ID   IPNS_STRCT              Reviewed;         321 AA.
AC   Q53932;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Isopenicillin N synthase;
DE            Short=IPNS;
DE            EC=1.21.3.1;
GN   Name=pcbC; Synonyms=ipnS;
OS   Streptomyces cattleya.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=29303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9206271;
RA   Wang Y., Li R.;
RT   "Cloning and sequencing the isopenicillin N synthetase (IPNS) gene from
RT   Streptomyces cattleya.";
RL   Wei Sheng Wu Xue Bao 36:87-92(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; D78166; BAA11234.1; -; Genomic_DNA.
DR   PIR; A58458; A58458.
DR   AlphaFoldDB; Q53932; -.
DR   SMR; Q53932; -.
DR   BRENDA; 1.21.3.1; 5990.
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; 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   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..321
FT                   /note="Isopenicillin N synthase"
FT                   /id="PRO_0000219505"
FT   DOMAIN          179..287
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         213
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         215
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         269
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   321 AA;  36577 MW;  BCC0CFFCF7C07AF1 CRC64;
     MPVLMPSADV PTIDISPQLF GTDPTPRRTS RGRSTRPARG SGFFYASHHG IDVRRLQTWS
     NESTTMTDQR STTWRSTRYN ENNSHVRNGY YMARPGRETV ESWCYLNPSF GEDHPMMKAG
     TPMHEVNVWP DEERHPDFGS FGEQYHREVS ASRRCCCGAS RWRRQAGESS SNEVTEEDTL
     SAVSMIRYPY LDPYPEAAIK TGPDGTRLSF EDHLDVSMIT VLSKTEVQNL QVETVDGWQS
     LPTSGENFLI NCGTYLGYLT NDYFPAPNHR VKYVNAERLS LPFFLHAGQN SVMKPFTRRT
     GDRKLNPAVT YGEYLQEGFT R