ID   IPNS_STRMI              Reviewed;         333 AA.
AC   P12438;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Isopenicillin N synthase;
DE            Short=IPNS;
DE            EC=1.21.3.1;
GN   Name=pcbC;
OS   Streptomyces microflavus (Streptomyces lipmanii).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3045077; DOI=10.1128/jb.170.9.3817-3826.1988;
RA   Weigel B.J., Burgett S.G., Chen V.J., Skatrud P.L., Frolik C.A.,
RA   Queener S.W., Ingolia T.D.;
RT   "Cloning and expression in Escherichia coli of isopenicillin N synthetase
RT   genes from Streptomyces lipmanii and Aspergillus nidulans.";
RL   J. Bacteriol. 170:3817-3826(1988).
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; M22081; AAA26771.1; -; Genomic_DNA.
DR   AlphaFoldDB; P12438; -.
DR   SMR; P12438; -.
DR   BRENDA; 1.21.3.1; 6051.
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..333
FT                   /note="Isopenicillin N synthase"
FT                   /id="PRO_0000219508"
FT   DOMAIN          180..290
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         216
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         218
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         272
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   333 AA;  38082 MW;  D55385664EA2CA26 CRC64;
     MPVLMPSADV PTIDISPLFG TDPDAKAHVA RQINEACRGS GFFYASHHGI DVRRLQDVVN
     EFHRTMTDQE KHDLAIHAYN ENNSHVRNGY YMARPGRKTV ESWCYLNPSF GEDHPMIKAG
     TPMHEVNVWP DEERHPDFRS FGEQYYREVF RLSKVLLLRG FALALGKPEE FFENEVTEED
     TLSCRSLMIR YPYLDPYPEA AIKTGPDGTR LSFEDHLDVS MITVLFQTEV QNLQVETVDG
     WQSLPTSGEN FLINCGTYLG YLTNDYFPAP NHRVKYVNAE RLSLPFFLHA GQNSVMKPFH
     PEDTGDRKLN PAVTYGEYLQ EGFHALIAKN VQT