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A5VVU1 (A5VVU1_BRUO2) 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 EMBL ABQ62093.1
Ordered Locus Names:BOV_A0976
OrganismBrucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512) [Complete proteome] [HAMAP]
Taxonomic identifier444178 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length187 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 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
A5VVU1 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: B6B16E9EDDFD7CCC

FASTA18721,001
        10         20         30         40         50         60 
MTILARPITE KSMSVKPLII LPDPVLRQVS KPVERFDDQL RKFASDMFDT MYDAPGIGLA 

        70         80         90        100        110        120 
AIQVGEPIRM LVIDLAKEGE PKAPHIFVNP TIVQSSDKRS TYEEGCLSIP DYYAEVERPA 

       130        140        150        160        170        180 
TVKVNYFDAD GKPQSMEADG LMATCLQHEI DHLNGVLFID HISKLKRDMV IKKFKKLASQ 


RASKKVL

« Hide

References

[1]Paulsen I.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000709 Genomic DNA. Translation: ABQ62093.1.
RefSeqYP_001257946.1. NC_009504.1.

3D structure databases

ProteinModelPortalA5VVU1.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5VVU1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5203756.
GenomeReviewsGene locus BOV_A0976 in contig CP000709_GR.
KEGGbov:BOV_A0976.
PATRIC17859375. VBIBruOvi136990_1123.
TIGRBOV_A0976.

Phylogenomic databases

HOGENOMHBG665227.
OMARITKVDE.
ProtClustDBPRK00150.

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 nameA5VVU1_BRUO2
AccessionPrimary (citable) accession number: A5VVU1
Entry history
Integrated into UniProtKB/TrEMBL: July 10, 2007
Last sequence update: July 10, 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)
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