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Reviewed, UniProtKB/Swiss-Prot O05100 (DEF1_CLOAB)

Last modified November 3, 2009. Version 66. 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: CA_C1722
OrganismClostridium acetobutylicum [Complete proteome] [HAMAP]
Taxonomic identifier1488 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length150 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. HAMAP 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
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 – 150150Peptide deformylase 1 HAMAP MF_00163
PRO_0000082766

Sites

Active site1311 By similarity
Metal binding881Iron By similarity
Metal binding1301Iron By similarity
Metal binding1341Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
O05100-1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 07760E6A5CB2606D

FASTA15016,617
        10         20         30         40         50         60 
MAIRSIRKYG DELLRKKSRK VEKIDKRLLT LIDDMFETMY NADGVGLAAP QVGILKRLVV 

        70         80         90        100        110        120 
IDVGEGPVVL INPEILETSG KAVDVEGCLS IPERQGEVER PTYVKAKALN EKGEEIVIEA 

       130        140        150 
EDLFARAICH ETDHLNGVLF VDKLAESEGN 

« Hide

References

« Hide 'large scale' references
[1]"Complementation of an Escherichia coli polypeptide deformylase mutant with a gene from Clostridium acetobutylicum ATCC 824."
Belouski E., Gui L., Rudolph F.B., Bennett G.N.
Curr. Microbiol. 36:248-249(1998) [PubMed: 9504995] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.
[2]"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum."
Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.
J. Bacteriol. 183:4823-4838(2001) [PubMed: 11466286] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

Cross-references

Sequence databases

U52368 Genomic DNA. Translation: AAB50347.1.
AE001437 Genomic DNA. Translation: AAK79688.1.
PIRE97112.
RefSeqNP_348348.1.

3D structure databases

HSSPHSSP built from PDB template 1LME based on UniProtKB P96113.
ModBaseSearch...

Genome annotation databases

GeneID1117905.
GenomeReviewsGene locus CA_C1722 in contig AE001437_GR.
KEGGcac:CAC1722.
NMPDRfig|272562.1.peg.1877.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO05100.
OMAIIMHEND.

Enzyme and pathway databases

BioCycCACE272562:CAC1722-MON.
BRENDA3.5.1.88. 2866.

Family and domain databases

HAMAPMF_00163.
[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.
ProDomPD003844. Fmet_deformylase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00079. pept_deformyl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDEF1_CLOAB
AccessionPrimary (citable) accession number: O05100
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: November 3, 2009
This is version 66 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