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.

O31410

- DEF2_GEOSE

UniProt

O31410 - DEF2_GEOSE

(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 2
Gene
N/A
Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 3 out of 5 - 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

Binds 1 Fe2+ ion By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi110 – 1101Iron By similarity
Metal bindingi153 – 1531Iron By similarity
Active sitei154 – 1541 By similarity
Metal bindingi157 – 1571Iron 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

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide deformylase 2 (EC:3.5.1.88)
Short name:
PDF 2
Alternative name(s):
Polypeptide deformylase 2
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 184184Peptide deformylase 2UniRule annotation
PRO_0000082738Add
BLAST

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 63
Helixi13 – 164
Helixi28 – 4417
Helixi47 – 537
Beta strandi59 – 624
Helixi63 – 664
Beta strandi70 – 789
Beta strandi84 – 9714
Beta strandi99 – 1046
Beta strandi123 – 13210
Beta strandi138 – 1447
Helixi145 – 15814
Helixi163 – 1664
Beta strandi180 – 1823

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LQYX-ray1.90A1-184[»]
ProteinModelPortaliO31410.
SMRiO31410. Positions 1-184.

Miscellaneous databases

EvolutionaryTraceiO31410.

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.

O31410-1 [UniParc]FASTAAdd to Basket

« Hide

MITMKDIIKE GHPTLRKVAE PVPLPPSEED KRILQSLLDY VKMSQDPELA    50
AKYGLRPGIG LAAPQINVSK RMIAVHVTDE NGTLYSYALF NPKIVSHSVQ 100
QCYLTTGEGC LSVDRDVPGY VLRYARITVT GTTLDGEEVT LRLKGLPAIV 150
FQHEIDHLNG IMFYDRINPA DPFQVPDGAI PIGR 184
Length:184
Mass (Da):20,383
Last modified:January 1, 1998 - v1
Checksum:i9CD85DEE53632FA0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y10549 Genomic DNA. Translation: CAA71581.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y10549 Genomic DNA. Translation: CAA71581.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LQY X-ray 1.90 A 1-184 [» ]
ProteinModelPortali O31410.
SMRi O31410. Positions 1-184.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei O31410.

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. "Structure-function relationships within the peptide deformylase family. Evidence for a conserved architecture of the active site involving three conserved motifs and a metal ion."
    Meinnel T., Lazennec C., Villoing S., Blanquet S.
    J. Mol. Biol. 267:749-761(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: ATCC 1518.

Entry informationi

Entry nameiDEF2_GEOSE
AccessioniPrimary (citable) accession number: O31410
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: February 19, 2014
This is version 80 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

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi