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B9KML4 (B9KML4_RHOSK) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 21. 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
Ordered Locus Names:RSKD131_2245
OrganismRhodobacter sphaeroides (strain KD131 / KCTC 12085) [Complete proteome] [HAMAP]
Taxonomic identifier557760 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length177 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
B9KML4 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 4C0DAF1618ED746D

FASTA17720,083
        10         20         30         40         50         60 
MIRPILIHPD PRLKKICDPV GQITDDLRRL ADDMLATMYD APGIGLAAPQ VGVVRRLIVL 

        70         80         90        100        110        120 
DCNKESDGAR RPVAMVNPEV VWRSEDVSTY EEGCLSLPNV FADVERPAEV KVRWTGLDGR 

       130        140        150        160        170 
EEEEQFAGLW ATCVQHEIDH LDGKLFIDYL RPLKRQMITR KMEKFKRAQA SGMVQKA

« Hide

References

[1]"Complete genome sequence of Rhodobacter sphaeroides KD131."
Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.
J. Bacteriol. 191:1118-1119(2009) [PubMed: 19028901] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001150 Genomic DNA. Translation: ACM02105.1.
RefSeqYP_002526606.1. NC_011963.1.

3D structure databases

ProteinModelPortalB9KML4.
ModBaseSearch...

Protein-protein interaction databases

STRINGB9KML4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7359341.
GenomeReviewsGene locus RSKD131_2245 in contig CP001150_GR.
KEGGrsk:RSKD131_2245.
PATRIC23183613. VBIRhoSph125910_3651.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAQKIVDDM.
ProtClustDBCLSK934098.

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 nameB9KML4_RHOSK
AccessionPrimary (citable) accession number: B9KML4
Entry history
Integrated into UniProtKB/TrEMBL: March 24, 2009
Last sequence update: March 24, 2009
Last modified: December 14, 2011
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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