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Reviewed, UniProtKB/Swiss-Prot Q8GAW0 (CPNB_COMS9)

Last modified November 4, 2008. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cyclopentanone 1,2-monooxygenase
      Short name=CPMO
    EC=1.14.13.16
Gene names
Name: cpnB
OrganismComamonas sp. (strain NCIMB 9872)
Taxonomic identifier213664 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeComamonas

Protein attributes

Sequence length550 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Cyclopentanone + NADPH + O2 = 5-valerolactone + NADP+ + H2O.

Cofactor

FAD By similarity.

Pathway

Alcohol metabolism; cyclopentanol degradation; 5-valerolactone from cyclopentanol: step 2/2.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the FAD-binding monooxygenase family.

Ontologies

Keywords
   LigandFAD
Flavoprotein
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncyclopentanone monooxygenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.3
Chain2 – 550549Cyclopentanone 1,2-monooxygenase
PRO_0000186453

Regions

Nucleotide binding31 – 322FAD By similarity

Sites

Binding site511FAD By similarity
Binding site601FAD By similarity
Binding site711FAD By similarity
Binding site771FAD By similarity
Binding site1231FAD; via amide nitrogen and carbonyl oxygen By similarity
Site3441Transition state stabilizer Potential

Sequences

Sequence LengthMass (Da)Tools
Q8GAW0-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8956EF95203F6173

FASTA55062,111
        10         20         30         40         50         60 
MTTMTTMTTE QLGMNNSVND KLDVLLIGAG FTGLYQLYHL RKLGYKVHLV DAGADIGGIW 

        70         80         90        100        110        120 
HWNCYPGARV DTHCQIYQYS IPELWQEFNW KELFPNWAQM REYFHFADKK LDLSKDISFN 

       130        140        150        160        170        180 
TRVQSAVFDE GTREWTVRSI GHQPIQARFV IANLGFGASP STPNVDGIET FKGQWYHTAL 

       190        200        210        220        230        240 
WPQEGVNMAG KRVAIIGTGS SGVQVAQEAA LDAKQVTVYQ RTPNLALPMH QKQLSAEDNL 

       250        260        270        280        290        300 
RMKPELPAAF ERRGKCFAGF DFDFIAKNAT ELSAAERTEI LEELWNAGGF RYWLANFQDY 

       310        320        330        340        350        360 
LFDDKANDYV YEFWRDKVRA RIKDPKVAEK LAPMKKPHPY GAKRPSLEQW YYEIFNQNNV 

       370        380        390        400        410        420 
TLVDVNETPV LRITEKGIVT AEGEAEFDLI VFATGFDAVT GGLTSIDFRN NQGQSFKDVW 

       430        440        450        460        470        480 
SDGIRTQLGV ATAGFPNLLF GYGPQSPAGF CNGPSSAEYQ GDLLIQLMNY LRDNNISRIE 

       490        500        510        520        530        540 
AQSEAQEEWS KLIADFWDSS LFPRAKSWYQ GSNIPGKKVE SLNFPLGLPT YISKFNESAE 

       550 
KGYAGFSLAS 

« Hide

References

[1]"Cloning and characterization of a gene cluster involved in cyclopentanol metabolism in Comamonas sp. strain NCIMB 9872 and biotransformations effected by Escherichia coli-expressed cyclopentanone 1,2-monooxygenase."
Iwaki H., Hasegawa Y., Wang S., Kayser M.M., Lau P.C.K.
Appl. Environ. Microbiol. 68:5671-5684(2002) [PubMed: 12406764] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-41.
[2]Erratum
Iwaki H., Hasegawa Y., Wang S., Kayser M.M., Lau P.C.K.
Appl. Environ. Microbiol. 69:2414-2414(2003)
[3]"Oxidative biotransformations by microorganisms: production of chiral synthons by cyclopentanone monooxygenase from Pseudomonas sp. NCIMB 9872."
Bes M.T., Villa R., Roberts S.M., Wan P.W.H., Willetts A.
J. Mol. Catal., B Enzym. 1:127-134(1996)
Cited for: PROTEIN SEQUENCE OF 2-30, CHARACTERIZATION.

Cross-references

Sequence databases

AB073151 Genomic DNA. Translation: BAC22652.1.
AB022102 Genomic DNA. Translation: BAC01269.1.

3D structure databases

ModBaseSearch...

Family and domain databases

InterProIPR006076. FAD-dep_OxRdtase.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
[Graphical view]
PfamPF01266. DAO. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameCPNB_COMS9
AccessionPrimary (citable) accession number: Q8GAW0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: January 23, 2007
Last modified: November 4, 2008
This is version 30 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents