Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q92IZ1 (DEF1_RICCN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptide deformylase 1
Short name=PDF 1
EC=3.5.1.88
Alternative name(s):
Polypeptide deformylase 1
Gene names
Name:def1
Ordered Locus Names:RC0278
OrganismRickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]
Taxonomic identifier272944 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › spotted fever group ›

Protein attributes

Sequence length175 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. HAMAP-Rule MF_00163

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 – 175175Peptide deformylase 1 HAMAP-Rule MF_00163
PRO_0000082829

Sites

Active site1421 By similarity
Metal binding991Iron By similarity
Metal binding1411Iron By similarity
Metal binding1451Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92IZ1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 93B050C6003C5A6D

FASTA17520,280
        10         20         30         40         50         60 
MSILPIVTAP DERLKQKSQP VLEFTDQTRK FMDDMLKTMY HEDGAGLAAV QVGVLKRILV 

        70         80         90        100        110        120 
IDIQDHDSVA RPKDFYPLFI VNPEIIEKAE ELVTANEGCI SLPEQRIEVA RPESIKIRYL 

       130        140        150        160        170 
DYHGKSRELK ANDWLARVIQ HEYDHLEGKL MIDYLSNLKR DVVLRKLKKL KNNIV

« Hide

References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE006914 Genomic DNA. Translation: AAL02816.1.
PIRF97734.
RefSeqNP_359915.1. NC_003103.1.

3D structure databases

ProteinModelPortalQ92IZ1.
ModBaseSearch...

Protein-protein interaction databases

STRING272944.RC0278.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL02816; AAL02816; RC0278.
GeneID927899.
KEGGrco:RC0278.
PATRIC17887717. VBIRicCon45613_0318.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243509.
KOK01462.
OMAMILPINI.
ProtClustDBPRK00150.

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 nameDEF1_RICCN
AccessionPrimary (citable) accession number: Q92IZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: December 1, 2001
Last modified: May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Rickettsia conorii

(strain Malish 7): entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents