ID   IPNS_AMYLA              Reviewed;         328 AA.
AC   P27744;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Isopenicillin N synthase;
DE            Short=IPNS;
DE            EC=1.21.3.1;
GN   Name=pcbC;
OS   Amycolatopsis lactamdurans (Nocardia lactamdurans).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=1913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VAR LC 411;
RX   PubMed=1956290; DOI=10.1111/j.1365-2958.1991.tb01885.x;
RA   Coque J.J.R., Martin J.F., Calzada J.G., Liras P.;
RT   "The cephamycin biosynthetic genes pcbAB, encoding a large multidomain
RT   peptide synthetase, and pcbC of Nocardia lactamdurans are clustered
RT   together in an organization different from the same genes in Acremonium
RT   chrysogenum and Penicillium chrysogenum.";
RL   Mol. Microbiol. 5:1125-1133(1991).
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; X57310; CAA40562.1; -; Genomic_DNA.
DR   PIR; S15284; S15284.
DR   AlphaFoldDB; P27744; -.
DR   SMR; P27744; -.
DR   BioCyc; MetaCyc:MON-13365; -.
DR   BRENDA; 1.21.3.1; 311.
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.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Iron; Metal-binding; Oxidoreductase; Vitamin C.
FT   CHAIN           1..328
FT                   /note="Isopenicillin N synthase"
FT                   /id="PRO_0000219502"
FT   DOMAIN          178..284
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         210
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         212
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         266
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   328 AA;  37466 MW;  F0DE8B0727AC3855 CRC64;
     MKMPSAEVPT IDVSPLFGDD AQEKVRVGQE INKACRGSGF FYAANHGVDV QRLQDVVNEF
     HRTMSPQEKY DLAIHAYNKN NSHVRNGYYM AIEGKKAVES FCYLNPSFSE DHPEIKAGTP
     MHEVNSWPDE EKHPSFRPFC EEYYWTMHRL SKVLMRGFAL ALGKDERFFE PELKEADTLS
     SVSLIRYPYL EDYPPVKTGP DGEKLSFEDH FDVSMITVLY QTQVQNLQVE TVDGWRDLPT
     SDTDFLVNAG TYLGHLTNDY FPSPLHRVKF VNAERLSLPF FFHAGQHTLI EPFFPDGAPE
     GKQGNEAVRY GDYLNHGLHS LIVKNGQT