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C2GUU1 (C2GUU1_BIFLN) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peptide deformylase 1 HAMAP MF_00163

Short name=PDF 1 HAMAP MF_00163
EC=3.5.1.88 HAMAP MF_00163
Alternative name(s):
Polypeptide deformylase 1 HAMAP MF_00163
Gene names
Name:def1 HAMAP MF_00163 EMBL EEI81218.1
ORF Names:HMPREF0175_0789 EMBL EEI81218.1
OrganismBifidobacterium longum subsp. longum ATCC 55813 EMBL EEI81218.1
Taxonomic identifier548480 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length217 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

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1721 By similarity HAMAP MF_00163
Metal binding1291Iron By similarity HAMAP MF_00163
Metal binding1711Iron By similarity HAMAP MF_00163
Metal binding1751Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
C2GUU1 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 52F5B469B6F47163

FASTA21724,443
        10         20         30         40         50         60 
MFGKNAKVDL ELNRDVEQLI KTGGKEKLLP IVQAGEPVLR QRTVAYNGQL SKRTLAKLID 

        70         80         90        100        110        120 
TMHTTMLEAP GVGLAATQIG LGLALAVVED HVRDDEDDPR EIAEFPFHVI INPSYKPTSD 

       130        140        150        160        170        180 
KTASFYEGCL SFDGYQAVRK RWLDITAEWD DEDGKHHSEP LHGWPARIFQ HETDHLSGEL 

       190        200        210 
YIDRAEIRSL TTNENLEDYW CEDPVPTEAA EELGFAL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
ACHI01000018 Genomic DNA. Translation: EEI81218.1.

3D structure databases

ProteinModelPortalC2GUU1.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC36942360. VBIBifLon7869_0270.

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.
PANTHERPTHR10458. Fmet_deformylase. 1 hit.
PfamPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFPIRSF004749. Pep_def. 1 hit.
PRINTSPR01576. PDEFORMYLASE.
SUPFAMSSF56420. Fmet_deformylase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameC2GUU1_BIFLN
AccessionPrimary (citable) accession number: C2GUU1
Entry history
Integrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: January 25, 2012
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)