ID   CEFD1_ACRCH             Reviewed;         609 AA.
AC   Q8J0E9;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Isopenicillin N epimerase component 1;
DE            Short=IPN epimerase component 1;
DE            EC=5.1.1.17;
DE   AltName: Full=Isopenicillin N epimerase acyl-CoA synthase component;
DE            EC=6.2.1.-;
GN   Name=cefD1;
OS   Acremonium chrysogenum (Cephalosporium acremonium).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreales incertae sedis; Acremonium.
OX   NCBI_TaxID=5044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 48278 / C10;
RX   PubMed=12228250; DOI=10.1074/jbc.m207482200;
RA   Ullan R.V., Casqueiro J., Banuelos O., Fernandez F.J., Gutierrez S.,
RA   Martin J.F.;
RT   "A novel epimerization system in fungal secondary metabolism involved in
RT   the conversion of isopenicillin N into penicillin N in Acremonium
RT   chrysogenum.";
RL   J. Biol. Chem. 277:46216-46225(2002).
CC   -!- FUNCTION: Together with cefD2, catalyzes the reversible isomerization
CC       between isopenicillin N and penicillin N. This two-component IPN
CC       epimerase system may function by two sequential steps, an activation of
CC       isopenicillin N by the acyl-CoA synthase component cefD1, followed by
CC       epimerization by the acyl-CoA racemase component cefD2.
CC       {ECO:0000269|PubMed:12228250}.
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   -!- PATHWAY: Antibiotic biosynthesis; cephalosporin C biosynthesis.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AJ507632; CAD45625.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8J0E9; -.
DR   SMR; Q8J0E9; -.
DR   UniPathway; UPA00172; -.
DR   GO; GO:0045439; F:isopenicillin-N epimerase activity; IMP:UniProtKB.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042318; P:penicillin biosynthetic process; IMP:UniProtKB.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF13193; AMP-binding_C; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Isomerase; Ligase.
FT   CHAIN           1..609
FT                   /note="Isopenicillin N epimerase component 1"
FT                   /id="PRO_0000418513"
FT   REGION          545..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..564
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         185..196
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   609 AA;  67197 MW;  4FA10009DD1CA681 CRC64;
     MAPGGLLTLA GAAAASTAAA AYLDAKLHLT KDLNQLARAE RGAQNFARAV EQRKASGFFL
     FEAAAARLGD APCIWSRGHP EYSWTQTYQR ACQYGHYFRD LGVVAGQHVG VYLYNSPELM
     FIWMGLLSIG AAPALINYNL GSDALVHCVR LSRSRFLIYD DASDCSSRIH EVGERLRDIN
     VEAIMLSGSG TTGLPKAAPI TVARNYPSAS LLPKTFGQKP GPNGDRTYYC IPLYHGTGGI
     AAMNDLMSGI SIALAPKFSL SRFWDDCIES GSTIFVYVGE LIRYLLSAPA SPKDRQHRVR
     LVWGNGLSPE LWTKFQDRFG VSDIGEFYAS TEGVLTLLKH YRGGGFGLGA VGHHGWLLRR
     KFHNDYVPVR IDPETGDIWR SPKTGFAERL PYERGGEILA RLPSRSAWAG YWHAEEATQK
     KLVENVFEKG DLYFRTGDAL RRDADGHWYF LDRLGDTYRW KGENVSTTEV GQVLGSHADI
     AEANVYGVQV PNHDGRAGCA AIALKNAATP DTLDWSRLTS LLRSELPSYA VPVFIRVRET
     VGGMSTDNHK HNKVPLRDEG VDPRSMGSKV PGSEKDRFFW LPAGASKYVP FTERDWDLLS
     GQSAARPRL