IPNS_STRGR
ID IPNS_STRGR Reviewed; 329 AA.
AC Q54243;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, 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 Streptomyces griseus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JCM 5012 / NBRC 13304 / NRRL 3851 / KCC S-1012 / MA-2837;
RX PubMed=1901702; DOI=10.1128/aac.35.1.44;
RA Garcia-Dominguea M., Liras P., Martin J.F.;
RT "Cloning and characterization of the isopenicillin N synthase gene of
RT Streptomyces griseus NRRL 3851 and studies of expression and
RT complementation of the cephamycin pathway in Streptomyces clavuligerus.";
RL Antimicrob. Agents Chemother. 35:44-52(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; X54609; CAA38431.1; -; Genomic_DNA.
DR PIR; A61155; A61155.
DR AlphaFoldDB; Q54243; -.
DR SMR; Q54243; -.
DR BRENDA; 1.21.3.1; 6035.
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_0000219506"
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; 37368 MW; 0CD96C8F7CF5A7EB CRC64;
MPIPMLPAHV PTIDISPLSG GDADDKKRVA QEINKACRES GFFYASHHGI DVQLLKDVVN
EFHRTMTDEE KYDLAINAYN KNNPRTRNGY YMAVKGKKAV ESWCYLNPSF SEDHPQIRSG
TPMHEGNIWP DEKRHQRFRP FCEQYYRDVF SLSKVLMRGF ALALGKPEDF FDASLSLADT
LSAVTLIHYP YLEDYPPVKT GPDGTKLSFE DHLDVSMITV LFQTEVQNLQ VETADGWQDL
PTSGENFLVN CGTYMGYLTN DYFPAPNHRV KFINAERLSL PFFLHAGHTT VMEPFSPEDT
RGKELNPPVR YGDYLQQASN ALIAKNGQT
