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ECOLI:DEF
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | def (synonyms: fms) | |
| Protein Name(s) | Peptide deformylase
PDF Polypeptide deformylase | |
| External Links | ||
| UniProt | P0A6K3 | |
| EMBL | X77800 X63666 X65946 X77091 U18997 U00096 AP009048 | |
| PIR | S23107 | |
| RefSeq | NP_417745.1 YP_492146.1 | |
| PDB | 1BS4 1BS5 1BS6 1BS7 1BS8 1BSJ 1BSK 1BSZ 1DEF 1DFF 1DTF 1G27 1G2A 1ICJ 1LRU 1XEM 1XEN 1XEO 2AI8 2DEF 2DTF 2KMN 2VHM 2W3T 2W3U 3K6L 4AL2 4AL3 | |
| PDBsum | 1BS4 1BS5 1BS6 1BS7 1BS8 1BSJ 1BSK 1BSZ 1DEF 1DFF 1DTF 1G27 1G2A 1ICJ 1LRU 1XEM 1XEN 1XEO 2AI8 2DEF 2DTF 2KMN 2VHM 2W3T 2W3U 3K6L 4AL2 4AL3 | |
| ProteinModelPortal | P0A6K3 | |
| SMR | P0A6K3 | |
| DIP | DIP-47953N | |
| IntAct | P0A6K3 | |
| STRING | 511145.b3287 | |
| BindingDB | P0A6K3 | |
| ChEMBL | CHEMBL4976 | |
| PaxDb | P0A6K3 | |
| PRIDE | P0A6K3 | |
| EnsemblBacteria | AAC76312 BAE78005 | |
| GeneID | 12934422 947780 | |
| KEGG | ecj:Y75_p3890 eco:b3287 | |
| PATRIC | 32122006 | |
| EchoBASE | EB1410 | |
| EcoGene | EG11440 | |
| eggNOG | COG0242 | |
| HOGENOM | HOG000243509 | |
| InParanoid | P0A6K3 | |
| KO | K01462 | |
| OMA | FDTMYEE | |
| OrthoDB | EOG664CMF | |
| PhylomeDB | P0A6K3 | |
| BioCyc | EcoCyc:EG11440-MONOMER ECOL316407:JW3248-MONOMER MetaCyc:EG11440-MONOMER | |
| SABIO-RK | P0A6K3 | |
| EvolutionaryTrace | P0A6K3 | |
| PRO | PR:P0A6K3 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P0A6K3 | |
| GO | GO:0008198 GO:0016787 GO:0042586 GO:0043022 GO:0008270 GO:0043686 GO:0031365 GO:0006412 | |
| Gene3D | 3.90.45.10 | |
| HAMAP | MF_00163 | |
| InterPro | IPR000181 IPR023635 | |
| PANTHER | PTHR10458 | |
| Pfam | PF01327 | |
| PIRSF | PIRSF004749 | |
| PRINTS | PR01576 | |
| SUPFAM | SSF56420 | |
| TIGRFAMs | TIGR00079 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0042586 |
peptide deformylase activity |
ECO:0000314 |
F |
The study suggests necessary information about peptide deformylase activity |
complete | |||||
|
involved_in |
GO:0043686 |
co-translational protein modification |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11440 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0042586 |
peptide deformylase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11440 |
F |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0031365 |
N-terminal protein amino acid modification |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11440 |
P |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0018206 |
peptidyl-methionine modification |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000048655 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0042586 |
peptide deformylase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0031365 |
N-terminal protein amino acid modification |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016787 |
hydrolase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008270 |
zinc ion binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008270 |
zinc ion binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008270 |
zinc ion binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0043686 |
co-translational protein modification |
ECO:0000353 |
physical interaction evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0043022 |
ribosome binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042586 |
peptide deformylase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0031365 |
N-terminal protein amino acid modification |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008198 |
ferrous iron binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042586 |
peptide deformylase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006412 |
translation |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000079166 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0042586 |
peptide deformylase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000079166 |
F |
Seeded From UniProt |
complete | ||
|
enables |
GO:0016787 |
hydrolase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006412 |
translation |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Randhawa, H et al. (2013) Overexpression of peptide deformylase in breast, colon, and lung cancers. BMC Cancer 13 321 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 2.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ 3.0 3.1 3.2 3.3 Meinnel, T & Blanquet, S (1995) Enzymatic properties of Escherichia coli peptide deformylase. J. Bacteriol. 177 1883-7 PubMed GONUTS page
- ↑ Meinnel, T & Blanquet, S (1993) Evidence that peptide deformylase and methionyl-tRNA(fMet) formyltransferase are encoded within the same operon in Escherichia coli. J. Bacteriol. 175 7737-40 PubMed GONUTS page
- ↑ Katayama, A et al. (2002) Systematic search for zinc-binding proteins in Escherichia coli. Eur. J. Biochem. 269 2403-13 PubMed GONUTS page
- ↑ Bingel-Erlenmeyer, R et al. (2008) A peptide deformylase-ribosome complex reveals mechanism of nascent chain processing. Nature 452 108-11 PubMed GONUTS page
- ↑ Sandikci, A et al. (2013) Dynamic enzyme docking to the ribosome coordinates N-terminal processing with polypeptide folding. Nat. Struct. Mol. Biol. 20 843-50 PubMed GONUTS page
- ↑ 8.0 8.1 Rajagopalan, PT et al. (1997) Purification, characterization, and inhibition of peptide deformylase from Escherichia coli. Biochemistry 36 13910-8 PubMed GONUTS page
- ↑ Groche, D et al. (1998) Isolation and crystallization of functionally competent Escherichia coli peptide deformylase forms containing either iron or nickel in the active site. Biochem. Biophys. Res. Commun. 246 342-6 PubMed GONUTS page
- ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
