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

B0RNU9 (BETA_XANCB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:xcc-b100_0793
OrganismXanthomonas campestris pv. campestris (strain B100) [Complete proteome] [HAMAP]
Taxonomic identifier509169 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length556 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 – 556556Oxygen-dependent choline dehydrogenase HAMAP-Rule MF_00750
PRO_1000133340

Regions

Nucleotide binding6 – 3530FAD By similarity

Sites

Active site4751 By similarity

Sequences

Sequence LengthMass (Da)Tools
B0RNU9 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 12409448073F6478

FASTA55661,445
        10         20         30         40         50         60 
MQREYDYIII GAGSAGNVLA ARLTEDPGVS VLLLEAGGPD YRLDFRTQMP AALAFPLQGR 

        70         80         90        100        110        120 
RYNWAYETEP EPHMDNRRME CGRGKGLGGS SLINGMCYIR GNALDFDHWA KRPGLEDWGY 

       130        140        150        160        170        180 
RDVLPYFRKA ETRDIGANDY HGGEGPVSVA TPKNDNNVLF QAMVDAGVQA GYPRTDDLNG 

       190        200        210        220        230        240 
YQQEGFGPMD RTVTPQGRRA STARGYLDMA KPRDSLHIVT HATTDRILFA GKRAVGVHYL 

       250        260        270        280        290        300 
VGNSSEGIDA HARREVLVCA GAIASPQLLQ RSGVGAPDLL RALDVQLVHD LPGVGQNLQD 

       310        320        330        340        350        360 
HLEVYMQYAC TKPVSLYPAL QWWNQPAIGA EWLFAGTGTG ASNQFEAGGF IRTREEFDWP 

       370        380        390        400        410        420 
NIQYHFLPVA INYNGSNAVK EHGFQAHVGS MRTPSRGRVH ARSRDPRQHP SILFNYQSTD 

       430        440        450        460        470        480 
QDWQEFRDAI RITREIIAQP ALDPYRGREI SPSADCKTDA ELDAFVRARA ETAYHPSCSC 

       490        500        510        520        530        540 
AMGTDDMAVV DGQGRVHGME GLRVIDASIM PRIITGNLNA TTIMIAEKIV DRIRGRAPLP 

       550 
RSTADYYVAG DAPVRR 

« 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: CAP50134.1.
RefSeqYP_001902198.1. NC_010688.1.

3D structure databases

ProteinModelPortalB0RNU9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING509169.xccb100_0793.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP50134; CAP50134; xcc-b100_0793.
GeneID6321210.
KEGGxca:xccb100_0793.
PATRIC24081409. VBIXanCam108527_0816.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2303.
KOK00108.
OMAYLQYACT.
OrthoDBEOG67HJQP.

Enzyme and pathway databases

BioCycXCAM509169:GHW4-809-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_XANCB
AccessionPrimary (citable) accession number: B0RNU9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 8, 2008
Last modified: May 14, 2014
This is version 52 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