ID   CEFD_STRCL              Reviewed;         398 AA.
AC   P18549;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Isopenicillin N epimerase;
DE            EC=5.1.1.17;
GN   Name=cefD;
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=1694525; DOI=10.1128/jb.172.7.3952-3958.1990;
RA   Kovacevic S., Tobin M.B., Miller J.R.;
RT   "The beta-lactam biosynthesis genes for isopenicillin N epimerase and
RT   deacetoxycephalosporin C synthetase are expressed from a single transcript
RT   in Streptomyces clavuligerus.";
RL   J. Bacteriol. 172:3952-3958(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-24.
RX   PubMed=2804141; DOI=10.1016/0167-4838(89)90033-2;
RA   Usui S., Yu C.-A.;
RT   "Purification and properties of isopenicillin N epimerase from Streptomyces
RT   clavuligerus.";
RL   Biochim. Biophys. Acta 999:78-85(1989).
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}.
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DR   EMBL; M32324; AAA26714.1; -; Genomic_DNA.
DR   PIR; T52311; T52311.
DR   RefSeq; WP_003952494.1; NZ_CP032052.1.
DR   AlphaFoldDB; P18549; -.
DR   SMR; P18549; -.
DR   STRING; 443255.SCLAV_4210; -.
DR   GeneID; 61469710; -.
DR   KEGG; ag:AAA26714; -.
DR   eggNOG; COG0520; Bacteria.
DR   OMA; VLGMTWV; -.
DR   OrthoDB; 446447at2; -.
DR   BioCyc; MetaCyc:MON-13381; -.
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   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Direct protein sequencing; Isomerase;
KW   Pyridoxal phosphate.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2804141"
FT   CHAIN           2..398
FT                   /note="Isopenicillin N epimerase"
FT                   /id="PRO_0000150241"
FT   MOD_RES         217
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   398 AA;  43498 MW;  EDE15C08246DA77A CRC64;
     MAVADWEEAR GRMLLDPTVV NLNTGSGGPL PRSAFERVTG FRAHLAAEPM DFLLREVPAL
     LWQARESLAR LIGGDPLRLA LATNVTAAVN LVASSLRLEA PGEILLSDDE YTPMRWCWER
     VARRHGLELR TFRLPELPSD PAEITAAAVA AMGPRTRLFF FSHVVSTTGL ILPAAELCEE
     ARARGITTVV DGAHAPGFLD LDLSRIPCDF YAGSGHKWLL APTGVGFLHL APGRLEELEP
     TQVSWAYEPP EGSGPPAARD RFGSTPGLRR LECEGTRDIC PWLATPESID FQAELGPGAI
     RARRRELTDH ARRLLADRPG RTLLTPDSPE LSGGMVAYRL PPGTDAAELR RGLWERFRIE
     AAVAEQPPGP VLRISANFYT TEEEIDRLAD ALDALTGE