NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
STRAIN=ATCC 1518;
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.
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

Y10549; CAA71581.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1LQY; X-ray; 1.90 A; A=1-184.

[ExPASy / RCSB / EBI]

PDBsum

1LQY; -.

ModBase

O31410.

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`	`1 184`	`184`	`Peptide deformylase 2.`	`PRO_0000082738`
`ACT_SITE`	`154 154`		`By similarity.`
`METAL`	`110 110`		`Iron (By similarity).`
`METAL`	`153 153`		`Iron (By similarity).`
`METAL`	`157 157`		`Iron (By similarity).`
`HELIX`	`4 6`	`3`
`HELIX`	`13 16`	`4`
`HELIX`	`28 44`	`17`
`HELIX`	`47 53`	`7`
`STRAND`	`59 62`	`4`
`HELIX`	`63 66`	`4`
`STRAND`	`70 78`	`9`
`STRAND`	`84 97`	`14`
`STRAND`	`99 104`	`6`
`STRAND`	`123 132`	`10`
`STRAND`	`138 144`	`7`
`HELIX`	`145 158`	`14`
`HELIX`	`163 166`	`4`
`STRAND`	`180 182`	`3`

Sequence information

Length: 184 AA [This is the length of the unprocessed precursor]

Molecular weight: 20383 Da [This is the MW of the unprocessed precursor]

CRC64: 9CD85DEE53632FA0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MITMKDIIKE GHPTLRKVAE PVPLPPSEED KRILQSLLDY VKMSQDPELA AKYGLRPGIG 

        70         80         90        100        110        120 
LAAPQINVSK RMIAVHVTDE NGTLYSYALF NPKIVSHSVQ QCYLTTGEGC LSVDRDVPGY 

       130        140        150        160        170        180 
VLRYARITVT GTTLDGEEVT LRLKGLPAIV FQHEIDHLNG IMFYDRINPA DPFQVPDGAI 


PIGR

O31410 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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