AFSA_STRGG
ID AFSA_STRGG Reviewed; 314 AA.
AC B1VN93;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=2-oxo-3-(phosphooxy)propyl 3-oxoalkanoate synthase {ECO:0000305};
DE EC=2.3.1.277 {ECO:0000269|PubMed:17277085};
DE AltName: Full=A-factor biosynthesis enzyme {ECO:0000305};
GN Name=afsA; OrderedLocusNames=SGR_6889 {ECO:0000312|EMBL:BAG23718.1};
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, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
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 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 (PubMed:17277085).
CC {ECO:0000269|PubMed:17277085}.
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:0000269|PubMed:17277085};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=204.6 uM for DHAP {ECO:0000269|PubMed:17277085};
CC Note=kcat is 2.0 min(-1). {ECO:0000269|PubMed:17277085};
CC pH dependence:
CC Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:17277085};
CC Temperature dependence:
CC Optimum temperature is 15 degrees Celsius.
CC {ECO:0000269|PubMed:17277085};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17277085}.
CC -!- SIMILARITY: Belongs to the AfsA family. {ECO:0000305}.
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DR EMBL; AP009493; BAG23718.1; -; Genomic_DNA.
DR RefSeq; WP_003971211.1; NC_010572.1.
DR AlphaFoldDB; B1VN93; -.
DR SMR; B1VN93; -.
DR STRING; 455632.SGR_6889; -.
DR EnsemblBacteria; BAG23718; BAG23718; SGR_6889.
DR GeneID; 6214846; -.
DR KEGG; sgr:SGR_6889; -.
DR PATRIC; fig|455632.4.peg.7071; -.
DR eggNOG; ENOG50342P2; Bacteria.
DR HOGENOM; CLU_061800_0_0_11; -.
DR OMA; NDHVPGM; -.
DR OrthoDB; 1418394at2; -.
DR Proteomes; UP000001685; Chromosome.
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 1: Evidence at protein level;
KW Transferase.
FT CHAIN 1..314
FT /note="2-oxo-3-(phosphooxy)propyl 3-oxoalkanoate synthase"
FT /id="PRO_0000450066"
SQ SEQUENCE 314 AA; 34041 MW; B034B9075A91A839 CRC64;
MPEAAVLIDP VPTMDAEAEV VHPVGIEMVH RTRPEDAFPR NWVRLGRDRF AVEAVLPHDH
PFFAPVGDDL HDPLLVAEAM RQAAMLAFHA GYGIPLGYHF LLTELDYVCH PEHLGVGGEP
TEIGLEVFCS DLKWRAGLPA QGRVGWAVHR GDRLAATGVA ATRFSTPKAY RRMRGDVPVE
GISLPETAPV PASPAGRARV EDVVLSGTGR EGVWELRVDT RHPTLFQRPN DHVPGMLLLE
AARQAACLVA GPAGIVPVEA RTRFHRYSEF GSPCWIGAVV QPGADEDTVT VRVTGHQDGE
TVFSTVLSGP RAHG