P12438 (IPNS_STRMI) 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 microflavus (Streptomyces lipmanii)

Taxonomic identifier

1919 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	333 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 – 333	333	Isopenicillin N synthase		PRO_0000219508
Regions
	Domain	180 – 290	111	Fe2OG dioxygenase
Sites
	Metal binding	216	1	Iron By similarity
	Metal binding	218	1	Iron By similarity
	Metal binding	272	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	P12438 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: D55385664EA2CA26	FASTA	333	38,082
	10 20 30 40 50 60 MPVLMPSADV PTIDISPLFG TDPDAKAHVA RQINEACRGS GFFYASHHGI DVRRLQDVVN 70 80 90 100 110 120 EFHRTMTDQE KHDLAIHAYN ENNSHVRNGY YMARPGRKTV ESWCYLNPSF GEDHPMIKAG 130 140 150 160 170 180 TPMHEVNVWP DEERHPDFRS FGEQYYREVF RLSKVLLLRG FALALGKPEE FFENEVTEED 190 200 210 220 230 240 TLSCRSLMIR YPYLDPYPEA AIKTGPDGTR LSFEDHLDVS MITVLFQTEV QNLQVETVDG 250 260 270 280 290 300 WQSLPTSGEN FLINCGTYLG YLTNDYFPAP NHRVKYVNAE RLSLPFFLHA GQNSVMKPFH 310 320 330 PEDTGDRKLN PAVTYGEYLQ EGFHALIAKN VQT

References

[1]

"Cloning and expression in Escherichia coli of isopenicillin N synthetase genes from Streptomyces lipmanii and Aspergillus nidulans." Weigel B.J., Burgett S.G., Chen V.J., Skatrud P.L., Frolik C.A., Queener S.W., Ingolia T.D. J. Bacteriol. 170:3817-3826(1988) [PubMed: 3045077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	M22081 Genomic DNA. Translation: AAA26771.1.
3D structure databases
ProteinModelPortal	P12438.
SMR	P12438. Positions 5-333.
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_STRMI

Accession

Primary (citable) accession number: P12438

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	October 19, 2011
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program