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P94601

- DEF_MICDP

UniProt

P94601 - DEF_MICDP

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Protein
Peptide deformylase
Gene
def
Organism
Microchaete diplosiphon (Fremyella diplosiphon)
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 bindingi107 – 1071Iron By similarity
Metal bindingi149 – 1491Iron By similarity
Active sitei150 – 1501 By similarity
Metal bindingi153 – 1531Iron 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

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
OrganismiMicrochaete diplosiphon (Fremyella diplosiphon)
Taxonomic identifieri1197 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesMicrochaetaceaeMicrochaete

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 187187Peptide deformylaseUniRule annotation
PRO_0000082783Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP94601.

Family & Domainsi

Sequence similaritiesi

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.

P94601-1 [UniParc]FASTAAdd to Basket

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MPSEIAVEKK KLKNPPLQLH YLGDRVLRQP AKRIAKVDDE LRQLIRDMLQ    50
TMYSKDGIGL AAPQVGIHKQ LIVIDLEPDN PANPPLVLIN PTIKQVSKEI 100
CVAQEGCLSI PNVYMDVKRP EVVEIAYKDE NGRPKTLKAT DLLARCIQHE 150
MDHLNGVVFV DRVDNSLTLA QELSKNGFSY QAVKPVA 187
Length:187
Mass (Da):20,938
Last modified:May 1, 1997 - v1
Checksum:iB58EC9BAA0EBF299
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y10305 Genomic DNA. Translation: CAA71353.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y10305 Genomic DNA. Translation: CAA71353.1 .

3D structure databases

ProteinModelPortali P94601.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. "A survey of polypeptide deformylase function throughout the eubacterial lineage."
    Mazel D., Coic E., Blanchard S., Saurin W., Marliere P.
    J. Mol. Biol. 266:939-949(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiDEF_MICDP
AccessioniPrimary (citable) accession number: P94601
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: February 19, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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