ID   CAS2_STRCL              Reviewed;         325 AA.
AC   Q05582;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=Clavaminate synthase 2;
DE            EC=1.14.11.21;
DE   AltName: Full=Clavaminic acid synthetase 2;
DE            Short=CAS2;
DE            Short=CS2;
GN   Name=cs2;
OS   Streptomyces clavuligerus.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-24.
RC   STRAIN=ATCC 27064 / DSM 738 / IFO 13307 / JCM 4710 / NRRL 3585;
RX   MEDLINE=93112607; PubMed=1472501; DOI=10.1021/bi00165a015;
RA   Marsh E.N., Chang M.D.-T., Townsend C.A.;
RT   "Two isozymes of clavaminate synthase central to clavulanic acid
RT   formation: cloning and sequencing of both genes from Streptomyces
RT   clavuligerus.";
RL   Biochemistry 31:12648-12657(1992).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 27064 / DSM 738 / IFO 13307 / JCM 4710 / NRRL 3585;
RX   PubMed=7876185; DOI=10.1074/jbc.270.9.4262;
RA   Busby R.W., Chang M.D.-T., Busby R.C., Wimp J., Townsend C.A.;
RT   "Expression and purification of two isozymes of clavaminate synthase
RT   and initial characterization of the iron binding site. General error
RT   analysis in polymerase chain reaction amplification.";
RL   J. Biol. Chem. 270:4262-4269(1995).
CC   -!- CATALYTIC ACTIVITY: Deoxyamidinoproclavaminate + 2-oxoglutarate +
CC       O(2) = amidinoproclavaminate + succinate + CO(2).
CC   -!- CATALYTIC ACTIVITY: Proclavaminate + 2-oxoglutarate + O(2) =
CC       dihydroclavaminate + succinate + CO(2) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: Dihydroclavaminate + 2-oxoglutarate + O(2) =
CC       clavaminate + succinate + CO(2) + H(2)O.
CC   -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity).
CC   -!- PATHWAY: Antibiotic biosynthesis; clavulanic acid biosynthesis;
CC       clavulanic acid from D-glyceraldehyde 3-phosphate and L-arginine:
CC       step 3/8.
CC   -!- PATHWAY: Antibiotic biosynthesis; clavulanic acid biosynthesis;
CC       clavulanic acid from D-glyceraldehyde 3-phosphate and L-arginine:
CC       step 5/8.
CC   -!- PATHWAY: Antibiotic biosynthesis; clavulanic acid biosynthesis;
CC       clavulanic acid from D-glyceraldehyde 3-phosphate and L-arginine:
CC       step 6/8.
CC   -!- SIMILARITY: Belongs to the clavaminate synthase family.
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DR   EMBL; L06214; AAA26723.1; -; Genomic_DNA.
DR   HSSP; Q05581; 1DRY.
DR   SMR; Q05582; 6-324.
DR   BioCyc; MetaCyc:MON-13487; -.
DR   BRENDA; 1.14.11.21; 229786.
DR   GO; GO:0033758; F:clavaminate synthase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion 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; IPR014503; Clavaminate_syn.
DR   InterPro; IPR003819; Taurine_dOase.
DR   Pfam; PF02668; TauD; 1.
DR   PIRSF; PIRSF019543; Clavaminate_syn; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Direct protein sequencing; Iron;
KW   Metal-binding; Oxidoreductase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    325       Clavaminate synthase 2.
FT                                /FTId=PRO_0000089323.
FT   METAL       145    145       Iron (By similarity).
FT   METAL       147    147       Iron (By similarity).
FT   METAL       280    280       Iron (By similarity).
FT   BINDING     294    294       2-oxoglutarate (By similarity).
SQ   SEQUENCE   325 AA;  35840 MW;  98C03A901B371B0E CRC64;
     MASPIVDCTP YRDELLALAS ELPEVPRADL HGFLDEAKTL AARLPEGLAA ALDTFNAVGS
     EDGYLLLRGL PVDDSELPET PTSTPAPLDR KRLVMEAMRA LAGRRLGLHT GYQELRSGTV
     YHDVYPSPGA HYLSSETSET LLEFHTEMAY HILQPNYVML ACSRADHENR AETLVGSVRK
     ALPLLDEKTR ARLFDRKVPC CVDVAFRGGV DDPGAIANVK PLYGDANDPF LGYDRELLAP
     EDPADKEAVA HLSQALDDVT VGVKLVPGDV LIIDNFRTTH ARTPFSPRWD GKDRWLHRVY
     IRTDRNGELS GGERAGDTIS FSPRR
//