ID   CEFF_STRCL              Reviewed;         318 AA.
AC   P42220;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 82.
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=cefF;
OS   Streptomyces clavuligerus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1987130; DOI=10.1128/jb.173.1.398-400.1991;
RA   Kovacevic S., Miller J.R.;
RT   "Cloning and sequencing of the beta-lactam hydroxylase gene (cefF) from
RT   Streptomyces clavuligerus: gene duplication may have led to separate
RT   hydroxylase and expandase activities in the actinomycetes.";
RL   J. Bacteriol. 173:398-400(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-29 AND 92-100, AND CHARACTERIZATION.
RX   PubMed=2002049; DOI=10.1016/s0021-9258(19)67759-8;
RA   Baker B.J., Dotzlaf J.E., Yeh W.K.;
RT   "Deacetoxycephalosporin C hydroxylase of Streptomyces clavuligerus.
RT   Purification, characterization, bifunctionality, and evolutionary
RT   implication.";
RL   J. Biol. Chem. 266:5087-5093(1991).
CC   -!- FUNCTION: Hydroxylation of desacetoxicephalosporin C in 3'position to
CC       form deacetylcephalosporin C.
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   -!- PATHWAY: Antibiotic biosynthesis; cephalosporin C biosynthesis.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; M63809; AAA26716.1; -; Genomic_DNA.
DR   PIR; A39204; A39204.
DR   AlphaFoldDB; P42220; -.
DR   SMR; P42220; -.
DR   STRING; 443255.SCLAV_4206; -.
DR   KEGG; ag:AAA26716; -.
DR   BioCyc; MetaCyc:MON-13408; -.
DR   BRENDA; 1.14.11.26; 5988.
DR   UniPathway; UPA00172; -.
DR   GO; GO:0045442; F:deacetoxycephalosporin-C hydroxylase activity; IEA:UniProtKB-EC.
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; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Direct protein sequencing; Iron; Oxidoreductase;
KW   Vitamin C.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2002049"
FT   CHAIN           2..318
FT                   /note="Deacetoxycephalosporin C hydroxylase"
FT                   /id="PRO_0000219513"
FT   DOMAIN          158..271
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   318 AA;  34585 MW;  B17CC1CBC1E67178 CRC64;
     MADTPVPIFN LAALREGADQ EKFRECVTGM GVFYLTGYGA GDKDHRLATD TAMDFFANGT
     EAEKAAVTTD VPTMRRGYSA LEAESTAQVT RTGSYTDYSM SFSMGISGNV FPSPEFERVW
     TEYFDKLYAA AQETARLVLT ASGGYDAEIV GSLDELLDAD PVLRLRYFPE VPEHRSAEHE
     PRRMAPHYDL SIITFIHQTP CANGFVSLQA EIGGELVSLP VVEDAVVVMC GAMAPLATQG
     ALPAPRHHVR SPGAGMREGS DRTSSVFFLR PTTDFSFSVA KARSYGLAVD LDMETATFGD
     WIGTNYVTMH AKNEPQAG