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Protein

Peptide deformylase 1

Gene

def1

Organism
Rickettsia conorii (strain ATCC VR-613 / Malish 7)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide.

Cofactori

Fe2+By similarityNote: Binds 1 Fe2+ ion.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi99 – 991IronBy similarity
Metal bindingi141 – 1411IronBy similarity
Active sitei142 – 1421By similarity
Metal bindingi145 – 1451IronBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide deformylase 1 (EC:3.5.1.88)
Short name:
PDF 1
Alternative name(s):
Polypeptide deformylase 1
Gene namesi
Name:def1
Ordered Locus Names:RC0278
OrganismiRickettsia conorii (strain ATCC VR-613 / Malish 7)
Taxonomic identifieri272944 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group
ProteomesiUP000000816 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 175175Peptide deformylase 1PRO_0000082829Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ92IZ1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the polypeptide deformylase family.Curated

Phylogenomic databases

eggNOGiCOG0242.
HOGENOMiHOG000243509.
KOiK01462.
OMAiFDTMYEE.
OrthoDBiEOG664CMF.

Family and domain databases

Gene3Di3.90.45.10. 1 hit.
HAMAPiMF_00163. Pep_deformylase.
InterProiIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
PANTHERiPTHR10458. PTHR10458. 1 hit.
PfamiPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFiPIRSF004749. Pep_def. 1 hit.
PRINTSiPR01576. PDEFORMYLASE.
SUPFAMiSSF56420. SSF56420. 1 hit.
TIGRFAMsiTIGR00079. pept_deformyl. 1 hit.

Sequencei

Sequence statusi: Complete.

Q92IZ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSILPIVTAP DERLKQKSQP VLEFTDQTRK FMDDMLKTMY HEDGAGLAAV
60 70 80 90 100
QVGVLKRILV IDIQDHDSVA RPKDFYPLFI VNPEIIEKAE ELVTANEGCI
110 120 130 140 150
SLPEQRIEVA RPESIKIRYL DYHGKSRELK ANDWLARVIQ HEYDHLEGKL
160 170
MIDYLSNLKR DVVLRKLKKL KNNIV
Length:175
Mass (Da):20,280
Last modified:December 1, 2001 - v1
Checksum:i93B050C6003C5A6D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006914 Genomic DNA. Translation: AAL02816.1.
PIRiF97734.
RefSeqiNP_359915.1. NC_003103.1.
WP_010976938.1. NC_003103.1.

Genome annotation databases

EnsemblBacteriaiAAL02816; AAL02816; RC0278.
GeneIDi927899.
KEGGirco:RC0278.
PATRICi17887717. VBIRicCon45613_0318.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006914 Genomic DNA. Translation: AAL02816.1.
PIRiF97734.
RefSeqiNP_359915.1. NC_003103.1.
WP_010976938.1. NC_003103.1.

3D structure databases

ProteinModelPortaliQ92IZ1.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL02816; AAL02816; RC0278.
GeneIDi927899.
KEGGirco:RC0278.
PATRICi17887717. VBIRicCon45613_0318.

Phylogenomic databases

eggNOGiCOG0242.
HOGENOMiHOG000243509.
KOiK01462.
OMAiFDTMYEE.
OrthoDBiEOG664CMF.

Family and domain databases

Gene3Di3.90.45.10. 1 hit.
HAMAPiMF_00163. Pep_deformylase.
InterProiIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
PANTHERiPTHR10458. PTHR10458. 1 hit.
PfamiPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFiPIRSF004749. Pep_def. 1 hit.
PRINTSiPR01576. PDEFORMYLASE.
SUPFAMiSSF56420. SSF56420. 1 hit.
TIGRFAMsiTIGR00079. pept_deformyl. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC VR-613 / Malish 7.

Entry informationi

Entry nameiDEF1_RICCN
AccessioniPrimary (citable) accession number: Q92IZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: December 1, 2001
Last modified: June 24, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Rickettsia conorii
    (strain Malish 7): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.