

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

Chain1 – 490490NAD/NADP-dependent betaine aldehyde dehydrogenase HAMAP-Rule MF_00804
PRO_1000133961

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 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
B0RNV0 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 25795922C6CA4786

FASTA49052,498
        10         20         30         40         50         60 
MPRFPDQLLY IGGRYVPARG GHTFEVVNPA TGEVLANVHN ADADDLDAAV DSAKAGQRHW 

        70         80         90        100        110        120 
AALTVVERSR ILLRAVALLR ERNDALAELE TLNTGKPLSE TRSVDIVTGA DVLEYYAGVA 

       130        140        150        160        170        180 
QALQGVQVPL REGSFFYTRH EPLGVVGAIG AWNYPIQIAL WKAAPALAAG NAMIFKPSEV 

       190        200        210        220        230        240 
TPLTALKLAE IFTEAGLPDG VFNVLPGDGA SVGHALTEHP EIEKISFTGG TATGRKVMAS 

       250        260        270        280        290        300 
ASSSSLKDVT MELGGKSPLI VCADADLDLA ADIAMMANFY SSGQVCTNGT RVFVPRALRT 

       310        320        330        340        350        360 
AFEARLLARV QRIHIGDPLD ERTTFGPMVS AAHMQRVLEH IEQGKAEGAR LLCGGERLRD 

       370        380        390        400        410        420 
GALAQGCYVA PTIFSDCTDV MTIVREEIFG PVLSLLTYDD EDEAITRANA TSYGLAAGVV 

       430        440        450        460        470        480 
TPDLSRAHRL IHRLEAGICW INTWGESPAP MPVGGYKQSG VGRENGLATL QAYTRTKSVQ 

       490 
VELERYASVF 

« Hide

References

[1]"The genome of Xanthomonas campestris pv. campestris B100 and its use for the reconstruction of metabolic pathways involved in xanthan biosynthesis."
Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puehler A.
J. Biotechnol. 134:33-45(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM920689 Genomic DNA. Translation: CAP50135.1.
RefSeqYP_001902199.1. NC_010688.1.

3D structure databases

ProteinModelPortalB0RNV0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING509169.xccb100_0794.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP50135; CAP50135; xcc-b100_0794.
GeneID6324332.
KEGGxca:xccb100_0794.
PATRIC24081411. VBIXanCam108527_0817.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1012.
KOK00130.
OMACTDEMTI.
OrthoDBEOG6BS8QW.

Enzyme and pathway databases

BioCycXCAM509169:GHW4-810-MONOMER.
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_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...

Entry information

Entry nameBETB_XANCB
AccessionPrimary (citable) accession number: B0RNV0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 8, 2008
Last modified: June 11, 2014
This is version 50 of the entry and version 1 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