O66847 (DEF_AQUAE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 73.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Peptide deformylase Short name=PDF EC=3.5.1.88 Alternative name(s): Polypeptide deformylase | ||||
| Gene names |
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| Organism | Aquifex aeolicus (strain VF5) | ||||
| Taxonomic identifier | 224324 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex |
Protein attributes
| Sequence length | 169 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | 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. HAMAP MF_00163 |
| Catalytic activity | Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. HAMAP MF_00163 |
| Cofactor | Binds 1 Fe2+ ion By similarity. HAMAP MF_00163 |
| Sequence similarities | Belongs to the polypeptide deformylase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Ligand | Iron Metal-binding |
| Molecular function | Hydrolase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | translation Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | iron ion binding Inferred from electronic annotation. Source: InterPro peptide deformylase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE000657 Genomic DNA. Translation: AAC06802.1. |
| PIR | C70352. |
| RefSeq | NP_213407.1. NC_000918.1. |
3D structure databases | |
| ProteinModelPortal | O66847. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1193265. |
| GenomeReviews | Gene locus aq_579 in contig AE000657_GR. |
| KEGG | aae:aq_579. |
| NMPDR | fig|224324.1.peg.422. |
| PATRIC | 20958680. VBIAquAeo85532_0474. |
Phylogenomic databases | |
| HOGENOM | HBG665227. |
| OMA | MINAHIE. |
| PhylomeDB | O66847. |
| ProtClustDB | CLSK2299438. |
Enzyme and pathway databases | |
| BioCyc | AAEO224324:AQ_579-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00163. Pep_deformylase. [Tree] |
| InterPro | IPR000181. Fmet_deformylase. IPR023635. Peptide_deformylase. [Graphical view] |
| Gene3D | G3DSA:3.90.45.10. Fmet_deformylase. 1 hit. |
| KO | K01462. |
| PANTHER | PTHR10458. Fmet_deformylase. 1 hit. |
| Pfam | PF01327. Pep_deformylase. 1 hit. [Graphical view] |
| PIRSF | PIRSF004749. Pep_def. 1 hit. |
| PRINTS | PR01576. PDEFORMYLASE. |
| SUPFAM | SSF56420. Fmet_deformylase. 1 hit. |
| TIGRFAMs | TIGR00079. Pept_deformyl. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | DEF_AQUAE | ||||||||
| Accession | Primary (citable) accession number: O66847 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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