FABH_STAAN
ID FABH_STAAN Reviewed; 313 AA.
AC P99159; Q99VA7;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3;
DE EC=2.3.1.180;
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III;
DE AltName: Full=Beta-ketoacyl-ACP synthase III;
DE Short=KAS III;
DE AltName: Full=SaFabH;
GN Name=fabH; OrderedLocusNames=SA0842;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP FUNCTION, HOMODIMERIZATION, AND SUBSTRATE SPECIFICITY.
RX PubMed=11959561; DOI=10.1128/aac.46.5.1310-1318.2002;
RA He X., Reynolds K.A.;
RT "Purification, characterization, and identification of novel inhibitors of
RT the beta-ketoacyl-acyl carrier protein synthase III (FabH) from
RT Staphylococcus aureus.";
RL Antimicrob. Agents Chemother. 46:1310-1318(2002).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=N315;
RX PubMed=15590099; DOI=10.1016/j.mimet.2004.09.017;
RA Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y.,
RA Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C.,
RA Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.;
RT "Correlation of proteomic and transcriptomic profiles of Staphylococcus
RT aureus during the post-exponential phase of growth.";
RL J. Microbiol. Methods 60:247-257(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
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 preference for
CC butyryl- and isobutyryl-CoA. Its substrate specificity determines the
CC biosynthesis of branched-chain of fatty acids.
CC {ECO:0000269|PubMed:11959561}.
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;
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The last Arg residue of the ACP-binding site is essential for
CC the weak association between ACP/AcpP and FabH. {ECO:0000250}.
CC -!- MISCELLANEOUS: Inhibited by the HR12 (5-chloro-4-phenyl-[1,2]-dithiol-
CC 3-one) and HR19 (4-phenyl-5-phenylimino-[1,2,4]dithiazolidin-3-one)
CC antibiotics. Weakly inhibited by thiolactomycin.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family.
CC {ECO:0000305}.
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DR EMBL; BA000018; BAB42083.1; -; Genomic_DNA.
DR PIR; H89865; H89865.
DR RefSeq; WP_001100526.1; NC_002745.2.
DR AlphaFoldDB; P99159; -.
DR SMR; P99159; -.
DR SWISS-2DPAGE; P99159; -.
DR EnsemblBacteria; BAB42083; BAB42083; BAB42083.
DR KEGG; sau:SA0842; -.
DR HOGENOM; CLU_039592_3_1_9; -.
DR OMA; WGSEGDK; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000751; 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; -; 2.
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; Transferase.
FT CHAIN 1..313
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT /id="PRO_0000110470"
FT REGION 239..243
FT /note="ACP-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 112
FT /evidence="ECO:0000250"
FT ACT_SITE 238
FT /evidence="ECO:0000250"
FT ACT_SITE 268
FT /evidence="ECO:0000250"
SQ SEQUENCE 313 AA; 33879 MW; 728D2DCCAB9B95F7 CRC64;
MNVGIKGFGA YAPEKIIDNA YFEQFLDTSD EWISKMTGIK ERHWADDDQD TSDLAYEASV
KAIADAGIQP EDIDMIIVAT ATGDMPFPTV ANMLQERLGT GKVASMDQLA ACSGFMYSMI
TAKQYVQSGD YHNILVVGAD KLSKITDLTD RSTAVLFGDG AGAVIIGEVS EGRGIISYEM
GSDGTGGKHL YLDKDTGKLK MNGREVFKFA VRIMGDASTR VVEKANLTSD DIDLFIPHQA
NIRIMESARE RLGISKDKMS VSVNKYGNTS AASIPLSIDQ ELKNGKLKDD DTIVLVGFGG
GLTWGAMTIK WGK
