Q54243 (IPNS_STRGR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Isopenicillin N synthase
Short name=IPNS
EC=1.21.3.1

Gene names

Name:

pcbC

Organism

Streptomyces griseus

Taxonomic identifier

1911 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	329 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	Antibiotic biosynthesis; penicillin G biosynthesis; penicillin G from L-alpha-aminoadipate and L-cysteine and L-valine: step 2/3.
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 binding Inferred from electronic annotation. Source: InterPro isopenicillin-N synthase activity Inferred 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 donors Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 329	329	Isopenicillin N synthase		PRO_0000219506
Regions
	Domain	180 – 286	107	Fe2OG dioxygenase
Sites
	Metal binding	212	1	Iron By similarity
	Metal binding	214	1	Iron By similarity
	Metal binding	268	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54243 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 0CD96C8F7CF5A7EB	FASTA	329	37,368
	10 20 30 40 50 60 MPIPMLPAHV PTIDISPLSG GDADDKKRVA QEINKACRES GFFYASHHGI DVQLLKDVVN 70 80 90 100 110 120 EFHRTMTDEE KYDLAINAYN KNNPRTRNGY YMAVKGKKAV ESWCYLNPSF SEDHPQIRSG 130 140 150 160 170 180 TPMHEGNIWP DEKRHQRFRP FCEQYYRDVF SLSKVLMRGF ALALGKPEDF FDASLSLADT 190 200 210 220 230 240 LSAVTLIHYP YLEDYPPVKT GPDGTKLSFE DHLDVSMITV LFQTEVQNLQ VETADGWQDL 250 260 270 280 290 300 PTSGENFLVN CGTYMGYLTN DYFPAPNHRV KFINAERLSL PFFLHAGHTT VMEPFSPEDT 310 320 RGKELNPPVR YGDYLQQASN ALIAKNGQT

References

[1]

"Cloning and characterization of the isopenicillin N synthase gene of Streptomyces griseus NRRL 3851 and studies of expression and complementation of the cephamycin pathway in Streptomyces clavuligerus." Garcia-Dominguea M., Liras P., Martin J.F. Antimicrob. Agents Chemother. 35:44-52(1991) [PubMed: 1901702] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NBRC 13304 / NRRL 3851 / KCC S-1012 / MA-2837.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X54609 Genomic DNA. Translation: CAA38431.1.
PIR	A61155.
3D structure databases
ProteinModelPortal	Q54243.
SMR	Q54243. Positions 5-329.
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_STRGR

Accession

Primary (citable) accession number: Q54243

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1996
Last modified:	October 19, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program