[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=WCUH29 / NCIMB 40771; Lonetto M.A., Sylvester D.R., Warren R.L.; "Staphylococcus aureus deformylase 1 encoding DNA."; Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
[2]	MASS SPECTROMETRY. STRAIN=MRSA-M2; DOI=10.1128/IAI.00392-06; PubMed=16714572 [NCBI, ExPASy, EBI, Israel, Japan] Brady R.A., Leid J.G., Camper A.K., Costerton J.W., Shirtliff M.E.; "Identification of Staphylococcus aureus proteins recognized by the antibody-mediated immune response to a biofilm infection."; Infect. Immun. 74:3415-3426(2006).
[3]	X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS). DOI=10.1016/S0022-2836(03)00596-5; PubMed=12823970 [NCBI, ExPASy, EBI, Israel, Japan] Kreusch A., Spraggon G., Lee C.C., Klock H., McMullan D., Ng K., Shin T., Vincent J., Warner I., Ericson C., Lesley S.A.; "Structure analysis of peptide deformylases from Streptococcus pneumoniae, Staphylococcus aureus, Thermotoga maritima and Pseudomonas aeruginosa: snapshots of the oxygen sensitivity of peptide deformylase."; J. Mol. Biol. 330:309-321(2003).

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).
MASS SPECTROMETRY: Mass=20600; Method=MALDI; Range=1-183; Source=PubMed:16714572;.
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

AY007227; AAG02249.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1LM4; X-ray; 1.45 A; A/B=1-183.	[ExPASy / RCSB / EBI]
1LMH; X-ray; 1.90 A; A=1-183.	[ExPASy / RCSB / EBI]
1LQW; X-ray; 1.87 A; A/B=1-183.	[ExPASy / RCSB / EBI]
1Q1Y; X-ray; 1.90 A; A=1-183.	[ExPASy / RCSB / EBI]
2AI9; X-ray; 2.50 A; A/B=1-183.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1LM4; -.
1LMH; -.
1LQW; -.
1Q1Y; -.
2AI9; -.

ModBase

P68826.

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`	`1 183`	`183`	`Peptide deformylase.`	`PRO_0000082843`
`ACT_SITE`	`155 155`		`By similarity.`
`METAL`	`111 111`		`Iron.`
`METAL`	`154 154`		`Iron.`
`METAL`	`158 158`		`Iron.`
`HELIX`	`4 6`	`3`
`HELIX`	`13 16`	`4`
`HELIX`	`28 45`	`18`
`HELIX`	`47 53`	`7`
`STRAND`	`58 62`	`5`
`HELIX`	`63 66`	`4`
`STRAND`	`70 77`	`8`
`STRAND`	`81 83`	`3`
`STRAND`	`86 98`	`13`
`STRAND`	`100 104`	`5`
`STRAND`	`124 133`	`10`
`STRAND`	`139 145`	`7`
`HELIX`	`146 159`	`14`
`HELIX`	`164 167`	`4`
`STRAND`	`170 172`	`3`

Sequence information

Length: 183 AA [This is the length of the unprocessed precursor]

Molecular weight: 20559 Da [This is the MW of the unprocessed precursor]

CRC64: 32A64066A6FEAB0E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLTMKDIIRD GHPTLRQKAA ELELPLTKEE KETLIAMREF LVNSQDEEIA KRYGLRSGVG 

        70         80         90        100        110        120 
LAAPQINISK RMIAVLIPDD GSGKSYDYML VNPKIVSHSV QEAYLPTGEG CLSVDDNVAG 

       130        140        150        160        170        180 
LVHRHNRITI KAKDIEGNDI QLRLKGYPAI VFQHEIDHLN GVMFYDHIDK NHPLQPHTDA 


VEV

P68826 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