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   04-NOV-2008, entry version 43.
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=cefF;
OS   Streptomyces clavuligerus.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=91100311; PubMed=1987130;
RA   Kovacevic S., Miller J.R.;
RT   "Cloning and sequencing of the beta-lactam hydroxylase gene (cefF)
RT   from Streptomyces clavuligerus: gene duplication may have led to
RT   separate 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;
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
CC       to form deacetylcephalosporin C.
CC   -!- CATALYTIC ACTIVITY: Deacetoxycephalosporin C + 2-oxoglutarate +
CC       O(2) = deacetylcephalosporin C + succinate + CO(2).
CC   -!- COFACTOR: Iron.
CC   -!- PATHWAY: Antibiotic biosynthesis; cephalosporin C biosynthesis.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M63809; AAA26716.1; -; Genomic_DNA.
DR   PIR; A39204; A39204.
DR   HSSP; P18548; 1RXF.
DR   BioCyc; MetaCyc:MON-13408; -.
DR   GO; GO:0045442; F:deacetoxycephalosporin-C hydroxylase 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; IPR005123; 2OG-FeII_Oase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Direct protein sequencing; Iron;
KW   Oxidoreductase; Vitamin C.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    318       Deacetoxycephalosporin C hydroxylase.
FT                                /FTId=PRO_0000219513.
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
//