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Q5LNI5 (Q5LNI5_SILPO) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 45. 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 3 HAMAP MF_00163
Short name=PDF 3 HAMAP MF_00163
EC=3.5.1.88 HAMAP MF_00163
Alternative name(s):
Polypeptide deformylase 3 HAMAP MF_00163
Gene names
Name:def-3 EMBL AAV96454.1
Synonyms:def3 HAMAP MF_00163
Ordered Locus Names:SPO3219
OrganismSilicibacter pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) [Complete proteome] [HAMAP]
Taxonomic identifier246200 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Ruegeria

Protein attributes

Sequence length172 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 site1371 By similarity HAMAP MF_00163
Metal binding941Iron By similarity HAMAP MF_00163
Metal binding1361Iron By similarity HAMAP MF_00163
Metal binding1401Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
Q5LNI5 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: F590C4E99E1B8518

FASTA17219,512
        10         20         30         40         50         60 
MKRAILIHPD PRLKKVCAPV ADISDELRAL ADDMLETMYD APGIGLAAPQ IGVLDRLIVL 

        70         80         90        100        110        120 
DCVKEESAPA RPLVMFNPRV VAASDETNIY EEGCLSIPEQ YAEVTRPKVV DVEWIDRDGK 

       130        140        150        160        170 
LQSETFDGLW ATCVQHEIDH LDGKLFIDYL KPLKRQMITR KMQKLKRERA RA

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000031 Genomic DNA. Translation: AAV96454.1.
RefSeqYP_168422.1. NC_003911.11.

3D structure databases

ProteinModelPortalQ5LNI5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3193782.
GenomeReviewsGene locus SPO3219 in contig CP000031_GR.
KEGGsil:SPO3219.
NMPDRfig|246200.3.peg.3592.
PATRIC23379885. VBIRuePom114501_3286.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG665227.
OMAEIVSKQG.
ProtClustDBCLSK934098.

Enzyme and pathway databases

BioCycRPOM246200:SPO_3219-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 nameQ5LNI5_SILPO
AccessionPrimary (citable) accession number: Q5LNI5
Entry history
Integrated into UniProtKB/TrEMBL: February 1, 2005
Last sequence update: February 1, 2005
Last modified: December 14, 2011
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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