Skip Header

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

P96113

- DEF_THEMA

UniProt

P96113 - DEF_THEMA

(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

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 2 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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

Binds 1 Fe2+ ion.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi87 – 871IronBy similarity
Metal bindingi129 – 1291IronBy similarity
Active sitei130 – 1301By similarity
Metal bindingi133 – 1331IronBy 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 (EC:3.5.1.88)
Short name:
PDF
Alternative name(s):
Polypeptide deformylase
Gene namesi
Name:def
Ordered Locus Names:TM_1661
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000008183: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 164164Peptide deformylasePRO_0000082866Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243274.TM1661.

Structurei

Secondary structure

1
164
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 123
Helixi24 – 3916
Beta strandi43 – 464
Helixi47 – 504
Beta strandi54 – 596
Beta strandi61 – 633
Beta strandi66 – 7611
Beta strandi80 – 856
Beta strandi95 – 10814
Beta strandi114 – 1207
Helixi121 – 13414
Helixi139 – 1424

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LMEX-ray2.20A/B1-164[»]
ProteinModelPortaliP96113.
SMRiP96113. Positions 1-145.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP96113.

Family & Domainsi

Sequence similaritiesi

Belongs to the polypeptide deformylase family.Curated

Phylogenomic databases

eggNOGiCOG0242.
InParanoidiP96113.
KOiK01462.
OMAiEETGEEW.
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.

P96113 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYRIRVFGDP VLRKRAKPVT KFDENLKKTI ERMIETMYHY DGVGLAAPQV
60 70 80 90 100
GISQRFFVMD VGNGPVAVIN PEILEIDPET EVAEEGCLSF PEIFVEIERS
110 120 130 140 150
KRIKVKYQNT RGEYVEEELE GYAARVFQHE FDHLNGVLII DRISPAKRLL
160
LRKKLMDIAR TVKR
Length:164
Mass (Da):19,024
Last modified:May 1, 1997 - v1
Checksum:i9FE94A206DE50842
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y10306 Genomic DNA. Translation: CAA71356.1.
AE000512 Genomic DNA. Translation: AAD36728.1.
PIRiC72224.
RefSeqiNP_229461.1. NC_000853.1.
WP_004082176.1. NC_023151.1.
YP_007978019.1. NC_021214.1.
YP_008991245.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD36728; AAD36728; TM_1661.
GeneIDi18093038.
897909.
KEGGitma:TM1661.
tmi:THEMA_05940.
tmm:Tmari_1670.
PATRICi23938296. VBITheMar51294_1680.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y10306 Genomic DNA. Translation: CAA71356.1 .
AE000512 Genomic DNA. Translation: AAD36728.1 .
PIRi C72224.
RefSeqi NP_229461.1. NC_000853.1.
WP_004082176.1. NC_023151.1.
YP_007978019.1. NC_021214.1.
YP_008991245.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LME X-ray 2.20 A/B 1-164 [» ]
ProteinModelPortali P96113.
SMRi P96113. Positions 1-145.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243274.TM1661.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD36728 ; AAD36728 ; TM_1661 .
GeneIDi 18093038.
897909.
KEGGi tma:TM1661.
tmi:THEMA_05940.
tmm:Tmari_1670.
PATRICi 23938296. VBITheMar51294_1680.

Phylogenomic databases

eggNOGi COG0242.
InParanoidi P96113.
KOi K01462.
OMAi EETGEEW.
OrthoDBi EOG664CMF.

Miscellaneous databases

EvolutionaryTracei P96113.

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

« Hide 'large scale' publications
  1. "A survey of polypeptide deformylase function throughout the eubacterial lineage."
    Mazel D., Coic E., Blanchard S., Saurin W., Marliere P.
    J. Mol. Biol. 266:939-949(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

Entry informationi

Entry nameiDEF_THEMA
AccessioniPrimary (citable) accession number: P96113
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: October 29, 2014
This is version 107 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, Complete proteome, Reference proteome

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