ID   Q2GL22_ANAPZ            Unreviewed;       319 AA.
AC   Q2GL22;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   10-JUN-2026, entry version 117.
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:ABD43384.1};
GN   OrderedLocusNames=APH_0317 {ECO:0000313|EMBL:ABD43384.1};
OS   Anaplasma phagocytophilum (strain HZ).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rickettsiales; Anaplasmataceae; Anaplasma; phagocytophilum group.
OX   NCBI_TaxID=212042 {ECO:0000313|EMBL:ABD43384.1, ECO:0000313|Proteomes:UP000001943};
RN   [1] {ECO:0000313|EMBL:ABD43384.1, ECO:0000313|Proteomes:UP000001943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HZ {ECO:0000313|EMBL:ABD43384.1,
RC   ECO:0000313|Proteomes:UP000001943};
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA   Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.,
RA   Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J., Daugherty S.C.,
RA   Davidsen T., Durkin A.S., Gwinn M., Haft D.H., Selengut J.D.,
RA   Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA   Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
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; CP000235; ABD43384.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2GL22; -.
DR   STRING; 212042.APH_0317; -.
DR   PaxDb; 212042-APH_0317; -.
DR   EnsemblBacteria; ABD43384; ABD43384; APH_0317.
DR   KEGG; aph:APH_0317; -.
DR   eggNOG; COG0332; Bacteria.
DR   HOGENOM; CLU_039592_3_1_5; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001943; 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   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:TreeGrafter.
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; PTHR34069; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE 3; 1.
DR   PANTHER; PTHR34069:SF2; BETA-KETOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE III; 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}; Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01815};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01815};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_01815}; Reference proteome {ECO:0000313|Proteomes:UP000001943};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01815}.
FT   DOMAIN          106..186
FT                   /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08545"
FT   DOMAIN          230..318
FT                   /note="Beta-ketoacyl-[acyl-carrier-protein] synthase III C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08541"
FT   REGION          247..251
FT                   /note="ACP-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT   ACT_SITE        112
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT   ACT_SITE        246
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
FT   ACT_SITE        276
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01815"
SQ   SEQUENCE   319 AA;  33304 MW;  59664A513D90A2DA CRC64;
     MKAVLCGVGS FLPHKAVTNE DLSLIVDTTD EWIFRRTGIK RRYLVSEGEA TSDMAVKAAE
     AALSDAGVSA EEVDLIVVAT STPDSTLPSC ATMVQGKLGC TKAFAFDMNA ACSGFVYAIS
     VVDSLIKTGQ VGVALLIGAE SMSKIVDWHD RSTCVLFGDG AGACVFKGDG KASNRGIVDT
     ALYTDGTLGD ILYTDGGVAS TCTAGHIRMK GTVLFEHAIL KLSSSVEGLL KKNAIGIDAI
     DWFIPHQANV RIVDLVAKRL GISQDKVVLG IGDHANTSAA SIPLAMSDAR RDGKLQEGQL
     VLLAAIGAGV TWGASLIRL
//