Reviewed,
UniProtKB/Swiss-Prot P43522 (DEF_THETH)
Last modified
June 16, 2009.
Version 58.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
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 |
| ||
| Organism | Thermus thermophilus | ||
| Taxonomic identifier | 274 [NCBI] | ||
| Taxonomic lineage | Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus |
Protein attributes
| Sequence length | 192 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
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 | 3D-structure |
| 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)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 192 | 192 | Peptide deformylase HAMAP MF_00163 | PRO_0000082867 | |||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||
| Active site | 146 | 1 | By similarity | ||||||||||||||||||||||||||||||||||
| Metal binding | 102 | 1 | Iron By similarity | ||||||||||||||||||||||||||||||||||
| Metal binding | 145 | 1 | Iron By similarity | ||||||||||||||||||||||||||||||||||
| Metal binding | 149 | 1 | Iron By similarity | ||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||
| Helix | 11 – 14 | 4 | |||||||||||||||||||||||||||||||||||
| Helix | 26 – 39 | 14 | |||||||||||||||||||||||||||||||||||
| Beta strand | 43 – 46 | 4 | |||||||||||||||||||||||||||||||||||
| Helix | 47 – 50 | 4 | |||||||||||||||||||||||||||||||||||
| Beta strand | 54 – 60 | 7 | |||||||||||||||||||||||||||||||||||
| Turn | 75 – 77 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 81 – 93 | 13 | |||||||||||||||||||||||||||||||||||
| Beta strand | 96 – 100 | 5 | |||||||||||||||||||||||||||||||||||
| Beta strand | 110 – 115 | 6 | |||||||||||||||||||||||||||||||||||
| Beta strand | 117 – 124 | 8 | |||||||||||||||||||||||||||||||||||
| Beta strand | 130 – 136 | 7 | |||||||||||||||||||||||||||||||||||
| Helix | 137 – 150 | 14 | |||||||||||||||||||||||||||||||||||
| Helix | 155 – 158 | 4 | |||||||||||||||||||||||||||||||||||
| Helix | 161 – 170 | 10 | |||||||||||||||||||||||||||||||||||
| Helix | 172 – 181 | 10 | |||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Characterization of the Thermus thermophilus locus encoding peptide deformylase and methionyl-tRNA(fMet) formyltransferase." Meinnel T., Blanquet S. J. Bacteriol. 176:7387-7390(1994) [PubMed: 7961514] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: VK1. |
| [2] | "Structure-function relationships within the peptide deformylase family. Evidence for a conserved architecture of the active site involving three conserved motifs and a metal ion." Meinnel T., Lazennec C., Villoing S., Blanquet S. J. Mol. Biol. 267:749-761(1997) [PubMed: 9126850] [Abstract] Cited for: CHARACTERIZATION. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| X79087 Genomic DNA. Translation: CAA55695.1. | |||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| ModBase | Search... | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 3.5.1.88. 245. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_00163. [Tree] | ||||||||||||
| InterPro | IPR000181. Fmet_deformylase. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.90.45.10. Fmet_deformylase. 1 hit. | ||||||||||||
| 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_THETH | ||||||||
| Accession | Primary (citable) accession number: P43522 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


