P12015 (CYMO_ACISP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Cyclohexanone 1,2-monooxygenase EC=1.14.13.22
Organism	Acinetobacter sp.
Taxonomic identifier	472 [NCBI]
Taxonomic lineage	Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	543 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Cyclohexanone + NADPH + O2 = hexano-6-lactone + NADP+ + H2O.
Cofactor	FAD.
Sequence similarities	Belongs to the FAD-binding monooxygenase family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro cyclohexanone monooxygenase activity Inferred from electronic annotation. Source: EC flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro flavin-containing monooxygenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.1
	Chain	2 – 543	542	Cyclohexanone 1,2-monooxygenase		PRO_0000186455
Sites
	Binding site	16	1	FAD; via amide nitrogen By similarity
	Binding site	37	1	FAD By similarity
	Binding site	46	1	FAD By similarity
	Binding site	57	1	FAD By similarity
	Binding site	63	1	FAD By similarity
	Binding site	110	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Site	327	1	Transition state stabilizer Potential

Sequences

	Sequence		Length	Mass (Da)
	P12015 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 4FBF0915C7BD25D2	FASTA	543	60,892
	10 20 30 40 50 60 MSQKMDFDAI VIGGGFGGLY AVKKLRDELE LKVQAFDKAT DVAGTWYWNR YPGALTDTET 70 80 90 100 110 120 HLYCYSWDKE LLQSLEIKKK YVQGPDVRKY LQQVAEKHDL KKSYQFNTAV QSAHYNEADA 130 140 150 160 170 180 LWEVTTEYGD KYTARFLITA LGLLSAPNLP NIKGINQFKG ELHHTSRWPD DVSFEGKRVG 190 200 210 220 230 240 VIGTGSTGVQ VITAVAPLAK HLTVFQRSAQ YSVPIGNDPL SEEDVKKIKD NYDKSLGWCM 250 260 270 280 290 300 NSALAFALNE STVPAMSVSA EERKAVFEKA WQTGGGFRFM FETFGDIATN MEANIEAQNF 310 320 330 340 350 360 IKGKIAEIVK DPAIAQKLMP QDLYAKRPLC DSGYYNTFNR DNVRLEDVKA NPIVEITENG 370 380 390 400 410 420 VKLENGDFVE LDMLICATGF DAVDGNYVRM DIQGKNGLAM KDYWKEGPSS YMGVTVNNYP 430 440 450 460 470 480 NMFMVLGPNG PFTNLPPSIE SQVEWISDTI QYTVENNVES IEATKEAEEQ WTQTCANIAE 490 500 510 520 530 540 MTLFPKAQSW IFGANIPGKK NTVYFYLGGL KEYRTCASNC KNHAYEGFDI QLQRSDIKQP ANA

References

[1]	"Acinetobacter cyclohexanone monooxygenase: gene cloning and sequence determination." Chen Y.-C.J., Peoples O.P., Walsh C.T. J. Bacteriol. 170:781-789(1988) [PubMed: 3338974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-12. Strain: NCIB 9871.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M19029 Genomic DNA. Translation: AAA21892.1.
PIR	A28550.
3D structure databases
ProteinModelPortal	P12015.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR020946. Flavin_mOase-like. [Graphical view]
Pfam	PF00743. FMO-like. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYMO_ACISP

Accession

Primary (citable) accession number: P12015

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	June 28, 2011
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program