FABH2_BACSU
ID FABH2_BACSU Reviewed; 325 AA.
AC O07600;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 protein 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01815};
DE AltName: Full=Beta-ketoacyl-ACP synthase III 2 {ECO:0000255|HAMAP-Rule:MF_01815};
DE Short=KAS III 2 {ECO:0000255|HAMAP-Rule:MF_01815};
DE AltName: Full=bFabH2 {ECO:0000303|PubMed:10629181};
GN Name=fabHB {ECO:0000255|HAMAP-Rule:MF_01815}; Synonyms=fabH2, yhfB;
GN OrderedLocusNames=BSU10170;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(1998).
RN [2]
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 [3]
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 [4]
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=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; Y14083; CAA74523.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12857.1; -; Genomic_DNA.
DR PIR; H69829; H69829.
DR RefSeq; NP_388898.1; NC_000964.3.
DR RefSeq; WP_003233200.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O07600; -.
DR SMR; O07600; -.
DR STRING; 224308.BSU10170; -.
DR SwissLipids; SLP:000000826; -.
DR PaxDb; O07600; -.
DR PRIDE; O07600; -.
DR EnsemblBacteria; CAB12857; CAB12857; BSU_10170.
DR GeneID; 939306; -.
DR KEGG; bsu:BSU10170; -.
DR PATRIC; fig|224308.179.peg.1093; -.
DR eggNOG; COG0332; Bacteria.
DR InParanoid; O07600; -.
DR OMA; AIENLCT; -.
DR PhylomeDB; O07600; -.
DR BioCyc; BSUB:BSU10170-MON; -.
DR BioCyc; MetaCyc:BSU10170-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: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..325
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3 protein
FT 2"
FT /id="PRO_0000110400"
FT REGION 251..255
FT /note="ACP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 113
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 250
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 280
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
SQ SEQUENCE 325 AA; 35424 MW; CE6E475F3C88E335 CRC64;
MSKAKITAIG TYAPSRRLTN ADLEKIVDTS DEWIVQRTGM RERRIADEHQ FTSDLCIEAV
KNLKSRYKGT LDDVDMILVA TTTSDYAFPS TACRVQEYFG WESTGALDIN ATCAGLTYGL
HLANGLITSG LHQKILVIAG ETLSKVTDYT DRTTCVLFGD AAGALLVERD EETPGFLASV
QGTSGNGGDI LYRAGLRNEI NGVQLVGSGK MVQNGREVYK WAARTVPGEF ERLLHKAGLS
SDDLDWFVPH SANLRMIESI CEKTPFPIEK TLTSVEHYGN TSSVSIVLAL DLAVKAGKLK
KDQIVLLFGF GGGLTYTGLL IKWGM
