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B4EHJ1 (BETB_BURCJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. 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:BceJ2315_57780
ORF Names:BCAM2342
OrganismBurkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)) [Complete proteome] [HAMAP]
Taxonomic identifier216591 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length489 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 – 489489NAD/NADP-dependent betaine aldehyde dehydrogenase HAMAP-Rule MF_00804
PRO_1000133942

Regions

Nucleotide binding150 – 1534NAD/NADP By similarity
Nucleotide binding176 – 1794NAD/NADP By similarity
Nucleotide binding228 – 2336NAD/NADP By similarity

Sites

Active site1621Charge relay system By similarity
Active site2511Proton acceptor By similarity
Active site4631Charge relay system By similarity
Metal binding261Potassium 1 By similarity
Metal binding931Potassium 1 By similarity
Metal binding1801Potassium 1; via carbonyl oxygen By similarity
Metal binding2451Potassium 2; via carbonyl oxygen By similarity
Metal binding4561Potassium 2; via carbonyl oxygen By similarity
Metal binding4591Potassium 2; via carbonyl oxygen By similarity
Binding site2091NAD/NADP; via amide nitrogen By similarity
Binding site2851NAD/NADP By similarity
Binding site3861NAD/NADP By similarity
Site2471Seems to be a necessary countercharge to the potassium cations By similarity

Amino acid modifications

Modified residue2851Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
B4EHJ1 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 76FA6D83F83DDEED

FASTA48952,332
        10         20         30         40         50         60 
MSVYGLQRLY IGGGYVDATS GKTFDTFDPA TGELLAQVQQ ASAADVDRAV ASAQEGQREW 

        70         80         90        100        110        120 
AAMTAMQRSR ILRRAVDLLR ERNDELAAIE TRDTGKPIGE TLAVDIVTGA DVIEYYAGLA 

       130        140        150        160        170        180 
TAIEGLQVPL RAESFVYTRR EPLGVCAGIG AWNYPIQIAC WKTAPALAAG NAMVFKPSEV 

       190        200        210        220        230        240 
TPLTALKLAE IYTEAGVPAG VFNVVQGDGS VGALLTGHPD IAKVSFTGGV ETGKKVMSLA 

       250        260        270        280        290        300 
GASSLKEVTM ELGGKSPLIV FDDADLDRAA DIAVTANFFS SGQVCTNGTR VFMHRSVKDA 

       310        320        330        340        350        360 
FTQKVLERVK RIRVGKPTDA DTNFGPLVSA AQLDKVLGFI ESGKAEGAKL LAGGTRLTDG 

       370        380        390        400        410        420 
HFGSGQYVAP TVFGDCRDDM KIVREEIFGP VMSILDFESE DEVIARANDT HYGLAAGVVT 

       430        440        450        460        470        480 
ENLSRAHRTI HRLEAGICWI NTWGESPAEM PVGGYKQSGV GRENGITTLE HYTRIKSVQV 


ELGRYNPVF 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM747721 Genomic DNA. Translation: CAR56201.1.
RefSeqYP_002234941.1. NC_011001.1.

3D structure databases

ProteinModelPortalB4EHJ1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING216591.BCAM2342.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6930398.
KEGGbcj:BCAM2342.
PATRIC19084036. VBIBurCen118154_6134.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271505.
KOK00130.
OMAAHRTIHR.
OrthoDBEOG6BS8QW.
ProtClustDBPRK13252.

Enzyme and pathway databases

BioCycBCEN216591:GJI4-5973-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.
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_BURCJ
AccessionPrimary (citable) accession number: B4EHJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: February 19, 2014
This is version 40 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