ID   EXPA_ACRCH              Reviewed;         332 AA.
AC   P11935;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Cephalosporin biosynthesis expandase/hydroxylase;
DE   Includes:
DE     RecName: Full=Deacetoxycephalosporin C synthase;
DE              Short=DAOCS;
DE              EC=1.14.20.1;
DE     AltName: Full=Expandase;
DE   Includes:
DE     RecName: Full=Deacetoxycephalosporin C hydroxylase;
DE              EC=1.14.11.26;
DE     AltName: Full=Beta-lactam hydroxylase;
DE     AltName: Full=Deacetylcephalosporin C synthase;
DE              Short=DACS;
GN   Name=CEFEF;
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.
RA   Samson S.M., Dotzlaf J.E., Slisz M.L., Becker G.W., van Frank R.M.,
RA   Veal L.E., Yeh W.K., Miller J.R., Queener S.W., Ingolia T.D.;
RT   "Cloning and expression of the fungal expandase/hydroxylase gene involved
RT   in cephalosporin biosynthesis.";
RL   Biotechnology (N.Y.) 5:1207-1214(1987).
CC   -!- FUNCTION: DAOCS catalyzes the step from penicillin N to deacetoxy-
CC       cephalosporin C, which is used as a substrate by DACS to form
CC       deacetylcephalosporin C.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + O2 + penicillin N = CO2 +
CC         deacetoxycephalosporin C + H2O + succinate; Xref=Rhea:RHEA:20748,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:58408,
CC         ChEBI:CHEBI:58415; EC=1.14.20.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + deacetoxycephalosporin C + O2 = CO2 +
CC         deacetylcephalosporin C + succinate; Xref=Rhea:RHEA:16805,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:58366, ChEBI:CHEBI:58415;
CC         EC=1.14.11.26;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC   -!- PATHWAY: Antibiotic biosynthesis; cephalosporin C biosynthesis.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   PIR; A29711; A29711.
DR   AlphaFoldDB; P11935; -.
DR   SMR; P11935; -.
DR   BioCyc; MetaCyc:MON-13406; -.
DR   BRENDA; 1.14.11.26; 114.
DR   BRENDA; 1.14.20.1; 114.
DR   SABIO-RK; P11935; -.
DR   UniPathway; UPA00172; -.
DR   GO; GO:0045442; F:deacetoxycephalosporin-C hydroxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050599; F:deacetoxycephalosporin-C synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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; Multifunctional enzyme;
KW   Oxidoreductase; Vitamin C.
FT   CHAIN           1..332
FT                   /note="Cephalosporin biosynthesis expandase/hydroxylase"
FT                   /id="PRO_0000219509"
FT   DOMAIN          155..268
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         184
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         186
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         244
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   332 AA;  36479 MW;  E0BD8CE68AA28B79 CRC64;
     MTSKVPVFRL DDLKSGKVLT ELAEAVTTKG IFYLTESGLV DDDHTSARET CVDFFKNGSE
     EEKRAVTLAD RNARRGFSAL EWESTAVVTE TGKYSDYSTC YSMGIGGNLF PNRGFEDVWQ
     DYFDRMYGAA KDVARAVLNS VGAPLAGEDI DDFVECDPLL RLRYFPEVPE DRVAEEEPLR
     MGPHYDLSTI TLVHQTACAN GFVSLQCEVD GEFVDLPTLP GAMVVFCGAV GTLATGGKVK
     APKHRVKSPG RDQRVGSSRT SSVFFLRPKP DFSFNVQQSR EWGFNVRIPS ERTTFREWLG
     GNYVNMRRDK PAAAEAAVPA AAPVSTAAPI AT