SALQ_STRA4
ID SALQ_STRA4 Reviewed; 410 AA.
AC A8D7K2; A0A0B5EQA8;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=2-epi-5-epi-valiolone synthase {ECO:0000303|PubMed:18648803};
DE Short=EEVS {ECO:0000305};
DE EC=4.2.3.152 {ECO:0000269|PubMed:18648803};
GN Name=salQ {ECO:0000303|PubMed:18648803};
GN ORFNames=SLNWT_0595 {ECO:0000312|EMBL:AJE80971.1};
OS Streptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 /
OS NBRC 107858).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1081613;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP COFACTOR.
RC STRAIN=ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858;
RX PubMed=18648803; DOI=10.1007/s00253-008-1591-2;
RA Choi W.S., Wu X., Choeng Y.H., Mahmud T., Jeong B.C., Lee S.H., Chang Y.K.,
RA Kim C.J., Hong S.K.;
RT "Genetic organization of the putative salbostatin biosynthetic gene cluster
RT including the 2-epi-5-epi-valiolone synthase gene in Streptomyces albus
RT ATCC 21838.";
RL Appl. Microbiol. Biotechnol. 80:637-645(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858;
RA Lu C.;
RT "Enhanced salinomycin production by adjusting the supply of polyketide
RT extender units in Streptomyce albus DSM 41398.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the cyclization of D-sedoheptulose 7-phosphate to
CC 2-epi-5-epi-valiolone. Involved in salbostatin biosynthesis.
CC {ECO:0000269|PubMed:18648803}.
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:18648803};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:18648803};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:18648803};
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. EEVS
CC family. {ECO:0000305}.
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DR EMBL; EU141958; ABV57470.1; -; Genomic_DNA.
DR EMBL; CP010519; AJE80971.1; -; Genomic_DNA.
DR RefSeq; WP_052482047.1; NZ_CP010519.1.
DR AlphaFoldDB; A8D7K2; -.
DR SMR; A8D7K2; -.
DR PRIDE; A8D7K2; -.
DR EnsemblBacteria; AJE80971; AJE80971; SLNWT_0595.
DR KEGG; sals:SLNWT_0595; -.
DR BRENDA; 4.2.3.152; 5971.
DR Proteomes; UP000031523; 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.
FT CHAIN 1..410
FT /note="2-epi-5-epi-valiolone synthase"
FT /id="PRO_0000435439"
FT ACT_SITE 167
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 66
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:H2K887"
FT BINDING 97..100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:H2K887"
FT BINDING 130..134
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:H2K887"
FT BINDING 154..155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:H2K887"
FT BINDING 167
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:H2K887"
FT BINDING 176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:H2K887"
FT BINDING 194..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:H2K887"
FT BINDING 209
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:H2K887"
FT BINDING 280
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:H2K887"
FT BINDING 296
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:H2K887"
SQ SEQUENCE 410 AA; 45124 MW; E3EB72821307A0EE CRC64;
MTGTSLTDTS SGLYFRDHSQ GWLLRAQKQI SYEVRLRDGI FRPECTDLLE QGAGTPGRSR
RFVVVDSNVD LMYGNRIRSY FDYHGVDCSI MVVEANETLK NLETATRIVD EIDAFGIARR
KEPLIVIGGG VLMDIVGLVA SLYRRGAPFV RVPTTLIGLV DAGVGVKTGV NFNGHKNRLG
TYTPADLTLL DRQFLATLDR RHIGNGLAEI LKIALIKDLS LFAALEEHGP TLLDEKFQGS
TAAGDRAARS VLHSAIHGML DELQPNLWEA ELERCVDYGH TFSPTVEMRA LPELLHGEAV
CVDMALTTVI AWRRGLLTEA QRDRIFAVMA ALELPSWHPI LDPDVLVNAL QDTVRHRDGL
QRLPLPVGIG GVTFVNDVTP RELEAAVTLQ QELGDARTPK TSGDRGGRNL
