ID   AFSA_STRGR              Reviewed;         301 AA.
AC   P18394;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 47.
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};
DE   AltName: Full=A-factor biosynthesis enzyme {ECO:0000305};
GN   Name=afsA {ECO:0000303|PubMed:2492509};
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2492509; DOI=10.1128/jb.171.2.1206-1210.1989;
RA   Horinouchi S., Suzuki H., Nishiyama M., Beppu T.;
RT   "Nucleotide sequence and transcriptional analysis of the Streptomyces
RT   griseus gene (afsA) responsible for A-factor biosynthesis.";
RL   J. Bacteriol. 171:1206-1210(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Umeyama T.;
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
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       (By similarity). Catalyzes beta-ketoacyl transfer from 8-methyl-3-
CC       oxononanoyl-acyl carrier protein (ACP) to the hydroxyl group of
CC       dihydroxyacetone phosphate (DHAP), thus producing an 8-methyl-3-
CC       oxononanoyl-DHAP ester (By similarity). {ECO:0000250|UniProtKB:B1VN93}.
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   -!- SIMILARITY: Belongs to the AfsA family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M24250; AAA26693.1; -; Genomic_DNA.
DR   EMBL; AB011413; BAA32134.1; -; Genomic_DNA.
DR   PIR; A32061; A32061.
DR   AlphaFoldDB; P18394; -.
DR   SMR; P18394; -.
DR   BioCyc; MetaCyc:MON-20192; -.
DR   BRENDA; 2.3.1.277; 6035.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR005509; AfsA_hotdog_dom.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   Pfam; PF03756; AfsA; 2.
DR   SUPFAM; SSF54637; SSF54637; 1.
PE   3: Inferred from homology;
KW   Plasmid; Transferase.
FT   CHAIN           1..301
FT                   /note="2-oxo-3-(phosphooxy)propyl 3-oxoalkanoate synthase"
FT                   /id="PRO_0000064486"
SQ   SEQUENCE   301 AA;  32706 MW;  E93302C7547065E3 CRC64;
     MDAEAEVVHP VGIEMVHRTR PEDAFPRNWV RLGRDRFAVE AVLPHDHPFF APVGDDLHDP
     LLVAEAMRQA AMLAFHAGYG IPLGYHFLLT ELDYVCHPEH LGVGGEPTEI GLEVFCSDLK
     WRAGLPAQGR VGWAVHRGDR LAATGVAATR FSTPKAYRRM RGDVPVEGIS LPETAPVPAS
     PAGRARVEDV VLSGTGREGV WELRVDTRHP TLFQRPNDHV PGMLLLEAAR QAACLVAGPA
     GIVPVEARTR FHRYSEFGSP CWIGAVVQPG ADEDTVTVRV TGHQDGETVF STVLSGPRAH
     G