ID Q6MLJ5_BDEBA Unreviewed; 331 AA. AC Q6MLJ5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 10-JUN-2026, entry version 125. DE RecName: Full=Beta-ketoacyl-[acyl-carrier-protein] synthase III {ECO:0000256|HAMAP-Rule:MF_01815}; DE Short=Beta-ketoacyl-ACP synthase III {ECO:0000256|HAMAP-Rule:MF_01815}; DE Short=KAS III {ECO:0000256|HAMAP-Rule:MF_01815}; DE EC=2.3.1.180 {ECO:0000256|HAMAP-Rule:MF_01815}; DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 {ECO:0000256|HAMAP-Rule:MF_01815}; DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III {ECO:0000256|HAMAP-Rule:MF_01815}; GN Name=fabH {ECO:0000256|HAMAP-Rule:MF_01815, GN ECO:0000313|EMBL:CAE79862.1}; GN OrderedLocusNames=Bd2014 {ECO:0000313|EMBL:CAE79862.1}; OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 / OS HD100). OC Bacteria; Pseudomonadati; Bdellovibrionota; Bdellovibrionia; OC Bdellovibrionales; Pseudobdellovibrionaceae; Bdellovibrio. OX NCBI_TaxID=264462 {ECO:0000313|EMBL:CAE79862.1, ECO:0000313|Proteomes:UP000008080}; RN [1] {ECO:0000313|EMBL:CAE79862.1, ECO:0000313|Proteomes:UP000008080} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100 RC {ECO:0000313|Proteomes:UP000008080}; RX PubMed=14752164; DOI=10.1126/science.1093027; RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E., RA Schuster S.C.; RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a RT genomic perspective."; RL Science 303:689-692(2004). 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:0000256|HAMAP-Rule:MF_01815}. CC -!- CATALYTIC ACTIVITY: CC Reaction=malonyl-[ACP] + acetyl-CoA + H(+) = 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:0000256|HAMAP-Rule:MF_01815}; CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|HAMAP- CC Rule:MF_01815}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01815}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01815}. CC -!- DOMAIN: The last Arg residue of the ACP-binding site is essential for CC the weak association between ACP/AcpP and FabH. {ECO:0000256|HAMAP- CC Rule:MF_01815}. CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family. CC {ECO:0000256|ARBA:ARBA00008642, ECO:0000256|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; BX842651; CAE79862.1; -; Genomic_DNA. DR RefSeq; WP_011164464.1; NC_005363.1. DR AlphaFoldDB; Q6MLJ5; -. DR STRING; 264462.Bd2014; -. DR GeneID; 93012963; -. DR KEGG; bba:Bd2014; -. DR eggNOG; COG0332; Bacteria. DR HOGENOM; CLU_039592_3_1_7; -. DR UniPathway; UPA00094; -. DR Proteomes; UP000008080; 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 FunFam; 3.40.47.10:FF:000004; 3-oxoacyl-[acyl-carrier-protein] synthase 3; 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 NCBIfam; NF006829; PRK09352.1; 1. DR PANTHER; PTHR43091; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE; 1. DR PANTHER; PTHR43091:SF1; BETA-KETOACYL-[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 3: Inferred from homology; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP- KW Rule:MF_01815}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01815}; KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP- KW Rule:MF_01815}; KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP- KW Rule:MF_01815}; KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP- KW Rule:MF_01815}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP- KW Rule:MF_01815}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP- KW Rule:MF_01815}; Reference proteome {ECO:0000313|Proteomes:UP000008080}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01815}. FT DOMAIN 111..190 FT /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF08545" FT DOMAIN 242..331 FT /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF08541" FT REGION 259..263 FT /note="ACP-binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815" FT ACT_SITE 116 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815" FT ACT_SITE 258 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815" FT ACT_SITE 288 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01815" SQ SEQUENCE 331 AA; 36252 MW; 77229E3B5C07A777 CRC64; MAGMYRSRVS GIGSYLPEKI LSNKDLEKMV ETNDQWIVER TGIERRHIAS EDQATSDLCV IAAKRALEDA NLKVEDIDMI LVGTVTGDHQ MPSTACFVQA KLGAKNIMAV DLNAACSGFL YGVSIADQFI RTGMYKNILV IGAEVLSRYM NYKDRETCIL FGDGAGAWVM SRAAEGQTNV IESSHLRADG TLADLLILPA GGSKIPQSHE AIDKGLNFMT MKGRDIFKNA VRTMASCCQE ALEHNKVAPE QVDWIVPHQA NKRIIEAVAD QFKFPMERVI VYLQETGNTS AASIPLAFDW AVKNGKIKRG QTILLTAFGA GLTSGSILLR Y //