ID   BPRA_STRGG              Reviewed;         282 AA.
AC   B1VN94;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=(4-alkanoyl-5-oxo-2,5-dihydrofuran-3-yl)methyl phosphate reductase {ECO:0000305};
DE            EC=1.3.1.113 {ECO:0000269|PubMed:17277085};
DE   AltName: Full=Butenolide phosphate reductase {ECO:0000303|PubMed:17277085};
GN   Name=bprA {ECO:0000303|PubMed:17277085};
GN   OrderedLocusNames=SGR_6890 {ECO:0000312|EMBL:BAG23719.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350;
RX   PubMed=18375553; DOI=10.1128/jb.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=JCM 4626 / NBRC 13350;
RX   PubMed=17277085; DOI=10.1073/pnas.0607472104;
RA   Kato J.Y., Funa N., Watanabe H., Ohnishi Y., Horinouchi S.;
RT   "Biosynthesis of gamma-butyrolactone autoregulators that switch on
RT   secondary metabolism and morphological development in Streptomyces.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2378-2383(2007).
CC   -!- FUNCTION: Involved in the biosynthesis of A factor (2-isocapryloyl-3R-
CC       hydroxymethyl-gamma-butyrolactone), a gamma-butyrolactone autoregulator
CC       that triggers secondary metabolism and morphogenesis in Streptomyces
CC       (PubMed:17277085). Catalyzes the reduction of the butenolide phosphate
CC       produced by nonenzymatic intramolecular condensation of the 8-methyl-3-
CC       oxononanoyl-DHAP ester (PubMed:17277085).
CC       {ECO:0000269|PubMed:17277085}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a [(3S,4R)-4-alkanoyl-5-oxooxolan-3-yl]methyl phosphate +
CC         NADP(+) = a (4-alkanoyl-5-oxo-2,5-dihydrofuran-3-yl)methyl phosphate
CC         + H(+) + NADPH; Xref=Rhea:RHEA:55148, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:138603,
CC         ChEBI:CHEBI:138621; EC=1.3.1.113;
CC         Evidence={ECO:0000269|PubMed:17277085};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:55150;
CC         Evidence={ECO:0000269|PubMed:17277085};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(3S,4R)-4-(6-methylheptanoyl)-5-oxooxolan-3-yl]methyl
CC         phosphate + NADP(+) = [4-(6-methylheptanoyl)-5-oxo-2H-furan-3-
CC         yl]methyl phosphate + H(+) + NADPH; Xref=Rhea:RHEA:55144,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:138604, ChEBI:CHEBI:138605; EC=1.3.1.113;
CC         Evidence={ECO:0000269|PubMed:17277085};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:55146;
CC         Evidence={ECO:0000269|PubMed:17277085};
CC   -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; AP009493; BAG23719.1; -; Genomic_DNA.
DR   RefSeq; WP_012382293.1; NC_010572.1.
DR   AlphaFoldDB; B1VN94; -.
DR   SMR; B1VN94; -.
DR   STRING; 455632.SGR_6890; -.
DR   EnsemblBacteria; BAG23719; BAG23719; SGR_6890.
DR   GeneID; 6209752; -.
DR   KEGG; sgr:SGR_6890; -.
DR   PATRIC; fig|455632.4.peg.7072; -.
DR   eggNOG; COG0702; Bacteria.
DR   HOGENOM; CLU_007383_10_6_11; -.
DR   OMA; MGRWHHE; -.
DR   OrthoDB; 1616572at2; -.
DR   BioCyc; MetaCyc:MON-20193; -.
DR   Proteomes; UP000001685; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF13460; NAD_binding_10; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   NADP; Oxidoreductase.
FT   CHAIN           1..282
FT                   /note="(4-alkanoyl-5-oxo-2,5-dihydrofuran-3-yl)methyl
FT                   phosphate reductase"
FT                   /id="PRO_0000450074"
FT   BINDING         6..11
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P39315"
SQ   SEQUENCE   282 AA;  30055 MW;  1962B0EFCEB325AF CRC64;
     MILVTGATGA VGREVAGRLA DAGPVRILAR RPERLTVRGT GVEVVQGAYG DRAALDRALR
     GVDAVFLVTN DPTEPDDERV AAAAAAAGVR HLVKLSMMAV EEPDAEDFIT RRQRENEQAV
     RDSGVPWTFV RPRTFMSNTL SWAPGIRSAG VVRALYGDAP VACVDPRDVA AVAVAALTGT
     GHEGRAYAVS GPEAITAREQ TAQLSRVLGR PLRFEELGVD AARTALMAKY PPPVAEAFLQ
     SAERQRTGAK ASVVPTVQEL TGRPARPFRD WSAEHAEAFA PE