ID   CEFD_AMYLA              Reviewed;         398 AA.
AC   Q03046;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Isopenicillin N epimerase;
DE            EC=5.1.1.17;
GN   Name=cefD;
OS   Amycolatopsis lactamdurans (Nocardia lactamdurans).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=1913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8437592; DOI=10.1007/bf00277148;
RA   Coque J.J.R., Martin J.F., Liras P.;
RT   "Characterization and expression in Streptomyces lividans of cefD and cefE
RT   genes from Nocardia lactamdurans: the organization of the cephamycin gene
RT   cluster differs from that in Streptomyces clavuligerus.";
RL   Mol. Gen. Genet. 236:453-458(1993).
CC   -!- FUNCTION: Catalyzes the reversible isomerization between isopenicillin
CC       N and penicillin N.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=isopenicillin N = penicillin N; Xref=Rhea:RHEA:20033,
CC         ChEBI:CHEBI:58399, ChEBI:CHEBI:58408; EC=5.1.1.17;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Antibiotic biosynthesis; cephalosporin C biosynthesis.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z13984; CAA78377.1; -; Genomic_DNA.
DR   PIR; S30901; S30901.
DR   AlphaFoldDB; Q03046; -.
DR   SMR; Q03046; -.
DR   UniPathway; UPA00172; -.
DR   GO; GO:0045439; F:isopenicillin-N epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Isomerase; Pyridoxal phosphate.
FT   CHAIN           1..398
FT                   /note="Isopenicillin N epimerase"
FT                   /id="PRO_0000150240"
FT   REGION          243..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         219
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   398 AA;  43619 MW;  71E5EC97FE4737C1 CRC64;
     MVATAWANAR EQVSLDPAVT NLNAGSCGPL PRPVFDRVTV RARMAAGPMD FLSRQLPPLL
     WTARERLAGY LGARPERLAF ATNVTGAVNL VASSVQPHLA AGGEILLSDQ EYAPMRWCWE
     RVARHQGLVV RTFRLPVQPL GSPDEVVEAA TAAMGPRTRL LFFSHVVSST GLVLPATRLC
     EEARRRGVLT VVDGAQAPGF TDLDLAALPC DYYAGSGHKW LLAPTGVGFL HFAEDQGGVL
     RPPQVSWGYR PDGENPSDER NRFGSTDRLR NLECEGTRDL CPWLAVPSAI DFQAGLGHGR
     VRERMRELAA FTRERLSGWR GLEPVTPAHP GLSGAMTAFR LPPGTDTAGL RHGLWDRFRI
     DVPVLDRPDG PLLRVSTHFY NTETEVERLA EALKELSK