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Protein

Peptide deformylase

Gene

def

Organism
Chlamydia trachomatis (strain D/UW-3/Cx)
Status
Reviewed-Annotation score: Annotation score: 3 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)DescriptionActionsGraphical viewLength
Metal bindingi99IronBy similarity1
Metal bindingi141IronBy similarity1
Active sitei142By similarity1
Metal bindingi145IronBy similarity1

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 (EC:3.5.1.88)
Short name:
PDF
Alternative name(s):
Polypeptide deformylase
Gene namesi
Name:def
Ordered Locus Names:CT_353
OrganismiChlamydia trachomatis (strain D/UW-3/Cx)
Taxonomic identifieri272561 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
Proteomesi
  • UP000000431 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000827641 – 181Peptide deformylaseAdd BLAST181

Interactioni

Protein-protein interaction databases

STRINGi272561.CT353.

Structurei

3D structure databases

ProteinModelPortaliO84357.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the polypeptide deformylase family.Curated

Phylogenomic databases

eggNOGiENOG4108Z02. Bacteria.
COG0242. LUCA.
InParanoidiO84357.
KOiK01462.
OMAiVCIQHEI.

Family and domain databases

CDDicd00487. Pep_deformylase. 1 hit.
Gene3Di3.90.45.10. 1 hit.
HAMAPiMF_00163. Pep_deformylase. 1 hit.
InterProiIPR023635. 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.

O84357-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIRDLEYYDS PILRKVAAPV TEITDELRQL VLDMSETMAF YKGVGLAAPQ
60 70 80 90 100
VGQSISLFIM GVERELEDGE LVFCDFPRVF INPVITQKSE QLVYGNEGCL
110 120 130 140 150
SIPGLRGEVA RPDKITVSAK NLDGQQFSLA LEGFLARIVM HETDHLHGVL
160 170 180
YIDRMSDKDK TKQFKNNLEK IRRKYSILRG L
Length:181
Mass (Da):20,523
Last modified:November 1, 1998 - v1
Checksum:iA3FD251E4DFB96DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001273 Genomic DNA. Translation: AAC67948.1.
PIRiB71526.
RefSeqiNP_219861.1. NC_000117.1.
WP_009871704.1. NC_000117.1.

Genome annotation databases

EnsemblBacteriaiAAC67948; AAC67948; CT_353.
GeneIDi884763.
KEGGictr:CT_353.
PATRICi20380251. VBIChlTra43535_0381.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001273 Genomic DNA. Translation: AAC67948.1.
PIRiB71526.
RefSeqiNP_219861.1. NC_000117.1.
WP_009871704.1. NC_000117.1.

3D structure databases

ProteinModelPortaliO84357.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272561.CT353.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC67948; AAC67948; CT_353.
GeneIDi884763.
KEGGictr:CT_353.
PATRICi20380251. VBIChlTra43535_0381.

Phylogenomic databases

eggNOGiENOG4108Z02. Bacteria.
COG0242. LUCA.
InParanoidiO84357.
KOiK01462.
OMAiVCIQHEI.

Family and domain databases

CDDicd00487. Pep_deformylase. 1 hit.
Gene3Di3.90.45.10. 1 hit.
HAMAPiMF_00163. Pep_deformylase. 1 hit.
InterProiIPR023635. 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...

Entry informationi

Entry nameiDEF_CHLTR
AccessioniPrimary (citable) accession number: O84357
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: October 5, 2016
This is version 99 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.