ID Q2YQQ9_BRUA2 Unreviewed; 407 AA. AC Q2YQQ9; DT 07-FEB-2006, integrated into UniProtKB/TrEMBL. DT 07-FEB-2006, sequence version 1. DT 27-MAR-2024, entry version 114. DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 1 {ECO:0000256|ARBA:ARBA00039450}; DE EC=2.3.1.41 {ECO:0000256|ARBA:ARBA00013191}; DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase I {ECO:0000256|ARBA:ARBA00041620}; DE AltName: Full=Beta-ketoacyl-ACP synthase I {ECO:0000256|ARBA:ARBA00042143}; GN Name=fabB {ECO:0000313|EMBL:CAJ12129.1}; GN OrderedLocusNames=BAB1_2173 {ECO:0000313|EMBL:CAJ12129.1}; OS Brucella abortus (strain 2308). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ12129.1, ECO:0000313|Proteomes:UP000002719}; RN [1] {ECO:0000313|EMBL:CAJ12129.1, ECO:0000313|Proteomes:UP000002719} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2308 {ECO:0000313|EMBL:CAJ12129.1, RC ECO:0000313|Proteomes:UP000002719}; RX PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005; RG Microbial Genomics Group; RG Lawrence Livermore National Laboratory; RG and the Genome Analysis Group; RG Oak Ridge National Laboratory; RA Chain P., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S., RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.; RT "Whole-genome analyses of speciation events in pathogenic Brucellae."; RL Infect. Immun. 73:8353-8361(2005). RN [2] {ECO:0007829|PDB:3LRF, ECO:0007829|PDB:3MQD} RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS). RX PubMed=31237717; DOI=10.1002/prot.25765; RA Patterson E.I., Nanson J.D., Abendroth J., Bryan C., Sankaran B., RA Myler P.J., Forwood J.K.; RT "Structural characterization of beta-ketoacyl ACP synthase I bound to RT platencin and fragment screening molecules at two substrate binding RT sites."; RL Proteins 88:47-56(2020). 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:0000256|ARBA:ARBA00035917}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54941; CC Evidence={ECO:0000256|ARBA:ARBA00035917}; 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:0000256|ARBA:ARBA00023389}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837; CC Evidence={ECO:0000256|ARBA:ARBA00023389}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. 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; AM040264; CAJ12129.1; -; Genomic_DNA. DR RefSeq; WP_002965234.1; NZ_KN046823.1. DR PDB; 3LRF; X-ray; 1.60 A; A=1-407. DR PDB; 3MQD; X-ray; 1.25 A; A=1-407. DR PDB; 3U0E; X-ray; 1.60 A; A=1-407. DR PDB; 3U0F; X-ray; 1.25 A; A=1-407. DR PDB; 4JV3; X-ray; 1.70 A; A=1-407. DR PDBsum; 3LRF; -. DR PDBsum; 3MQD; -. DR PDBsum; 3U0E; -. DR PDBsum; 3U0F; -. DR PDBsum; 4JV3; -. DR AlphaFoldDB; Q2YQQ9; -. DR SMR; Q2YQQ9; -. DR STRING; 359391.BAB1_2173; -. DR GeneID; 3788695; -. DR KEGG; bmf:BAB1_2173; -. DR PATRIC; fig|359391.11.peg.1410; -. DR HOGENOM; CLU_000022_69_2_5; -. DR PhylomeDB; Q2YQQ9; -. DR BRENDA; 2.3.1.41; 995. DR EvolutionaryTrace; Q2YQQ9; -. DR Proteomes; UP000002719; Chromosome I. 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:InterPro. DR CDD; cd00834; KAS_I_II; 1. DR Gene3D; 3.40.47.10; -; 2. 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 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:3LRF, ECO:0007829|PDB:3MQD}; KW Acyltransferase {ECO:0000313|EMBL:CAJ12129.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002719}; KW Transferase {ECO:0000256|RuleBase:RU003694, ECO:0000313|EMBL:CAJ12129.1}. FT DOMAIN 1..404 FT /note="Ketosynthase family 3 (KS3)" FT /evidence="ECO:0000259|PROSITE:PS52004" SQ SEQUENCE 407 AA; 43311 MW; 26DB912A67F0AD07 CRC64; MRRVVVTGMG IVSSIGSNTE EVTASLREAK SGISRAEEYA ELGFRCQVHG APDIDIESLV DRRAMRFHGR GTAWNHIAMD QAIADAGLTE EEVSNERTGI IMGSGGPSTR TIVDSADITR EKGPKRVGPF AVPKAMSSTA SATLATFFKI KGINYSISSA CATSNHCIGN AYEMIQYGKQ DRMFAGGCED LDWTLSVLFD AMGAMSSKYN DTPSTASRAY DKNRDGFVIA GGAGVLVLED LETALARGAK IYGEIVGYGA TSDGYDMVAP SGEGAIRCMK MALSTVTSKI DYINPHATST PAGDAPEIEA IRQIFGAGDV CPPIAATKSL TGHSLGATGV QEAIYSLLMM QNNFICESAH IEELDPAFAD MPIVRKRIDN VQLNTVLSNS FGFGGTNATL VFQRYQG //