Reviewed,
UniProtKB/Swiss-Prot Q819U0 (DEF1_BACCR)
Last modified
November 3, 2009.
Version 44.
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 1 Short name=PDF 1 EC=3.5.1.88 Alternative name(s): Polypeptide deformylase 1 | ||||
| Gene names |
| ||||
| Organism | Bacillus cereus (strain ATCC 14579 / DSM 31) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 226900 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 156 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 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)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 156 | 156 | Peptide deformylase 1 HAMAP MF_00163 | PRO_0000082735 | |||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||
| Active site | 133 | 1 | By similarity | ||||||||||||||||||||||||||||
| Metal binding | 90 | 1 | Iron By similarity | ||||||||||||||||||||||||||||
| Metal binding | 132 | 1 | Iron By similarity | ||||||||||||||||||||||||||||
| Metal binding | 136 | 1 | Iron By similarity | ||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||
| Helix | 12 – 15 | 4 | |||||||||||||||||||||||||||||
| Helix | 26 – 41 | 16 | |||||||||||||||||||||||||||||
| Beta strand | 45 – 48 | 4 | |||||||||||||||||||||||||||||
| Helix | 49 – 52 | 4 | |||||||||||||||||||||||||||||
| Beta strand | 56 – 62 | 7 | |||||||||||||||||||||||||||||
| Turn | 65 – 67 | 3 | |||||||||||||||||||||||||||||
| Beta strand | 69 – 88 | 20 | |||||||||||||||||||||||||||||
| Beta strand | 98 – 111 | 14 | |||||||||||||||||||||||||||||
| Beta strand | 117 – 123 | 7 | |||||||||||||||||||||||||||||
| Helix | 124 – 137 | 14 | |||||||||||||||||||||||||||||
| Helix | 142 – 144 | 3 | |||||||||||||||||||||||||||||
| Beta strand | 146 – 149 | 4 | |||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis." Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. Kyrpides N.C.Nature 423:87-91(2003) [PubMed: 12721630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AE016877 Genomic DNA. Translation: AAP10787.1. | |||||||||||||||||||
| RefSeq | NP_833586.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| |||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| STRING | Q819U0. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| GeneID | 1206210. | ||||||||||||||||||
| GenomeReviews | Gene locus BC_3865 in contig AE016877_GR. | ||||||||||||||||||
| KEGG | bce:BC3865. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CMR | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOGENOM | Q819U0. | ||||||||||||||||||
| OMA | IGVPRRM. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| BioCyc | BCER226900:BC_3865-MON. | ||||||||||||||||||
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 | DEF1_BACCR | ||||||||
| Accession | Primary (citable) accession number: Q819U0 | ||||||||
| 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


