ID   IPNS_STRCL              Reviewed;         329 AA.
AC   P10621;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Isopenicillin N synthase;
DE            Short=IPNS;
DE            EC=1.21.3.1;
GN   Name=pcbC;
OS   Streptomyces clavuligerus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC   3585 / VKM Ac-602;
RX   PubMed=3130293; DOI=10.1016/0378-1119(88)90557-4;
RA   Leskiw B.K., Aharonowitz Y., Mevarech M., Wolfe S., Vining L.C.,
RA   Westlake D.W.S., Jensen S.E.;
RT   "Cloning and nucleotide sequence determination of the isopenicillin N
RT   synthetase gene from Streptomyces clavuligerus.";
RL   Gene 62:187-196(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; M19421; AAA26770.1; -; Genomic_DNA.
DR   PIR; A29894; A29894.
DR   RefSeq; WP_003952506.1; NZ_CP032052.1.
DR   AlphaFoldDB; P10621; -.
DR   SMR; P10621; -.
DR   STRING; 443255.SCLAV_4199; -.
DR   GeneID; 61469720; -.
DR   eggNOG; COG3491; Bacteria.
DR   OrthoDB; 400496at2; -.
DR   BRENDA; 1.21.3.1; 5988.
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_0000219504"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         214
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         268
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   329 AA;  36959 MW;  71AA1CCE9514761C CRC64;
     MPVLMPSAHV PTIDISPLFG TDAAAKKRVA EEIHGACRGS GFFYATNHGV DVQQLQDVVN
     EFHGAMTDQE KHDLAIHAYN PDNPHVRNGY YKAVPGRKAV ESFCYLNPDF GEDHPMIAAG
     TPMHEVNLWP DEERHPRFRP FCEGYYRQML KLSTVLMRGL ALALGRPEHF FDAALAEQDS
     LSSVSLIRYP YLEEYPPVKT GPDGQLLSFE DHLDVSMITV LFQTQVQNLQ VETVDGWRDI
     PTSENDFLVN CGTYMAHVTN DYFPAPNHRV KFVNAERLSL PFFLNGGHEA VIEPFVPEGA
     SEEVRNEALS YGDYLQHGLR ALIVKNGQT