FABF_STAAN
ID FABF_STAAN Reviewed; 414 AA.
AC Q7A6F8;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 2;
DE EC=2.3.1.179 {ECO:0000250|UniProtKB:P0AAI5};
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase II;
DE AltName: Full=Beta-ketoacyl-ACP synthase II;
DE Short=KAS II;
GN Name=fabF; OrderedLocusNames=SA0843;
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 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 [3]
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: Involved in the type II fatty acid elongation cycle.
CC Catalyzes the elongation of a wide range of acyl-ACP by the addition of
CC two carbons from malonyl-ACP to an acyl acceptor. Can efficiently
CC catalyze the conversion of palmitoleoyl-ACP (cis-hexadec-9-enoyl-ACP)
CC to cis-vaccenoyl-ACP (cis-octadec-11-enoyl-ACP), an essential step in
CC the thermal regulation of fatty acid composition.
CC {ECO:0000250|UniProtKB:P0AAI5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC Evidence={ECO:0000250|UniProtKB:P0AAI5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(11Z)-
CC octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:55040,
CC Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:10800,
CC Rhea:RHEA-COMP:14074, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:83989,
CC ChEBI:CHEBI:138538; EC=2.3.1.179;
CC Evidence={ECO:0000250|UniProtKB:P0AAI5};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:P0AAI5}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000305}.
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; BA000018; BAB42084.1; -; Genomic_DNA.
DR PIR; A89866; A89866.
DR RefSeq; WP_000081231.1; NC_002745.2.
DR AlphaFoldDB; Q7A6F8; -.
DR SMR; Q7A6F8; -.
DR SWISS-2DPAGE; Q7A6F8; -.
DR EnsemblBacteria; BAB42084; BAB42084; BAB42084.
DR KEGG; sau:SA0843; -.
DR HOGENOM; CLU_000022_69_2_9; -.
DR OMA; YRYIKYK; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000751; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00834; KAS_I_II; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR017568; 3-oxoacyl-ACP_synth-2.
DR InterPro; IPR000794; Beta-ketoacyl_synthase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR11712; PTHR11712; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR PIRSF; PIRSF000447; KAS_II; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR03150; fabF; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Transferase.
FT CHAIN 1..414
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 2"
FT /id="PRO_0000180322"
FT ACT_SITE 165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
SQ SEQUENCE 414 AA; 43725 MW; 46C0005B584824C5 CRC64;
MSQNKRVVIT GMGALSPIGN DVKTTWENAL KGVNGIDKIT RIDTEPYSVH LAGELKNFNI
EDHIDKKEAR RMDRFTQYAI VAAREAVKDA QLDINDNTAD RIGVWIGSGI GGMETFEIAH
KQLMDKGPRR VSPFFVPMLI PDMATGQVSI DLGAKGPNGA TVTACATGTN SIGEAFKIVQ
RGDADAMITG GTEAPITHMA IAGFSASRAL STNDDIETAC RPFQEGRDGF VMGEGAGILV
IESLESAQAR GANIYAEIVG YGTTGDAYHI TAPAPEGEGG SRAMQAAMDD AGIEPKDVQY
LNAHGTSTPV GDLNEVKAIK NTFGEAAKHL KVSSTKSMTG HLLGATGGIE AIFSALSIKD
SKVAPTIHAV TPDPECDLDI VPNEAQDLDI TYAMSNSLGF GGHNAVLVFK KFEA
