FABH_STAAR
ID FABH_STAAR Reviewed; 313 AA.
AC Q6GIA4;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 {ECO:0000255|HAMAP-Rule:MF_01815};
DE EC=2.3.1.180 {ECO:0000255|HAMAP-Rule:MF_01815};
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III {ECO:0000255|HAMAP-Rule:MF_01815};
DE AltName: Full=Beta-ketoacyl-ACP synthase III {ECO:0000255|HAMAP-Rule:MF_01815};
DE Short=KAS III {ECO:0000255|HAMAP-Rule:MF_01815};
GN Name=fabH {ECO:0000255|HAMAP-Rule:MF_01815}; OrderedLocusNames=SAR0946;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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. Its substrate specificity determines
CC the biosynthesis of branched-chain and/or straight-chain of fatty
CC acids. {ECO:0000255|HAMAP-Rule:MF_01815}.
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 -!- 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:0000255|HAMAP-Rule:MF_01815}.
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; BX571856; CAG39952.1; -; Genomic_DNA.
DR RefSeq; WP_001100526.1; NC_002952.2.
DR PDB; 3IL7; X-ray; 2.60 A; A/B=1-313.
DR PDBsum; 3IL7; -.
DR AlphaFoldDB; Q6GIA4; -.
DR SMR; Q6GIA4; -.
DR KEGG; sar:SAR0946; -.
DR HOGENOM; CLU_039592_3_1_9; -.
DR OMA; WGSEGDK; -.
DR OrthoDB; 872193at2; -.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; Q6GIA4; -.
DR Proteomes; UP000000596; 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 3D-structure; Acyltransferase; Cytoplasm; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW Multifunctional enzyme; Transferase.
FT CHAIN 1..313
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT /id="PRO_0000110471"
FT REGION 239..243
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 238
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 268
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:3IL7"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:3IL7"
FT HELIX 19..24
FT /evidence="ECO:0007829|PDB:3IL7"
FT HELIX 30..37
FT /evidence="ECO:0007829|PDB:3IL7"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:3IL7"
FT HELIX 51..65
FT /evidence="ECO:0007829|PDB:3IL7"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:3IL7"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:3IL7"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3IL7"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:3IL7"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:3IL7"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:3IL7"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:3IL7"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:3IL7"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:3IL7"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:3IL7"
FT STRAND 159..168
FT /evidence="ECO:0007829|PDB:3IL7"
FT STRAND 174..182
FT /evidence="ECO:0007829|PDB:3IL7"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:3IL7"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:3IL7"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:3IL7"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:3IL7"
FT HELIX 203..224
FT /evidence="ECO:0007829|PDB:3IL7"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:3IL7"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:3IL7"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:3IL7"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:3IL7"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:3IL7"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:3IL7"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:3IL7"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:3IL7"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:3IL7"
FT STRAND 303..310
FT /evidence="ECO:0007829|PDB:3IL7"
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
