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Q8UH56 (BETB_AGRT5) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 80. 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:Atu0829
ORF Names:AGR_C_1515
OrganismAgrobacterium tumefaciens (strain C58 / ATCC 33970) [Reference proteome] [HAMAP]
Taxonomic identifier176299 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
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 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 Probable. Ref.3

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 493493NAD/NADP-dependent betaine aldehyde dehydrogenase HAMAP-Rule MF_00804
PRO_0000056535

Regions

Nucleotide binding156 – 1594NAD/NADP By similarity
Nucleotide binding182 – 1854NAD/NADP By similarity
Nucleotide binding234 – 2396NAD/NADP By similarity

Sites

Active site1681Charge relay system By similarity
Active site2561Proton acceptor By similarity
Active site4671Charge relay system By similarity
Metal binding321Potassium 1 By similarity
Metal binding331Potassium 1; via carbonyl oxygen By similarity
Metal binding991Potassium 1 By similarity
Metal binding2501Potassium 2; via carbonyl oxygen By similarity
Metal binding4601Potassium 2; via carbonyl oxygen By similarity
Metal binding4631Potassium 2; via carbonyl oxygen By similarity
Binding site2901NAD/NADP By similarity
Binding site3901NAD/NADP By similarity

Amino acid modifications

Modified residue2901Cysteine sulfenic acid (-SOH) By similarity

Secondary structure

............................................................................. 493
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8UH56 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 7636ADEEB5327833

FASTA49352,204
        10         20         30         40         50         60 
MTIATPLKAQ PKASHFIDGD YVEDNTGTPF ESIFPATGEM IAKLHAATPA IVERAIASAK 

        70         80         90        100        110        120 
RAQKEWAAMS PMARGRILKR AADIMRERND ALSTLETLDT GKPIQETIVA DPTSGADAFE 

       130        140        150        160        170        180 
FFGGIAPSAL NGDYIPLGGD FAYTKRVPLG VCVGIGAWNY PQQIACWKAA PALVAGNAMV 

       190        200        210        220        230        240 
FKPSENTPLG ALKIAEILIE AGLPKGLFNV IQGDRDTGPL LVNHPDVAKV SLTGSVPTGR 

       250        260        270        280        290        300 
KVAAAAAGHL KHVTMELGGK SPMIVFDDAD IESAVGGAML GNFYSSGQVC SNGTRVFVQK 

       310        320        330        340        350        360 
KAKARFLENL KRRTEAMILG DPLDYATHLG PLVSKAQQEK VLSYIEKGKA EGATLITGGG 

       370        380        390        400        410        420 
IPNNVAGEGA YVQPTVFADV TDDMTIAREE IFGPVMCVLD FDDEDEVLAR ANATEFGLAG 

       430        440        450        460        470        480 
GVFTADLARA HRVVDGLEAG TLWINTYNLC PVEIPFGGSK QSGFGRENSA AALEHYSELK 

       490 
TVYVSTGKVD APY 

« Hide

References

« Hide 'large scale' references
[1]"The genome of the natural genetic engineer Agrobacterium tumefaciens C58."
Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., Clendenning J. expand/collapse author list , Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V., Nester E.W.
Science 294:2317-2323(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C58 / ATCC 33970.
[2]"Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58."
Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C. expand/collapse author list , Allinger M., Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.
Science 294:2323-2328(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C58 / ATCC 33970.
[3]"Crystal structure of betaine aldehyde dehydrogenase from Agrobacterium tumefaciens."
New York structural genomics research consortium (NYSGRC)
Submitted (MAR-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE007869 Genomic DNA. Translation: AAK86635.1.
PIRAE2678.
B97460.
RefSeqNP_353850.1. NC_003062.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3R31X-ray2.15A/B1-493[»]
ProteinModelPortalQ8UH56.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176299.Atu0829.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK86635; AAK86635; Atu0829.
GeneID1132867.
KEGGatu:Atu0829.
PATRIC20811367. VBIAgrTum91616_0825.

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271505.
KOK00130.
OMACEHQLVA.
OrthoDBEOG6BS8QW.

Enzyme and pathway databases

BioCycAGRO:ATU0829-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_AGRT5
AccessionPrimary (citable) accession number: Q8UH56
Secondary accession number(s): Q7D0K9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: June 1, 2002
Last modified: June 11, 2014
This is version 80 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways