[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=VK1; PubMed=7961514 [NCBI, ExPASy, EBI, Israel, Japan] Meinnel T., Blanquet S.; "Characterization of the Thermus thermophilus locus encoding peptide deformylase and methionyl-tRNA(fMet) formyltransferase."; J. Bacteriol. 176:7387-7390(1994).
[2]	CHARACTERIZATION. DOI=10.1006/jmbi.1997.0904; PubMed=9126850 [NCBI, ExPASy, EBI, Israel, Japan] Meinnel T., Lazennec C., Villoing S., Blanquet S.; "Structure-function relationships within the peptide deformylase family. Evidence for a conserved architecture of the active site involving three conserved motifs and a metal ion."; J. Mol. Biol. 267:749-761(1997).

Comments

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

X79087; CAA55695.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1V3Y; X-ray; 1.81 A; A/B=1-192.

[ExPASy / RCSB / EBI]

PDBsum

1V3Y; -.

ModBase

P43522.

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.

Other

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

Keywords

3D-structure; Hydrolase; Iron; Metal-binding; Protein biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 192`	`192`	`Peptide deformylase.`	`PRO_0000082867`
`ACT_SITE`	`146 146`		`By similarity.`
`METAL`	`102 102`		`Iron (By similarity).`
`METAL`	`145 145`		`Iron (By similarity).`
`METAL`	`149 149`		`Iron (By similarity).`
`HELIX`	`11 14`	`4`
`HELIX`	`26 39`	`14`
`STRAND`	`43 46`	`4`
`HELIX`	`47 50`	`4`
`STRAND`	`54 60`	`7`
`TURN`	`75 77`	`3`
`STRAND`	`81 93`	`13`
`STRAND`	`96 100`	`5`
`STRAND`	`110 115`	`6`
`STRAND`	`117 124`	`8`
`STRAND`	`130 136`	`7`
`HELIX`	`137 150`	`14`
`HELIX`	`155 158`	`4`
`HELIX`	`161 170`	`10`
`HELIX`	`172 181`	`10`

Sequence information

Length: 192 AA [This is the length of the unprocessed precursor]

Molecular weight: 22092 Da [This is the MW of the unprocessed precursor]

CRC64: 665945183A251361 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVYPIRLYGD PVLRRKARPV EDFSGIKRLA EDMLETMFEA KGVGLAAPQI GLSQRLFVAV 

        70         80         90        100        110        120 
EYADEPEGEE ERPLRELVRR VYVVANPVIT YREGLVEGTE GCLSLPGLYS EEVPRAERIR 

       130        140        150        160        170        180 
VEYQDEEGRG RVLELEGYMA RVFQHEIDHL DGILFFERLP KPKREAFLEA NRAELVRFQK 

       190 
EARALLKELS QG

P43522 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