ID FABH_AQUAE Reviewed; 309 AA. AC O67185; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 134. DE RecName: Full=Beta-ketoacyl-[acyl-carrier-protein] synthase III {ECO:0000255|HAMAP-Rule:MF_01815}; DE Short=Beta-ketoacyl-ACP synthase III {ECO:0000255|HAMAP-Rule:MF_01815}; DE Short=KAS III {ECO:0000255|HAMAP-Rule:MF_01815}; DE EC=2.3.1.180 {ECO:0000255|HAMAP-Rule:MF_01815}; DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 {ECO:0000255|HAMAP-Rule:MF_01815}; DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III {ECO:0000255|HAMAP-Rule:MF_01815}; GN Name=fabH {ECO:0000255|HAMAP-Rule:MF_01815}; GN OrderedLocusNames=aq_1099; OS Aquifex aeolicus (strain VF5). OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex. OX NCBI_TaxID=224324; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VF5; RX PubMed=9537320; DOI=10.1038/32831; RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.; RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."; RL Nature 392:353-358(1998). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RC STRAIN=VF5; RG RIKEN structural genomics initiative (RSGI); RT "Crystal structure of 3-oxoacyl-[acyl-carrier-protein] synthase III from RT Aquifex aeolicus VF5."; RL Submitted (AUG-2007) to the PDB data bank. CC -!- FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis CC by the addition to an acyl acceptor of two carbons from malonyl-ACP. CC Catalyzes the first condensation reaction which initiates fatty acid CC synthesis and may therefore play a role in governing the total rate of CC fatty acid production. Possesses both acetoacetyl-ACP synthase and CC acetyl transacylase activities. Its substrate specificity determines CC the biosynthesis of branched-chain and/or straight-chain of fatty CC acids. {ECO:0000255|HAMAP-Rule:MF_01815}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 CC + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA- CC COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; CC EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815}; CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP- CC Rule:MF_01815}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01815}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01815, CC ECO:0000305}. CC -!- DOMAIN: The last Arg residue of the ACP-binding site is essential for CC the weak association between ACP/AcpP and FabH. {ECO:0000255|HAMAP- CC Rule:MF_01815}. CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family. CC {ECO:0000255|HAMAP-Rule:MF_01815}. 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; AE000657; AAC07144.1; -; Genomic_DNA. DR PIR; F70394; F70394. DR RefSeq; NP_213748.1; NC_000918.1. DR RefSeq; WP_010880686.1; NC_000918.1. DR PDB; 2EBD; X-ray; 2.10 A; A/B=1-309. DR PDBsum; 2EBD; -. DR AlphaFoldDB; O67185; -. DR SMR; O67185; -. DR STRING; 224324.aq_1099; -. DR EnsemblBacteria; AAC07144; AAC07144; aq_1099. DR KEGG; aae:aq_1099; -. DR PATRIC; fig|224324.8.peg.857; -. DR eggNOG; COG0332; Bacteria. DR HOGENOM; CLU_039592_3_1_0; -. DR InParanoid; O67185; -. DR OrthoDB; 9815506at2; -. DR UniPathway; UPA00094; -. DR EvolutionaryTrace; O67185; -. DR Proteomes; UP000000798; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro. DR GO; GO:0033818; F:beta-ketoacyl-acyl-carrier-protein synthase III activity; IEA:UniProtKB-UniRule. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd00830; KAS_III; 1. DR Gene3D; 3.40.47.10; -; 1. DR HAMAP; MF_01815; FabH; 1. DR InterPro; IPR013747; ACP_syn_III_C. DR InterPro; IPR013751; ACP_syn_III_N. DR InterPro; IPR004655; FabH. DR InterPro; IPR016039; Thiolase-like. DR NCBIfam; TIGR00747; fabH; 1. DR PANTHER; PTHR43091; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE; 1. DR PANTHER; PTHR43091:SF1; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE III, CHLOROPLASTIC; 1. DR Pfam; PF08545; ACP_syn_III; 1. DR Pfam; PF08541; ACP_syn_III_C; 1. DR SUPFAM; SSF53901; Thiolase-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Cytoplasm; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; KW Multifunctional enzyme; Reference proteome; Transferase. FT CHAIN 1..309 FT /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III" FT /id="PRO_0000110392" FT REGION 237..241 FT /note="ACP-binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815" FT ACT_SITE 111 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815" FT ACT_SITE 236 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815" FT ACT_SITE 266 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815" FT STRAND 3..11 FT /evidence="ECO:0007829|PDB:2EBD" FT STRAND 14..18 FT /evidence="ECO:0007829|PDB:2EBD" FT HELIX 19..23 FT /evidence="ECO:0007829|PDB:2EBD" FT HELIX 30..37 FT /evidence="ECO:0007829|PDB:2EBD" FT STRAND 41..44 FT /evidence="ECO:0007829|PDB:2EBD" FT HELIX 50..65 FT /evidence="ECO:0007829|PDB:2EBD" FT HELIX 69..71 FT /evidence="ECO:0007829|PDB:2EBD" FT STRAND 73..78 FT /evidence="ECO:0007829|PDB:2EBD" FT STRAND 83..87 FT /evidence="ECO:0007829|PDB:2EBD" FT HELIX 89..97 FT /evidence="ECO:0007829|PDB:2EBD" FT STRAND 103..108 FT /evidence="ECO:0007829|PDB:2EBD" FT HELIX 110..112 FT /evidence="ECO:0007829|PDB:2EBD" FT HELIX 113..126 FT /evidence="ECO:0007829|PDB:2EBD" FT STRAND 131..140 FT /evidence="ECO:0007829|PDB:2EBD" FT HELIX 141..143 FT /evidence="ECO:0007829|PDB:2EBD" FT TURN 150..155 FT /evidence="ECO:0007829|PDB:2EBD" FT STRAND 158..167 FT /evidence="ECO:0007829|PDB:2EBD" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:2EBD" FT STRAND 173..181 FT /evidence="ECO:0007829|PDB:2EBD" FT HELIX 183..188 FT /evidence="ECO:0007829|PDB:2EBD" FT STRAND 189..191 FT /evidence="ECO:0007829|PDB:2EBD" FT STRAND 197..199 FT /evidence="ECO:0007829|PDB:2EBD" FT HELIX 201..223 FT /evidence="ECO:0007829|PDB:2EBD" FT HELIX 227..229 FT /evidence="ECO:0007829|PDB:2EBD" FT STRAND 231..235 FT /evidence="ECO:0007829|PDB:2EBD" FT HELIX 240..249 FT /evidence="ECO:0007829|PDB:2EBD" FT HELIX 254..256 FT /evidence="ECO:0007829|PDB:2EBD" FT HELIX 261..264 FT /evidence="ECO:0007829|PDB:2EBD" FT HELIX 268..270 FT /evidence="ECO:0007829|PDB:2EBD" FT HELIX 271..281 FT /evidence="ECO:0007829|PDB:2EBD" FT STRAND 290..297 FT /evidence="ECO:0007829|PDB:2EBD" FT TURN 298..300 FT /evidence="ECO:0007829|PDB:2EBD" FT STRAND 301..308 FT /evidence="ECO:0007829|PDB:2EBD" SQ SEQUENCE 309 AA; 33825 MW; EB97518DB168140D CRC64; MGTKIIGTGV YLPKNVLTNF DLEKIVDTSD EWITTRTGIK ERRIAKEETI TYMATQAAKE ALREANLSPE ELDLIILATL TPQKRFPSTA CLVQAQLKAK GVYAFDISAA CSGFIYALDI ADSFIKSGKA KNVLVIGAEK LSEAVDWEDR STCVLFGDGA GAVVVTRSED KSDILATRMY AEGSLEELLH ADNCGYIRMK GRELFKVAVR SMEEVCREVL EKAGVKPEEV SLVIPHQANV RIINALAEKL NIPKEKVFVN IQKYGNTSAA SIPIALHEAI KEGKVKRGDL ILMTAMGGGL TWGAVLLRY //