[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-41. PubMed=12406764 [NCBI, ExPASy, EBI, Israel, Japan] Iwaki H., Hasegawa Y., Wang S., Kayser M.M., Lau P.C.K.; "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."; Appl. Environ. Microbiol. 68:5671-5684(2002).
[2]	ERRATUM. Iwaki H., Hasegawa Y., Wang S., Kayser M.M., Lau P.C.K.; Appl. Environ. Microbiol. 69:2414-2414(2003).
[3]	PROTEIN SEQUENCE OF 2-30, AND CHARACTERIZATION. Bes M.T., Villa R., Roberts S.M., Wan P.W.H., Willetts A.; "Oxidative biotransformations by microorganisms: production of chiral synthons by cyclopentanone monooxygenase from Pseudomonas sp. NCIMB 9872."; J. Mol. Catal., B Enzym. 1:127-134(1996).

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: Homotetramer.
SIMILARITY: Belongs to the FAD-binding monooxygenase family.

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

AB073151; BAC22652.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB022102; BAC01269.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q8GAW0.

Family and domain databases

InterPro

IPR006076; FAD-dep_OxRdtase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
Graphical view of domain structure.

Pfam

PF01266; DAO; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 550`	`549`	`Cyclopentanone 1,2-monooxygenase.`	`PRO_0000186453`
`NP_BIND`	`31 32`	`2`	`FAD (By similarity).`
`BINDING`	`51 51`		`FAD (By similarity).`
`BINDING`	`60 60`		`FAD (By similarity).`
`BINDING`	`71 71`		`FAD (By similarity).`
`BINDING`	`77 77`		`FAD (By similarity).`
`BINDING`	`123 123`		`FAD; via amide nitrogen and carbonyl oxygen (By similarity).`
`SITE`	`344 344`	`1`	`Transition state stabilizer (Potential).`

Sequence information

Length: 550 AA [This is the length of the unprocessed precursor]

Molecular weight: 62111 Da [This is the MW of the unprocessed precursor]

CRC64: 8956EF95203F6173 [This is a checksum on the sequence]

        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

Q8GAW0 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 submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools