Q5N5L5 (Q5N5L5_SYNP6) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 54.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Peptide deformylase HAMAP-Rule MF_00163 Short name=PDF HAMAP-Rule MF_00163 EC=3.5.1.88 HAMAP-Rule MF_00163 Alternative name(s): Polypeptide deformylase HAMAP-Rule MF_00163 | ||||
| Gene names |
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| Organism | Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 269084 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechococcus › ![]() |
Protein attributes
| Sequence length | 192 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-Rule MF_00163 |
| Catalytic activity | Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. HAMAP-Rule MF_00163 SAAS SAAS023635 |
| Cofactor | Binds 1 Fe2+ ion By similarity. HAMAP-Rule MF_00163 |
| Sequence similarities | Belongs to the polypeptide deformylase family. HAMAP-Rule MF_00163 RuleBase RU003335 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis HAMAP-Rule MF_00163 SAAS SAAS023635 |
| Ligand | Iron HAMAP-Rule MF_00163 Metal-binding HAMAP-Rule MF_00163 SAAS SAAS023635 |
| Molecular function | Hydrolase HAMAP-Rule MF_00163 SAAS SAAS023635 |
| Technical term | 3D-structure PDB 4DR8 PDB 4DR9 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 | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Active site | 152 | 1 | By similarity HAMAP-Rule MF_00163 | ||||||
| Metal binding | 109 | 1 | Iron By similarity HAMAP-Rule MF_00163 | ||||||
| Metal binding | 151 | 1 | Iron By similarity HAMAP-Rule MF_00163 | ||||||
| Metal binding | 155 | 1 | Iron By similarity HAMAP-Rule MF_00163 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Complete nucleotide sequence of the freshwater unicellular cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene content and organization." Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M., Kanehisa M., Omata T., Sugiura M., Sugita M. Photosyn. Res. 93:55-67(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27144 / PCC 6301 / SAUG 1402/1. |
| [2] | "Structure and function of a cyanophage-encoded peptide deformylase." Frank J.A., Lorimer D., Youle M., Witte P., Craig T., Abendroth J., Rohwer F., Edwards R.A., Segall A.M., Burgin A.B. ISME J. 0:0-0(2013) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2-192. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AP008231 Genomic DNA. Translation: BAD78403.1. | ||||||||||||||||||
| RefSeq | YP_170923.1. NC_006576.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | Q5N5L5. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| STRING | 269084.syc0213_d. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| EnsemblBacteria | BAD78403; BAD78403; syc0213_d. | ||||||||||||||||||
| GeneID | 3199121. | ||||||||||||||||||
| KEGG | syc:syc0213_d. | ||||||||||||||||||
| PATRIC | 32485956. VBISynElo117686_0255. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CMR | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | COG0242. | ||||||||||||||||||
| HOGENOM | HOG000243509. | ||||||||||||||||||
| KO | K01462. | ||||||||||||||||||
| OMA | IQIGVPR. | ||||||||||||||||||
| ProtClustDB | PRK00150. | ||||||||||||||||||
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... | ||||||||||||||||||
Entry information
| Entry name | Q5N5L5_SYNP6 | ||||||||
| Accession | Primary (citable) accession number: Q5N5L5 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
