Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q7V5F9 (DEF2_PROMM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptide deformylase 2
Short name=PDF 2
EC=3.5.1.88
Alternative name(s):
Polypeptide deformylase 2
Gene names
Name:def2
Ordered Locus Names:PMT_1601
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length201 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

Cofactor

Binds 1 Fe2+ ion By similarity. HAMAP MF_00163

Sequence similarities

Belongs to the polypeptide deformylase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   LigandIron
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtranslation

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioniron ion binding

Inferred from electronic annotation. Source: InterPro

peptide deformylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 201201Peptide deformylase 2 HAMAP MF_00163
PRO_0000082817

Sites

Active site1641 By similarity
Metal binding1211Iron By similarity
Metal binding1631Iron By similarity
Metal binding1671Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7V5F9 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: F8E336410A3AEC3E

FASTA20122,311
        10         20         30         40         50         60 
MARSFAQLAR TAEKTKGSVA VPKEPLDHPP LQIHTLGNGV LRQSTRRIGK VDESVRDLVR 

        70         80         90        100        110        120 
DMLRSMYAAK GIGLAAPQVG IHKQLLVLDL DLETPTTPPV VLINPEIISS SATVETYEEG 

       130        140        150        160        170        180 
CLSIPGVYLN VVRPSEIVLS FRDEMGRPRK MKADGLMARC IQHEMDHLEG VLFVDRVTDE 

       190        200 
NELSLELKEH GFKRADVRPL V

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed: 12917642] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9313.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX548175 Genomic DNA. Translation: CAE21776.1.
RefSeqNP_895428.1. NC_005071.1.

3D structure databases

ProteinModelPortalQ7V5F9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7V5F9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1728260.
GenomeReviewsGene locus PMT_1601 in contig BX548175_GR.
KEGGpmt:PMT1601.
NMPDRfig|74547.1.peg.1595.
PATRIC23011843. VBIProMar135351_2063.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHBG665227.
OMAGVLFVDY.
PhylomeDBQ7V5F9.
ProtClustDBPRK00150.

Enzyme and pathway databases

BioCycPMAR74547:PMT1601-MONOMER.

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 nameDEF2_PROMM
AccessionPrimary (citable) accession number: Q7V5F9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents