Reviewed, UniProtKB/Swiss-Prot Q8XJX0 (DEF2_CLOPE)

Names and origin

Protein names

Recommended name:
    Peptide deformylase 2
      Short name=PDF 2
    EC=3.5.1.88
Alternative name(s):
    Polypeptide deformylase 2

Gene names

Name:	def2
Ordered Locus Names:	CPE1633

Organism

Clostridium perfringens [Complete proteome] [HAMAP]

Taxonomic identifier

1502 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	155 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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. HAMAP MF_00163
Cofactor	Binds 1 Fe2+ ion By similarity.
Sequence similarities	Belongs to the polypeptide deformylase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Ligand	Iron Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	translation Inferred from electronic annotation. Source: HAMAP
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW peptide deformylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 155	155	Peptide deformylase 2 HAMAP MF_00163		PRO_0000082770
Sites
	Active site	133	1	By similarity
	Metal binding	90	1	Iron By similarity
	Metal binding	132	1	Iron By similarity
	Metal binding	136	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8XJX0-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 6E2AD1401F72B337	FASTA	155	17,505
	10 20 30 40 50 60 MAVKKIVQIG HEALKKVSEP VKDVNEVKGL IQDLKDTLAT VEGIGLAAPQ IAVNKRVVYI 70 80 90 100 110 120 NFGDGENEYV LINPEVTGVS KETYEDYEGC LSYVMHEGLV ERPRAVRIQA LNEKGELKVY 130 140 150 EAQDLLARCF LHEIDHLEGI MYVDRAKEMY ELVEK

References

[1]

"Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater." Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H. Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002) [PubMed: 11792842] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 13 / Type A.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000016 Genomic DNA. Translation: BAB81339.1.
RefSeq	NP_562549.1.
3D structure databases
HSSP	HSSP built from PDB template 1DEF based on UniProtKB P27251.
ModBase	Search...
Genome annotation databases
GeneID	989943.
GenomeReviews	Gene locus CPE1633 in contig BA000016_GR.
KEGG	cpe:CPE1633.
NMPDR	fig|195102.1.peg.1696.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8XJX0.
OMA	YITHISA.
Enzyme and pathway databases
BioCyc	CPER195102:CPE1633-MON.
BRENDA	3.5.1.88. 2406.
Family and domain databases
HAMAP	MF_00163. [Tree]
InterPro	IPR000181. Fmet_deformylase. [Graphical view]
Gene3D	G3DSA:3.90.45.10. Fmet_deformylase. 1 hit.
PANTHER	PTHR10458. Fmet_deformylase. 1 hit.
Pfam	PF01327. Pep_deformylase. 1 hit. [Graphical view]
PIRSF	PIRSF004749. Pep_def. 1 hit.
PRINTS	PR01576. PDEFORMYLASE.
ProDom	PD003844. Fmet_deformylase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00079. pept_deformyl. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DEF2_CLOPE

Accession

Primary (citable) accession number: Q8XJX0

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	March 1, 2002
Last modified:	November 3, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)