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Database: UniProt
Entry: G8S006_ACTS5
LinkDB: G8S006_ACTS5
Original site: G8S006_ACTS5 
ID   G8S006_ACTS5            Unreviewed;       264 AA.
AC   G8S006;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=2-epi-5-epi-valiolone synthase {ECO:0000256|ARBA:ARBA00024092};
DE            EC=4.2.3.152 {ECO:0000256|ARBA:ARBA00024060};
GN   OrderedLocusNames=ACPL_6250 {ECO:0000313|EMBL:AEV87135.1};
OS   Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV87135.1, ECO:0000313|Proteomes:UP000005440};
RN   [1] {ECO:0000313|Proteomes:UP000005440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31044 / CBS 674.73 / SE50/110
RC   {ECO:0000313|Proteomes:UP000005440};
RA   Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA   Wehmeier U.F., Stoye J., Puehler A.;
RT   "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT   SE50/110.";
RL   Submitted (DEC-2011) 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; CP003170; AEV87135.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8S006; -.
DR   STRING; 134676.ACPL_6250; -.
DR   KEGG; ase:ACPL_6250; -.
DR   PATRIC; fig|134676.3.peg.6145; -.
DR   eggNOG; COG0337; Bacteria.
DR   HOGENOM; CLU_1052244_0_0_11; -.
DR   Proteomes; UP000005440; Chromosome.
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, ECO:0000313|EMBL:AEV87135.1};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005440}.
FT   DOMAIN          2..212
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
SQ   SEQUENCE   264 AA;  28930 MW;  32FC4E59A7B9421A CRC64;
     MTDTVGLAAS LYRRGTPYVR IPTTLVGMID AAIGAKTGIN VGEHKNRLGT YYPATNTLVD
     PQFLRTLPAR HVRNGMAEII KMAIVKEPVL FKLLESDPEG LIAAQLVSDD GQEIMNRAIT
     SMLEELEPNL WENELRRLVD FGHTFSPRLE MCAKPPLLHG EAVAIDMALC CALAYGRGLI
     SATDVKRILN LLHRYSLPIT HPTCDVDLLQ EGLEESTRHR NGNQYCPLPV GIGAAEFVEG
     VTNAELARAG ELLAMFAQAE EAQV
//
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