Database: SPTrEMBLEntry: EXPA_CEPAC
LinkDB: EXPA_CEPAC
Original site: EXPA_CEPAC
ID EXPA_CEPAC Reviewed; 332 AA.
AC P11935;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 19-JAN-2010, entry version 60.
DE RecName: Full=Cephalosporin biosynthesis expandase/hydroxylase;
DE Includes:
DE RecName: Full=Deacetoxycephalosporin C synthetase;
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=Deacetylcephalosporin C synthetase;
DE Short=DACS;
DE AltName: Full=Beta-lactam hydroxylase;
GN Name=CEFEF;
OS Cephalosporium acremonium (Acremonium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC Sordariomycetes; Hypocreomycetidae; Hypocreales;
OC mitosporic Hypocreales; 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
RT involved 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: Penicillin N + 2-oxoglutarate + O(2) =
CC deacetoxycephalosporin C + succinate + CO(2) + H(2)O.
CC -!- CATALYTIC ACTIVITY: Deacetoxycephalosporin C + 2-oxoglutarate +
CC O(2) = deacetylcephalosporin C + succinate + CO(2).
CC -!- COFACTOR: Iron.
CC -!- COFACTOR: Ascorbate.
CC -!- PATHWAY: Antibiotic biosynthesis; cephalosporin C biosynthesis.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family.
CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain.
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DR PIR; A29711; A29711.
DR SMR; P11935; 1-310.
DR BioCyc; MetaCyc:MONOMER-13406; -.
DR BRENDA; 1.14.11.26; 66776.
DR BRENDA; 1.14.20.1; 66776.
DR GO; GO:0045442; F:deacetoxycephalosporin-C hydroxylase activity; IEA:EC.
DR GO; GO:0050599; F:deacetoxycephalosporin-C synthase activity; IEA:EC.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR InterPro; IPR002057; Isopenicillin-N_synth_CS.
DR InterPro; IPR005123; Oxoglutarate/Fe-dep_oxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 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 Cephalosporin biosynthesis
FT expandase/hydroxylase.
FT /FTId=PRO_0000219509.
FT DOMAIN 155 268 Fe2OG dioxygenase.
FT METAL 184 184 Iron (By similarity).
FT METAL 186 186 Iron (By similarity).
FT METAL 244 244 Iron (By similarity).
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
//
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