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Protein

Peptide deformylase

Gene

def

Organism
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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).By similarity

Catalytic activityi

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

Cofactori

Fe2+By similarityNote: Binds 1 Fe2+ ion.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi131 – 1311IronBy similarity
Metal bindingi174 – 1741IronBy similarity
Active sitei175 – 1751By similarity
Metal bindingi178 – 1781IronBy 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

Enzyme and pathway databases

BioCyciSPYO286636:GHNO-1757-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide deformylase (EC:3.5.1.88)
Short name:
PDF
Alternative name(s):
Polypeptide deformylase
Gene namesi
Name:def
Ordered Locus Names:M6_Spy1677
OrganismiStreptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Taxonomic identifieri286636 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
ProteomesiUP000001167: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 204204Peptide deformylasePRO_0000082861Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi286636.M6_Spy1677.

Structurei

3D structure databases

ProteinModelPortaliQ5X9V1.
SMRiQ5X9V1. Positions 2-204.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the polypeptide deformylase family.Curated

Phylogenomic databases

eggNOGiCOG0242.
HOGENOMiHOG000243507.
KOiK01462.
OMAiQDPVMGE.
OrthoDBiEOG6PZXGQ.

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.

Q5X9V1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAQDKLIKP SHLITMDDII REGNPTLRAV AKEVSLPLCD EDILLGEKMM
60 70 80 90 100
QFLKHSQDPV MAEKLGLRAG VGLAAPQIDV SKRIIAVLVP NLPDKEGNPP
110 120 130 140 150
KEAYSWQEVL YNPKIVSHSV QDAALSDGEG CLSVDRVVEG YVVRHARVTV
160 170 180 190 200
DYYDKEGQQH RIKLKGYNAI VVQHEIDHIN GVLFYDRINA KNPFETKEEL

LILD
Length:204
Mass (Da):22,862
Last modified:November 23, 2004 - v1
Checksum:i89F8EDE94D94DC05
GO

Mass spectrometryi

Molecular mass is 22862.28 Da from positions 1 - 204. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000003 Genomic DNA. Translation: AAT87812.1.
RefSeqiYP_060995.1. NC_006086.1.

Genome annotation databases

EnsemblBacteriaiAAT87812; AAT87812; M6_Spy1677.
GeneIDi2941572.
KEGGispa:M6_Spy1677.
PATRICi19725638. VBIStrPyo30273_1743.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000003 Genomic DNA. Translation: AAT87812.1.
RefSeqiYP_060995.1. NC_006086.1.

3D structure databases

ProteinModelPortaliQ5X9V1.
SMRiQ5X9V1. Positions 2-204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi286636.M6_Spy1677.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT87812; AAT87812; M6_Spy1677.
GeneIDi2941572.
KEGGispa:M6_Spy1677.
PATRICi19725638. VBIStrPyo30273_1743.

Phylogenomic databases

eggNOGiCOG0242.
HOGENOMiHOG000243507.
KOiK01462.
OMAiQDPVMGE.
OrthoDBiEOG6PZXGQ.

Enzyme and pathway databases

BioCyciSPYO286636:GHNO-1757-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Progress toward characterization of the group A Streptococcus metagenome: complete genome sequence of a macrolide-resistant serotype M6 strain."
    Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E., Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.
    J. Infect. Dis. 190:727-738(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-946 / MGAS10394.
  2. "Two-dimensional gel electrophoresis map of Streptococcus pyogenes proteins."
    Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J., VanBogelen R.A.
    Submitted (MAY-2000) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 7-20; 68-101; 148-161; 166-187 AND 192-204, MASS SPECTROMETRY.
    Strain: JRS4 / Serotype M6.

Entry informationi

Entry nameiDEF_STRP6
AccessioniPrimary (citable) accession number: Q5X9V1
Secondary accession number(s): P82590
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: November 23, 2004
Last modified: January 7, 2015
This is version 68 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, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.