ID   BARS1_STRVG             Reviewed;         257 AA.
AC   Q9LBV3;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=A-factor type gamma-butyrolactone 1'-reductase (1S-forming) {ECO:0000305};
DE            EC=1.1.1.413 {ECO:0000269|PubMed:12193632};
DE   AltName: Full=6-dehydro-VB-A reductase {ECO:0000303|PubMed:12193632};
DE   AltName: Full=Butyrolactone autoregulator synthesis {ECO:0000303|PubMed:12193632};
GN   Name=barS1 {ECO:0000303|PubMed:12193632};
GN   Synonyms=orf4 {ECO:0000303|PubMed:10792718};
OS   Streptomyces virginiae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces virginiae group.
OX   NCBI_TaxID=1961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=MAFF10-06014;
RX   PubMed=10792718; DOI=10.1046/j.1365-2958.2000.01819.x;
RA   Kawachi R., Akashi T., Kamitani Y., Sy A., Wangchaisoonthorn U., Nihira T.,
RA   Yamada Y.;
RT   "Identification of an AfsA homologue (BarX) from Streptomyces virginiae as
RT   a pleiotropic regulator controlling autoregulator biosynthesis,
RT   virginiamycin biosynthesis and virginiamycin M1 resistance.";
RL   Mol. Microbiol. 36:302-313(2000).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=MAFF10-06014;
RX   PubMed=12193632; DOI=10.1128/jb.184.18.5151-5157.2002;
RA   Shikura N., Yamamura J., Nihira T.;
RT   "barS1, a gene for biosynthesis of a gamma-butyrolactone autoregulator, a
RT   microbial signaling molecule eliciting antibiotic production in
RT   Streptomyces species.";
RL   J. Bacteriol. 184:5151-5157(2002).
CC   -!- FUNCTION: Involved in the biosynthesis of virginiae butanolide (VB),
CC       which regulates the production of antibiotic virginiamycin. Catalyzes
CC       the reduction of 6-dehydro-VB-A to VB-A, the last catalytic step in VB
CC       biosynthesis. In vitro, can use various synthetic A-factor-type
CC       analogs. {ECO:0000269|PubMed:12193632}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R,4R)-3-[(1S)-1-hydroxyalkyl]-4-(hydroxymethyl)oxolan-2-
CC         one + NADP(+) = a (3R,4R)-3-alkanoyl-4-(hydroxymethyl)oxolan-2-one +
CC         H(+) + NADPH; Xref=Rhea:RHEA:18941, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:138440,
CC         ChEBI:CHEBI:138441; EC=1.1.1.413;
CC         Evidence={ECO:0000269|PubMed:12193632};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18943;
CC         Evidence={ECO:0000269|PubMed:12193632};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=11.1 uM for 6-dehydro-VB-A {ECO:0000269|PubMed:12193632};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:12193632};
CC       Temperature dependence:
CC         Optimum temperature is 25 degrees Celsius.
CC         {ECO:0000269|PubMed:12193632};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12193632}.
CC   -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:10792718}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant cannot produce VB or
CC       virginiamycin. {ECO:0000269|PubMed:12193632}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AB035548; BAA96298.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9LBV3; -.
DR   SMR; Q9LBV3; -.
DR   KEGG; ag:BAA96298; -.
DR   BioCyc; MetaCyc:MON-20201; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   NADP; Oxidoreductase.
FT   CHAIN           1..257
FT                   /note="A-factor type gamma-butyrolactone 1'-reductase (1S-
FT                   forming)"
FT                   /id="PRO_0000447188"
FT   ACT_SITE        161
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
SQ   SEQUENCE   257 AA;  27096 MW;  159D84E9CAD5CFE8 CRC64;
     MTDRQGLLTD RIALITGASS GIGAAQRGLF AREGAAVVVT ARREERLAGL VDELRAQGAR
     AAYVVADVTR SEDAVRAVEF TVERFGRLDA AFNKRRHGAG RTPLHLMDDP VYDDIMDTNV
     RGVFNCLRPE IAAMLASGAG GSIVNTSSTG GLVATPVAAP YVVSKHAVLG LTKGPAAEYG
     AHGIRVNAIA PGTTRSEMVA DWFAQNPDAE ELLHRATPQP RTAEPQEIAE AAAWLCSERA
     SFVTGSTLVV DGGFTIL