SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B0SHH1

- DEF_LEPBA

UniProt

B0SHH1 - DEF_LEPBA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Peptide deformylase
Gene
def, LBF_1521
Organism
Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames)
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 bindingi103 – 1031Iron By similarity
Metal bindingi145 – 1451Iron By similarity
Active sitei146 – 1461 By similarity
Metal bindingi149 – 1491Iron 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

BioCyciLBIF355278:GHTJ-1519-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:LBF_1521
OrganismiLeptospira biflexa serovar Patoc (strain Patoc 1 / Ames)
Taxonomic identifieri355278 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira
ProteomesiUP000001846: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 179179Peptide deformylaseUniRule annotation
PRO_1000097321Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi355278.LBF_1521.

Structurei

3D structure databases

ProteinModelPortaliB0SHH1.
SMRiB0SHH1. Positions 2-179.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0242.
HOGENOMiHOG000243508.
KOiK01462.
OMAiALEYPSE.
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.

B0SHH1-1 [UniParc]FASTAAdd to Basket

« Hide

MAVRKILKIG NPILRQTSED VSESEIQTKD FKKLIRDMFE TMRHADGVGL    50
AAPQIGVLKK LVVVGQEDDN ERYPGTPEVP NQIILNPEIT PLSPPRDGFW 100
EGCLSVPGMR GYVERPNKIR MKWRDENYVE HDEIIEGYRA IVLQHECDHL 150
FGVLYVDRLK STKLFGYNED IDTAGKLLD 179
Length:179
Mass (Da):20,479
Last modified:April 8, 2008 - v1
Checksum:i50A5293F6C91CCE5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000777 Genomic DNA. Translation: ABZ94032.1.
RefSeqiYP_001962610.1. NC_010842.1.

Genome annotation databases

EnsemblBacteriaiABZ94032; ABZ94032; LBF_1521.
GeneIDi6388120.
KEGGilbf:LBF_1521.
PATRICi22342115. VBILepBif95142_1617.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000777 Genomic DNA. Translation: ABZ94032.1 .
RefSeqi YP_001962610.1. NC_010842.1.

3D structure databases

ProteinModelPortali B0SHH1.
SMRi B0SHH1. Positions 2-179.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 355278.LBF_1521.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABZ94032 ; ABZ94032 ; LBF_1521 .
GeneIDi 6388120.
KEGGi lbf:LBF_1521.
PATRICi 22342115. VBILepBif95142_1617.

Phylogenomic databases

eggNOGi COG0242.
HOGENOMi HOG000243508.
KOi K01462.
OMAi ALEYPSE.
OrthoDBi EOG664CMF.

Enzyme and pathway databases

BioCyci LBIF355278:GHTJ-1519-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. "Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis."
    Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., Rood J.I., Lajus A.
    , Davies J.K., Medigue C., Adler B.
    PLoS ONE 3:E1607-E1607(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Patoc 1 / Ames.

Entry informationi

Entry nameiDEF_LEPBA
AccessioniPrimary (citable) accession number: B0SHH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
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