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Q1LT56

- DEF_BAUCH

UniProt

Q1LT56 - DEF_BAUCH

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Protein
Peptide deformylase
Gene
def, BCI_0416
Organism
Baumannia cicadellinicola subsp. Homalodisca coagulata
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 bindingi91 – 911Iron By similarity
Metal bindingi133 – 1331Iron By similarity
Active sitei134 – 1341 By similarity
Metal bindingi137 – 1371Iron 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

BioCyciBCIC374463:GI6Q-416-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:BCI_0416
OrganismiBaumannia cicadellinicola subsp. Homalodisca coagulata
Taxonomic identifieri374463 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia
ProteomesiUP000002427: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 167167Peptide deformylaseUniRule annotation
PRO_0000301009Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi374463.BCI_0416.

Structurei

3D structure databases

ProteinModelPortaliQ1LT56.
SMRiQ1LT56. Positions 2-164.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0242.
HOGENOMiHOG000243509.
KOiK01462.
OMAiELLAICI.
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.

Q1LT56-1 [UniParc]FASTAAdd to Basket

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MSLLPILYYP DHRLRQISKP VNKINNSIYR IVYDMFDTMY HKNGIGLAAP    50
QVNINLNIIV IDVSENKEQR LVLINPELLA KSGETGIHEG CLSIPEQHGF 100
VPRAKNIKVR ALDLNGNSFN LETNDLQAIC IQHEMDHLVG KLFIDYLSPL 150
KRQRLLKKMK QLIRNLD 167
Length:167
Mass (Da):19,211
Last modified:May 30, 2006 - v1
Checksum:i981018CB933502D1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000238 Genomic DNA. Translation: ABF13812.1.
RefSeqiWP_011520591.1. NC_007984.1.
YP_588858.1. NC_007984.1.

Genome annotation databases

EnsemblBacteriaiABF13812; ABF13812; BCI_0416.
GeneIDi4056394.
KEGGibci:BCI_0416.
PATRICi21074339. VBIBauCic75062_0397.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000238 Genomic DNA. Translation: ABF13812.1 .
RefSeqi WP_011520591.1. NC_007984.1.
YP_588858.1. NC_007984.1.

3D structure databases

ProteinModelPortali Q1LT56.
SMRi Q1LT56. Positions 2-164.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 374463.BCI_0416.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABF13812 ; ABF13812 ; BCI_0416 .
GeneIDi 4056394.
KEGGi bci:BCI_0416.
PATRICi 21074339. VBIBauCic75062_0397.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci BCIC374463:GI6Q-416-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. "Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
    Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
    PLoS Biol. 4:1079-1092(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiDEF_BAUCH
AccessioniPrimary (citable) accession number: Q1LT56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: May 30, 2006
Last modified: September 3, 2014
This is version 54 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