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A9AMZ9 (BETA_BURM1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:
Oxygen-dependent choline dehydrogenase

Short name=CDH
Short name=CHD
EC=1.1.99.1
Alternative name(s):
Betaine aldehyde dehydrogenase
Short name=BADH
EC=1.2.1.8
Gene names
Name:betA
Ordered Locus Names:Bmul_3536, BMULJ_04981
OrganismBurkholderia multivorans (strain ATCC 17616 / 249) [Complete proteome] [HAMAP]
Taxonomic identifier395019 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length566 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate By similarity. HAMAP-Rule MF_00750

Catalytic activity

Choline + acceptor = betaine aldehyde + reduced acceptor. HAMAP-Rule MF_00750

Betaine aldehyde + NAD+ + H2O = betaine + NADH. HAMAP-Rule MF_00750

Cofactor

FAD By similarity. HAMAP-Rule MF_00750

Pathway

Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. HAMAP-Rule MF_00750

Sequence similarities

Belongs to the GMC oxidoreductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 566566Oxygen-dependent choline dehydrogenase HAMAP-Rule MF_00750
PRO_1000133323

Regions

Nucleotide binding7 – 3630FAD By similarity

Sites

Active site4741 By similarity

Sequences

Sequence LengthMass (Da)Tools
A9AMZ9 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 1D3CFF0E9E050550

FASTA56662,958
        10         20         30         40         50         60 
MTTREYDYII CGAGSAGNVL ATRLTEDPNV TVLLLEAGGP DYRFDFRTQM PAALAYPLQG 

        70         80         90        100        110        120 
RRYNWAYETD PEPHMDNRRM ECGRGKGLGG SSLINGMCYI RGNALDYDNW ATHQGLENWT 

       130        140        150        160        170        180 
YLDCLPYFKK AETRDIGPND YHGGDGPVSV TTSKPGVNPL FEAMVEAGVQ AGYPRTEDLN 

       190        200        210        220        230        240 
GYQQEGFGPM DRTVTPKGRR ASTARGYLDQ AKTRPNLEIV THALADRILF DGKRASGVTY 

       250        260        270        280        290        300 
LRGNERATAH ARREVLVCSG AIASPQLLQR SGVGPGAWLK ELDIPIVLDL PGVGQNLQDH 

       310        320        330        340        350        360 
LEMYIQYECK EPVSLYPALK WWNQPKIGLE WMLNGTGLGA SNHFEAGGFI RTRDDDPWPN 

       370        380        390        400        410        420 
IQYHFLPVAI NYNGSNAIEM HGFQAHVGSM RSPSRGRVKL RSRDPNAHPS ILFNYMAEAL 

       430        440        450        460        470        480 
DWREFRDAIR ATREIMRQPA LDRYRGRELN PGADLKSDKE LDAFVRARAE TAFHPSCSCK 

       490        500        510        520        530        540 
MGYDDMAVVD NEGRVHGLEG LRVVDASIMP IITTGNLNAP TIMIAEKIAD KIRGRKPLER 

       550        560 
ANVPYFVANG APARNVAKAV RQPETV 

« Hide

References

[1]"Complete sequence of chromosome 2 of Burkholderia multivorans ATCC 17616."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17616 / 249.
[2]"Complete genome sequence of Burkholderia multivorans ATCC 17616."
Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E., Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N., Hattori M., Tsuda M.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17616 / 249.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000869 Genomic DNA. Translation: ABX17220.1.
AP009386 Genomic DNA. Translation: BAG46827.1.
RefSeqYP_001583512.1. NC_010086.1.
YP_001949363.1. NC_010805.1.

3D structure databases

ProteinModelPortalA9AMZ9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395019.Bmul_3536.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX17220; ABX17220; Bmul_3536.
BAG46827; BAG46827; BMULJ_04981.
GeneID5769978.
6361992.
KEGGbmj:BMULJ_04981.
bmu:Bmul_3536.
PATRIC19172105. VBIBurMul203716_6088.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2303.
HOGENOMHOG000139600.
KOK00108.
OMAYLQYACT.
OrthoDBEOG67HJQP.

Enzyme and pathway databases

BioCycBMUL395019:GIYO-4978-MONOMER.
UniPathwayUPA00529; UER00385.

Family and domain databases

HAMAPMF_00750. Choline_dehydrogen.
InterProIPR011533. Choline_dehydrogenase.
IPR012132. GMC_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PIRSFPIRSF000137. Alcohol_oxidase. 1 hit.
TIGRFAMsTIGR01810. betA. 1 hit.
PROSITEPS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBETA_BURM1
AccessionPrimary (citable) accession number: A9AMZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: January 15, 2008
Last modified: May 14, 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