Skip Header

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

Q3B2U9 (DEF_PELLD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
Short name=PDF
EC=3.5.1.88
Alternative name(s):
Polypeptide deformylase
Gene names
Name:def
Ordered Locus Names:Plut_1473
OrganismPelodictyon luteolum (strain DSM 273) (Chlorobium luteolum (strain DSM 273)) [Complete proteome] [HAMAP]
Taxonomic identifier319225 [NCBI]
Taxonomic lineageBacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobium/Pelodictyon group › Pelodictyon

Protein attributes

Sequence length190 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 MF_00163

Catalytic activity

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

Cofactor

Binds 1 Fe2+ ion By similarity. HAMAP 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: UniProtKB-KW

   Molecular functioniron ion binding

Inferred from electronic annotation. Source: InterPro

peptide deformylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 190190Peptide deformylase HAMAP MF_00163
PRO_0000301076

Sites

Active site1371 By similarity
Metal binding941Iron By similarity
Metal binding1361Iron By similarity
Metal binding1401Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3B2U9 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 107111E44D2FD063

FASTA19021,026
        10         20         30         40         50         60 
MILPINTYSD EVLHQKAKPL KGVDADISSL IDSMFESMEN ASGIGLAAPQ VGCSIRLLVL 

        70         80         90        100        110        120 
DVSCMKSYED VPPMVVINPN VLAVRGKNLM EEGCLSVPGV QGDVLRPSEI TLKYRDRNFQ 

       130        140        150        160        170        180 
EHTEEFSGML ARVLQHEIDH LNGTLFVDRM EKRDRRRIQQ ELDDIAAGLV PADYPIAREC 

       190 
SRGGEGPACM

« Hide

References

[1]"Complete sequence of Pelodictyon luteolum DSM 273."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 273.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000096 Genomic DNA. Translation: ABB24332.1.
RefSeqYP_375375.1. NC_007512.1.

3D structure databases

HSSPHSSP built from PDB template 1XEO based on UniProtKB P0A6K3.
ProteinModelPortalQ3B2U9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3B2U9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3745461.
GenomeReviewsGene locus Plut_1473 in contig CP000096_GR.
KEGGplt:Plut_1473.
NMPDRfig|319225.3.peg.1457.
PATRIC21380584. VBIChlLut1287_1550.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHBG665227.
OMAGRCIQHE.
PhylomeDBQ3B2U9.
ProtClustDBPRK14598.

Enzyme and pathway databases

BioCycPLUT319225:PLUT_1473-MONOMER.

Family and domain databases

HAMAPMF_00163. Pep_deformylase.
[Tree]
InterProIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
Gene3DG3DSA:3.90.45.10. Fmet_deformylase. 1 hit.
KOK01462.
PANTHERPTHR10458. Fmet_deformylase. 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_PELLD
AccessionPrimary (citable) accession number: Q3B2U9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: November 22, 2005
Last modified: January 25, 2012
This is version 40 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

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