O08450 (DEF_CLOB8) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 79.
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 |
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| Organism | Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium acetobutylicum) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 290402 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium › ![]() |
Protein attributes
| Sequence length | 136 AA. |
| Sequence status | Complete. |
| 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. 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 | Complete proteome |
| 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 – 136 | 136 | Peptide deformylase HAMAP-Rule MF_00163 | PRO_0000082768 | |||||
Sites | |||||||||
| Active site | 127 | 1 | By similarity | ||||||
| Metal binding | 85 | 1 | Iron By similarity | ||||||
| Metal binding | 126 | 1 | Iron By similarity | ||||||
| Metal binding | 130 | 1 | Iron By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Truncation of peptide deformylase reduces the growth rate and stabilizes solvent production in Clostridium beijerinckii NCIMB 8052." Evans V.J., Liyanage H., Ravagnani A., Young M., Kashket E.R. Appl. Environ. Microbiol. 64:1780-1785(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Complete sequence of Clostridium beijerinckii NCIMB 8052." US DOE Joint Genome Institute 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., Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J., Larimer F. Richardson P.Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51743 / NCIMB 8052. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z96934 Genomic DNA. Translation: CAB09662.1. CP000721 Genomic DNA. Translation: ABR35634.1. |
| RefSeq | YP_001310590.1. NC_009617.1. |
3D structure databases | |
| ProteinModelPortal | O08450. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 290402.Cbei_3511. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABR35634; ABR35634; Cbei_3511. |
| GeneID | 5294680. |
| KEGG | cbe:Cbei_3511. |
| PATRIC | 19351248. VBICloBei69853_3642. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0242. |
| HOGENOM | HOG000243509. |
| KO | K01462. |
| OMA | YETEESC. |
| ProtClustDB | PRK09218. |
Enzyme and pathway databases | |
| BioCyc | CBEI290402:GHL5-3650-MONOMER. |
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. |
| ProtoNet | Search... |
Entry information
| Entry name | DEF_CLOB8 | ||||||||
| Accession | Primary (citable) accession number: O08450 Secondary accession number(s): A6LZ54 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
