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Protein

Cyclopentanone 1,2-monooxygenase

Gene

cpnB

Organism
Comamonas sp. (strain NCIMB 9872)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes a Baeyer-Villiger oxidation reaction, i.e. the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters or lactones using NADPH as an electron donor. Converts cyclopentanone to 5-valerolactone, a step in the degradation pathway of cyclopentanol. Besides cycloalkanones, can also act on methylated and other alkylated cycloalkanones, and on methylated cycloalkenones, with high enantioselectivity in some cases. Cannot use NADH instead of NADPH.3 Publications

Catalytic activityi

Cyclopentanone + NADPH + O2 = 5-valerolactone + NADP+ + H2O.2 Publications

Cofactori

FAD2 Publications

Pathwayi: cyclopentanol degradation

This protein is involved in step 2 of the subpathway that synthesizes 5-valerolactone from cyclopentanol.1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Cyclopentanol dehydrogenase (cpnA)
  2. Cyclopentanone 1,2-monooxygenase (cpnB)
This subpathway is part of the pathway cyclopentanol degradation, which is itself part of Alcohol metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-valerolactone from cyclopentanol, the pathway cyclopentanol degradation and in Alcohol metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511FADBy similarity
Binding sitei60 – 601FADBy similarity
Binding sitei71 – 711FADBy similarity
Binding sitei77 – 771FADBy similarity
Binding sitei123 – 1231FAD; via amide nitrogen and carbonyl oxygenBy similarity
Sitei344 – 3441Transition state stabilizerSequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi31 – 322FADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BRENDAi1.14.13.16. 1588.
SABIO-RKQ8GAW0.
UniPathwayiUPA00764; UER00750.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclopentanone 1,2-monooxygenase (EC:1.14.13.16)
Short name:
CPMO
Alternative name(s):
Baeyer-Villiger monooxygenase
Short name:
BVMO
Gene namesi
Name:cpnB
Synonyms:cpmA
OrganismiComamonas sp. (strain NCIMB 9872)
Taxonomic identifieri213664 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeComamonas

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene are not capable of growth on cyclopentanol or cyclopentanone as a sole carbon and energy source.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 550549Cyclopentanone 1,2-monooxygenasePRO_0000186453Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ8GAW0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FAD-binding monooxygenase family.Curated

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR020946. Flavin_mOase-like.
[Graphical view]
PfamiPF00743. FMO-like. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 3 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8GAW0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTMTTMTTE QLGMNNSVND KLDVLLIGAG FTGLYQLYHL RKLGYKVHLV
60 70 80 90 100
DAGADIGGIW HWNCYPGARV DTHCQIYQYS IPELWQEFNW KELFPNWAQM
110 120 130 140 150
REYFHFADKK LDLSKDISFN TRVQSAVFDE GTREWTVRSI GHQPIQARFV
160 170 180 190 200
IANLGFGASP STPNVDGIET FKGQWYHTAL WPQEGVNMAG KRVAIIGTGS
210 220 230 240 250
SGVQVAQEAA LDAKQVTVYQ RTPNLALPMH QKQLSAEDNL RMKPELPAAF
260 270 280 290 300
ERRGKCFAGF DFDFIAKNAT ELSAAERTEI LEELWNAGGF RYWLANFQDY
310 320 330 340 350
LFDDKANDYV YEFWRDKVRA RIKDPKVAEK LAPMKKPHPY GAKRPSLEQW
360 370 380 390 400
YYEIFNQNNV TLVDVNETPV LRITEKGIVT AEGEAEFDLI VFATGFDAVT
410 420 430 440 450
GGLTSIDFRN NQGQSFKDVW SDGIRTQLGV ATAGFPNLLF GYGPQSPAGF
460 470 480 490 500
CNGPSSAEYQ GDLLIQLMNY LRDNNISRIE AQSEAQEEWS KLIADFWDSS
510 520 530 540 550
LFPRAKSWYQ GSNIPGKKVE SLNFPLGLPT YISKFNESAE KGYAGFSLAS
Length:550
Mass (Da):62,111
Last modified:January 23, 2007 - v3
Checksum:i8956EF95203F6173
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB073151 Genomic DNA. Translation: BAC22652.1.
AB022102 Genomic DNA. Translation: BAC01269.1.
AJ418060 Genomic DNA. Translation: CAD10798.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB073151 Genomic DNA. Translation: BAC22652.1.
AB022102 Genomic DNA. Translation: BAC01269.1.
AJ418060 Genomic DNA. Translation: CAD10798.1.

3D structure databases

ProteinModelPortaliQ8GAW0.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00764; UER00750.
BRENDAi1.14.13.16. 1588.
SABIO-RKQ8GAW0.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR020946. Flavin_mOase-like.
[Graphical view]
PfamiPF00743. FMO-like. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 3 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiCPMO_COMS9
AccessioniPrimary (citable) accession number: Q8GAW0
Secondary accession number(s): Q937L5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 54 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.