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B1LB14

- DEF_THESQ

UniProt

B1LB14 - DEF_THESQ

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Protein

Peptide deformylase

Gene

def

Organism
Thermotoga sp. (strain RQ2)
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

Binds 1 Fe2+ ion.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi87 – 871IronUniRule annotation
Metal bindingi129 – 1291IronUniRule annotation
Active sitei130 – 1301UniRule annotation
Metal bindingi133 – 1331IronUniRule 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

BioCyciTSP126740:GH49-1204-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:TRQ2_1168
OrganismiThermotoga sp. (strain RQ2)
Taxonomic identifieri126740 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000001687: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 164164Peptide deformylasePRO_1000097355Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi126740.TRQ2_1168.

Structurei

3D structure databases

ProteinModelPortaliB1LB14.
SMRiB1LB14. Positions 1-145.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the polypeptide deformylase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0242.
HOGENOMiHOG000243509.
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.

B1LB14-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYRIRVFGDP VLRKRAKPVT KFDDNLKKTI 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):19,010
Last modified:April 29, 2008 - v1
Checksum:i9FE94BFB1D7B7907
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000969 Genomic DNA. Translation: ACB09512.1.
RefSeqiYP_001739195.1. NC_010483.1.

Genome annotation databases

EnsemblBacteriaiACB09512; ACB09512; TRQ2_1168.
GeneIDi6092603.
KEGGitrq:TRQ2_1168.
PATRICi23948938. VBITheSp108950_1189.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000969 Genomic DNA. Translation: ACB09512.1 .
RefSeqi YP_001739195.1. NC_010483.1.

3D structure databases

ProteinModelPortali B1LB14.
SMRi B1LB14. Positions 1-145.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 126740.TRQ2_1168.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACB09512 ; ACB09512 ; TRQ2_1168 .
GeneIDi 6092603.
KEGGi trq:TRQ2_1168.
PATRICi 23948938. VBITheSp108950_1189.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci TSP126740:GH49-1204-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: RQ2.

Entry informationi

Entry nameiDEF_THESQ
AccessioniPrimary (citable) accession number: B1LB14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: October 1, 2014
This is version 45 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