CEFE_STRCL
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 03-AUG-2022, entry version 110.
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; 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=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 / 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).
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}.
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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; 443255.SCLAV_4211; -.
DR DrugBank; DB03229; alpha-Ketoisocaproic acid.
DR DrugBank; DB04074; alpha-Ketoisovalerate.
DR DrugBank; DB03938; Deacetoxycephalosporin C.
DR eggNOG; COG3491; Bacteria.
DR BioCyc; MetaCyc:MON-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 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; 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
