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Protein

Peptide deformylase

Gene

def

Organism
Psychrobacter cryohalolentis (strain K5)
Status
Reviewed-Annotation score: 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.UniRule annotation

Catalytic activityi

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

Cofactori

Fe2+UniRule annotationNote: Binds 1 Fe2+ ion.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi92 – 921IronUniRule annotation
Metal bindingi134 – 1341IronUniRule annotation
Active sitei135 – 1351UniRule annotation
Metal bindingi138 – 1381IronUniRule annotation

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

BioCyciPCRY335284:GHE9-38-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide deformylaseUniRule annotation (EC:3.5.1.88UniRule annotation)
Short name:
PDFUniRule annotation
Alternative name(s):
Polypeptide deformylaseUniRule annotation
Gene namesi
Name:defUniRule annotation
Ordered Locus Names:Pcryo_0038
OrganismiPsychrobacter cryohalolentis (strain K5)
Taxonomic identifieri335284 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
ProteomesiUP000002425 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 184184Peptide deformylasePRO_0000301085Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi335284.Pcryo_0038.

Structurei

3D structure databases

ProteinModelPortaliQ1QET1.
SMRiQ1QET1. Positions 1-162.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the polypeptide deformylase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0242.
HOGENOMiHOG000243509.
KOiK01462.
OMAiFDTMYEE.
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.

Q1QET1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLPILSYP DPRLRTIATP VKEVTAEIKT LITDMIETMY DAQGIGLAAS
60 70 80 90 100
QVDHHIQLIV MDLSEDKDSP RVFINPKVTP LVEEKQPYEE GCLSVPDVYD
110 120 130 140 150
KVERPNKVRI EALDENGNKI DEEVEGLLAV CIQHEMDHLN GVIFVDYLSR
160 170 180
LKQTRARDKV RKVLKIREKQ GEQVAEKEPQ PANS
Length:184
Mass (Da):20,855
Last modified:May 15, 2006 - v1
Checksum:i601C9E16E475FEE2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000323 Genomic DNA. Translation: ABE73822.1.
RefSeqiWP_011512414.1. NC_007969.1.
YP_579306.1. NC_007969.1.

Genome annotation databases

EnsemblBacteriaiABE73822; ABE73822; Pcryo_0038.
KEGGipcr:Pcryo_0038.
PATRICi23059459. VBIPsyCry128170_0083.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000323 Genomic DNA. Translation: ABE73822.1.
RefSeqiWP_011512414.1. NC_007969.1.
YP_579306.1. NC_007969.1.

3D structure databases

ProteinModelPortaliQ1QET1.
SMRiQ1QET1. Positions 1-162.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi335284.Pcryo_0038.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE73822; ABE73822; Pcryo_0038.
KEGGipcr:Pcryo_0038.
PATRICi23059459. VBIPsyCry128170_0083.

Phylogenomic databases

eggNOGiCOG0242.
HOGENOMiHOG000243509.
KOiK01462.
OMAiFDTMYEE.
OrthoDBiEOG664CMF.

Enzyme and pathway databases

BioCyciPCRY335284:GHE9-38-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

  1. "Complete sequence of chromosome of Psychrobacter cryohalolentis K5."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J.
    , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
    Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K5.

Entry informationi

Entry nameiDEF_PSYCK
AccessioniPrimary (citable) accession number: Q1QET1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 10, 2007
Last sequence update: May 15, 2006
Last modified: March 31, 2015
This is version 63 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

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.