Reviewed,
UniProtKB/Swiss-Prot P11935 (EXPA_CEPAC)
Last modified
June 16, 2009.
Version 57.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cephalosporin biosynthesis expandase/hydroxylase Including the following 2 domains: 1- Recommended name: Deacetoxycephalosporin C synthetase Short name=DAOCS EC=1.14.20.1 Alternative name(s): Expandase 2- Recommended name: Deacetoxycephalosporin C hydroxylase EC=1.14.11.26 Alternative name(s): Deacetylcephalosporin C synthetase Short name=DACS Beta-lactam hydroxylase | ||
| Gene names |
| ||
| Organism | Cephalosporium acremonium (Acremonium chrysogenum) | ||
| Taxonomic identifier | 5044 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › mitosporic Hypocreales › Acremonium |
Protein attributes
| Sequence length | 332 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | DAOCS catalyzes the step from penicillin N to deacetoxy-cephalosporin C, which is used as a substrate by DACS to form deacetylcephalosporin C. |
| Catalytic activity | Penicillin N + 2-oxoglutarate + O2 = deacetoxycephalosporin C + succinate + CO2 + H2O. Deacetoxycephalosporin C + 2-oxoglutarate + O2 = deacetylcephalosporin C + succinate + CO2. |
| Cofactor | Iron. Ascorbate. |
| Pathway | |
| Sequence similarities | Belongs to the iron/ascorbate-dependent oxidoreductase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Antibiotic biosynthesis |
| Ligand | Iron Metal-binding Vitamin C |
| Molecular function | Oxidoreductase |
| Technical term | Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | antibiotic biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW deacetoxycephalosporin-C hydroxylase activityInferred from electronic annotation. Source: EC deacetoxycephalosporin-C synthase activityInferred from electronic annotation. Source: EC iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Cloning and expression of the fungal expandase/hydroxylase gene involved in cephalosporin biosynthesis." Samson S.M., Dotzlaf J.E., Slisz M.L., Becker G.W., van Frank R.M., Veal L.E., Yeh W.K., Miller J.R., Queener S.W., Ingolia T.D. Biotechnology (N.Y.) 5:1207-1214(1987) Cited for: NUCLEOTIDE SEQUENCE. |
Cross-references
Sequence databases | |
|---|---|
| PIR | A29711. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1RXG based on UniProtKB P18548. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MON-13406. |
| BRENDA | 1.14.11.26. 66776. 1.14.20.1. 66776. |
Family and domain databases | |
| InterPro | IPR002057. Isopenicillin-N_synth_CS. IPR005123. Oxoglutarate/Fe-dep_Oase. [Graphical view] |
| Pfam | PF03171. 2OG-FeII_Oxy. 1 hit. [Graphical view] |
| PROSITE | PS00185. IPNS_1. 1 hit. PS00186. IPNS_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | EXPA_CEPAC | ||||||||
| Accession | Primary (citable) accession number: P11935 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


