[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CRYSTALLIZATION. STRAIN=Lai / Serogroup Icterohaemorrhagiae / Serovar lai; DOI=10.1107/S0907444902003736; PubMed=11976499 [NCBI, ExPASy, EBI, Israel, Japan] Li Y., Ren S., Gong W.; "Cloning, high-level expression, purification and crystallization of peptide deformylase from Leptospira interrogans."; Acta Crystallogr. D 58:846-848(2002).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=56601 / Serogroup Icterohaemorrhagiae / Serovar lai; DOI=10.1038/nature01597; PubMed=12712204 [NCBI, ExPASy, EBI, Israel, Japan] Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.; "Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing."; Nature 422:888-893(2003).
[3]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND SUBUNIT. STRAIN=Lai / Serogroup Icterohaemorrhagiae / Serovar lai; DOI=10.1016/j.jmb.2004.03.045; PubMed=15123432 [NCBI, ExPASy, EBI, Israel, Japan] Zhou Z., Song X., Li Y., Gong W.; "Unique structural characteristics of peptide deformylase from pathogenic bacterium Leptospira interrogans."; J. Mol. Biol. 339:207-215(2004).

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).
SUBUNIT: Homodimer.
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

AY040678; AAK70806.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE010300; AAN49637.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_712619.1; -.

3D structure databases

PDB

1SV2; X-ray; 3.00 A; A/B=2-178.	[ExPASy / RCSB / EBI]
1SZZ; X-ray; 3.30 A; A/B/C/D/E/F/G/H=2-178.	[ExPASy / RCSB / EBI]
1VEV; X-ray; 2.51 A; A/B=2-178.	[ExPASy / RCSB / EBI]
1VEY; X-ray; 3.30 A; A/B=2-178.	[ExPASy / RCSB / EBI]
1VEZ; X-ray; 2.30 A; A/B=2-178.	[ExPASy / RCSB / EBI]
1Y6H; X-ray; 2.20 A; A/B=2-178.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1SV2; -.
1SZZ; -.
1VEV; -.
1VEY; -.
1VEZ; -.
1Y6H; -.

ModBase

Q93LE9.

Enzyme and pathway databases

BioCyc

LINT-130-01:LINT-130-01-001471-MON; -.
LINT189518:LA2438-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.

BLOCKS

Q93LE9.

Genome annotation databases

GeneID

1151781; -.

GenomeReviews

AE010300_GR; LA_2438.

KEGG

lil:LA2438; -.

Phylogenomic databases

HOGENOM

Q93LE9; -.

Genome annotation databases

CMR

Q93LE9; LA_2438.

Other

ProtoNet

Q93LE9.

UniRef

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

Keywords

3D-structure; 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_0000082795`
`ACT_SITE`	`145 145`		`By similarity.`
`METAL`	`102 102`		`Iron (By similarity).`
`METAL`	`144 144`		`Iron (By similarity).`
`METAL`	`148 148`		`Iron (By similarity).`
`HELIX`	`12 15`	`4`
`HELIX`	`25 27`	`3`
`HELIX`	`29 44`	`16`
`STRAND`	`48 51`	`4`
`HELIX`	`52 55`	`4`
`STRAND`	`59 64`	`6`
`STRAND`	`70 72`	`3`
`STRAND`	`81 90`	`10`
`STRAND`	`98 100`	`3`
`STRAND`	`108 112`	`5`
`STRAND`	`115 123`	`9`
`STRAND`	`129 135`	`7`
`HELIX`	`136 149`	`14`
`HELIX`	`154 157`	`4`
`STRAND`	`163 166`	`4`
`HELIX`	`167 171`	`5`

Sequence information

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

Molecular weight: 20379 Da [This is the MW of the unprocessed precursor]

CRC64: 8F6F3D2449A48B10 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSVRKILRMG DPILRKISEP VTEDEIQTKE FKKLIRDMFD TMRHAEGVGL AAPQIGILKQ 

        70         80         90        100        110        120 
IVVVGSEDNE RYPGTPDVPE RIILNPVITP LTKDTSGFWE GCLSVPGMRG YVERPNQIRM 

       130        140        150        160        170 
QWMDEKGNQF DETIDGYKAI VYQHECDHLQ GILYVDRLKD TKLFGFNETL DSSHNVLD

Q93LE9 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