ID E3E980_PAEPS Unreviewed; 415 AA.
AC E3E980;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Polyketide beta-ketoacyl:ACP synthase {ECO:0000313|EMBL:ADO57353.1};
GN Name=fabF5 {ECO:0000313|EMBL:ADO57353.1};
GN ORFNames=PPSC2_15900 {ECO:0000313|EMBL:ADO57353.1};
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO57353.1, ECO:0000313|Proteomes:UP000006868};
RN [1] {ECO:0000313|EMBL:ADO57353.1, ECO:0000313|Proteomes:UP000006868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:ADO57353.1,
RC ECO:0000313|Proteomes:UP000006868};
RX PubMed=21037012; DOI=10.1128/JB.01234-10;
RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT activity.";
RL J. Bacteriol. 193:311-312(2011).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467,
CC ECO:0000256|RuleBase:RU003694}.
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; CP002213; ADO57353.1; -; Genomic_DNA.
DR RefSeq; WP_013371939.1; NC_014622.2.
DR AlphaFoldDB; E3E980; -.
DR STRING; 1406.LK13_03595; -.
DR KEGG; ppm:PPSC2_15900; -.
DR PATRIC; fig|886882.15.peg.3394; -.
DR eggNOG; COG0304; Bacteria.
DR HOGENOM; CLU_000022_69_2_9; -.
DR OrthoDB; 9808669at2; -.
DR Proteomes; UP000006868; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProt.
DR CDD; cd00834; KAS_I_II; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR000794; Beta-ketoacyl_synthase.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR11712:SF336; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11712; POLYKETIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006868};
KW Transferase {ECO:0000256|RuleBase:RU003694}.
FT DOMAIN 9..410
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 415 AA; 45169 MW; 615D200A0E74AE52 CRC64;
MRSMPNYKQP ELVITGIGVT SAIGQGKTAF ASALFKGQHA FGVMQRPGRE GEASFIGAEL
PSLSYPESIS KRMLRTASFS GQVAMVTLQE AWDDAKLDHV DPSRIGLVIG GSNFQQRELF
QTYEAYREKM HFVPPTYGLS FMDTDLCGLC TEQFGIQGLA YTVGGASASG QVAIIQAIEA
IQANRVDVCI AMGALMDISY LECQALRSLG AMGSDRYANE PAKACRPFDQ MRDGFIYGES
CGVIVIERSD FAMKRQGKSY AKLTGWDMGM DRNRNPNPSY EGEVQVIKRA LKKAKLQPEK
IDYINPHGTG SVVGDEIEIK AIQDCNLSHA YINATKSIIG HGLSAAGTVE IIATLLQMKE
SKLHPTRNLE KPIGVDCNWV KNEPIPAAIH NTMNLSMGFG GINTAICMQK CESGI
//