FABH1_BACSU
ID FABH1_BACSU Reviewed; 312 AA.
AC O34746;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 1 {ECO:0000255|HAMAP-Rule:MF_01815};
DE EC=2.3.1.180 {ECO:0000255|HAMAP-Rule:MF_01815, ECO:0000269|PubMed:10629181};
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III protein 1 {ECO:0000255|HAMAP-Rule:MF_01815};
DE AltName: Full=Beta-ketoacyl-ACP synthase III 1 {ECO:0000255|HAMAP-Rule:MF_01815};
DE Short=KAS III 1 {ECO:0000255|HAMAP-Rule:MF_01815};
DE AltName: Full=bFabH1 {ECO:0000303|PubMed:10629181};
GN Name=fabHA {ECO:0000255|HAMAP-Rule:MF_01815}; Synonyms=fabH, fabH1, yjaX;
GN OrderedLocusNames=BSU11330;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION, SUBSTRATE SPECIFICITY, AND CATALYTIC ACTIVITY.
RX PubMed=10629181; DOI=10.1128/jb.182.2.365-370.2000;
RA Choi K.-H., Heath R.J., Rock C.O.;
RT "Beta-ketoacyl-acyl carrier protein synthase III (FabH) is a determining
RT factor in branched-chain fatty acid biosynthesis.";
RL J. Bacteriol. 182:365-370(2000).
RN [3]
RP INDUCTION.
RX PubMed=12737802; DOI=10.1016/s1534-5807(03)00123-0;
RA Schujman G.E., Paoletti L., Grossman A.D., de Mendoza D.;
RT "FapR, a bacterial transcription factor involved in global regulation of
RT membrane lipid biosynthesis.";
RL Dev. Cell 4:663-672(2003).
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. Has some substrate specificity for
CC branched chain acyl-CoA, determining the biosynthesis of branched-chain
CC of fatty acids instead of straight-chain.
CC {ECO:0000269|PubMed:10629181}.
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 ECO:0000269|PubMed:10629181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12081;
CC Evidence={ECO:0000269|PubMed:10629181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-[ACP] + propanoyl-CoA = 3-oxopentanoyl-[ACP] +
CC CO2 + CoA; Xref=Rhea:RHEA:42244, Rhea:RHEA-COMP:9623, Rhea:RHEA-
CC COMP:9939, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57392, ChEBI:CHEBI:78449, ChEBI:CHEBI:78818;
CC Evidence={ECO:0000269|PubMed:10629181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42245;
CC Evidence={ECO:0000269|PubMed:10629181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + H(+) + malonyl-[ACP] = 3-oxohexanoyl-[ACP] +
CC CO2 + CoA; Xref=Rhea:RHEA:42248, Rhea:RHEA-COMP:9623, Rhea:RHEA-
CC COMP:9629, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:78449, ChEBI:CHEBI:78456;
CC Evidence={ECO:0000269|PubMed:10629181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42249;
CC Evidence={ECO:0000269|PubMed:10629181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-[ACP] + pentanoyl-CoA = 3-oxoheptanoyl-[ACP] +
CC CO2 + CoA; Xref=Rhea:RHEA:42252, Rhea:RHEA-COMP:9623, Rhea:RHEA-
CC COMP:9943, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57389, ChEBI:CHEBI:78449, ChEBI:CHEBI:78824;
CC Evidence={ECO:0000269|PubMed:10629181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42253;
CC Evidence={ECO:0000269|PubMed:10629181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexanoyl-CoA + malonyl-[ACP] = 3-oxooctanoyl-[ACP] +
CC CO2 + CoA; Xref=Rhea:RHEA:42256, Rhea:RHEA-COMP:9623, Rhea:RHEA-
CC COMP:9633, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:62620, ChEBI:CHEBI:78449, ChEBI:CHEBI:78460;
CC Evidence={ECO:0000269|PubMed:10629181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42257;
CC Evidence={ECO:0000269|PubMed:10629181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + heptanoyl-CoA + malonyl-[ACP] = 3-oxononanoyl-[ACP] +
CC CO2 + CoA; Xref=Rhea:RHEA:42260, Rhea:RHEA-COMP:9623, Rhea:RHEA-
CC COMP:9944, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78811, ChEBI:CHEBI:78826;
CC Evidence={ECO:0000269|PubMed:10629181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42261;
CC Evidence={ECO:0000269|PubMed:10629181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + malonyl-[ACP] + octanoyl-CoA = 3-oxodecanoyl-[ACP] +
CC CO2 + CoA; Xref=Rhea:RHEA:42264, Rhea:RHEA-COMP:9623, Rhea:RHEA-
CC COMP:9637, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57386, ChEBI:CHEBI:78449, ChEBI:CHEBI:78464;
CC Evidence={ECO:0000269|PubMed:10629181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42265;
CC Evidence={ECO:0000269|PubMed:10629181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylpropanoyl-CoA + H(+) + malonyl-[ACP] = 4-methyl-3-
CC oxopentanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42268, Rhea:RHEA-
CC COMP:9623, Rhea:RHEA-COMP:9940, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57338, ChEBI:CHEBI:78449,
CC ChEBI:CHEBI:78820; Evidence={ECO:0000269|PubMed:10629181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42269;
CC Evidence={ECO:0000269|PubMed:10629181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methylbutanoyl-CoA + H(+) + malonyl-[ACP] = 5-methyl-3-
CC oxohexanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42272, Rhea:RHEA-
CC COMP:9623, Rhea:RHEA-COMP:9941, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57345, ChEBI:CHEBI:78449,
CC ChEBI:CHEBI:78822; Evidence={ECO:0000269|PubMed:10629181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42273;
CC Evidence={ECO:0000269|PubMed:10629181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-methylbutanoyl-CoA + H(+) + malonyl-[ACP] = (4S)-4-
CC methyl-3-oxohexanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42276,
CC Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:17148, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:78449,
CC ChEBI:CHEBI:88166, ChEBI:CHEBI:167462;
CC Evidence={ECO:0000269|PubMed:10629181};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42277;
CC Evidence={ECO:0000269|PubMed:10629181};
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:0000305}.
CC -!- INDUCTION: Down-regulated by FapR. {ECO:0000269|PubMed:12737802}.
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; AL009126; CAB12974.1; -; Genomic_DNA.
DR PIR; F69842; F69842.
DR RefSeq; NP_389015.1; NC_000964.3.
DR RefSeq; WP_003232971.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O34746; -.
DR SMR; O34746; -.
DR STRING; 224308.BSU11330; -.
DR SwissLipids; SLP:000000824; -.
DR jPOST; O34746; -.
DR PaxDb; O34746; -.
DR PRIDE; O34746; -.
DR EnsemblBacteria; CAB12974; CAB12974; BSU_11330.
DR GeneID; 936392; -.
DR KEGG; bsu:BSU11330; -.
DR PATRIC; fig|224308.179.peg.1218; -.
DR eggNOG; COG0332; Bacteria.
DR InParanoid; O34746; -.
DR OMA; WGSEGDK; -.
DR PhylomeDB; O34746; -.
DR BioCyc; BSUB:BSU11330-MON; -.
DR BioCyc; MetaCyc:BSU11330-MON; -.
DR BRENDA; 2.3.1.180; 658.
DR BRENDA; 2.3.1.300; 658.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001570; 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:0061990; F:beta-ketodecanoyl-[acyl-carrier-protein] synthase activity; IEA:RHEA.
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 Acyltransferase; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Multifunctional enzyme;
KW Reference proteome; Transferase.
FT CHAIN 1..312
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3 protein
FT 1"
FT /id="PRO_0000110399"
FT REGION 238..242
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 237
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 267
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
SQ SEQUENCE 312 AA; 33732 MW; CC8174D32E8AAD0A CRC64;
MKAGILGVGR YIPEKVLTNH DLEKMVETSD EWIRTRTGIE ERRIAADDVF SSHMAVAAAK
NALEQAEVAA EDLDMILVAT VTPDQSFPTV SCMIQEQLGA KKACAMDISA ACAGFMYGVV
TGKQFIESGT YKHVLVVGVE KLSSITDWED RNTAVLFGDG AGAAVVGPVS DDRGILSFEL
GADGTGGQHL YLNEKRHTIM NGREVFKFAV RQMGESCVNV IEKAGLSKED VDFLIPHQAN
IRIMEAARER LELPVEKMSK TVHKYGNTSA ASIPISLVEE LEAGKIKDGD VVVMVGFGGG
LTWGAIAIRW GR
