Q6NC51 (DEF_RHOPA) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 46.
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 | Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 258594 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Rhodopseudomonas |
Protein attributes
| Sequence length | 175 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 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 | 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)
Sequences
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References
| [1] | "Complete genome sequence of the metabolically versatile photosynthetic bacterium Rhodopseudomonas palustris." Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L., Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R., Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C., Harrison F.H., Gibson J., Harwood C.S. Nat. Biotechnol. 22:55-61(2004) [PubMed: 14704707] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-98 / CGA009. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX572594 Genomic DNA. Translation: CAE26065.1. |
| RefSeq | NP_945974.1. NC_005296.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1N5N based on UniProtKB Q9I7A8. |
| ProteinModelPortal | Q6NC51. |
| SMR | Q6NC51. Positions 2-171. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2692860. |
| GenomeReviews | Gene locus RPA0621 in contig BX571963_GR. |
| KEGG | rpa:RPA0621. |
| NMPDR | fig|258594.1.peg.618. |
| PATRIC | 23285421. VBIRhoPal84835_0656. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG665227. |
| OMA | EIVSKQG. |
| ProtClustDB | PRK00150. |
Enzyme and pathway databases | |
| BioCyc | RPAL258594:RPA0621-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_RHOPA | ||||||||
| Accession | Primary (citable) accession number: Q6NC51 | ||||||||
| 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