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Protein

Peptide deformylase

Gene

def

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: -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.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)DescriptionActionsGraphical viewLength
Metal bindingi92IronUniRule annotation1
Metal bindingi134IronUniRule annotation1
Active sitei135UniRule annotation1
Metal bindingi138IronUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processProtein biosynthesis
LigandIron, Metal-binding

Enzyme and pathway databases

BioCyciPAER208964:G1FZ6-19-MONOMER
BRENDAi3.5.1.88 5087

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:PA0019
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA0019

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1649054
DrugBankiDB04310 2-[(Formyl-Hydroxy-Amino)-Methyl]-Heptanoic Acid [1-(2-Hydroxymethyl-Pyrrolidine-1-Carbonyl)-2-Methyl-Propyl]-Amide
DB02810 N-(2-Acetamido)Iminodiacetic Acid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000828191 – 168Peptide deformylaseAdd BLAST168

Proteomic databases

PaxDbiQ9I7A8

Interactioni

Protein-protein interaction databases

STRINGi208964.PA0019

Chemistry databases

BindingDBiQ9I7A8

Structurei

Secondary structure

1168
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 15Combined sources4
Helixi26 – 41Combined sources16
Beta strandi45 – 48Combined sources4
Helixi49 – 52Combined sources4
Beta strandi56 – 62Combined sources7
Beta strandi64 – 67Combined sources4
Beta strandi70 – 81Combined sources12
Beta strandi85 – 90Combined sources6
Beta strandi100 – 106Combined sources7
Beta strandi108 – 113Combined sources6
Beta strandi119 – 124Combined sources6
Helixi126 – 139Combined sources14
Helixi144 – 147Combined sources4
Helixi150 – 166Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IX1X-ray1.85A/B1-168[»]
1LRYX-ray2.60A2-168[»]
1N5NX-ray1.80A/B1-168[»]
1S17X-ray1.95A/B1-168[»]
ProteinModelPortaliQ9I7A8
SMRiQ9I7A8
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9I7A8

Family & Domainsi

Sequence similaritiesi

Belongs to the polypeptide deformylase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108Z02 Bacteria
COG0242 LUCA
InParanoidiQ9I7A8
KOiK01462
OMAiVCIQHEI
PhylomeDBiQ9I7A8

Family and domain databases

CDDicd00487 Pep_deformylase, 1 hit
Gene3Di3.90.45.10, 1 hit
HAMAPiMF_00163 Pep_deformylase, 1 hit
InterProiView protein in InterPro
IPR023635 Peptide_deformylase
IPR036821 Peptide_deformylase_sf
PANTHERiPTHR10458 PTHR10458, 1 hit
PfamiView protein in Pfam
PF01327 Pep_deformylase, 1 hit
PIRSFiPIRSF004749 Pep_def, 1 hit
PRINTSiPR01576 PDEFORMYLASE
SUPFAMiSSF56420 SSF56420, 1 hit
TIGRFAMsiTIGR00079 pept_deformyl, 1 hit

Sequencei

Sequence statusi: Complete.

Q9I7A8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAILNILEFP DPRLRTIAKP VEVVDDAVRQ LIDDMFETMY EAPGIGLAAT
60 70 80 90 100
QVNVHKRIVV MDLSEDKSEP RVFINPEFEP LTEDMDQYQE GCLSVPGFYE
110 120 130 140 150
NVDRPQKVRI KALDRDGNPF EEVAEGLLAV CIQHECDHLN GKLFVDYLST
160
LKRDRIRKKL EKQHRQQA
Length:168
Mass (Da):19,365
Last modified:March 1, 2001 - v1
Checksum:iA95F6B921E5F3189
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA Translation: AAG03409.1
PIRiH83643
RefSeqiNP_248709.1, NC_002516.2
WP_003107059.1, NC_002516.2

Genome annotation databases

EnsemblBacteriaiAAG03409; AAG03409; PA0019
GeneIDi879306
KEGGipae:PA0019
PATRICifig|208964.12.peg.18

Similar proteinsi

Entry informationi

Entry nameiDEF_PSEAE
AccessioniPrimary (citable) accession number: Q9I7A8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: March 1, 2001
Last modified: May 23, 2018
This is version 118 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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