ID   CETB_ACTSX              Reviewed;         183 AA.
AC   A1YPR3;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=2-epi-5-epi-valiolone epimerase {ECO:0000303|PubMed:19101977};
DE            Short=EVE {ECO:0000303|PubMed:19101977};
DE            EC=5.1.3.33 {ECO:0000269|PubMed:19101977};
GN   Name=cetB {ECO:0000303|PubMed:17195255};
OS   Actinomyces sp.
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; Actinomyces.
OX   NCBI_TaxID=29317;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Lu 9419;
RX   PubMed=17195255; DOI=10.1002/cbic.200600446;
RA   Wu X., Flatt P.M., Schlorke O., Zeeck A., Dairi T., Mahmud T.;
RT   "A comparative analysis of the sugar phosphate cyclase superfamily involved
RT   in primary and secondary metabolism.";
RL   ChemBioChem 8:239-248(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   PATHWAY, SUBUNIT, AND MUTAGENESIS OF HIS-14; GLU-76; HIS-99 AND GLU-151.
RC   STRAIN=Lu 9419;
RX   PubMed=19101977; DOI=10.1002/cbic.200800527;
RA   Wu X., Flatt P.M., Xu H., Mahmud T.;
RT   "Biosynthetic gene cluster of cetoniacytone A, an unusual aminocyclitol
RT   from the endosymbiotic Bacterium Actinomyces sp. Lu 9419.";
RL   ChemBioChem 10:304-314(2009).
CC   -!- FUNCTION: Catalyzes the epimerization of 2-epi-5-epi-valiolone to 5-
CC       epi-valiolone. Involved in cetoniacytone A biosynthesis.
CC       {ECO:0000269|PubMed:19101977}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-epi-5-epi-valiolone = 5-epi-valiolone; Xref=Rhea:RHEA:45564,
CC         ChEBI:CHEBI:84187, ChEBI:CHEBI:84361; EC=5.1.3.33;
CC         Evidence={ECO:0000269|PubMed:19101977};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000269|PubMed:19101977};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:19101977}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19101977}.
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DR   EMBL; EF120454; ABL74382.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1YPR3; -.
DR   SMR; A1YPR3; -.
DR   KEGG; ag:ABL74382; -.
DR   BRENDA; 5.1.3.33; 136.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.180.10; -; 1.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR037523; VOC.
DR   SUPFAM; SSF54593; SSF54593; 1.
DR   PROSITE; PS51819; VOC; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Isomerase; Metal-binding.
FT   CHAIN           1..183
FT                   /note="2-epi-5-epi-valiolone epimerase"
FT                   /id="PRO_0000435441"
FT   DOMAIN          11..155
FT                   /note="VOC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   BINDING         14
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000305|PubMed:19101977"
FT   BINDING         76
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000305|PubMed:19101977"
FT   BINDING         99
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000305|PubMed:19101977"
FT   BINDING         151
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000305|PubMed:19101977"
FT   MUTAGEN         14
FT                   /note="H->G: Lack of activity; when associated with G-76;
FT                   G-99 or G-151."
FT                   /evidence="ECO:0000269|PubMed:19101977"
FT   MUTAGEN         76
FT                   /note="E->G: Lack of activity; when associated with G-14;
FT                   G-99 or G-151."
FT                   /evidence="ECO:0000269|PubMed:19101977"
FT   MUTAGEN         99
FT                   /note="H->G: Lack of activity; when associated with G-14;
FT                   G-76 or G-151."
FT                   /evidence="ECO:0000269|PubMed:19101977"
FT   MUTAGEN         151
FT                   /note="E->G: Lack of activity; when associated with G-14;
FT                   G-76 or G-99."
FT                   /evidence="ECO:0000269|PubMed:19101977"
SQ   SEQUENCE   183 AA;  20047 MW;  BF2B86742020501B CRC64;
     MTGRGIPGAV AVHHVAYTVP DLDQAVEFFT EVIGAELAYT LVQDAAGDWM TRKLDVDATA
     TARIAMLRLG PVTNLELFEY AAPDQRRQLP RNSDWGGHHL AIHVADVDAA AEYLRAQPGV
     RVLGDPETIT DGPIAGDRWV YFATPWGMQL ELINLPAGAP FEQQTEVRLY QPEGSWSDHR
     GAS