Reviewed,
UniProtKB/Swiss-Prot Q5HKI0 (PFLA_STAEQ)
Last modified
June 16, 2009.
Version 29.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Pyruvate formate-lyase-activating enzyme Short name=PFL-activating enzyme EC=1.97.1.4 | ||||
| Gene names |
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| Organism | Staphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 176279 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 251 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Activation of pyruvate formate-lyase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine By similarity. |
| Catalytic activity | S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical. |
| Cofactor | Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the organic radical-activating enzymes family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Glucose metabolism |
| Cellular component | Cytoplasm |
| Ligand | 4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW oxygen and reactive oxygen species metabolic processInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW [formate-C-acetyltransferase]-activating enzyme activityInferred from electronic annotation. Source: EC iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 251 | 251 | Pyruvate formate-lyase-activating enzyme | PRO_0000271717 | |||||
Sites | |||||||||
| Metal binding | 29 | 1 | Iron-sulfur (4Fe-4S-S-AdoMet) By similarity | ||||||
| Metal binding | 33 | 1 | Iron-sulfur (4Fe-4S-S-AdoMet) By similarity | ||||||
| Metal binding | 36 | 1 | Iron-sulfur (4Fe-4S-S-AdoMet) By similarity | ||||||
Sequences
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References
| [1] | "Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain." Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. Fraser C.M.J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000029 Genomic DNA. Translation: AAW53178.1. | |
| RefSeq | YP_189913.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3240431. |
| GenomeReviews | Gene locus SERP2365 in contig CP000029_GR. |
| KEGG | ser:SERP2365. |
| TIGR | SERP2365. |
Phylogenomic databases | |
| HOGENOM | Q5HKI0. |
| OMA | Q5HKI0. RFVVFMQ. |
Enzyme and pathway databases | |
| BioCyc | SEPI176279:SERP2365-MON. |
Family and domain databases | |
| InterPro | IPR012838. PFLA. IPR001989. Radical_activat_CS. IPR007197. Radical_SAM. [Graphical view] |
| Pfam | PF04055. Radical_SAM. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR02493. PFLA. 1 hit. |
| PROSITE | PS01087. RADICAL_ACTIVATING. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PFLA_STAEQ | ||||||||
| Accession | Primary (citable) accession number: Q5HKI0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


