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Q72S74 (DEF_LEPIC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peptide deformylase
Short name=PDF
EC=3.5.1.88
Alternative name(s):
Polypeptide deformylase
Gene names
Name:def
Ordered Locus Names:LIC_11511
OrganismLeptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130) [Complete proteome] [HAMAP]
Taxonomic identifier267671 [NCBI]
Taxonomic lineageBacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira ›

Protein attributes

Sequence length178 AA.
Sequence statusComplete.
Protein existenceInferred 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. HAMAP-Rule MF_00163

Catalytic activity

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. HAMAP-Rule MF_00163

Cofactor

Binds 1 Fe2+ ion By similarity.

Sequence similarities

Belongs to the polypeptide deformylase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   LigandIron
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtranslation

Inferred from electronic annotation. Source: HAMAP

   Molecular_functioniron ion binding

Inferred from electronic annotation. Source: InterPro

peptide deformylase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 178178Peptide deformylase HAMAP-Rule MF_00163
PRO_0000082794

Sites

Active site1451 By similarity
Metal binding1021Iron By similarity
Metal binding1441Iron By similarity
Metal binding1481Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q72S74 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 8F6F3D2449A48B10

FASTA17820,379
        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

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016823 Genomic DNA. Translation: AAS70108.1.
RefSeqYP_001471.1. NC_005823.1.

3D structure databases

ProteinModelPortalQ72S74.
SMRQ72S74. Positions 2-178.
ModBaseSearch...

Protein-protein interaction databases

STRING267671.LIC11511.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS70108; AAS70108; LIC_11511.
GeneID2771725.
KEGGlic:LIC11511.
PATRIC22375369. VBILepInt6257_1851.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01462.
OMAEGCESIR.
ProtClustDBPRK12846.

Enzyme and pathway databases

BioCycLINT267671:GHQI-1780-MONOMER.

Family and domain databases

Gene3D3.90.45.10. 1 hit.
HAMAPMF_00163. Pep_deformylase.
InterProIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
PANTHERPTHR10458. PTHR10458. 1 hit.
PfamPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFPIRSF004749. Pep_def. 1 hit.
PRINTSPR01576. PDEFORMYLASE.
SUPFAMSSF56420. Fmet_deformylase. 1 hit.
TIGRFAMsTIGR00079. pept_deformyl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDEF_LEPIC
AccessionPrimary (citable) accession number: Q72S74
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: July 5, 2004
Last modified: May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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