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Reviewed, UniProtKB/Swiss-Prot Q7V8G6 (DEF1_PROMM)

Last modified February 9, 2010. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptide deformylase 1
      Short name=PDF 1
    EC=3.5.1.88
Alternative name(s):
    Polypeptide deformylase 1
Gene names
Name: def1
Ordered Locus Names: PMT_0384
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchlorophytesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length192 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: HAMAP

   Molecular functioniron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptide deformylase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 192192Peptide deformylase 1 HAMAP MF_00163
PRO_0000082816

Sites

Active site1441 By similarity
Metal binding1011Iron By similarity
Metal binding1431Iron By similarity
Metal binding1471Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7V8G6-1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: B4E6FE0084A6FC95

FASTA19220,788
        10         20         30         40         50         60 
MAVKEILRMG NPQLRKVSNV VDDASDELII SLIKDLQDTV KAHQGAGLAA PQIGVPLRVV 

        70         80         90        100        110        120 
LFGGGGPNPR YPEAPSIPQT LLINPVLTPI GSDLEDGWEG CLSVPGLRGK VSRWSRIHYR 

       130        140        150        160        170        180 
ALNEDGFEVE HCLEGFPARV IQHECDHLDG VLFPDRLVDS ASFGFTGELE TAGIIEKLSS 

       190 
AEQKASQQSR AD 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed: 12917642] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548175 Genomic DNA. Translation: CAE20559.1.
RefSeqNP_894217.1.

3D structure databases

SMRQ7V8G6. Positions 2-171.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7V8G6.

Genome annotation databases

GeneID1728773.
GenomeReviewsGene locus PMT_0384 in contig BX548175_GR.
KEGGpmt:PMT0384.
NMPDRfig|74547.1.peg.384.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHBG665227.
OMARVIQHEC.

Enzyme and pathway databases

BioCycPMAR74547:PMT0384-MONOMER.

Family and domain databases

HAMAPMF_00163. Pep_deformylase.
[Tree]
InterProIPR000181. Fmet_deformylase.
[Graphical view]
Gene3DG3DSA:3.90.45.10. Fmet_deformylase. 1 hit.
PANTHERPTHR10458. Fmet_deformylase. 1 hit.
PfamPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFPIRSF004749. Pep_def. 1 hit.
PRINTSPR01576. PDEFORMYLASE.
TIGRFAMsTIGR00079. pept_deformyl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDEF1_PROMM
AccessionPrimary (citable) accession number: Q7V8G6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: February 9, 2010
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents