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Q2A4V7 (Q2A4V7_FRATH) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 39. 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:FTL_0473
OrganismFrancisella tularensis subsp. holarctica (strain LVS) [Complete proteome] [HAMAP]
Taxonomic identifier376619 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Protein attributes

Sequence length211 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 site1571 By similarity HAMAP MF_00163
Metal binding1131Iron By similarity HAMAP MF_00163
Metal binding1561Iron By similarity HAMAP MF_00163
Metal binding1601Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
Q2A4V7 [UniParc].

Last modified April 4, 2006. Version 1.
Checksum: 7A4DB1315F7FCB4E

FASTA21124,262
        10         20         30         40         50         60 
MMVVNIKMQQ MKSQFIQYND SNNKVLYQKC KPVADIQNAE IQNIITEMHE KMQGNGIGLA 

        70         80         90        100        110        120 
ANQIGYPYQI FMIEFDSSNA RYPFSFDSVP YQVFINPKIT KASKQRVSFW HGCLSALGEK 

       130        140        150        160        170        180 
RGKLATYKEI EYEAYNQHGE KITGKLDSIA AVIFQHEFNH LLGSVYVDFD TEYIDNEELQ 

       190        200        210 
AKFASGELKP YQECGEEVPL LLEKYQIGKN I 

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References

[1]"Complete genome sequence of Francisella tularensis LVS (Live Vaccine Strain)."
Chain P., Larimer F., Land M., Stilwagen S., Larsson P., Bearden S., Chu M., Oyston P., Forsman M., Andersson S., Lindler L., Titball R., Garcia E.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM233362 Genomic DNA. Translation: CAJ78913.1.
RefSeqYP_513245.1. NC_007880.1.

3D structure databases

ProteinModelPortalQ2A4V7.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3952531.
GenomeReviewsGene locus FTL_0473 in contig AM233362_GR.
KEGGftl:FTL_0473.
PATRIC17941898. VBIFraTul90181_0517.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG482680.
OMAHNERYPD.
ProtClustDBCLSK934502.

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.
ProtoNetSearch...

Entry information

Entry nameQ2A4V7_FRATH
AccessionPrimary (citable) accession number: Q2A4V7
Entry history
Integrated into UniProtKB/TrEMBL: April 4, 2006
Last sequence update: April 4, 2006
Last modified: December 14, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)