Reviewed, UniProtKB/Swiss-Prot P18286 (IPNS_STRJU)

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 jumonjinensis

Taxonomic identifier

1945 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	329 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 – 329	329	Isopenicillin N synthetase		PRO_0000219507
Sites
	Metal binding	212	1	Iron
	Metal binding	214	1	Iron
	Metal binding	268	1	Iron

Sequences

	Sequence		Length	Mass (Da)
	P18286-1 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: 9C8F1EB8FB8BDFC6	FASTA	329	37,305
	10 20 30 40 50 60 MPILMPSAEV PTIDISPLSG DDAKAKQRVA QEINKAARGS GFFYASNHGV DVQLLQDVVN 70 80 90 100 110 120 EFHRNMSDQE KHDLAINAYN KDNPHVRNGY YKAIKGKKAV ESFCYLNPSF SDDHPMIKSE 130 140 150 160 170 180 TPMHEVNLWP DEEKHPRFRP FCEDYYRQLL RLSTVIMRGY ALALGRREDF FDEALAEADT 190 200 210 220 230 240 LSSVSLIRYP YLEEYPPVKT GADGTKLSFE DHLDVSMITV LYQTEVQNLQ VETVDGWQDI 250 260 270 280 290 300 PRSDEDFLVN CGTYMGHITH DYFPAPNHRV KFINAERLSL PFFLNAGHNS VIEPFVPEGA 310 320 AGTVKNPTTS YGEYLQHGLR ALIVKNGQT

References

[1]	"Cloning and comparative sequence analysis of the gene coding for isopenicillin N synthase in Streptomyces." Shiffman D., Mevarech M., Jensen S.E., Cohen G., Aharonowitz Y. Mol. Gen. Genet. 214:562-569(1988) [PubMed: 3216857] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Ferrous active site of isopenicillin N synthase: genetic and sequence analysis of the endogenous ligands." Borovok I., Landman O., Kreisberg-Zakarin R., Aharonowitz Y., Cohen G. Biochemistry 35:1981-1987(1996) [PubMed: 8639682] [Abstract] Cited for: MUTAGENESIS OF HISTIDINE AND ASPARTIC ACID RESIDUES.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M36687 Genomic DNA. Translation: AAA26772.1.
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. 261270.
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_STRJU

Accession

Primary (citable) accession number: P18286

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	June 16, 2009
This is version 59 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)