B2DYI4 (B2DYI4_STRPN) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 15.
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 MF_00163 Short name=PDF HAMAP MF_00163 EC=3.5.1.88 HAMAP MF_00163 Alternative name(s): Polypeptide deformylase HAMAP MF_00163 | ||||||
| Gene names |
| ||||||
| Organism | Streptococcus pneumoniae CDC3059-06 EMBL EDT97259.1 | ||||||
| Taxonomic identifier | 453365 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus |
Protein attributes
| Sequence length | 203 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 SAAS SAAS000181 |
| Cofactor | Binds 1 Fe2+ ion By similarity. HAMAP MF_00163 |
| Sequence similarities | Belongs to the polypeptide deformylase family. HAMAP MF_00163 RuleBase RU003335 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis HAMAP MF_00163 SAAS SAAS000181 |
| Ligand | Iron HAMAP MF_00163 Metal-binding HAMAP MF_00163 SAAS SAAS000181 |
| Molecular function | Hydrolase HAMAP MF_00163 SAAS SAAS000181 EMBL EDT97259.1 |
| 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 | 174 | 1 | By similarity HAMAP MF_00163 | ||||||
| Metal binding | 130 | 1 | Iron By similarity HAMAP MF_00163 | ||||||
| Metal binding | 173 | 1 | Iron By similarity HAMAP MF_00163 | ||||||
| Metal binding | 177 | 1 | Iron By similarity HAMAP MF_00163 | ||||||
Sequences
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References
| [1] | "Genome Sequence of Streptococcus pneumoniae CDC3059-06." Dunning Hotopp J., Dodson R., Masignani V., Coan P., Kumar N., Covacci A., Beall B., Rappuoli R., Hollingshead S., Tettelin H. Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: CDC3059-06 EMBL EDT97259.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | ABGG01000002 Genomic DNA. Translation: EDT97259.1. |
3D structure databases | |
| ProteinModelPortal | B2DYI4. |
| SMR | B2DYI4. Positions 2-203. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| PATRIC | 28632669. VBIStrPne114647_0746. |
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. |
| 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 | B2DYI4_STRPN | ||||||||
| Accession | Primary (citable) accession number: B2DYI4 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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