ID   BARX_STRVG              Reviewed;         294 AA.
AC   O24738;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=2-oxo-3-(phosphooxy)propyl 3-oxoalkanoate synthase {ECO:0000250|UniProtKB:B1VN93};
DE            EC=2.3.1.277 {ECO:0000250|UniProtKB:B1VN93};
GN   Name=barX {ECO:0000303|PubMed:9371444};
OS   Streptomyces virginiae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces virginiae group.
OX   NCBI_TaxID=1961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MAFF10-06014;
RX   PubMed=9371444; DOI=10.1128/jb.179.22.6986-6993.1997;
RA   Kinoshita H., Ipposhi H., Okamoto S., Nakano H., Nihira T., Yamada Y.;
RT   "Butyrolactone autoregulator receptor protein (BarA) as a transcriptional
RT   regulator in Streptomyces virginiae.";
RL   J. Bacteriol. 179:6986-6993(1997).
RN   [2]
RP   PRELIMINARY FUNCTION.
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   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19778967; DOI=10.1099/mic.0.032003-0;
RA   Lee Y.J., Kitani S., Nihira T.;
RT   "Null mutation analysis of an afsA-family gene, barX, that is involved in
RT   biosynthesis of the {gamma}-butyrolactone autoregulator in Streptomyces
RT   virginiae.";
RL   Microbiology 156:206-210(2010).
CC   -!- FUNCTION: Involved in the biosynthesis of virginiae butanolide (VB), a
CC       gamma-butyrolactone autoregulator that triggers the production of the
CC       streptogramin antibiotic virginiamycin. {ECO:0000269|PubMed:19778967}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a medium-chain 3-oxoacyl-[ACP] + dihydroxyacetone phosphate =
CC         a 2-oxo-3-(phosphooxy)propyl medium-chain 3-oxoalkanoate + holo-
CC         [ACP]; Xref=Rhea:RHEA:56860, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC         COMP:14764, ChEBI:CHEBI:57642, ChEBI:CHEBI:64479, ChEBI:CHEBI:141052,
CC         ChEBI:CHEBI:141053; EC=2.3.1.277;
CC         Evidence={ECO:0000250|UniProtKB:B1VN93};
CC   -!- DISRUPTION PHENOTYPE: Null mutant is unable to produce virginiamycin.
CC       Addition of VB restores the deficiency of virginiamycin production.
CC       {ECO:0000269|PubMed:19778967}.
CC   -!- SIMILARITY: Belongs to the AfsA family. {ECO:0000305}.
CC   -!- CAUTION: It was originally suggested that BarX is likely to participate
CC       in the regulatory pathway for the production of VB, rather than in the
CC       biosynthetic pathway of VB itself. {ECO:0000305|PubMed:10792718}.
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DR   EMBL; AB001608; BAA23611.1; -; Genomic_DNA.
DR   AlphaFoldDB; O24738; -.
DR   SMR; O24738; -.
DR   BioCyc; MetaCyc:MON-20202; -.
DR   BRENDA; 2.3.1.277; 5959.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR005509; AfsA_hotdog_dom.
DR   Pfam; PF03756; AfsA; 2.
PE   3: Inferred from homology;
KW   Transferase.
FT   CHAIN           1..294
FT                   /note="2-oxo-3-(phosphooxy)propyl 3-oxoalkanoate synthase"
FT                   /id="PRO_0000450067"
SQ   SEQUENCE   294 AA;  32379 MW;  7192024EB68F7892 CRC64;
     MTSTVPRELV HRAAVAEVFL TGWSRTAENR FALTAQWPRA HSYFTPVNGC YDPLLASETI
     RQVGTLLSHA EFGVSFGDQF LMWDLHHSVR PEQAGVGAAP ADLELDVICS DIRRRGRRLA
     GMRYEVTLYC GGQVIATGGA AFDCTSPAVY QRLRGDRVGA TGVRPLPQPL APASVGRFLT
     TDVVLSATER PLEWQLRVDE QHPVLFDHPV DHVPGMVLME SARQAAQAID PSRPFLPTTM
     RSEFSRYAEL DRPCWIQAEP LPAADNGDRQ VRVTGHQDDT TVFSCLIGTR GAAE