FABH_PSEAE
ID FABH_PSEAE Reviewed; 330 AA.
AC Q9HYR2;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=PA3333;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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}.
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; AE004091; AAG06721.1; -; Genomic_DNA.
DR PIR; A83230; A83230.
DR RefSeq; NP_252023.1; NC_002516.2.
DR RefSeq; WP_003091712.1; NZ_QZGE01000017.1.
DR PDB; 2X3E; X-ray; 1.81 A; A/B=1-330.
DR PDBsum; 2X3E; -.
DR AlphaFoldDB; Q9HYR2; -.
DR SMR; Q9HYR2; -.
DR STRING; 287.DR97_4594; -.
DR PaxDb; Q9HYR2; -.
DR PRIDE; Q9HYR2; -.
DR EnsemblBacteria; AAG06721; AAG06721; PA3333.
DR GeneID; 882498; -.
DR KEGG; pae:PA3333; -.
DR PATRIC; fig|208964.12.peg.3491; -.
DR PseudoCAP; PA3333; -.
DR HOGENOM; CLU_039592_4_0_6; -.
DR InParanoid; Q9HYR2; -.
DR OMA; QFVFKNA; -.
DR PhylomeDB; Q9HYR2; -.
DR BioCyc; PAER208964:G1FZ6-3397-MON; -.
DR BRENDA; 2.3.1.180; 5087.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; Q9HYR2; -.
DR Proteomes; UP000002438; 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 3D-structure; Acyltransferase; Cytoplasm; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW Multifunctional enzyme; Reference proteome; Transferase.
FT CHAIN 1..330
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 3"
FT /id="PRO_0000110455"
FT REGION 250..254
FT /note="ACP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 111
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 249
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT ACT_SITE 279
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01815"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:2X3E"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:2X3E"
FT HELIX 21..27
FT /evidence="ECO:0007829|PDB:2X3E"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:2X3E"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2X3E"
FT HELIX 52..67
FT /evidence="ECO:0007829|PDB:2X3E"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:2X3E"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:2X3E"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:2X3E"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:2X3E"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2X3E"
FT HELIX 113..126
FT /evidence="ECO:0007829|PDB:2X3E"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:2X3E"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:2X3E"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:2X3E"
FT STRAND 159..168
FT /evidence="ECO:0007829|PDB:2X3E"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:2X3E"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:2X3E"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:2X3E"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:2X3E"
FT HELIX 214..236
FT /evidence="ECO:0007829|PDB:2X3E"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:2X3E"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:2X3E"
FT HELIX 253..263
FT /evidence="ECO:0007829|PDB:2X3E"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:2X3E"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:2X3E"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:2X3E"
FT HELIX 284..294
FT /evidence="ECO:0007829|PDB:2X3E"
FT STRAND 303..310
FT /evidence="ECO:0007829|PDB:2X3E"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:2X3E"
FT STRAND 314..321
FT /evidence="ECO:0007829|PDB:2X3E"
SQ SEQUENCE 330 AA; 34004 MW; 6F032604DF695F1E CRC64;
MPRAAVVCGL GSYLPEAVLS NDMLAAELDT SDAWISSRTG VRQRHIAGDL GSGDLALRAA
SAALASAGLE RVDAVVLATS TGDFCCPATA PRVAARLGLV GALAFDLSAA CTGFVYGLAS
VGSLISAGLA DSALLVGVDT FSHTLDPADR STRALFGDGA GAVVLRAGDA EEEGALLAFD
LGSDGHQFDL LMTPAVSRAE RSSGQASNYF RMDGKAVFGQ AVTQMSDSVR RVLDRVGWQA
SDLHHLVPHQ ANTRILAAVA DQLDLPVERV VSNIAEVGNT VAASIPLALA HGLRQGILRD
GGNMVLTGFG AGLTWGSVAL RWPKIVPTMD
