FUNCTION: Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity).
CATALYTIC ACTIVITY: Formyl-L-methionyl peptide + H₂O = formate + methionyl peptide.
COFACTOR: Binds 1 Fe(2+) ion (By similarity).
SIMILARITY: Belongs to the polypeptide deformylase 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

BA000016; BAB81339.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_562549.1; -.

3D structure databases

HSSP

P27251; 1DEF. [HSSP ENTRY / PDB]

ModBase

Q8XJX0.

Enzyme and pathway databases

BioCyc

CPER195102:CPE1633-MON; -.

Ontologies

GO:0042586;	Molecular function: peptide deformylase activity (inferred from electronic annotation from HAMAP).
GO:0006412;	Biological process: translation (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00163; -; 1.
PBIL [Tree]

InterPro

IPR000181; Fmet_deformylase.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.45.10; Fmet_deformylase; 1.

PANTHER

PTHR10458; Fmet_deformylase; 1.

Pfam

PF01327; Pep_deformylase; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF004749; Pep_def; 1.

PRINTS

PR01576; PDEFORMYLASE.

ProDom

PD003844; Fmet_deformylase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00079; pept_deformyl; 1.

Genome annotation databases

GeneID

989943; -.

GenomeReviews

BA000016_GR; CPE1633.

KEGG

cpe:CPE1633; -.

NMPDR

fig|195102.1.peg.1696; -.

Phylogenomic databases

HOGENOM

Q8XJX0; -.

Genome annotation databases

CMR

Q8XJX0; CPE1633.

Other

UniRef

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

Keywords

Complete proteome; Hydrolase; Iron; Metal-binding; Protein biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 155`	`155`	`Peptide deformylase 2.`	`PRO_0000082770`
`ACT_SITE`	`133 133`		`By similarity.`
`METAL`	`90 90`		`Iron (By similarity).`
`METAL`	`132 132`		`Iron (By similarity).`
`METAL`	`136 136`		`Iron (By similarity).`

Sequence information

Length: 155 AA [This is the length of the unprocessed precursor]

Molecular weight: 17505 Da [This is the MW of the unprocessed precursor]

CRC64: 6E2AD1401F72B337 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVKKIVQIG HEALKKVSEP VKDVNEVKGL IQDLKDTLAT VEGIGLAAPQ IAVNKRVVYI 

        70         80         90        100        110        120 
NFGDGENEYV LINPEVTGVS KETYEDYEGC LSYVMHEGLV ERPRAVRIQA LNEKGELKVY 

       130        140        150 
EAQDLLARCF LHEIDHLEGI MYVDRAKEMY ELVEK

Q8XJX0 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