ID   U5YRG9_9ACTN            Unreviewed;       405 AA.
AC   U5YRG9;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=2-epi-5-epi-valiolone synthase {ECO:0000256|ARBA:ARBA00024092};
DE            EC=4.2.3.152 {ECO:0000256|ARBA:ARBA00024060};
GN   ORFNames=ADK57_29280 {ECO:0000313|EMBL:KOU60813.1};
OS   Streptomyces sp. MMG1533.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415546 {ECO:0000313|EMBL:AGZ94062.1};
RN   [1] {ECO:0000313|EMBL:AGZ94062.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MMG1533 {ECO:0000313|EMBL:AGZ94062.1};
RX   PubMed=24297932; DOI=10.1073/pnas.1315107110;
RA   Yu X., Doroghazi J.R., Janga S.C., Zhang J.K., Circello B., Griffin B.M.,
RA   Labeda D.P., Metcalf W.W.;
RT   "Diversity and abundance of phosphonate biosynthetic genes in nature.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:20759-20764(2013).
RN   [2] {ECO:0000313|Proteomes:UP000037741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMG1533 {ECO:0000313|Proteomes:UP000037741};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KOU60813.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMG1533 {ECO:0000313|EMBL:KOU60813.1};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00023993};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
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DR   EMBL; KF386870; AGZ94062.1; -; Genomic_DNA.
DR   EMBL; LGDG01000232; KOU60813.1; -; Genomic_DNA.
DR   RefSeq; WP_053752608.1; NZ_LGDG01000232.1.
DR   AlphaFoldDB; U5YRG9; -.
DR   STRING; 1415546.ADK57_29280; -.
DR   PATRIC; fig|1415546.3.peg.6350; -.
DR   OrthoDB; 9806583at2; -.
DR   Proteomes; UP000037741; Unassembled WGS sequence.
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:InterPro.
DR   CDD; cd08199; EEVS; 1.
DR   Gene3D; 3.40.50.1970; -; 1.
DR   Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR   InterPro; IPR030960; DHQS/DOIS.
DR   InterPro; IPR035872; EEVS-like.
DR   PANTHER; PTHR43622; 3-DEHYDROQUINATE SYNTHASE; 1.
DR   PANTHER; PTHR43622:SF1; 3-DEHYDROQUINATE SYNTHASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01761; DHQ_synthase; 1.
DR   SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037741}.
FT   DOMAIN          90..346
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
SQ   SEQUENCE   405 AA;  44520 MW;  0A2F6CDCE078785A CRC64;
     MTRDNAPTGL FTRSAQVDVW QVNAVKPVSY EIRMCDDAFD PADEALLEPA SVTGGNRRRF
     VVIDAHVERL HGERIRAYLD HHRVDYRMHV VEVDETLKEL ATLEDIVRAL DAFSIDRRRE
     PLIAIGGGVL MDIVGLVASL YRRGTPVVRV PTTLIGLVDA GVGVKTGVNF NGHKNRLGTY
     FPASLTLLDR SFLATVDRRH ISNGLAEILK MALIKDARLF DLLEAHGPSL IENRLQGSRW
     GAGRTACEVV QRAIHSMLEE LQPNLWEAQL ERVVDYGHTF SPTIEMHALP ALLHGEAVCV
     DMALTTVMAA RRGMVSAADR DRILAVMDAL ELPTWNDLLE PGLLARALAD TVRHRDGRQR
     LPLPVGIGEA AFVNDVTPAE LAAAIDDLRT LGTAGRRGAV LEEAA
//