Reviewed,
UniProtKB/Swiss-Prot A0LUE1 (DEF_ACIC1)
Last modified
November 3, 2009.
Version 17.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names 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 | Acidothermus cellulolyticus (strain ATCC 43068 / 11B) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 351607 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Frankineae › Acidothermaceae › Acidothermus |
Protein attributes
| Sequence length | 180 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| Catalytic activity | Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. HAMAP MF_00163 |
| Cofactor | Binds 1 Fe2+ ion By similarity. |
| 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 |
| Gene Ontology (GO) | |
| Biological process | translation Inferred from electronic annotation. Source: HAMAP |
| Molecular function | iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW peptide deformylase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Complete sequence of Acidothermus cellulolyticus 11B." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. Richardson P.Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000481 Genomic DNA. Translation: ABK53051.1. | |
| RefSeq | YP_873037.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A0LUE1. |
Genome annotation databases | |
| GeneID | 4486350. |
| GenomeReviews | Gene locus Acel_1279 in contig CP000481_GR. |
| KEGG | ace:Acel_1279. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | MAIRRIC. |
Family and domain databases | |
| HAMAP | MF_00163. [Tree] |
| InterPro | IPR000181. Fmet_deformylase. [Graphical view] |
| PANTHER | PTHR10458. Fmet_deformylase. 1 hit. |
| Pfam | PF01327. Pep_deformylase. 1 hit. [Graphical view] |
| PIRSF | PIRSF004749. Pep_def. 1 hit. |
| PRINTS | PR01576. PDEFORMYLASE. |
| ProDom | PD003844. Fmet_deformylase. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR00079. pept_deformyl. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | DEF_ACIC1 | ||||||||
| Accession | Primary (citable) accession number: A0LUE1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


