ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q2KB43


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name BETA_RHIEC
Primary accession number Q2KB43
Secondary accession numbers None
Integrated into Swiss-Prot on October 31, 2006
Sequence was last modified on March 7, 2006 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 22)
Name and origin of the protein
Protein name Choline dehydrogenase
Synonyms CHD
CDH
EC 1.1.99.1
Gene name
Name: betA
OrderedLocusNames: RHE_CH01136
From
Rhizobium etli (strain CFN 42 / ATCC 51251) [TaxID: 347834] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0508502103; PubMed=16505379 [NCBI, ExPASy, EBI, Israel, Japan]
Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I., Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A., Jimenez-Jacinto V., Collado-Vides J., Davila G.;
"The partitioned Rhizobium etli genome: genetic and metabolic redundancy in seven interacting replicons.";
Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CP000133; ABC89943.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_468670.1; -.
3D structure databases
ModBase Q2KB43.
Ontologies
GO
GO:0008812; Molecular function: choline dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0006066; Biological process: cellular alcohol metabolic process (inferred from electronic annotation from InterPro).
GO:0019285; Biological process: glycine betaine biosynthetic process from choline (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_00750; -; 1.
PBIL [Tree]
InterPro IPR011533; Choline_dehydrogenase.
IPR012132; GMC_OxRdtase.
IPR000172; GMC_OxRdtase_N.
IPR007867; GMC_OxRtase_C.
Graphical view of domain structure.
Pfam PF05199; GMC_oxred_C; 1.
PF00732; GMC_oxred_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000137; Alcohol_oxidase; 1.
TIGRFAMs TIGR01810; betA; 1.
PROSITE PS00623; GMC_OXRED_1; 1.
PS00624; GMC_OXRED_2; 1.
ProtoNet Q2KB43.
Genome annotation databases
GeneID 3890646; -.
GenomeReviews CP000133_GR; RHE_CH01136.
KEGG ret:RHE_CH01136; -.
Phylogenomic databases
HOGENOM Q2KB43; -.
Genome annotation databases
CMR Q2KB43; RHE_CH01136.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; FAD; Flavoprotein; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   549  549     Choline dehydrogenase. PRO_0000258932
NP_BIND   4    33  30     FAD (Probable). 
ACT_SITE   465   465        By similarity. 
Sequence information
Length: 549 AA [This is the length of the unprocessed precursor] Molecular weight: 60398 Da [This is the MW of the unprocessed precursor] CRC64: C262E284AEAB953F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQADFVIIGS GSAGSALAYR LSEDGKNSVL VIEAGGSDFG PFIQMPAALA WPMSMKRYNW 

        70         80         90        100        110        120 
GYLSEPEPNL NNRRITAPRG KVIGGSSSIN GMVYVRGHAE DFNRWEELGA SGWAYADVLP 

       130        140        150        160        170        180 
YFKRMEHSHG GEEGWRGTDG PLHVQRGGFT NPLFRAFIEA GKQAGFETTE DYNGSKQEGF 

       190        200        210        220        230        240 
GLMEQTIFAG RRWSAANAYL KPALKRDNVG IVYGLARRIV IENGRATGVE IERGGRTEVV 

       250        260        270        280        290        300 
KANREVIVSA SSFNSPKLLM LSGIGPAKHL KEMGIEVKAD RPGVGANLQD HMEFYFQQVS 

       310        320        330        340        350        360 
TKPVSLYSWL PWFWQGVAGA QWLLSKGGLG ASNQFEACAF LRSAPGLKQP DIQYHFLPVA 

       370        380        390        400        410        420 
ISYDGKAAAK SHGFQVHVGY NLSKSRGSVT LRSPDPKADP VLRFNYMSHP EDWEKFRHCV 

       430        440        450        460        470        480 
RLTREIFGQK AFDAYRGPEI QPGEGVQSDE QIDSFLREHL ESAYHPCGTC KMGAKDDPMA 

       490        500        510        520        530        540 
VVDPQTRVIG VDGLRVADSS IFPHVTYGNL NGPSIMTGEK AADHILGKQP LARSNQEPWI 


NPRAAVSDR 

Q2KB43 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!