O31410 (DEF2_GEOSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 78.
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 2 Short name=PDF 2 EC=3.5.1.88 Alternative name(s): Polypeptide deformylase 2 |
| Organism | Geobacillus stearothermophilus (Bacillus stearothermophilus) |
| Taxonomic identifier | 1422 [NCBI] |
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Geobacillus![]() |
Protein attributes
| Sequence length | 184 AA. |
| Sequence status | Complete. |
| 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. HAMAP-Rule MF_00163 |
| Catalytic activity | Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. HAMAP-Rule 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: InterPro 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 – 184 | 184 | Peptide deformylase 2 HAMAP-Rule MF_00163 | PRO_0000082738 | |||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||
| Active site | 154 | 1 | By similarity | ||||||||||||||||||||||||||||||||
| Metal binding | 110 | 1 | Iron By similarity | ||||||||||||||||||||||||||||||||
| Metal binding | 153 | 1 | Iron By similarity | ||||||||||||||||||||||||||||||||
| Metal binding | 157 | 1 | Iron By similarity | ||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||
| Helix | 4 – 6 | 3 | |||||||||||||||||||||||||||||||||
| Helix | 13 – 16 | 4 | |||||||||||||||||||||||||||||||||
| Helix | 28 – 44 | 17 | |||||||||||||||||||||||||||||||||
| Helix | 47 – 53 | 7 | |||||||||||||||||||||||||||||||||
| Beta strand | 59 – 62 | 4 | |||||||||||||||||||||||||||||||||
| Helix | 63 – 66 | 4 | |||||||||||||||||||||||||||||||||
| Beta strand | 70 – 78 | 9 | |||||||||||||||||||||||||||||||||
| Beta strand | 84 – 97 | 14 | |||||||||||||||||||||||||||||||||
| Beta strand | 99 – 104 | 6 | |||||||||||||||||||||||||||||||||
| Beta strand | 123 – 132 | 10 | |||||||||||||||||||||||||||||||||
| Beta strand | 138 – 144 | 7 | |||||||||||||||||||||||||||||||||
| Helix | 145 – 158 | 14 | |||||||||||||||||||||||||||||||||
| Helix | 163 – 166 | 4 | |||||||||||||||||||||||||||||||||
| Beta strand | 180 – 182 | 3 | |||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: ATCC 1518. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | Y10549 Genomic DNA. Translation: CAA71581.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | O31410. | ||||||||||||
| SMR | O31410. Positions 1-184. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| Gene3D | 3.90.45.10. 1 hit. | ||||||||||||
| HAMAP | MF_00163. Pep_deformylase. | ||||||||||||
| InterPro | IPR000181. Fmet_deformylase. IPR023635. Peptide_deformylase. [Graphical view] | ||||||||||||
| PANTHER | PTHR10458. PTHR10458. 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... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | O31410. | ||||||||||||
Entry information
| Entry name | DEF2_GEOSE | ||||||||
| Accession | Primary (citable) accession number: O31410 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
