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Q1BEJ4

- DEF_MYCSS

UniProt

Q1BEJ4 - DEF_MYCSS

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Protein
Peptide deformylase
Gene
def, Mmcs_0569
Organism
Mycobacterium sp. (strain MCS)
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 bindingi106 – 1061Iron By similarity
Metal bindingi148 – 1481Iron By similarity
Active sitei149 – 1491 By similarity
Metal bindingi152 – 1521Iron By similarity

GO - Molecular functioni

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

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

BioCyciMSP164756:GHQ8-574-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:Mmcs_0569
OrganismiMycobacterium sp. (strain MCS)
Taxonomic identifieri164756 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000001972: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 197197Peptide deformylaseUniRule annotation
PRO_0000301062Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi164756.Mmcs_0569.

Structurei

3D structure databases

ProteinModelPortaliQ1BEJ4.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0242.
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.

Q1BEJ4-1 [UniParc]FASTAAdd to Basket

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MAVVPIRIVG DPVLRTETTP IPVGDDGSLP AEVADLIRDL YETMDAANGV    50
GLAANQIGVS QRVFVYDCPD SRGRAGRRRG VVINPVLETS DIPETMPDPD 100
DDEEGCLSVP GEQFPTGRAD WARVTGLDAD GSPITVEGTG LFARMLQHET 150
GHLDGFLYLD RLIGRHARAA KRAVKHNGWG VPGLSWTPGE DPDPFGH 197
Length:197
Mass (Da):21,146
Last modified:July 11, 2006 - v1
Checksum:iCA23ED63701DC671
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000384 Genomic DNA. Translation: ABG06690.1.
RefSeqiYP_637746.1. NC_008146.1.

Genome annotation databases

EnsemblBacteriaiABG06690; ABG06690; Mmcs_0569.
GeneIDi4109415.
KEGGimmc:Mmcs_0569.
PATRICi18111247. VBIMycSp106721_0586.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000384 Genomic DNA. Translation: ABG06690.1 .
RefSeqi YP_637746.1. NC_008146.1.

3D structure databases

ProteinModelPortali Q1BEJ4.
ModBasei Search...

Protein-protein interaction databases

STRINGi 164756.Mmcs_0569.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABG06690 ; ABG06690 ; Mmcs_0569 .
GeneIDi 4109415.
KEGGi mmc:Mmcs_0569.
PATRICi 18111247. VBIMycSp106721_0586.

Phylogenomic databases

eggNOGi COG0242.
HOGENOMi HOG000243508.
KOi K01462.
OMAi DMYDTMD.
OrthoDBi EOG664CMF.

Enzyme and pathway databases

BioCyci MSP164756:GHQ8-574-MONOMER.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MCS.

Entry informationi

Entry nameiDEF_MYCSS
AccessioniPrimary (citable) accession number: Q1BEJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 11, 2006
Last modified: May 14, 2014
This is version 58 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

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