ID   SCBA_STRCO              Reviewed;         314 AA.
AC   Q7AKF0;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, 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=Signaling molecule synthase ScbA {ECO:0000303|PubMed:21342469};
GN   Name=scbA {ECO:0000303|PubMed:17464053};
GN   OrderedLocusNames=SCO6266 {ECO:0000312|EMBL:CAB60185.1};
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [2]
RP   FUNCTION, AND MUTAGENESIS OF GLU-78; GLU-240 AND ARG-243.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=17464053; DOI=10.1099/mic.0.2006/004432-0;
RA   Hsiao N.H., Soeding J., Linke D., Lange C., Hertweck C., Wohlleben W.,
RA   Takano E.;
RT   "ScbA from Streptomyces coelicolor A3(2) has homology to fatty acid
RT   synthases and is able to synthesize gamma-butyrolactones.";
RL   Microbiology 153:1394-1404(2007).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=21342469; DOI=10.1111/j.1751-7915.2010.00232.x;
RA   D'Alia D., Eggle D., Nieselt K., Hu W.S., Breitling R., Takano E.;
RT   "Deletion of the signalling molecule synthase ScbA has pleiotropic effects
RT   on secondary metabolite biosynthesis, morphological differentiation and
RT   primary metabolism in Streptomyces coelicolor A3(2).";
RL   Microb. Biotechnol. 4:239-251(2011).
CC   -!- FUNCTION: Involved of the biosynthesis of S.coelicolor butanolide 1
CC       (SCB1), a gamma-butyrolactone that triggers antibiotic production.
CC       {ECO:0000269|PubMed:17464053}.
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: Deletion of the gene leads to a strong
CC       perturbation in the expression of three pigmented antibiotic clusters.
CC       It also affects the secondary metabolite cluster responsible for
CC       synthesis of the siderophore desferrioxamine and expression of the
CC       genes encoding enzymes for primary metabolism pathways, which supply
CC       antibiotic precursors and genes for morphological differentiation.
CC       {ECO:0000269|PubMed:21342469}.
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; AL939127; CAB60185.1; -; Genomic_DNA.
DR   RefSeq; NP_630366.1; NC_003888.3.
DR   RefSeq; WP_003972659.1; NZ_VNID01000009.1.
DR   AlphaFoldDB; Q7AKF0; -.
DR   SMR; Q7AKF0; -.
DR   STRING; 100226.SCO6266; -.
DR   GeneID; 1101707; -.
DR   KEGG; sco:SCO6266; -.
DR   PATRIC; fig|100226.15.peg.6381; -.
DR   eggNOG; ENOG50342P2; Bacteria.
DR   HOGENOM; CLU_061800_0_0_11; -.
DR   OMA; NDHVPGM; -.
DR   PhylomeDB; Q7AKF0; -.
DR   BioCyc; MetaCyc:SCO6266-MON; -.
DR   BRENDA; 2.3.1.277; 5998.
DR   Proteomes; UP000001973; 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   Reference proteome; Transferase.
FT   CHAIN           1..314
FT                   /note="2-oxo-3-(phosphooxy)propyl 3-oxoalkanoate synthase"
FT                   /id="PRO_0000450068"
FT   MUTAGEN         78
FT                   /note="E->A: Cannot produce active gamma-butyrolactones."
FT                   /evidence="ECO:0000269|PubMed:17464053"
FT   MUTAGEN         240
FT                   /note="E->A: Cannot produce active gamma-butyrolactones."
FT                   /evidence="ECO:0000269|PubMed:17464053"
FT   MUTAGEN         243
FT                   /note="R->K: Cannot produce active gamma-butyrolactones."
FT                   /evidence="ECO:0000269|PubMed:17464053"
SQ   SEQUENCE   314 AA;  33747 MW;  0F74C9669B6CF389 CRC64;
     MPEAVVLINS ASDANSIEQT ALPVPMALVH RTRVQDAFPV SWIPKGGDRF SVTAVLPHDH
     PFFAPVHGDR HDPLLIAETL RQAAMLVFHA GYGVPVGYHF LMATLDYTCH LDHLGVSGEV
     AELEVEVACS QLKFRGGQPV QGQVDWAVRR AGRLAATGTA TTRFTSPQVY RRMRGDFATP
     TASVPGTAPV PAARAGRTRD EDVVLSASSQ QDTWRLRVDT SHPTLFQRPN DHVPGMLLLE
     AARQAACLVT GPAPFVPSIG GTRFVRYAEF DSPCWIQATV RPGPAAGLTT VRVTGHQDGS
     LVFLTTLSGP AFSG