Q9F2F0 (DEF_STRPN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 76.
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 |
| ||||
| Organism | Streptococcus pneumoniae [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1313 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus |
Protein attributes
| Sequence length | 203 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 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 | 3D-structure Complete 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)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 203 | 203 | Peptide deformylase HAMAP MF_00163 | PRO_0000082857 | ||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||
| Active site | 174 | 1 | By similarity | |||||||||||||||||||||||||||||||||||
| Metal binding | 130 | 1 | Iron By similarity | |||||||||||||||||||||||||||||||||||
| Metal binding | 173 | 1 | Iron By similarity | |||||||||||||||||||||||||||||||||||
| Metal binding | 177 | 1 | Iron By similarity | |||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||
| Helix | 3 – 7 | 5 | ||||||||||||||||||||||||||||||||||||
| Helix | 16 – 18 | 3 | ||||||||||||||||||||||||||||||||||||
| Helix | 25 – 28 | 4 | ||||||||||||||||||||||||||||||||||||
| Helix | 40 – 56 | 17 | ||||||||||||||||||||||||||||||||||||
| Helix | 59 – 65 | 7 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 71 – 74 | 4 | ||||||||||||||||||||||||||||||||||||
| Helix | 75 – 78 | 4 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 82 – 89 | 8 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 105 – 117 | 13 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 119 – 124 | 6 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 143 – 145 | 3 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 147 – 152 | 6 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 158 – 163 | 6 | ||||||||||||||||||||||||||||||||||||
| Helix | 165 – 178 | 14 | ||||||||||||||||||||||||||||||||||||
| Helix | 183 – 186 | 4 | ||||||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Peptide deformylase as an antibacterial drug target: target validation and resistance development." Apfel C.M., Locher H., Evers S., Takacs B., Hubschwerlen C., Pirson W., Page M.G., Keck W. Antimicrob. Agents Chemother. 45:1058-1064(2001) [PubMed: 11257016] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Complete genome sequence of a virulent isolate of Streptococcus pneumoniae." Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D., Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J., Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D., Umayam L.A., White O., Salzberg S.L. Fraser C.M.Science 293:498-506(2001) [PubMed: 11463916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-334 / TIGR4. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AJ278785 Genomic DNA. Translation: CAC15392.1. AE005672 Genomic DNA. Translation: AAK75550.1. | ||||||||||||
| PIR | E95169. | ||||||||||||
| RefSeq | NP_345910.1. NC_003028.3. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q9F2F0. | ||||||||||||
| SMR | Q9F2F0. Positions 2-203. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | EBSTRT00000025540; EBSTRP00000024632; EBSTRG00000025540. | ||||||||||||
| GeneID | 931384. | ||||||||||||
| GenomeReviews | Gene locus SP_1456 in contig AE005672_GR. | ||||||||||||
| KEGG | spn:SP_1456. | ||||||||||||
| PATRIC | 19707331. VBIStrPne105772_1508. | ||||||||||||
| TIGR | SP_1456. | ||||||||||||
Phylogenomic databases | |||||||||||||
| GeneTree | EBGT00050000026595. | ||||||||||||
| HOGENOM | HBG665227. | ||||||||||||
| OMA | ADGEGCL. | ||||||||||||
| ProtClustDB | PRK00150. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | SPNE170187-1:SP_1456-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_STRPN | ||||||||
| Accession | Primary (citable) accession number: Q9F2F0 | ||||||||
| 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