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A0QQP8 (DEF_MYCS2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:MSMEG_0832, MSMEI_0813
OrganismMycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP]
Taxonomic identifier246196 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium ›

Protein attributes

Sequence length197 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.

Sequence similarities

Belongs to the polypeptide deformylase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   LigandIron
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference 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 – 197197Peptide deformylase HAMAP-Rule MF_00163
PRO_0000301059

Sites

Active site1491 By similarity
Metal binding1061Iron By similarity
Metal binding1481Iron By similarity
Metal binding1521Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
A0QQP8 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 6305E1E7B6598980

FASTA19721,208
        10         20         30         40         50         60 
MAVVPIRIVG DPVLHTPTEP VPVGPDGSLP DDLPALIQDM FDTMDAANGV GLAANQIGVA 

        70         80         90        100        110        120 
KRLFVYDCAP TRGQTTRRRG VVINPVLETS EVPETMPDPD EDEEGCLSVP GENFPTGRAD 

       130        140        150        160        170        180 
WARVTGLDAD GSPITLEGED LFARMLQHET GHLDGFLYLD RLVGRYARAA KKAVKRNGWG 

       190 
VPGLSWMPGE VPDPFGH

« Hide

References

[1]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[2]"Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[3]"Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000480 Genomic DNA. Translation: ABK72853.1.
CP001663 Genomic DNA. Translation: AFP37293.1.
RefSeqYP_006565588.1. NC_018289.1.
YP_885236.1. NC_008596.1.

3D structure databases

ProteinModelPortalA0QQP8.
ModBaseSearch...

Protein-protein interaction databases

STRING246196.MSMEG_0832.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK72853; ABK72853; MSMEG_0832.
GeneID13427983.
4534679.
KEGGmsg:MSMEI_0813.
msm:MSMEG_0832.
PATRIC18074128. VBIMycSme59918_0825.

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243508.
KOK01462.
OMALIGRWKR.
ProtClustDBPRK00150.

Enzyme and pathway databases

BioCycMSME246196:GJ4Y-832-MONOMER.

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 nameDEF_MYCS2
AccessionPrimary (citable) accession number: A0QQP8
Secondary accession number(s): I7FEH2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: January 9, 2007
Last modified: May 1, 2013
This is version 50 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

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