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C1AKA5 (DEF_MYCBT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 35. 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

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:JTY_0438
OrganismMycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019) [Complete proteome] [HAMAP]
Taxonomic identifier561275 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

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. HAMAP-Rule 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-HAMAP

   Molecular_functioniron ion binding

Inferred from electronic annotation. Source: InterPro

peptide deformylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 197197Peptide deformylase HAMAP-Rule MF_00163
PRO_1000200740

Sites

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

Sequences

Sequence LengthMass (Da)Tools
C1AKA5 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 14F2F655EDF01C93

FASTA19720,939
        10         20         30         40         50         60 
MAVVPIRIVG DPVLHTATTP VTVAADGSLP ADLAQLIATM YDTMDAANGV GLAANQIGCS 

        70         80         90        100        110        120 
LRLFVYDCAA DRAMTARRRG VVINPVLETS EIPETMPDPD TDDEGCLSVP GESFPTGRAK 

       130        140        150        160        170        180 
WARVTGLDAD GSPVSIEGTG LFARMLQHET GHLDGFLYLD RLIGRYARNA KRAVKSHGWG 

       190 
VPGLSWLPGE DPDPFGH 

« Hide

References

[1]"Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains."
Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.
Vaccine 27:1710-1716(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BCG / Tokyo 172 / ATCC 35737 / TMC 1019.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP010918 Genomic DNA. Translation: BAH24734.1.
RefSeqYP_002643502.1. NC_012207.1.

3D structure databases

ProteinModelPortalC1AKA5.
SMRC1AKA5. Positions 2-197.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561275.JTY_0438.

Chemistry

BindingDBC1AKA5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH24734; BAH24734; JTY_0438.
GeneID7561137.
KEGGmbt:JTY_0438.
PATRIC18020154. VBIMycBov85238_0475.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243508.
KOK01462.
OMARVCQVGD.
OrthoDBEOG664CMF.
ProtClustDBPRK00150.

Enzyme and pathway databases

BioCycMBOV561275:GHDN-442-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. SSF56420. 1 hit.
TIGRFAMsTIGR00079. pept_deformyl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDEF_MYCBT
AccessionPrimary (citable) accession number: C1AKA5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 2009
Last modified: February 19, 2014
This is version 35 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