IPNS_FLASS
ID IPNS_FLASS Reviewed; 326 AA.
AC P16020;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Isopenicillin N synthase;
DE Short=IPNS;
DE EC=1.21.3.1;
GN Name=pcbC;
OS Flavobacterium sp. (strain SC 12,154).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium; unclassified Flavobacterium.
OX NCBI_TaxID=241;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2308852; DOI=10.1093/nar/18.3.660;
RA Shiffman D., Cohen G., Aharonowitz Y., von Dohren H., Kleinkauf H.,
RA Mevarech M.;
RT "Nucleotide sequence of the isopenicillin N synthase gene (pcbC) of the
RT Gram-negative Flavobacterium sp. SC 12,154.";
RL Nucleic Acids Res. 18:660-660(1990).
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; X17355; CAA35233.1; -; Genomic_DNA.
DR AlphaFoldDB; P16020; -.
DR SMR; P16020; -.
DR BRENDA; 1.21.3.1; 15631.
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_0000219500"
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; 36465 MW; 256E274316395837 CRC64;
MNRHADVPVI DISGLSGNDM DVKKDIAARI DRACRGSGFF YAANHGVDLA ALQKFTTDWH
MAMSAEEKWE LAIRAYNPAN PRNRNGYYMA VEGKKANESF CYLNPSFDAD HATIKAGLPS
HEVNIWPDEA RHPGMRRFYE AYFSDVFDVA AVILRGFAIA LGREESFFER HFSMDDTLSA
VSLIRYPFLE NYPPLKLGPD GEKLSFEHHQ DVSLITVLYQ TAIPNLQVET AEGYLDIPVS
DEHFLVNCGT YMAHITNGYY PAPVHRVKYI NAERLSIPFF ANLSHASAID PFAPPPYAPP
GGNPTVSYGD YLQHGLLDLI RANGQT
