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Q9ABF5

- DEF_CAUCR

UniProt

Q9ABF5 - DEF_CAUCR

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Protein

Peptide deformylase

Gene

def

Organism
Caulobacter crescentus (strain ATCC 19089 / CB15)
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.UniRule annotation

Catalytic activityi

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

Cofactori

Fe2+UniRule annotationNote: Binds 1 Fe(2+) ion.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi98 – 981IronUniRule annotation
Metal bindingi140 – 1401IronUniRule annotation
Active sitei141 – 1411UniRule annotation
Metal bindingi144 – 1441IronUniRule 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

BioCyciCAULO:CC0272-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:CC_0272
OrganismiCaulobacter crescentus (strain ATCC 19089 / CB15)
Taxonomic identifieri190650 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter
ProteomesiUP000001816: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 173173Peptide deformylasePRO_0000082759Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ9ABF5.
SMRiQ9ABF5. Positions 18-171.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the polypeptide deformylase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0242.
HOGENOMiHOG000243509.
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.

Q9ABF5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAIRRILTVD NAADLATLKK ISTPVEAVTD ELRALMDDML ETMYDAPGIG
60 70 80 90 100
LAAVQVGEPV RVIVMDLARE GEDKAPRYFV NPEILASSED LQGYEEGCLS
110 120 130 140 150
VPEYYDEVER PSKVTLRYMN YQGETVVEEA EGLFAVCIQH EMDHLEGVLF
160 170
IDHLSRLRRD RAMAKVKKAR RAA
Length:173
Mass (Da):19,445
Last modified:June 1, 2001 - v1
Checksum:i7BE0E9341CF9195F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005673 Genomic DNA. Translation: AAK22259.1.
PIRiG87282.
RefSeqiNP_419091.1. NC_002696.2.
WP_010918161.1. NC_002696.2.

Genome annotation databases

EnsemblBacteriaiAAK22259; AAK22259; CC_0272.
GeneIDi942379.
KEGGiccr:CC_0272.
PATRICi21297462. VBICauCre124313_0269.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005673 Genomic DNA. Translation: AAK22259.1 .
PIRi G87282.
RefSeqi NP_419091.1. NC_002696.2.
WP_010918161.1. NC_002696.2.

3D structure databases

ProteinModelPortali Q9ABF5.
SMRi Q9ABF5. Positions 18-171.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK22259 ; AAK22259 ; CC_0272 .
GeneIDi 942379.
KEGGi ccr:CC_0272.
PATRICi 21297462. VBICauCre124313_0269.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci CAULO:CC0272-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: ATCC 19089 / CB15.

Entry informationi

Entry nameiDEF_CAUCR
AccessioniPrimary (citable) accession number: Q9ABF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: June 1, 2001
Last modified: November 26, 2014
This is version 79 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3