EEVS_STRGA
ID EEVS_STRGA Reviewed; 388 AA.
AC B0B0T7;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=2-epi-5-epi-valiolone synthase {ECO:0000303|PubMed:28182402};
DE Short=EEVS {ECO:0000303|PubMed:28182402};
DE EC=4.2.3.152 {ECO:0000269|PubMed:28182402};
GN Name=gacC {ECO:0000312|EMBL:CAL64849.1};
GN ORFNames=SGLAU_01035 {ECO:0000312|EMBL:AIR96235.1};
OS Streptomyces glaucescens.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1907;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=DSM 40922 / GLA O;
RX PubMed=19059289; DOI=10.1016/j.jbiotec.2008.10.016;
RA Rockser Y., Wehmeier U.F.;
RT "The gac-gene cluster for the production of acarbose from Streptomyces
RT glaucescens GLA.O: identification, isolation and characterization.";
RL J. Biotechnol. 140:114-123(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40922 / GLA O;
RX PubMed=25499805; DOI=10.1016/j.jbiotec.2014.11.036;
RA Ortseifen V., Winkler A., Albersmeier A., Wendler S., Puhler A.,
RA Kalinowski J., Ruckert C.;
RT "Complete genome sequence of the actinobacterium Streptomyces glaucescens
RT GLA.O (DSM 40922) consisting of a linear chromosome and one linear
RT plasmid.";
RL J. Biotechnol. 194:81-83(2015).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=DSM 40922 / GLA O;
RX PubMed=28182402; DOI=10.1021/acschembio.7b00066;
RA Osborn A.R., Kean K.M., Alseud K.M., Almabruk K.H., Asamizu S., Lee J.A.,
RA Karplus P.A., Mahmud T.;
RT "Evolution and distribution of C7-cyclitol synthases in prokaryotes and
RT eukaryotes.";
RL ACS Chem. Biol. 12:979-988(2017).
CC -!- FUNCTION: Catalyzes the cyclization of D-sedoheptulose 7-phosphate to
CC 2-epi-5-epi-valiolone (PubMed:28182402). Probably involved in acarbose
CC biosynthesis (Probable). {ECO:0000269|PubMed:28182402,
CC ECO:0000305|PubMed:19059289}.
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:28182402};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:28182402};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:28182402};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:28182402};
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. EEVS-
CC like family. {ECO:0000305}.
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DR EMBL; AM409314; CAL64849.1; -; Genomic_DNA.
DR EMBL; CP009438; AIR96235.1; -; Genomic_DNA.
DR AlphaFoldDB; B0B0T7; -.
DR SMR; B0B0T7; -.
DR STRING; 1907.SGLAU_01035; -.
DR KEGG; sgu:SGLAU_01035; -.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_001201_0_4_11; -.
DR OMA; INRAGIH; -.
DR Proteomes; UP000029482; 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 InterPro; IPR030960; DHQS/DOIS.
DR InterPro; IPR035872; EEVS-like.
DR Pfam; PF01761; DHQ_synthase; 1.
PE 1: Evidence at protein level;
KW Cobalt; Lyase; Metal-binding; NAD; Nucleotide-binding; Reference proteome;
KW Zinc.
FT CHAIN 1..388
FT /note="2-epi-5-epi-valiolone synthase"
FT /id="PRO_0000441286"
FT BINDING 92..95
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 124..128
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 148..149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 170
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 188..191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
SQ SEQUENCE 388 AA; 41726 MW; 608D7C15E7794B44 CRC64;
MSGQALAQLE GVREDAGGFD LLAPDGTQYR VDVTDGVFDP HNPLLAGYVA GRRVVAFVGP
TVDRIYGDRL RAYLDARLEP GSWSVHTIDS GERNKTLASV ERVCAIAKAS GLDRHGVMLA
VGGGIVADIV GFAASMYARG IRYIKVNTTL VGQVDVGVGV KTGVNALNTK NMFGAYHPAH
ASLNDPALLA TLPAREIRCG LAEIVKMAVI LDAGLFEALE EHPDAFLRSS DGALETYVVR
TSMRLMMEEL CPNLREHDLA RLVDFGHTFS PVIETAGGHR LEHGEAVAVD MALSAHLARL
LGLADAESCR RVVTLLRRIG LPVFDPATCT PELMTQALHA SWQRRGRELH LVVPTGIGKA
TFVERLEDVP AEVLRAALDA LAREGRTS
