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A5CVP6 (A5CVP6_VESOH) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 32. 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 HAMAP MF_00163

Short name=PDF HAMAP MF_00163
EC=3.5.1.88 HAMAP MF_00163
Alternative name(s):
Polypeptide deformylase HAMAP MF_00163
Gene names
Name:def HAMAP MF_00163
Ordered Locus Names:COSY_0868
OrganismVesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA) [Complete proteome] [HAMAP] EMBL BAF61973.1
Taxonomic identifier412965 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriasulfur-oxidizing symbionts

Protein attributes

Sequence length180 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 site1491 By similarity HAMAP MF_00163
Metal binding1061Iron By similarity HAMAP MF_00163
Metal binding1481Iron By similarity HAMAP MF_00163
Metal binding1521Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
A5CVP6 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: E611FCFC73023416

FASTA18020,801
        10         20         30         40         50         60 
MILPILSYPD KRLRIKAKNV NIVNKTIQTL IKNMFETMYA RNGIGLAATQ VNQHLQIVVI 

        70         80         90        100        110        120 
DVPNSQFLFK NRKNNSQKLL QKQHPLCFIN PEIKEKYGQE KHTEGCLSVS DFQAEIQRAN 

       130        140        150        160        170        180 
HIKVKALNEK GEIFILQATG LLAICIQHEI DHLKGILFVD YLSKLKQKRL LERIKKMTKV 

« Hide

References

[1]"Reduced genome of the thioautotrophic intracellular symbiont in a deep-sea clam, Calyptogena okutanii."
Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M., Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y., Sato T., Kato C., Kitagawa M., Kato I., Maruyama T.
Curr. Biol. 17:881-886(2007) [PubMed: 17493812] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009247 Genomic DNA. Translation: BAF61973.1.
RefSeqYP_001219697.1. NC_009465.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA5CVP6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5172012.
GenomeReviewsGene locus COSY_0868 in contig AP009247_GR.
KEGGvok:COSY_0868.
PATRIC32021615. VBICanVes128383_0874.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHBG665227.
OMAPLKRQRM.
ProtClustDBCLSK850831.

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 nameA5CVP6_VESOH
AccessionPrimary (citable) accession number: A5CVP6
Entry history
Integrated into UniProtKB/TrEMBL: June 12, 2007
Last sequence update: June 12, 2007
Last modified: December 14, 2011
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)