Reviewed, UniProtKB/Swiss-Prot P10621 (IPNS_STRCL)

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 clavuligerus

Taxonomic identifier

1901 [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_0000219504
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)
	P10621-1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 71AA1CCE9514761C	FASTA	329	36,959
	10 20 30 40 50 60 MPVLMPSAHV PTIDISPLFG TDAAAKKRVA EEIHGACRGS GFFYATNHGV DVQQLQDVVN 70 80 90 100 110 120 EFHGAMTDQE KHDLAIHAYN PDNPHVRNGY YKAVPGRKAV ESFCYLNPDF GEDHPMIAAG 130 140 150 160 170 180 TPMHEVNLWP DEERHPRFRP FCEGYYRQML KLSTVLMRGL ALALGRPEHF FDAALAEQDS 190 200 210 220 230 240 LSSVSLIRYP YLEEYPPVKT GPDGQLLSFE DHLDVSMITV LFQTQVQNLQ VETVDGWRDI 250 260 270 280 290 300 PTSENDFLVN CGTYMAHVTN DYFPAPNHRV KFVNAERLSL PFFLNGGHEA VIEPFVPEGA 310 320 SEEVRNEALS YGDYLQHGLR ALIVKNGQT

References

[1]

"Cloning and nucleotide sequence determination of the isopenicillin N synthetase gene from Streptomyces clavuligerus." Leskiw B.K., Aharonowitz Y., Mevarech M., Wolfe S., Vining L.C., Westlake D.W.S., Jensen S.E. Gene 62:187-196(1988) [PubMed: 3130293] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 27064 / DSM 738 / IFO 13307 / JCM 4710 / NRRL 3585.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M19421 Genomic DNA. Translation: AAA26770.1.
PIR	A29894.
3D structure databases
HSSP	HSSP built from PDB template 1QJE based on UniProtKB P05326.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.21.3.1. 229786.
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_STRCL

Accession

Primary (citable) accession number: P10621

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
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)