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A8GR64 (A8GR64_RICRS) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 25. 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 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:def2 HAMAP MF_00163
Ordered Locus Names:A1G_01595
OrganismRickettsia rickettsii (strain Sheila Smith) [Complete proteome] [HAMAP] EMBL ABV75889.1
Taxonomic identifier392021 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length175 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1421 By similarity HAMAP MF_00163
Metal binding991Iron By similarity HAMAP MF_00163
Metal binding1411Iron By similarity HAMAP MF_00163
Metal binding1451Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
A8GR64 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 91FB3D72903C5A6D

FASTA17520,252
        10         20         30         40         50         60 
MSILPIVTAP DERLKQKSQP VLEFTDQTRK FMDDMLKTMY HEDGAGLAAV QVGVLKRILV 

        70         80         90        100        110        120 
IDIQDHDSVA RPKDFYPLFI VNPEIIEKAE ELVTANEGCI SLPEQRIEVA RPESIKIRYL 

       130        140        150        160        170 
DYHGKSQELK ANDWLARVIQ HEYDHLEGKL MIDYLSNLKR DVVLRKLKKL KNNIV 

« Hide

References

[1]"Complete genome sequence of Rickettsia rickettsii."
Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Dasch G., Eremeeva M.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000848 Genomic DNA. Translation: ABV75889.1.
RefSeqYP_001494397.1. NC_009882.1.

3D structure databases

ProteinModelPortalA8GR64.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8GR64.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5647853.
GenomeReviewsGene locus A1G_01595 in contig CP000848_GR.
KEGGrri:A1G_01595.
PATRIC17903331. VBIRicRic5337_0333.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHBG665227.
OMAETMIASE.
ProtClustDBPRK00150.

Enzyme and pathway databases

BioCycRRIC392021:A1G_01595-MONOMER.

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 nameA8GR64_RICRS
AccessionPrimary (citable) accession number: A8GR64
Entry history
Integrated into UniProtKB/TrEMBL: November 13, 2007
Last sequence update: November 13, 2007
Last modified: December 14, 2011
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)