Reviewed,
UniProtKB/Swiss-Prot P27744 (IPNS_NOCLA)
Last modified
June 16, 2009.
Version 55.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Isopenicillin N synthetase EC=1.21.3.1 Alternative name(s): Isopenicillin N synthase Short name=IPNS | ||
| Gene names |
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| Organism | Nocardia lactamdurans | ||
| Taxonomic identifier | 1913 [NCBI] | ||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Pseudonocardineae › Pseudonocardiaceae › Amycolatopsis |
Protein attributes
| Sequence length | 328 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Removes, in the presence of oxygen, 4 hydrogen atoms from delta-L-(alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV) to form the azetidinone and thiazolidine rings of isopenicillin. |
| Catalytic activity | N-((5S)-5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + O2 = isopenicillin N + 2 H2O. |
| 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 |
| 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 iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW isopenicillin-N synthase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "The cephamycin biosynthetic genes pcbAB, encoding a large multidomain peptide synthetase, and pcbC of Nocardia lactamdurans are clustered together in an organization different from the same genes in Acremonium chrysogenum and Penicillium chrysogenum." Coque J.J.R., Martin J.F., Calzada J.G., Liras P. Mol. Microbiol. 5:1125-1133(1991) [PubMed: 1956290] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: VAR LC 411. |
Cross-references
Sequence databases | |
|---|---|
| X57310 Genomic DNA. Translation: CAA40562.1. | |
| PIR | S15284. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1ODM based on UniProtKB P05326. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MON-13365. |
| BRENDA | 1.21.3.1. 261149. |
Family and domain databases | |
| InterPro | IPR002057. Isopenicillin-N_synth_CS. IPR002283. Isopenicillin-N_synthase. IPR005123. Oxoglutarate/Fe-dep_Oase. [Graphical view] |
| Pfam | PF03171. 2OG-FeII_Oxy. 1 hit. [Graphical view] |
| PRINTS | PR00682. IPNSYNTHASE. |
| PROSITE | PS00185. IPNS_1. 1 hit. PS00186. IPNS_2. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | IPNS_NOCLA | ||||||||
| Accession | Primary (citable) accession number: P27744 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


