ID FABB_BUCAI Reviewed; 406 AA. AC P57193; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 27-MAR-2024, entry version 117. 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=BU092; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon OS pisum symbiotic bacterium). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=107806; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=APS; RX PubMed=10993077; DOI=10.1038/35024074; RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera RT sp. APS."; RL Nature 407:81-86(2000). 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; BA000003; BAB12811.1; -; Genomic_DNA. DR RefSeq; NP_239925.1; NC_002528.1. DR RefSeq; WP_009874045.1; NC_002528.1. DR AlphaFoldDB; P57193; -. DR SMR; P57193; -. DR STRING; 563178.BUAP5A_090; -. DR EnsemblBacteria; BAB12811; BAB12811; BAB12811. DR KEGG; buc:BU092; -. DR PATRIC; fig|107806.10.peg.99; -. DR eggNOG; COG0304; Bacteria. DR HOGENOM; CLU_000022_69_2_6; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000001806; 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..406 FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 1" FT /id="PRO_0000180308" 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 406 AA; 44119 MW; 8AF83C2E87D4649E CRC64; MRRVVITGIG IVSSIGNNKK EVLASLYKGV SGIVSSEEMK KLGMRSAVWG NIKLESINII TQKLSRFMNN ASRYSFVAMM EAIKDAKIDR EYYQKNPRVG LISGSGCSFS KNTLTSDIHL MKNKHISKGI SPYLAVKTMP SGISACLSTL FKIYGVTYSI SSACATSAHC IGNAFELIQF GRQDLIFAGG GEEISLELAM QFDAMRALST CFNNDPKKAS RVYDVYRDGF VISGGAGMLV IEELNSALSR SAYIYAEIIG YAATSDGSNI VVPSGDGAIR CMNLARKGKN IPIDYLNVHG TGTKIGDLIE LEAIRKVFLN EKKPMISATK SMTGHGLGAS GVHEMIYTLL MLKYNFIAPT INIENLEPCA ENMNIIQKTT NIEINTAMSN SFGFGGTNVS LIVKKY //