Q48739 (IPNS_LYSLA) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 19, 2011.
Version 62.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Isopenicillin N synthase Short name=IPNS EC=1.21.3.1 | ||
| Gene names |
| ||
| Organism | Lysobacter lactamgenus | ||
| Taxonomic identifier | 39596 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Lysobacter |
Protein attributes
| Sequence length | 326 AA. |
| Sequence status | Complete. |
| 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. Contains 1 Fe2OG dioxygenase domain. |
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 |
| Molecular function | L-ascorbic acid binding Inferred from electronic annotation. Source: UniProtKB-KW iron ion bindingInferred from electronic annotation. Source: InterPro isopenicillin-N synthase activityInferred from electronic annotation. Source: EC oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donorsInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
| ||||||||||||||||||
References
| [1] | "Molecular analysis of the gene cluster involved in cephalosporin biosynthesis from Lysobacter lactamgenus YK90." Kimura H., Izawa M., Sumino Y. Appl. Microbiol. Biotechnol. 44:589-596(1996) [PubMed: 8703429] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: YK90. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X56660 Genomic DNA. Translation: CAA39983.1. |
| PIR | S54099. |
3D structure databases | |
| ProteinModelPortal | Q48739. |
| SMR | Q48739. Positions 4-326. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR002057. Isopenicillin-N_synth_CS. IPR002283. Isopenicillin-N_synthase. IPR005123. Oxoglutarate/Fe-dep_oxygenase. [Graphical view] |
| Pfam | PF03171. 2OG-FeII_Oxy. 1 hit. [Graphical view] |
| PRINTS | PR00682. IPNSYNTHASE. |
| PROSITE | PS51471. FE2OG_OXY. 1 hit. PS00185. IPNS_1. 1 hit. PS00186. IPNS_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | IPNS_LYSLA | ||||||||
| Accession | Primary (citable) accession number: Q48739 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with