FABH_STAA8
ID FABH_STAA8 Reviewed; 313 AA.
AC Q2FZS0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 {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 III {ECO:0000255|HAMAP-Rule:MF_01815};
DE AltName: Full=Beta-ketoacyl-ACP synthase III {ECO:0000255|HAMAP-Rule:MF_01815};
DE Short=KAS III {ECO:0000255|HAMAP-Rule:MF_01815};
GN Name=fabH {ECO:0000255|HAMAP-Rule:MF_01815};
GN OrderedLocusNames=SAOUHSC_00920;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (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: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 -!- 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}.
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DR EMBL; CP000253; ABD30045.1; -; Genomic_DNA.
DR RefSeq; WP_001100525.1; NZ_LS483365.1.
DR RefSeq; YP_499473.1; NC_007795.1.
DR PDB; 6KVS; X-ray; 2.30 A; A/B=1-313.
DR PDBsum; 6KVS; -.
DR AlphaFoldDB; Q2FZS0; -.
DR SMR; Q2FZS0; -.
DR STRING; 1280.SAXN108_0977; -.
DR BindingDB; Q2FZS0; -.
DR EnsemblBacteria; ABD30045; ABD30045; SAOUHSC_00920.
DR GeneID; 3920807; -.
DR KEGG; sao:SAOUHSC_00920; -.
DR PATRIC; fig|93061.5.peg.841; -.
DR eggNOG; COG0332; Bacteria.
DR HOGENOM; CLU_039592_3_1_9; -.
DR OMA; WGSEGDK; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q2FZS0; -.
DR Proteomes; UP000008816; 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 Gene3D; 3.40.47.10; -; 1.
DR HAMAP; MF_01815; FabH; 1.
DR InterPro; IPR013751; ACP_syn_III.
DR InterPro; IPR013747; ACP_syn_III_C.
DR InterPro; IPR004655; FabH_synth.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF08545; ACP_syn_III; 1.
DR Pfam; PF08541; ACP_syn_III_C; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR TIGRFAMs; TIGR00747; fabH; 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..313
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT /id="PRO_1000056416"
FT REGION 239..243
FT /note="ACP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 112
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 238
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 268
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
SQ SEQUENCE 313 AA; 33879 MW; 325F4A9CFF461769 CRC64;
MNVGIKGFGA YAPEKIIDNA YFEQFLDTSD EWISKMTGIK ERHWADDDQD TSDLAYEASL
KAIADAGIQP EDIDMIIVAT ATGDMPFPTV ANMLQERLGT GKVASMDQLA ACSGFMYSMI
TAKQYVQSGD YHNILVVGAD KLSKITDLTD RSTAVLFGDG AGAVIIGEVS DGRGIISYEM
GSDGTGGKHL YLDKDTGKLK MNGREVFKFA VRIMGDASTR VVEKANLTSD DIDLFIPHQA
NIRIMESARE RLGISKDKMS VSVNKYGNTS AASIPLSIDQ ELKNGKIKDD DTIVLVGFGG
GLTWGAMTIK WGK
