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B7MCQ2

- DEF_ECO45

UniProt

B7MCQ2 - DEF_ECO45

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Protein
Peptide deformylase
Gene
def, ECS88_3674
Organism
Escherichia coli O45:K1 (strain S88 / ExPEC)
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 bindingi91 – 911Iron By similarity
Metal bindingi133 – 1331Iron By similarity
Active sitei134 – 1341 By similarity
Metal bindingi137 – 1371Iron 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

Enzyme and pathway databases

BioCyciECOL585035:GJWP-3662-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:ECS88_3674
OrganismiEscherichia coli O45:K1 (strain S88 / ExPEC)
Taxonomic identifieri585035 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000747: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 169169Peptide deformylaseUniRule annotation
PRO_1000200730Add
BLAST

Proteomic databases

PRIDEiB7MCQ2.

Interactioni

Protein-protein interaction databases

STRINGi585035.ECS88_3674.

Structurei

3D structure databases

ProteinModelPortaliB7MCQ2.
SMRiB7MCQ2. Positions 2-168.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0242.
HOGENOMiHOG000243509.
KOiK01462.
OMAiELLAICI.
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.

B7MCQ2-1 [UniParc]FASTAAdd to Basket

« Hide

MSVLQVLHIP DERLRKVAKP VEEVNAEIQR IVDDMFETMY AEEGIGLAAT    50
QVDIHQRIIV IDVSENRDER LVLINPELLE KSGETGIEEG CLSIPEQRAL 100
VPRAEKVKIR ALDRDGKPFE LEADGLLAIC IQHEMDHLVG KLFMDYLSPL 150
KQQRIRQKVE KLDRLKARA 169
Length:169
Mass (Da):19,328
Last modified:March 24, 2009 - v1
Checksum:iC485EB6C1D2D91B8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU928161 Genomic DNA. Translation: CAR04891.1.
RefSeqiYP_002393261.1. NC_011742.1.

Genome annotation databases

EnsemblBacteriaiCAR04891; CAR04891; ECS88_3674.
GeneIDi7130611.
KEGGiecz:ECS88_3674.
PATRICi18415019. VBIEscCol91599_3601.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU928161 Genomic DNA. Translation: CAR04891.1 .
RefSeqi YP_002393261.1. NC_011742.1.

3D structure databases

ProteinModelPortali B7MCQ2.
SMRi B7MCQ2. Positions 2-168.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 585035.ECS88_3674.

Chemistry

BindingDBi B7MCQ2.

Proteomic databases

PRIDEi B7MCQ2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAR04891 ; CAR04891 ; ECS88_3674 .
GeneIDi 7130611.
KEGGi ecz:ECS88_3674.
PATRICi 18415019. VBIEscCol91599_3601.

Phylogenomic databases

eggNOGi COG0242.
HOGENOMi HOG000243509.
KOi K01462.
OMAi ELLAICI.
OrthoDBi EOG664CMF.

Enzyme and pathway databases

BioCyci ECOL585035:GJWP-3662-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: S88 / ExPEC.

Entry informationi

Entry nameiDEF_ECO45
AccessioniPrimary (citable) accession number: B7MCQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 41 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