VALA_STRHJ
ID VALA_STRHJ Reviewed; 414 AA.
AC H2K887; Q3T6E4;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=2-epi-5-epi-valiolone synthase {ECO:0000303|PubMed:16151088};
DE Short=EEVS {ECO:0000303|PubMed:24832673};
DE EC=4.2.3.152 {ECO:0000269|PubMed:16151088};
DE AltName: Full=Sedoheptulose 7-phosphate cyclase {ECO:0000303|PubMed:24832673};
GN Name=valA {ECO:0000303|PubMed:16151088};
GN OrderedLocusNames=SHJG_0276 {ECO:0000312|EMBL:AEY85554.1};
OS Streptomyces hygroscopicus subsp. jinggangensis (strain 5008).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=1133850;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=5008;
RX PubMed=16151088; DOI=10.1128/aem.71.9.5066-5076.2005;
RA Yu Y., Bai L., Minagawa K., Jian X., Li L., Li J., Chen S., Cao E.,
RA Mahmud T., Floss H.G., Zhou X., Deng Z.;
RT "Gene cluster responsible for validamycin biosynthesis in Streptomyces
RT hygroscopicus subsp. jinggangensis 5008.";
RL Appl. Environ. Microbiol. 71:5066-5076(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=5008;
RX PubMed=16632251; DOI=10.1016/j.chembiol.2006.02.002;
RA Bai L., Li L., Xu H., Minagawa K., Yu Y., Zhang Y., Zhou X., Floss H.G.,
RA Mahmud T., Deng Z.;
RT "Functional analysis of the validamycin biosynthetic gene cluster and
RT engineered production of validoxylamine A.";
RL Chem. Biol. 13:387-397(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5008;
RA Wu H., Bai L.;
RT "Genomic analysis of Streptomyces hygroscopicus subsp. jinggangensis
RT 5008.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007744|PDB:4P53}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC, AND
RP COFACTOR.
RX PubMed=24832673; DOI=10.1021/bi5003508;
RA Kean K.M., Codding S.J., Asamizu S., Mahmud T., Karplus P.A.;
RT "Structure of a sedoheptulose 7-phosphate cyclase: ValA from Streptomyces
RT hygroscopicus.";
RL Biochemistry 53:4250-4260(2014).
CC -!- FUNCTION: Catalyzes the cyclization of D-sedoheptulose 7-phosphate to
CC 2-epi-5-epi-valiolone. Involved in validamycin biosynthesis.
CC {ECO:0000269|PubMed:16151088}.
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:16151088};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:24832673};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:24832673};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:16151088}.
CC -!- DISRUPTION PHENOTYPE: Deletion abolishes validamycin production.
CC {ECO:0000269|PubMed:16151088}.
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. EEVS
CC family. {ECO:0000305}.
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DR EMBL; AY753181; AAW88569.1; -; Genomic_DNA.
DR EMBL; DQ164098; ABA41506.1; -; Genomic_DNA.
DR EMBL; CP003275; AEY85554.1; -; Genomic_DNA.
DR RefSeq; WP_014668902.1; NC_017765.1.
DR PDB; 4P53; X-ray; 2.10 A; A=1-414.
DR PDBsum; 4P53; -.
DR AlphaFoldDB; H2K887; -.
DR SMR; H2K887; -.
DR STRING; 1133850.SHJG_0276; -.
DR EnsemblBacteria; AEY85554; AEY85554; SHJG_0276.
DR KEGG; shy:SHJG_0276; -.
DR PATRIC; fig|1133850.20.peg.416; -.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_001201_0_4_11; -.
DR OMA; INRAGIH; -.
DR OrthoDB; 1677032at2; -.
DR BioCyc; MetaCyc:MON-13772; -.
DR BRENDA; 4.2.3.152; 6043.
DR Proteomes; UP000007170; 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:UniProtKB-KW.
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 3D-structure; Antibiotic biosynthesis; Lyase; Metal-binding; NAD;
KW Nucleotide-binding; Reference proteome; Zinc.
FT CHAIN 1..414
FT /note="2-epi-5-epi-valiolone synthase"
FT /id="PRO_0000435440"
FT ACT_SITE 171
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 70
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:24832673"
FT BINDING 101..104
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:24832673"
FT BINDING 134..138
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:24832673"
FT BINDING 158..159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:24832673"
FT BINDING 171
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:24832673"
FT BINDING 180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:24832673"
FT BINDING 198..201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:24832673"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24832673"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24832673"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24832673"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:4P53"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:4P53"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:4P53"
FT HELIX 71..87
FT /evidence="ECO:0007829|PDB:4P53"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:4P53"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4P53"
FT HELIX 106..119
FT /evidence="ECO:0007829|PDB:4P53"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:4P53"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:4P53"
FT HELIX 134..146
FT /evidence="ECO:0007829|PDB:4P53"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:4P53"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:4P53"
FT HELIX 160..164
FT /evidence="ECO:0007829|PDB:4P53"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:4P53"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:4P53"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:4P53"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:4P53"
FT HELIX 196..201
FT /evidence="ECO:0007829|PDB:4P53"
FT HELIX 204..221
FT /evidence="ECO:0007829|PDB:4P53"
FT HELIX 223..238
FT /evidence="ECO:0007829|PDB:4P53"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:4P53"
FT HELIX 251..267
FT /evidence="ECO:0007829|PDB:4P53"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:4P53"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:4P53"
FT HELIX 287..294
FT /evidence="ECO:0007829|PDB:4P53"
FT HELIX 300..317
FT /evidence="ECO:0007829|PDB:4P53"
FT HELIX 323..335
FT /evidence="ECO:0007829|PDB:4P53"
FT HELIX 347..360
FT /evidence="ECO:0007829|PDB:4P53"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:4P53"
FT STRAND 367..372
FT /evidence="ECO:0007829|PDB:4P53"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:4P53"
FT HELIX 384..397
FT /evidence="ECO:0007829|PDB:4P53"
SQ SEQUENCE 414 AA; 45018 MW; 5711612F171D9BC1 CRC64;
MTMTKQSSLS PGSRLYDYTT QDGAAWRVSA LKEVSYDVVV QPRLLDPANP ALADALSSGT
TPARRLIVID ATVRSLYGEQ LAAYLAGHDV EFHLCVIDAH ESAKVMETVF EVVDAMDAFG
VPRRHAPVLA MGGGVLTDIV GLAASLYRRA TPYVRIPTTL IGMIDAGIGA KTGVNFREHK
NRLGTYHPSS LTLIDPGFLA TLDARHLRNG LAEILKVALV KDAELFDLLE GHGASLVEQR
MQPGEGGTGG AALTVLRRAV QGMLEELQPN LWEHQLRRLV DFGHSFSPSV EMAALPELLH
GEAVCIDMAL SSVLAHHRGL LTEAELGRVL DVMRLLHLPV LHPVCTPDLM RAALADTVKH
RDGWQHMPLP RGIGDAVFVN DVTQREIEAA LLTLAERDRV PRWRALHGAV DMGV
