ID FABB_BUCAP Reviewed; 407 AA.
AC Q8KA28;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 111.
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=BUsg_084;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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}.
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DR EMBL; AE013218; AAM67654.1; -; Genomic_DNA.
DR RefSeq; WP_011053620.1; NC_004061.1.
DR AlphaFoldDB; Q8KA28; -.
DR SMR; Q8KA28; -.
DR STRING; 198804.BUsg_084; -.
DR GeneID; 75259041; -.
DR KEGG; bas:BUsg_084; -.
DR eggNOG; COG0304; Bacteria.
DR HOGENOM; CLU_000022_69_2_6; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000416; 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; Transferase.
FT CHAIN 1..407
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 1"
FT /id="PRO_0000180309"
FT DOMAIN 1..406
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 300
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT ACT_SITE 336
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
SQ SEQUENCE 407 AA; 44523 MW; CBCFC30445A34679 CRC64;
MKRVVITGFG IISSIGNNKK EVLNSLYNGI SGITFSEEMK ESGMRSQVWG NIKLENKKFF
KKNKISRFMN NGSIYAFLSM EQAIKDANLQ TKQYQKNPRI GIIAGSGGGF PKYHIQGIDA
IRSNRGLNSV SPYIAIKAMN SGISACLSTL FKIYGVNYSI SSACATSGHC IGNAFELIKF
GKQDLIFAGG GEEVSWELAY EFDAMKALSS NFNKNPTKSS RVYDVNRDGF VISGGGGIIV
IEELNCALSR SAHIYAEIIG YAATSDGKDM VVPSGDGAVR CMNLAKKQNK MLFIDYLNVH
GTSTKIGDLI ELEAIKKSFF HEKKPMISAT KSMTGHALGV SGVHEIIYTL LMMKYNFIAP
SINIETIEPS ADNMNIVQKT FHKKIKTALS NSFGFGGTNV SLILKKY
//
