ID   CETA_ACTSX              Reviewed;         381 AA.
AC   A1YPR2;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=2-epi-5-epi-valiolone synthase {ECO:0000303|PubMed:17195255};
DE            Short=EEVS {ECO:0000305};
DE            EC=4.2.3.152 {ECO:0000269|PubMed:17195255};
GN   Name=cetA {ECO:0000303|PubMed:17195255};
OS   Actinomyces sp.
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; Actinomyces.
OX   NCBI_TaxID=29317;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   AND PATHWAY.
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].
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 cyclization of D-sedoheptulose 7-phosphate to
CC       2-epi-5-epi-valiolone. Involved in cetoniacytone A biosynthesis.
CC       {ECO:0000269|PubMed:17195255}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-sedoheptulose 7-phosphate = 2-epi-5-epi-valiolone +
CC         phosphate; Xref=Rhea:RHEA:44184, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57483, ChEBI:CHEBI:84187; EC=4.2.3.152;
CC         Evidence={ECO:0000269|PubMed:17195255};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000269|PubMed:17195255};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:17195255};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:17195255}.
CC   -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. EEVS
CC       family. {ECO:0000305}.
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DR   EMBL; EF120454; ABL74381.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1YPR2; -.
DR   SMR; A1YPR2; -.
DR   KEGG; ag:ABL74381; -.
DR   BRENDA; 4.2.3.152; 136.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd08199; EEVS; 1.
DR   InterPro; IPR030960; DHQS/DOIS.
DR   InterPro; IPR035872; EEVS-like.
DR   Pfam; PF01761; DHQ_synthase; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Cobalt; Lyase; Metal-binding; NAD;
KW   Nucleotide-binding.
FT   CHAIN           1..381
FT                   /note="2-epi-5-epi-valiolone synthase"
FT                   /id="PRO_0000435438"
FT   ACT_SITE        151
FT                   /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT   BINDING         50
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:H2K887"
FT   BINDING         81..84
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:H2K887"
FT   BINDING         114..118
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:H2K887"
FT   BINDING         138..139
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:H2K887"
FT   BINDING         151
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:H2K887"
FT   BINDING         160
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:H2K887"
FT   BINDING         178..181
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:H2K887"
FT   BINDING         193
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:H2K887"
FT   BINDING         264
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:H2K887"
FT   BINDING         280
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:H2K887"
SQ   SEQUENCE   381 AA;  41960 MW;  34BB3FEB70459641 CRC64;
     MANQWQAQAE QTITYEVQMT DGVLDPSNRA LLDAGATVRT DQPRRFIVID ANVHEIYGDA
     LRKYLAHHNC EYRLCVLSAS EEAKTMESVF TVVDGLDSFG ISRRHEPIIA IGGGIVLDIA
     GLAASMYRRS TPYVRVPTSL IGLVDAGVGI KTGVNFGSHK NRLGTYFAPT AALLDRGFLD
     TVDDRHISNG LAEILKIALV KDAELFRLME EHAELLLAER LTGRTPTGDV VAREVFSRAV
     GGMLEELEPN LWEQELERLV DYGHSFSPTL EMRALPALLH GEAVTVDMAL TTVLAEARGL
     VSTSDRERIF QVMRRLRLPV WHPLLEAGLL EHALRETTRH RDGLQRMPIP VGIGGARFLH
     DLTVAELTGA AESLRELGGG E