ID FABF_SYNY3 Reviewed; 416 AA. AC P73283; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 02-SEP-2026, entry version 152. DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 2; DE EC=2.3.1.179 {ECO:0000250|UniProtKB:P0AAI5}; DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase II; DE AltName: Full=Beta-ketoacyl-ACP synthase II; DE Short=KAS II; GN Name=fabF; OrderedLocusNames=sll1069; OS Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Merismopediaceae; Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27184 / PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). RN [2] {ECO:0007744|PDB:1E5M} RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS), AND SUBUNIT. RX PubMed=11152607; DOI=10.1006/jmbi.2000.4272; RA Moche M., Dehesh K., Edwards P., Lindqvist Y.; RT "The crystal structure of beta-ketoacyl-acyl carrier protein synthase II RT from Synechocystis sp. at 1.54 A resolution and its relationship to other RT condensing enzymes."; RL J. Mol. Biol. 305:491-503(2001). 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 efficiently CC catalyze the conversion of palmitoleoyl-ACP (cis-hexadec-9-enoyl-ACP) CC to cis-vaccenoyl-ACP (cis-octadec-11-enoyl-ACP), an essential step in CC the thermal regulation of fatty acid composition. CC {ECO:0000250|UniProtKB:P0AAI5}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a fatty acyl-[ACP] + malonyl-[ACP] + H(+) = a 3-oxoacyl-[ACP] CC + holo-[ACP] + CO2; 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 Evidence={ECO:0000250|UniProtKB:P0AAI5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(9Z)-hexadecenoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxo-(11Z)- CC octadecenoyl-[ACP] + holo-[ACP] + CO2; Xref=Rhea:RHEA:55040, CC Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:10800, CC Rhea:RHEA-COMP:14074, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:83989, CC ChEBI:CHEBI:138538; EC=2.3.1.179; CC Evidence={ECO:0000250|UniProtKB:P0AAI5}; CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {ECO:0000250|UniProtKB:P0AAI5}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11152607}. 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; BA000022; BAA17311.1; -; Genomic_DNA. DR PIR; S77464; S77464. DR PDB; 1E5M; X-ray; 1.54 A; A=1-416. DR AlphaFoldDB; P73283; -. DR SMR; P73283; -. DR FunCoup; P73283; 445. DR STRING; 1148.gene:10498174; -. DR PaxDb; 1148-gene:10498174; -. DR EnsemblBacteria; BAA17311; BAA17311; BAA17311. DR KEGG; syn:sll1069; -. DR eggNOG; COG0304; Bacteria. DR InParanoid; P73283; -. DR PhylomeDB; P73283; -. DR BRENDA; 2.3.1.179; 382. DR UniPathway; UPA00094; -. DR EvolutionaryTrace; P73283; -. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; ISS:UniProtKB. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd00834; KAS_I_II; 1. DR FunFam; 3.40.47.10:FF:000009; 3-oxoacyl-[acyl-carrier-protein] synthase 2; 1. DR Gene3D; 3.40.47.10; -; 2. DR InterPro; IPR017568; 3-oxoacyl-ACP_synth-2. DR InterPro; IPR000794; Beta-ketoacyl_synthase. DR InterPro; IPR014031; KAS_C. DR InterPro; IPR014030; KAS_N. DR InterPro; IPR018201; Ketoacyl_synth_AS. DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom. DR InterPro; IPR016039; Thiolase-like. DR NCBIfam; TIGR03150; fabF; 1. DR NCBIfam; NF004970; PRK06333.1; 1. DR NCBIfam; NF005589; PRK07314.1; 1. 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 PIRSF; PIRSF000447; KAS_II; 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. DR PDBsum; 1E5M; -. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; KW Reference proteome; Transferase. FT CHAIN 1..416 FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 2" FT /id="PRO_0000180326" FT DOMAIN 6..414 FT /note="Ketosynthase family 3 (KS3)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 167 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 307 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 344 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT STRAND 9..18 FT /evidence="ECO:0007829|PDB:1E5M" FT STRAND 21..23 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 24..32 FT /evidence="ECO:0007829|PDB:1E5M" FT STRAND 38..40 FT /evidence="ECO:0007829|PDB:1E5M" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 62..64 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 68..72 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 76..92 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 94..96 FT /evidence="ECO:0007829|PDB:1E5M" FT TURN 98..100 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 101..103 FT /evidence="ECO:0007829|PDB:1E5M" FT STRAND 104..109 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 115..128 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 130..132 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 137..141 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 145..154 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 166..168 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 169..182 FT /evidence="ECO:0007829|PDB:1E5M" FT STRAND 187..195 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 200..208 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 219..221 FT /evidence="ECO:0007829|PDB:1E5M" FT STRAND 238..246 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 247..252 FT /evidence="ECO:0007829|PDB:1E5M" FT STRAND 259..268 FT /evidence="ECO:0007829|PDB:1E5M" FT STRAND 273..275 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 281..294 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 298..300 FT /evidence="ECO:0007829|PDB:1E5M" FT STRAND 303..305 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 312..326 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 327..332 FT /evidence="ECO:0007829|PDB:1E5M" FT STRAND 333..336 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 339..342 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 346..348 FT /evidence="ECO:0007829|PDB:1E5M" FT HELIX 349..363 FT /evidence="ECO:0007829|PDB:1E5M" FT STRAND 373..375 FT /evidence="ECO:0007829|PDB:1E5M" FT STRAND 385..387 FT /evidence="ECO:0007829|PDB:1E5M" FT STRAND 394..402 FT /evidence="ECO:0007829|PDB:1E5M" FT TURN 403..405 FT /evidence="ECO:0007829|PDB:1E5M" FT STRAND 406..413 FT /evidence="ECO:0007829|PDB:1E5M" SQ SEQUENCE 416 AA; 44004 MW; B0740A438A91A6C1 CRC64; MANLEKKRVV VTGLGAITPI GNTLQDYWQG LMEGRNGIGP ITRFDASDQA CRFGGEVKDF DATQFLDRKE AKRMDRFCHF AVCASQQAIN DAKLVINELN ADEIGVLIGT GIGGLKVLED QQTILLDKGP SRCSPFMIPM MIANMASGLT AINLGAKGPN NCTVTACAAG SNAIGDAFRL VQNGYAKAMI CGGTEAAITP LSYAGFASAR ALSFRNDDPL HASRPFDKDR DGFVMGEGSG ILILEELESA LARGAKIYGE MVGYAMTCDA YHITAPVPDG RGATRAIAWA LKDSGLKPEM VSYINAHGTS TPANDVTETR AIKQALGNHA YNIAVSSTKS MTGHLLGGSG GIEAVATVMA IAEDKVPPTI NLENPDPECD LDYVPGQSRA LIVDVALSNS FGFGGHNVTL AFKKYQ //