Skip Header

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

Q0TPL0 (Q0TPL0_CLOP1) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Peptide deformylase 2 HAMAP MF_00163

Short name=PDF 2 HAMAP MF_00163
EC=3.5.1.88 HAMAP MF_00163
Alternative name(s):
Polypeptide deformylase 2 HAMAP MF_00163
Gene names
Name:def EMBL ABG83585.1
Synonyms:def2 HAMAP MF_00163
Ordered Locus Names:CPF_1997
OrganismClostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier195103 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length147 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 SAAS SAAS000181

Cofactor

Binds 1 Fe2+ ion By similarity. HAMAP MF_00163

Sequence similarities

Belongs to the polypeptide deformylase family. HAMAP MF_00163 RuleBase RU003335

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1331 By similarity HAMAP MF_00163
Metal binding901Iron By similarity HAMAP MF_00163
Metal binding1321Iron By similarity HAMAP MF_00163
Metal binding1361Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
Q0TPL0 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 048318C9F9F7D956

FASTA14716,672
        10         20         30         40         50         60 
MAIRNLRFND DEILRKKCRV VDDINDRIKV LVEDMIETMY ENNGVGLAAP QVGILKRIFV 

        70         80         90        100        110        120 
VDAMDGAGSR VFINPEILEK SGEQTDEEGC LSLPGRHKPV KRANKIKIKA LDVNGNEFVL 

       130        140 
DAEEFLARAI QHEYDHLEGV LFIDHEL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000246 Genomic DNA. Translation: ABG83585.1.
RefSeqYP_696430.1. NC_008261.1.

3D structure databases

ProteinModelPortalQ0TPL0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0TPL0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4203791.
GenomeReviewsGene locus CPF_1997 in contig CP000246_GR.
KEGGcpf:CPF_1997.
PATRIC19486246. VBICloPer106549_1942.
TIGRCPF_1997.

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHBG665227.
OMAGVLFVDY.
ProtClustDBPRK00150.

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 nameQ0TPL0_CLOP1
AccessionPrimary (citable) accession number: Q0TPL0
Entry history
Integrated into UniProtKB/TrEMBL: September 5, 2006
Last sequence update: September 5, 2006
Last modified: December 14, 2011
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)