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

Q8X6C6 (BETA_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 83. 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:Z0398, ECs0357
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length562 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

Subcellular location

Cell membrane; Peripheral membrane protein By similarity HAMAP-Rule MF_00750.

Sequence similarities

Belongs to the GMC oxidoreductase family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   LigandFAD
Flavoprotein
NAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycine betaine biosynthetic process from choline

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbetaine-aldehyde dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

choline dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 562562Oxygen-dependent choline dehydrogenase HAMAP-Rule MF_00750
PRO_0000205587

Regions

Nucleotide binding4 – 3330FAD By similarity

Sites

Active site4731 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8X6C6 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 7DC9B36EC06D24ED

FASTA56262,633
        10         20         30         40         50         60 
MQFDYIIIGA GSAGNVLATR LTEDPNTSVL LLEAGGPDYR FDFRTQMPAA LAFPLQGKRY 

        70         80         90        100        110        120 
NWAYETEPEP FMNNRRMECG RGKGLGGSSL INGMCYIRGN AMDLDNWAKE PGLENWSYLD 

       130        140        150        160        170        180 
CLPYYRKAET RDVGENDYHG GDGPVSVTTS KPGVNPLFEA MIEAGVQAGY PRTDDLNGYQ 

       190        200        210        220        230        240 
QEGFGPMDRT VTPQGRRAST ARGYLDQAKS RPNLTIRTHA MTDHIIFDCK RAVGVEWLEG 

       250        260        270        280        290        300 
DSTIPTRATA NKEVLLCAGA IASPQILQRS GVGNAELLAE FDIPLVHDLP GVGENLQDHL 

       310        320        330        340        350        360 
EMYLQYECKE PVSLYPALQW WNQPKIGAEW LFGGTGVGAS NHFEAGGFIR SREEFAWPNI 

       370        380        390        400        410        420 
QYHFLPVAIN YNGSNAVKEH GFQCHVGSMR SPSRGHVRIK SRDPHQHPAI LFNYMSHEQD 

       430        440        450        460        470        480 
WQEFRDAIRI TREIMHQPAL DQYRGREISP GTECQTDEQL DEFVRNHAET AFHPCGTCKM 

       490        500        510        520        530        540 
GYDEMSVVDG EGRVHGLEGL RVVDASIMPQ IITGNLNATT IMIGEKMADM IRGKEALPRS 

       550        560 
TAGYFVANGM PVRAKKMSRD LN 

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG54653.1.
BA000007 Genomic DNA. Translation: BAB33780.1.
PIRA85524.
E90673.
RefSeqNP_286045.1. NC_002655.2.
NP_308384.1. NC_002695.1.

3D structure databases

ProteinModelPortalQ8X6C6.
SMRQ8X6C6. Positions 1-531.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z0398.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG54653; AAG54653; Z0398.
BAB33780; BAB33780; BAB33780.
GeneID914458.
957211.
KEGGece:Z0398.
ecs:ECs0357.
PATRIC18349652. VBIEscCol44059_0348.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2303.
HOGENOMHOG000139600.
KOK00108.
OMAYLQYACT.
OrthoDBEOG67HJQP.

Enzyme and pathway databases

BioCycECOL386585:GJFA-354-MONOMER.
ECOO157:BETA-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_ECO57
AccessionPrimary (citable) accession number: Q8X6C6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: March 1, 2002
Last modified: May 14, 2014
This is version 83 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