Reviewed, UniProtKB/Swiss-Prot P12438 (IPNS_STRMI)

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

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.
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	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.

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 reduction 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: UniProtKB-KW isopenicillin-N synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 333	333	Isopenicillin N synthetase		PRO_0000219508
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)
	P12438-1 [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
EMBLGenBankDDBJ	M22081 Genomic DNA. Translation: AAA26771.1.
3D structure databases
HSSP	HSSP built from PDB template 1ODM based on UniProtKB P05326.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.21.3.1. 295835.
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. 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:	June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)