ID CEFE_STRCL Reviewed; 311 AA. AC P18548; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 27-MAR-2024, entry version 116. DE RecName: Full=Deacetoxycephalosporin C synthase; DE Short=DAOCS; DE EC=1.14.20.1; DE AltName: Full=Expandase; GN Name=cefE; OS Streptomyces clavuligerus. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1901; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / RC NRRL 3585 / VKM Ac-602; RX PubMed=2644235; DOI=10.1128/jb.171.2.754-760.1989; RA Kovacevic S., Weigel B.J., Tobin M.B., Ingolia T.D., Miller J.R.; RT "Cloning, characterization, and expression in Escherichia coli of the RT Streptomyces clavuligerus gene encoding deacetoxycephalosporin C RT synthetase."; RL J. Bacteriol. 171:754-760(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / RC NRRL 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). CC -!- FUNCTION: Catalyzes the step from penicillin N to deacetoxy- CC cephalosporin 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 -!- 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}. 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; M32324; AAA26715.1; -; Genomic_DNA. DR PIR; A32043; A32043. DR PIR; T52312; T52312. DR PDB; 1DCS; X-ray; 1.30 A; A=1-311. DR PDB; 1E5H; X-ray; 1.96 A; A=1-308. DR PDB; 1E5I; X-ray; 2.10 A; A=1-306. DR PDB; 1HJF; X-ray; 1.60 A; A=1-311. DR PDB; 1HJG; X-ray; 1.50 A; A=1-311. DR PDB; 1RXF; X-ray; 1.50 A; A=1-311. DR PDB; 1RXG; X-ray; 1.50 A; A=1-311. DR PDB; 1UNB; X-ray; 1.50 A; A=1-311. DR PDB; 1UO9; X-ray; 1.50 A; A=1-311. DR PDB; 1UOB; X-ray; 1.70 A; A=1-311. DR PDB; 1UOF; X-ray; 1.60 A; A=1-311. DR PDB; 1UOG; X-ray; 1.70 A; A=1-311. DR PDB; 1W28; X-ray; 2.30 A; A=1-311. DR PDB; 1W2A; X-ray; 2.51 A; X=1-311. DR PDB; 1W2N; X-ray; 2.70 A; A=1-311. DR PDB; 1W2O; X-ray; 3.00 A; A=1-311. DR PDB; 2JB8; X-ray; 1.53 A; A=1-311. DR PDBsum; 1DCS; -. DR PDBsum; 1E5H; -. DR PDBsum; 1E5I; -. DR PDBsum; 1HJF; -. DR PDBsum; 1HJG; -. DR PDBsum; 1RXF; -. DR PDBsum; 1RXG; -. DR PDBsum; 1UNB; -. DR PDBsum; 1UO9; -. DR PDBsum; 1UOB; -. DR PDBsum; 1UOF; -. DR PDBsum; 1UOG; -. DR PDBsum; 1W28; -. DR PDBsum; 1W2A; -. DR PDBsum; 1W2N; -. DR PDBsum; 1W2O; -. DR PDBsum; 2JB8; -. DR AlphaFoldDB; P18548; -. DR SMR; P18548; -. DR STRING; 1901.BB341_07740; -. DR DrugBank; DB03229; alpha-Ketoisocaproic acid. DR DrugBank; DB04074; alpha-Ketoisovalerate. DR DrugBank; DB03938; Deacetoxycephalosporin C. DR eggNOG; COG3491; Bacteria. DR BioCyc; MetaCyc:MONOMER-13407; -. DR BRENDA; 1.14.20.1; 5988. DR SABIO-RK; P18548; -. DR UniPathway; UPA00172; -. DR EvolutionaryTrace; P18548; -. 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 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 PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1. DR Pfam; PF03171; 2OG-FeII_Oxy; 1. DR SUPFAM; SSF51197; Clavaminate synthase-like; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. DR PROSITE; PS00186; IPNS_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic biosynthesis; Iron; Oxidoreductase; Vitamin C. FT CHAIN 1..311 FT /note="Deacetoxycephalosporin C synthase" FT /id="PRO_0000219511" FT DOMAIN 154..267 FT /note="Fe2OG dioxygenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT STRAND 7..9 FT /evidence="ECO:0007829|PDB:1DCS" FT HELIX 10..14 FT /evidence="ECO:0007829|PDB:1DCS" FT TURN 15..18 FT /evidence="ECO:0007829|PDB:1RXF" FT HELIX 19..28 FT /evidence="ECO:0007829|PDB:1DCS" FT STRAND 31..38 FT /evidence="ECO:0007829|PDB:1DCS" FT HELIX 41..57 FT /evidence="ECO:0007829|PDB:1DCS" FT HELIX 60..65 FT /evidence="ECO:0007829|PDB:1DCS" FT STRAND 73..79 FT /evidence="ECO:0007829|PDB:1DCS" FT HELIX 94..96 FT /evidence="ECO:0007829|PDB:1RXG" FT STRAND 99..103 FT /evidence="ECO:0007829|PDB:1DCS" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:1DCS" FT HELIX 113..140 FT /evidence="ECO:0007829|PDB:1DCS" FT HELIX 149..153 FT /evidence="ECO:0007829|PDB:1DCS" FT STRAND 158..164 FT /evidence="ECO:0007829|PDB:1DCS" FT STRAND 180..185 FT /evidence="ECO:0007829|PDB:1DCS" FT STRAND 187..195 FT /evidence="ECO:0007829|PDB:1DCS" FT STRAND 204..208 FT /evidence="ECO:0007829|PDB:1DCS" FT STRAND 211..214 FT /evidence="ECO:0007829|PDB:1DCS" FT STRAND 222..226 FT /evidence="ECO:0007829|PDB:1DCS" FT HELIX 228..233 FT /evidence="ECO:0007829|PDB:1DCS" FT TURN 234..236 FT /evidence="ECO:0007829|PDB:1W2A" FT STRAND 243..245 FT /evidence="ECO:0007829|PDB:1DCS" FT HELIX 250..252 FT /evidence="ECO:0007829|PDB:1UO9" FT STRAND 258..265 FT /evidence="ECO:0007829|PDB:1DCS" FT STRAND 272..274 FT /evidence="ECO:0007829|PDB:1DCS" FT HELIX 275..280 FT /evidence="ECO:0007829|PDB:1DCS" FT STRAND 289..293 FT /evidence="ECO:0007829|PDB:1DCS" FT HELIX 294..298 FT /evidence="ECO:0007829|PDB:1DCS" FT STRAND 305..307 FT /evidence="ECO:0007829|PDB:1E5H" SQ SEQUENCE 311 AA; 34556 MW; 9C64E1FC37F524BC CRC64; MDTTVPTFSL AELQQGLHQD EFRRCLRDKG LFYLTDCGLT DTELKSAKDL VIDFFEHGSE AEKRAVTSPV PTMRRGFTGL ESESTAQITN TGSYSDYSMC YSMGTADNLF PSGDFERIWT QYFDRQYTAS RAVAREVLRA TGTEPDGGVE AFLDCEPLLR FRYFPQVPEH RSAEEQPLRM APHYDLSMVT LIQQTPCANG FVSLQAEVGG AFTDLPYRPD AVLVFCGAIA TLVTGGQVKA PRHHVAAPRR DQIAGSSRTS SVFFLRPNAD FTFSVPLARE CGFDVSLDGE TATFQDWIGG NYVNIRRTSK A //