EEVS_STIAD
ID EEVS_STIAD Reviewed; 406 AA.
AC E3FKM2; Q09B53;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 55.
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:ADO69190.1};
GN OrderedLocusNames=STAUR_1386 {ECO:0000312|EMBL:ADO69190.1};
GN ORFNames=STIAU_0325 {ECO:0000312|EMBL:EAU68992.1};
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, AND COFACTOR.
RC STRAIN=DW4/3-1;
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. {ECO:0000269|PubMed:28182402}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU68992.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AAMD01000010; EAU68992.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002271; ADO69190.1; -; Genomic_DNA.
DR RefSeq; WP_013374650.1; NZ_AAMD01000010.1.
DR AlphaFoldDB; E3FKM2; -.
DR SMR; E3FKM2; -.
DR STRING; 378806.STAUR_1386; -.
DR EnsemblBacteria; ADO69190; ADO69190; STAUR_1386.
DR EnsemblBacteria; EAU68992; EAU68992; STIAU_0325.
DR KEGG; sur:STAUR_1386; -.
DR PATRIC; fig|378806.16.peg.8350; -.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_001201_0_4_7; -.
DR OMA; INRAGIH; -.
DR OrthoDB; 1677032at2; -.
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 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..406
FT /note="2-epi-5-epi-valiolone synthase"
FT /id="PRO_0000441285"
FT BINDING 91..94
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 123..127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 147..148
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 160
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 169
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 187..190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 202
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 406 AA; 44417 MW; 45A28335DBB87274 CRC64;
MAHIKVVGGG TSVRGSTLQV SAQADFGYGV HNEEGLFDPG QPLLLELCRD ARMLVCISPS
VDRLHGERIR QYFRTHFAPE QYRFLVLSTS ESNKSIENVL RICEAAKAFW LDRHGLLVAI
GGGIVLDMVG FAASIYRRGI RYIKVPTTLV GQVDVAVGVK TGVNLSGSKN LIGTYYPAYA
TLNDRGFLST LPAREMRCGL AEIIKMGLVC DPEIFTALEA HFLPPVSRHL EHPLPQEAVL
GAMVRMIEEL QPNLFELNLE RLVDFGHTFS MSLETVSGYA HAHGEAVAMD MALSACLSNE
LGILGEAEFE RILALLEVVG LPVFDEALCS VDAMWQALME VNVHRGHRIN LVIPARIGEG
MFLHRLEDVP RDALARAIRR MSVLSQRHAV AALGSAGEPL ERASGA
