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   03-AUG-2022, entry version 88.
DE   RecName: Full=Clavaminate synthase 2;
DE            EC=1.14.11.21;
DE   AltName: Full=Clavaminic acid synthase 2;
DE            Short=CAS2;
DE            Short=CS2;
GN   Name=cs2;
OS   Streptomyces clavuligerus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-24.
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC   3585 / VKM Ac-602;
RX   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 formation:
RT   cloning and sequencing of both genes from Streptomyces clavuligerus.";
RL   Biochemistry 31:12648-12657(1992).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL
RC   3585 / VKM Ac-602;
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 and
RT   initial characterization of the iron binding site. General error analysis
RT   in polymerase chain reaction amplification.";
RL   J. Biol. Chem. 270:4262-4269(1995).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + deoxyamidinoproclavaminate + O2 =
CC         amidinoproclavaminate + CO2 + succinate; Xref=Rhea:RHEA:20021,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:57303, ChEBI:CHEBI:58647;
CC         EC=1.14.11.21;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + O2 + proclavaminate = CO2 +
CC         dihydroclavaminate + H2O + succinate; Xref=Rhea:RHEA:12773,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57301,
CC         ChEBI:CHEBI:57302; EC=1.14.11.21;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + dihydroclavaminate + O2 = clavaminate + CO2 +
CC         H2O + succinate; Xref=Rhea:RHEA:19785, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:57300, ChEBI:CHEBI:57301;
CC         EC=1.14.11.21;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Antibiotic biosynthesis; clavulanate biosynthesis; clavulanate
CC       from D-glyceraldehyde 3-phosphate and L-arginine: step 3/8.
CC   -!- PATHWAY: Antibiotic biosynthesis; clavulanate biosynthesis; clavulanate
CC       from D-glyceraldehyde 3-phosphate and L-arginine: step 5/8.
CC   -!- PATHWAY: Antibiotic biosynthesis; clavulanate biosynthesis; clavulanate
CC       from D-glyceraldehyde 3-phosphate and L-arginine: step 6/8.
CC   -!- SIMILARITY: Belongs to the clavaminate synthase family. {ECO:0000305}.
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DR   EMBL; L06214; AAA26723.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q05582; -.
DR   SMR; Q05582; -.
DR   STRING; 443255.SCLAV_4194; -.
DR   eggNOG; COG2175; Bacteria.
DR   BioCyc; MetaCyc:MON-13487; -.
DR   BRENDA; 1.14.11.21; 5988.
DR   UniPathway; UPA00112; UER00244.
DR   UniPathway; UPA00112; UER00246.
DR   UniPathway; UPA00112; UER00247.
DR   GO; GO:0033758; F:clavaminate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0033050; P:clavulanic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.60.130.10; -; 1.
DR   InterPro; IPR014503; Clavaminate_syn-like.
DR   InterPro; IPR042098; TauD-like_sf.
DR   InterPro; IPR003819; TauD/TfdA-like.
DR   Pfam; PF02668; TauD; 1.
DR   PIRSF; PIRSF019543; Clavaminate_syn; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Direct protein sequencing; Iron; Metal-binding;
KW   Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1472501"
FT   CHAIN           2..325
FT                   /note="Clavaminate synthase 2"
FT                   /id="PRO_0000089323"
FT   BINDING         145
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         294
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250"
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