FABF_STAAW
ID FABF_STAAW Reviewed; 414 AA.
AC Q8NXE1;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 112.
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=MW0866;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
RN [2] {ECO:0007744|PDB:2GQD}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS).
RA Miller D.J., Zhang Y.M., Rock C.O., White S.W.;
RT "The crystal structure of B-ketoacyl-ACP synthase II (FabF) from
RT Staphylococcus aureus.";
RL Submitted (APR-2006) to the PDB data bank.
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}.
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DR EMBL; BA000033; BAB94731.1; -; Genomic_DNA.
DR RefSeq; WP_000081240.1; NC_003923.1.
DR PDB; 2GQD; X-ray; 2.30 A; A/B=1-414.
DR PDBsum; 2GQD; -.
DR AlphaFoldDB; Q8NXE1; -.
DR SMR; Q8NXE1; -.
DR EnsemblBacteria; BAB94731; BAB94731; BAB94731.
DR KEGG; sam:MW0866; -.
DR HOGENOM; CLU_000022_69_2_9; -.
DR OMA; YRYIKYK; -.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; Q8NXE1; -.
DR Proteomes; UP000000418; 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 3D-structure; Acyltransferase; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Transferase.
FT CHAIN 1..414
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 2"
FT /id="PRO_0000180325"
FT ACT_SITE 165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT STRAND 7..16
FT /evidence="ECO:0007829|PDB:2GQD"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 22..30
FT /evidence="ECO:0007829|PDB:2GQD"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:2GQD"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:2GQD"
FT TURN 67..71
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 74..90
FT /evidence="ECO:0007829|PDB:2GQD"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:2GQD"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 113..126
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 143..152
FT /evidence="ECO:0007829|PDB:2GQD"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 167..180
FT /evidence="ECO:0007829|PDB:2GQD"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 198..206
FT /evidence="ECO:0007829|PDB:2GQD"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:2GQD"
FT STRAND 235..243
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:2GQD"
FT STRAND 256..265
FT /evidence="ECO:0007829|PDB:2GQD"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 278..291
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:2GQD"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 309..323
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:2GQD"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 346..360
FT /evidence="ECO:0007829|PDB:2GQD"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:2GQD"
FT STRAND 391..398
FT /evidence="ECO:0007829|PDB:2GQD"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:2GQD"
FT STRAND 403..410
FT /evidence="ECO:0007829|PDB:2GQD"
SQ SEQUENCE 414 AA; 43739 MW; 2DB06BB5DD48D175 CRC64;
MSQNKRVVIT GMGALSPIGN DVKTTWENAL KGVNGIDKIT RIDTEPYSVH LAGELKNFNI
EDHIDKKEAR RMDRFTQYAI VAAREAVKDA QLDINENTAD 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
