Reviewed,
UniProtKB/Swiss-Prot A6L7J9 (DEF_BACV8)
Last modified
November 3, 2009.
Version 18.
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 | Bacteroides vulgatus (strain ATCC 8482 / DSM 1447 / NCTC 11154) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 435590 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides |
Protein attributes
| Sequence length | 184 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] | "Evolution of symbiotic bacteria in the distal human intestine." Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I. PLoS Biol. 5:1574-1586(2007) [PubMed: 17579514] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000139 Genomic DNA. Translation: ABR41663.1. | |
| RefSeq | YP_001301285.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A6L7J9. |
Genome annotation databases | |
| GeneID | 5305020. |
| GenomeReviews | Gene locus BVU_4061 in contig CP000139_GR. |
| KEGG | bvu:BVU_4061. |
| NMPDR | fig|435590.6.peg.3775. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | KELIANM. |
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_BACV8 | ||||||||
| Accession | Primary (citable) accession number: A6L7J9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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