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Q8FMD0

- DEF2_COREF

UniProt

Q8FMD0 - DEF2_COREF

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Protein

Peptide deformylase 2

Gene
def2, CE2577
Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Status
Reviewed - Annotation score: 2 out of 5 - Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide.UniRule annotation

Cofactori

Binds 1 Fe2+ ion By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi100 – 1001Iron By similarity
Metal bindingi142 – 1421Iron By similarity
Active sitei143 – 1431 By similarity
Metal bindingi146 – 1461Iron By similarity

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. peptide deformylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide deformylase 2 (EC:3.5.1.88)
Short name:
PDF 2
Alternative name(s):
Polypeptide deformylase 2
Gene namesi
Name:def2
Ordered Locus Names:CE2577
OrganismiCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Taxonomic identifieri196164 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000001409: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 193193Peptide deformylase 2UniRule annotationPRO_0000082773Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi196164.CE2577.

Structurei

3D structure databases

ProteinModelPortaliQ8FMD0.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000243508.
KOiK01462.
OMAiDMYDTMD.
OrthoDBiEOG664CMF.

Family and domain databases

Gene3Di3.90.45.10. 1 hit.
HAMAPiMF_00163. Pep_deformylase.
InterProiIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
PANTHERiPTHR10458. PTHR10458. 1 hit.
PfamiPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFiPIRSF004749. Pep_def. 1 hit.
PRINTSiPR01576. PDEFORMYLASE.
SUPFAMiSSF56420. SSF56420. 1 hit.
TIGRFAMsiTIGR00079. pept_deformyl. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8FMD0-1 [UniParc]FASTAAdd to Basket

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MTVRPIVIHG DPVLHNPTRE VTEPISELQE LIADMYETME VANGVGLAAN    50
QIGVSKRIFV FNCPDDEGTM HRGCFINPVL ETSEIPETMP ADDGSDEEGC 100
LSVPGEGFPT GRADWAKVTG LNEDGEEWSM EGTGFLARCF QHEVGHLDGV 150
VYTDTLIGRW KRLAKKTIKA NGWTEPGLTW TPGVDEDPFG HDV 193
Length:193
Mass (Da):21,168
Last modified:March 1, 2003 - v1
Checksum:i8596E2B1D2337925
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000035 Genomic DNA. Translation: BAC19387.1.
RefSeqiNP_739187.1. NC_004369.1.

Genome annotation databases

EnsemblBacteriaiBAC19387; BAC19387; BAC19387.
GeneIDi1034243.
KEGGicef:CE2577.
PATRICi21491301. VBICorEff9312_2544.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000035 Genomic DNA. Translation: BAC19387.1 .
RefSeqi NP_739187.1. NC_004369.1.

3D structure databases

ProteinModelPortali Q8FMD0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 196164.CE2577.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC19387 ; BAC19387 ; BAC19387 .
GeneIDi 1034243.
KEGGi cef:CE2577.
PATRICi 21491301. VBICorEff9312_2544.

Phylogenomic databases

HOGENOMi HOG000243508.
KOi K01462.
OMAi DMYDTMD.
OrthoDBi EOG664CMF.

Family and domain databases

Gene3Di 3.90.45.10. 1 hit.
HAMAPi MF_00163. Pep_deformylase.
InterProi IPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view ]
PANTHERi PTHR10458. PTHR10458. 1 hit.
Pfami PF01327. Pep_deformylase. 1 hit.
[Graphical view ]
PIRSFi PIRSF004749. Pep_def. 1 hit.
PRINTSi PR01576. PDEFORMYLASE.
SUPFAMi SSF56420. SSF56420. 1 hit.
TIGRFAMsi TIGR00079. pept_deformyl. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
    Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
    Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Entry informationi

Entry nameiDEF2_COREF
AccessioniPrimary (citable) accession number: Q8FMD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi