ID FABB_BUCBP Reviewed; 407 AA. AC Q89AY4; DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2003, sequence version 1. DT 27-MAR-2024, entry version 112. DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 1 {ECO:0000250|UniProtKB:P0A953}; DE EC=2.3.1.41 {ECO:0000250|UniProtKB:P0A953}; DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase I {ECO:0000250|UniProtKB:P0A953}; DE AltName: Full=Beta-ketoacyl-ACP synthase I {ECO:0000250|UniProtKB:P0A953}; DE Short=KAS I {ECO:0000250|UniProtKB:P0A953}; GN Name=fabB; OrderedLocusNames=bbp_086; OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=224915; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bp; RX PubMed=12522265; DOI=10.1073/pnas.0235981100; RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.; RT "Reductive genome evolution in Buchnera aphidicola."; RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003). CC -!- FUNCTION: Involved in the type II fatty acid elongation cycle. CC Catalyzes the elongation of a wide range of acyl-ACP by the addition of CC two carbons from malonyl-ACP to an acyl acceptor. Can also use CC unsaturated fatty acids. Catalyzes a key reaction in unsaturated fatty CC acid (UFA) synthesis, the elongation of the cis-3-decenoyl-ACP produced CC by FabA. {ECO:0000250|UniProtKB:P0A953}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651; CC EC=2.3.1.41; Evidence={ECO:0000250|UniProtKB:P0A953}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837; CC Evidence={ECO:0000250|UniProtKB:P0A953}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(3Z)-decenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(5Z)- CC dodecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:54940, Rhea:RHEA- CC COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9927, Rhea:RHEA- CC COMP:14042, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78798, ChEBI:CHEBI:138410; CC Evidence={ECO:0000250|UniProtKB:P0A953}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54941; CC Evidence={ECO:0000250|UniProtKB:P0A953}; CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {ECO:0000250|UniProtKB:P0A953}. CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0A953}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A953}. CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP CC synthases 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; AE016826; AAO26821.1; -; Genomic_DNA. DR RefSeq; WP_011091222.1; NC_004545.1. DR AlphaFoldDB; Q89AY4; -. DR SMR; Q89AY4; -. DR STRING; 224915.bbp_086; -. DR KEGG; bab:bbp_086; -. DR eggNOG; COG0304; Bacteria. DR HOGENOM; CLU_000022_69_2_6; -. DR OrthoDB; 9808669at2; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000000601; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd00834; KAS_I_II; 1. DR Gene3D; 3.40.47.10; -; 1. DR InterPro; IPR000794; Beta-ketoacyl_synthase. DR InterPro; IPR018201; Ketoacyl_synth_AS. 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:SF306; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE 1; 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; PS00606; KS3_1; 1. DR PROSITE; PS52004; KS3_2; 1. PE 3: Inferred from homology; KW Acyltransferase; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism; KW Lipid biosynthesis; Lipid metabolism; Reference proteome; Transferase. FT CHAIN 1..407 FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 1" FT /id="PRO_0000180310" FT DOMAIN 1..405 FT /note="Ketosynthase family 3 (KS3)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 164 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 299 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 335 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" SQ SEQUENCE 407 AA; 44482 MW; F2A07A7744977193 CRC64; MKRVVITGLG IISSIGNNKI EVLTSLLETK SGISFSKEME RSGMRSHVWG NIKLDNYQEN IDRKIFRFMN DASIYSYLSM KQAIEDAKLT SKMYQNNPRV GVIIGSSSGS PRCQINGVSI IKKTKRLKSV SPYTVIKSMT SSISACLSTL FKIQGVNYSI SSACATSAHC IGNAMELIQL GKQDLIFAGG GEELSWELAC AFDSMGALST MYNSQPILSS RVFDYYRDGF VISGGAGILV VEELNYALSR SAHIYAEIVG YGTSSDGYNV VVPSGNGAMR CMNIAMSNIQ EPIDYLNVHS TSTKIGDLIE LNAIQQVFRK TSIPILSSTK SITGHSLGAS GVQEMIYSLL MLKYNFIVPS INIFKLDPKA KNCNILTTMM RKELSIIMSN SFGFGGTNVS LIIKKFV //