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Q5HCU1 (BETA_STAAC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:SACOL2627
OrganismStaphylococcus aureus (strain COL) [Complete proteome] [HAMAP]
Taxonomic identifier93062 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length569 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 – 569569Oxygen-dependent choline dehydrogenase HAMAP-Rule MF_00750
PRO_0000205595

Regions

Nucleotide binding9 – 3830FAD By similarity

Sites

Active site4751 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HCU1 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: A6E35293AADDDFA6

FASTA56963,610
        10         20         30         40         50         60 
MSNKNKSYDY VIIGGGSAGS VLGNRLSEDK DKEVLVLEAG RSDYFWDLFI QMPAALMFPS 

        70         80         90        100        110        120 
GNKFYDWIYS TDEEPHMGGR KVAHARGKVL GGSSSINGMI YQRGNPMDYE GWAEPEGMET 

       130        140        150        160        170        180 
WDFAHCLPYF KKLEKTYGAA PYDKFRGHDG PIKLKRGPAT NPLFQSFFDA GVEAGYHKTP 

       190        200        210        220        230        240 
DVNGFRQEGF GPFDSQVHRG RRMSASRAYL HPAMKRKNLT VETRAFVTEI HYEGRRATGV 

       250        260        270        280        290        300 
TYKKNGKLHT IDANEVILSG GAFNTPQLLQ LSGIGDSEFL KSKGIEPRVH LPGVGENFED 

       310        320        330        340        350        360 
HLEVYIQHKC KEPVSLQPSL DIKRMPFIGL QWIFTRTGAA ASNHFEGGGF VRSNNEVDYP 

       370        380        390        400        410        420 
NLMFHFLPIA VRYDGQKAAV AHGYQVHVGP MYSNSRGSLK IKSKDPFEKP SIRFNYLSTE 

       430        440        450        460        470        480 
EDKKEWVEAI RVARNILSQK AMDPFNGGEI SPGPEVQTDE EILDWVRRDG ETALHPSCSA 

       490        500        510        520        530        540 
KMGPASDPMA VVDPLTMKVH GMENLRVVDA SAMPRTTNGN IHAPVLMLAE KAADIIRGRK 

       550        560 
PLEPQYIDYY KHGVHDENEG AIEVKPYAK 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: COL.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000046 Genomic DNA. Translation: AAW38626.1.
RefSeqYP_187416.1. NC_002951.2.

3D structure databases

ProteinModelPortalQ5HCU1.
SMRQ5HCU1. Positions 5-540.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93062.SACOL2627.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW38626; AAW38626; SACOL2627.
GeneID3237169.
KEGGsac:SACOL2627.
PATRIC19531510. VBIStaAur112458_2556.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2303.
HOGENOMHOG000139600.
KOK00108.
OMAYLQYACT.
OrthoDBEOG67HJQP.

Enzyme and pathway databases

BioCycSAUR93062:GCEP-2611-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_STAAC
AccessionPrimary (citable) accession number: Q5HCU1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: February 15, 2005
Last modified: June 11, 2014
This is version 69 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