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A2SGT3 (A2SGT3_METPP) Unreviewed, UniProtKB/TrEMBL

Last modified November 16, 2011. Version 33. 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:Mpe_A1813
OrganismMethylibium petroleiphilum (strain PM1) [Complete proteome] [HAMAP] EMBL ABM94772.1
Taxonomic identifier420662 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Methylibium

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1431 By similarity HAMAP MF_00163
Metal binding1001Iron By similarity HAMAP MF_00163
Metal binding1421Iron By similarity HAMAP MF_00163
Metal binding1461Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
A2SGT3 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 765FF4FC8DDEC16C

FASTA17719,860
        10         20         30         40         50         60 
MAVRDILKMG DPRLLRIAHP VREFDTPALH ALIEDMFDTM EAANGAGLAA PQIGVDLQLV 

        70         80         90        100        110        120 
IFGFTKSERY PEAPPVPRTV LINPQITPLS EDLEDGWEGC LSVPGLRGVV PRHQRIRYTG 

       130        140        150        160        170 
FDPQGRRIER EAEGFHARVV QHECDHLAGV LYPMRVRDFS RFGYTEVLFP GLDDGDD

« Hide

References

[1]"Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1."
Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R.
J. Bacteriol. 189:1931-1945(2007) [PubMed: 17158667] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000555 Genomic DNA. Translation: ABM94772.1.
RefSeqYP_001021007.1. NC_008825.1.

3D structure databases

ProteinModelPortalA2SGT3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2SGT3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4786812.
GenomeReviewsGene locus Mpe_A1813 in contig CP000555_GR.
KEGGmpt:Mpe_A1813.
NMPDRfig|279263.3.peg.1275.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHBG665227.
OMAIRYEGFD.
ProtClustDBCLSK2321979.

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 nameA2SGT3_METPP
AccessionPrimary (citable) accession number: A2SGT3
Entry history
Integrated into UniProtKB/TrEMBL: March 6, 2007
Last sequence update: March 6, 2007
Last modified: November 16, 2011
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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