ID   IPNS_LYSLA              Reviewed;         326 AA.
AC   Q48739;
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;
OS   Lysobacter lactamgenus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=39596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YK90;
RX   PubMed=8703429; DOI=10.1007/bf00172490;
RA   Kimura H., Izawa M., Sumino Y.;
RT   "Molecular analysis of the gene cluster involved in cephalosporin
RT   biosynthesis from Lysobacter lactamgenus YK90.";
RL   Appl. Microbiol. Biotechnol. 44:589-596(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; X56660; CAA39983.1; -; Genomic_DNA.
DR   PIR; S54099; S54099.
DR   AlphaFoldDB; Q48739; -.
DR   SMR; Q48739; -.
DR   BRENDA; 1.21.3.1; 3119.
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..326
FT                   /note="Isopenicillin N synthase"
FT                   /id="PRO_0000219501"
FT   DOMAIN          183..283
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         209
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         211
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         265
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   326 AA;  36564 MW;  25731F67173F8447 CRC64;
     MNRHADVPVI DISGLSGNDM DVKKDIAARI DRACRGSGFF YAANHGVDLA ALQKFTTDWH
     MAMSPEEKWE LAIRAYNPAN PRNRNGYYMA VEGKKANESF CYLNPSFDAD HATIKAGLPS
     HEVNIWPDEA RHPGMRRFYE AYFSDVFDVA AVILRGFAIA LGREESFFER HFSMDDTLSA
     VSLIRYPFLE NYPPLKLGPD GEKLSFEHHQ DVSLITVLYQ TAIPNLQVET AEGYLDIPVS
     DEHFLVNCGT YMAHITNGYY PAPVHRVKYI NAERLSIPFF ANLSHASAID PFAPPPYAPA
     RGNPTVSYGD YLQHGLLDLI RANGQT