ID   IPNS_STRJU              Reviewed;         329 AA.
AC   P18286;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Isopenicillin N synthase;
DE            Short=IPNS;
DE            EC=1.21.3.1;
GN   Name=pcbC;
OS   Streptomyces jumonjinensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3216857; DOI=10.1007/bf00330495;
RA   Shiffman D., Mevarech M., Jensen S.E., Cohen G., Aharonowitz Y.;
RT   "Cloning and comparative sequence analysis of the gene coding for
RT   isopenicillin N synthase in Streptomyces.";
RL   Mol. Gen. Genet. 214:562-569(1988).
RN   [2]
RP   MUTAGENESIS OF HISTIDINE AND ASPARTIC ACID RESIDUES.
RX   PubMed=8639682; DOI=10.1021/bi951534t;
RA   Borovok I., Landman O., Kreisberg-Zakarin R., Aharonowitz Y., Cohen G.;
RT   "Ferrous active site of isopenicillin N synthase: genetic and sequence
RT   analysis of the endogenous ligands.";
RL   Biochemistry 35:1981-1987(1996).
CC   -!- FUNCTION: Removes, in the presence of oxygen, 4 hydrogen atoms from
CC       delta-L-(alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV) to form the
CC       azetidinone and thiazolidine rings of isopenicillin.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
CC         = 2 H2O + isopenicillin N; Xref=Rhea:RHEA:22428, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:58399, ChEBI:CHEBI:58572; EC=1.21.3.1;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC   -!- PATHWAY: Antibiotic biosynthesis; penicillin G biosynthesis; penicillin
CC       G from L-alpha-aminoadipate and L-cysteine and L-valine: step 2/3.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; M36687; AAA26772.1; -; Genomic_DNA.
DR   AlphaFoldDB; P18286; -.
DR   SMR; P18286; -.
DR   BRENDA; 1.21.3.1; 6045.
DR   UniPathway; UPA00149; UER00240.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016216; F:isopenicillin-N synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.330; -; 1.
DR   InterPro; IPR026992; DIOX_N.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR027443; IPNS-like_sf.
DR   InterPro; IPR002057; Isopenicillin-N_synth_CS.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
DR   PROSITE; PS00185; IPNS_1; 1.
DR   PROSITE; PS00186; IPNS_2; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Iron; Metal-binding; Oxidoreductase; Vitamin C.
FT   CHAIN           1..329
FT                   /note="Isopenicillin N synthase"
FT                   /id="PRO_0000219507"
FT   DOMAIN          180..286
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         212
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         214
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT   BINDING         268
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
SQ   SEQUENCE   329 AA;  37305 MW;  9C8F1EB8FB8BDFC6 CRC64;
     MPILMPSAEV PTIDISPLSG DDAKAKQRVA QEINKAARGS GFFYASNHGV DVQLLQDVVN
     EFHRNMSDQE KHDLAINAYN KDNPHVRNGY YKAIKGKKAV ESFCYLNPSF SDDHPMIKSE
     TPMHEVNLWP DEEKHPRFRP FCEDYYRQLL RLSTVIMRGY ALALGRREDF FDEALAEADT
     LSSVSLIRYP YLEEYPPVKT GADGTKLSFE DHLDVSMITV LYQTEVQNLQ VETVDGWQDI
     PRSDEDFLVN CGTYMGHITH DYFPAPNHRV KFINAERLSL PFFLNAGHNS VIEPFVPEGA
     AGTVKNPTTS YGEYLQHGLR ALIVKNGQT