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Protein

Peptide deformylase

Gene

def

Organism
Mycobacterium sp. (strain MCS)
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.UniRule annotation

Catalytic activityi

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

Cofactori

Fe2+UniRule annotationNote: Binds 1 Fe2+ ion.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi106 – 1061IronUniRule annotation
Metal bindingi148 – 1481IronUniRule annotation
Active sitei149 – 1491UniRule annotation
Metal bindingi152 – 1521IronUniRule annotation

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. peptide deformylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMSP164756:GHQ8-574-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide deformylaseUniRule annotation (EC:3.5.1.88UniRule annotation)
Short name:
PDFUniRule annotation
Alternative name(s):
Polypeptide deformylaseUniRule annotation
Gene namesi
Name:defUniRule annotation
Ordered Locus Names:Mmcs_0569
OrganismiMycobacterium sp. (strain MCS)
Taxonomic identifieri164756 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000001972: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 197197Peptide deformylasePRO_0000301062Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi164756.Mmcs_0569.

Structurei

3D structure databases

ProteinModelPortaliQ1BEJ4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the polypeptide deformylase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0242.
HOGENOMiHOG000243508.
KOiK01462.
OMAiEHMLGSA.
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.

Q1BEJ4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVVPIRIVG DPVLRTETTP IPVGDDGSLP AEVADLIRDL YETMDAANGV
60 70 80 90 100
GLAANQIGVS QRVFVYDCPD SRGRAGRRRG VVINPVLETS DIPETMPDPD
110 120 130 140 150
DDEEGCLSVP GEQFPTGRAD WARVTGLDAD GSPITVEGTG LFARMLQHET
160 170 180 190
GHLDGFLYLD RLIGRHARAA KRAVKHNGWG VPGLSWTPGE DPDPFGH
Length:197
Mass (Da):21,146
Last modified:July 11, 2006 - v1
Checksum:iCA23ED63701DC671
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000384 Genomic DNA. Translation: ABG06690.1.
RefSeqiYP_637746.1. NC_008146.1.

Genome annotation databases

EnsemblBacteriaiABG06690; ABG06690; Mmcs_0569.
GeneIDi4109415.
KEGGimmc:Mmcs_0569.
PATRICi18111247. VBIMycSp106721_0586.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000384 Genomic DNA. Translation: ABG06690.1.
RefSeqiYP_637746.1. NC_008146.1.

3D structure databases

ProteinModelPortaliQ1BEJ4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi164756.Mmcs_0569.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABG06690; ABG06690; Mmcs_0569.
GeneIDi4109415.
KEGGimmc:Mmcs_0569.
PATRICi18111247. VBIMycSp106721_0586.

Phylogenomic databases

eggNOGiCOG0242.
HOGENOMiHOG000243508.
KOiK01462.
OMAiEHMLGSA.
OrthoDBiEOG664CMF.

Enzyme and pathway databases

BioCyciMSP164756:GHQ8-574-MONOMER.

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: MCS.

Entry informationi

Entry nameiDEF_MYCSS
AccessioniPrimary (citable) accession number: Q1BEJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 11, 2006
Last modified: January 7, 2015
This is version 61 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. 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.