EVS_STIAD
ID EVS_STIAD Reviewed; 406 AA.
AC Q08VU0;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=2-epi-valiolone synthase {ECO:0000303|PubMed:22741921};
DE Short=EVS {ECO:0000303|PubMed:22741921};
DE EC=4.2.3.155 {ECO:0000269|PubMed:22741921};
DE AltName: Full=Sedoheptulose 7-phosphate cyclase {ECO:0000303|PubMed:22741921};
GN OrderedLocusNames=STAUR_3140 {ECO:0000312|EMBL:ADO70932.1};
GN ORFNames=STIAU_4466 {ECO:0000312|EMBL:EAU64596.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1;
RA Nierman W.C.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1;
RX PubMed=21037205; DOI=10.1093/molbev/msq292;
RA Huntley S., Hamann N., Wegener-Feldbruegge S., Treuner-Lange A., Kube M.,
RA Reinhardt R., Klages S., Mueller R., Ronning C.M., Nierman W.C.,
RA Sogaard-Andersen L.;
RT "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL Mol. Biol. Evol. 28:1083-1097(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DW4/3-1;
RX PubMed=22741921; DOI=10.1021/ja3041866;
RA Asamizu S., Xie P., Brumsted C.J., Flatt P.M., Mahmud T.;
RT "Evolutionary divergence of sedoheptulose 7-phosphate cyclases leads to
RT several distinct cyclic products.";
RL J. Am. Chem. Soc. 134:12219-12229(2012).
CC -!- FUNCTION: Catalyzes the conversion of sedoheptulose 7-phosphate to 2-
CC epi-valiolone, which may serve as an alternative precursor for
CC aminocyclitol biosynthesis. {ECO:0000269|PubMed:22741921}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-sedoheptulose 7-phosphate = 2-epi-valiolone + phosphate;
CC Xref=Rhea:RHEA:49564, ChEBI:CHEBI:43474, ChEBI:CHEBI:57483,
CC ChEBI:CHEBI:131717; EC=4.2.3.155;
CC Evidence={ECO:0000269|PubMed:22741921};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:22741921};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:22741921};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:22741921};
CC Note=Binds 1 divalent metal cation per subunit. Co(2+) is the preferred
CC cofactor. {ECO:0000269|PubMed:22741921};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=38.6 uM for sedoheptulose 7-phosphate
CC {ECO:0000269|PubMed:22741921};
CC Note=kcat is 3.7 min(-1). {ECO:0000269|PubMed:22741921};
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. EVS
CC family. {ECO:0000305}.
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DR EMBL; AAMD01000110; EAU64596.1; -; Genomic_DNA.
DR EMBL; CP002271; ADO70932.1; -; Genomic_DNA.
DR RefSeq; WP_002616331.1; NZ_AAMD01000110.1.
DR AlphaFoldDB; Q08VU0; -.
DR SMR; Q08VU0; -.
DR STRING; 378806.STAUR_3140; -.
DR EnsemblBacteria; ADO70932; ADO70932; STAUR_3140.
DR EnsemblBacteria; EAU64596; EAU64596; STIAU_4466.
DR KEGG; sur:STAUR_3140; -.
DR PATRIC; fig|378806.16.peg.3586; -.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_001201_0_1_7; -.
DR OMA; YGVIWDA; -.
DR OrthoDB; 1677032at2; -.
DR BRENDA; 4.2.3.155; 5908.
DR Proteomes; UP000001351; Chromosome.
DR Proteomes; UP000032702; 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 InterPro; IPR030960; DHQS/DOIS.
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..406
FT /note="2-epi-valiolone synthase"
FT /id="PRO_0000441284"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105..108
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 137..141
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 161..162
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 201..204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
SQ SEQUENCE 406 AA; 43439 MW; 2DE3C2AB813DDD16 CRC64;
MPSTGSTPIL AHDVKSPHRG SLALDGGKTG YRVTVHREDR YEIIIGRGTL ARLGELLRPV
MAANEADSAV IITDNHVGPL YAELVTKRIS ATGAPVQCIV IPAGEPSKSI AQAHRLWDEL
RSRSVRRRTF LVALGGGVLC DLVGFVATTY LRGIPYVNVA TSLMGQVDGA IGGKVGVDHS
TGKNLIGGFY HPDLVVIDPS CLATLPLAEV INGLAEAVKV ALIGTPGLFE QLERLPMSTA
WPLDQAAPER LIEGLGPIIP AAIGKKLELL APDPFEQDLR RLLNLGHSVG HGLEAATHFV
RYRHGEAVAI GTATVTAIST GLGLTSVDTL RRILRLLQKL RLPVTVPDDL REVVWQHLET
ARLVRNGRLL LVMPTAIDHS VIIDDITRGQ YDAACQLVAQ EAPACG
