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Reviewed, UniProtKB/Swiss-Prot Q937L5 (CPNB_COMTE)

Last modified November 24, 2009. Version 34. 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

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Names and origin

Protein namesRecommended name:
    Cyclopentanone 1,2-monooxygenase
      Short name=CPMO
    EC=1.14.13.16
Gene names
Name: cpnB
Synonyms: cpmA
OrganismComamonas testosteroni (Pseudomonas testosteroni)
Taxonomic identifier285 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Comamonas

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Protein attributes

Sequence length550 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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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 By similarity.

Sequence similarities

Belongs to the FAD-binding monooxygenase family.

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Ontologies

Keywords
   LigandFAD
Flavoprotein
NADP
   Molecular functionMonooxygenase
Oxidoreductase
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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 550549Cyclopentanone 1,2-monooxygenase
PRO_0000186454

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

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Sequences

Sequence LengthMass (Da)Tools
Q937L5-1 [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

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References

[1]"Cloning of Baeyer-Villiger monooxygenases from Comamonas, Xanthobacter and Rhodococcus via PCR with highly degenerate primers."
van Beilen J.B., Mourlane F., Seeger M.A., Kovac J., Li Z., Smits T.H.M., Fritsche U., Witholt B.
Environ. Microbiol. 5:174-182(2003) [PubMed: 12588297] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

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Cross-references

Sequence databases

AJ418060 Genomic DNA. Translation: CAD10798.1.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA1.14.13.16. 4566.

Family and domain databases

InterProIPR006076. FAD-dep_OxRdtase.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
[Graphical view]
PfamPF01266. DAO. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
ProtoNetSearch...

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Entry information

Entry nameCPNB_COMTE
AccessionPrimary (citable) accession number: Q937L5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: January 23, 2007
Last modified: November 24, 2009
This is version 34 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)

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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