Reviewed,
UniProtKB/Swiss-Prot Q7V5F9 (DEF2_PROMM)
Last modified
February 9, 2010.
Version 39.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Peptide deformylase 2 Short name=PDF 2 EC=3.5.1.88 Alternative name(s): Polypeptide deformylase 2 | ||||
| Gene names |
| ||||
| Organism | Prochlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 74547 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus |
Protein attributes
| Sequence length | 201 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: 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)
Sequences
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References
| [1] | "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation." Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. Chisholm S.W.Nature 424:1042-1047(2003) [PubMed: 12917642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX548175 Genomic DNA. Translation: CAE21776.1. |
| RefSeq | NP_895428.1. |
3D structure databases | |
| SMR | Q7V5F9. Positions 31-181. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q7V5F9. |
Genome annotation databases | |
| GeneID | 1728260. |
| GenomeReviews | Gene locus PMT_1601 in contig BX548175_GR. |
| KEGG | pmt:PMT1601. |
| NMPDR | fig|74547.1.peg.1595. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0242. |
| HOGENOM | HBG665227. |
| OMA | RITKVDE. |
Enzyme and pathway databases | |
| BioCyc | PMAR74547:PMT1601-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00163. Pep_deformylase. [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. |
| TIGRFAMs | TIGR00079. pept_deformyl. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | DEF2_PROMM | ||||||||
| Accession | Primary (citable) accession number: Q7V5F9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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