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

CP000453; ABI57968.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_743458.1; -.

3D structure databases

ModBase

Q0A5B9.

Ontologies

GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
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

4270673; -.

GenomeReviews

CP000453_GR; Mlg_2628.

KEGG

aeh:Mlg_2628; -.

NMPDR

fig|187272.6.peg.2505; -.

Phylogenomic databases

HOGENOM

Q0A5B9; -.

Genome annotation databases

CMR

Q0A5B9; Mlg_2628.

Other

ProtoNet

Q0A5B9.

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`	`1 178`	`178`	`Peptide deformylase.`	`PRO_0000301001`
`ACT_SITE`	`135 135`		`By similarity.`
`METAL`	`92 92`		`Iron (By similarity).`
`METAL`	`134 134`		`Iron (By similarity).`
`METAL`	`138 138`		`Iron (By similarity).`

Sequence information

Length: 178 AA [This is the length of the unprocessed precursor]

Molecular weight: 20034 Da [This is the MW of the unprocessed precursor]

CRC64: 861FC10DE50CB5E7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAILDILVYP DPRLREVAAP VAQVDDDIRR LADDMLETMY DAQGIGLAAT QVGVNQRVVV 

        70         80         90        100        110        120 
MDLAEEGARQ PLVLINPEIL DREGAATGQE GCLSIPGFYE DVERAERIRF RALDREGRPW 

       130        140        150        160        170 
EQEAEGLMAV CVQHEIDHLD GKLFVDYLSE LKRKRIRRKL EKLVRQGRVN VGGQTGRA

Q0A5B9 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