FABY_PSEAE
ID FABY_PSEAE Reviewed; 634 AA.
AC Q9HU15;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Beta-ketoacyl-[acyl-carrier-protein] synthase FabY {ECO:0000303|PubMed:22753059};
DE Short=Beta-ketoacyl-ACP synthase {ECO:0000303|PubMed:22753059};
DE Short=KAS {ECO:0000303|PubMed:22753059};
DE EC=2.3.1.180 {ECO:0000269|PubMed:22753059};
DE AltName: Full=Beta-ketoacyl synthase KAS I/II domain-containing enzyme {ECO:0000303|PubMed:22753059};
GN Name=fabY; OrderedLocusNames=PA5174;
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).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=22753059; DOI=10.1128/jb.00792-12;
RA Yuan Y., Sachdeva M., Leeds J.A., Meredith T.C.;
RT "Fatty acid biosynthesis in Pseudomonas aeruginosa is initiated by the FabY
RT class of beta-ketoacyl acyl carrier protein synthases.";
RL J. Bacteriol. 194:5171-5184(2012).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=24145528; DOI=10.1128/aac.01804-13;
RA Six D.A., Yuan Y., Leeds J.A., Meredith T.C.;
RT "Deletion of the beta-acetoacetyl synthase FabY in Pseudomonas aeruginosa
RT induces hypoacylation of lipopolysaccharide and increases antimicrobial
RT susceptibility.";
RL Antimicrob. Agents Chemother. 58:153-161(2014).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS), AND SUBUNIT.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=25456814; DOI=10.1016/j.str.2014.09.016;
RA Bukhari H.S., Jakob R.P., Maier T.;
RT "Evolutionary origins of the multienzyme architecture of giant fungal fatty
RT acid synthase.";
RL Structure 22:1775-1785(2014).
CC -!- FUNCTION: Involved in the initiation of the fatty acid biosynthesis.
CC Catalyzes the condensation of acetyl coenzyme A (acetyl-CoA) with
CC malonyl-acyl carrier protein (ACP) to make the fatty acid synthesis
CC (FAS) primer beta-acetoacetyl-ACP. It can also use short-chain acyl-CoA
CC as substrates, including butyryl-CoA, and hexanoyl-CoA, but does not
CC use any of the longer chain acyl-CoA substrates.
CC {ECO:0000269|PubMed:22753059, ECO:0000269|PubMed:24145528}.
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:0000269|PubMed:22753059};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000305|PubMed:22753059}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25456814}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show an attenuated growth
CC due to a defect in de novo fatty acid biosynthesis. Siderophore
CC secretion and quorum-sensing signaling, particularly in the rhl and
CC Pseudomonas quinolone signal (PQS) systems, is significantly muted in
CC the absence of fabY (PubMed:22753059). In vitro, the deletion of fabY
CC results in an increased susceptibility to a number of antibiotics,
CC including vancomycin and cephalosporins. The antibiotic susceptibility
CC is influenced by changes in membrane lipid composition which lack a
CC single secondary lauroyl group, resulting in hypoacylated lipid A
CC (PubMed:24145528). {ECO:0000269|PubMed:22753059,
CC ECO:0000269|PubMed:24145528}.
CC -!- MISCELLANEOUS: FabY is a FabB/F homolog that functions as a FabH.
CC {ECO:0000305|PubMed:22753059}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000305}.
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DR EMBL; AE004091; AAG08559.1; -; Genomic_DNA.
DR PIR; E82999; E82999.
DR RefSeq; NP_253861.1; NC_002516.2.
DR RefSeq; WP_003114068.1; NZ_QZGE01000002.1.
DR PDB; 4CW4; X-ray; 1.35 A; A=1-634.
DR PDBsum; 4CW4; -.
DR AlphaFoldDB; Q9HU15; -.
DR SMR; Q9HU15; -.
DR DIP; DIP-61329N; -.
DR STRING; 287.DR97_2542; -.
DR PaxDb; Q9HU15; -.
DR PRIDE; Q9HU15; -.
DR EnsemblBacteria; AAG08559; AAG08559; PA5174.
DR GeneID; 881783; -.
DR KEGG; pae:PA5174; -.
DR PATRIC; fig|208964.12.peg.5422; -.
DR PseudoCAP; PA5174; -.
DR HOGENOM; CLU_030172_0_0_6; -.
DR InParanoid; Q9HU15; -.
DR OMA; CATFLYN; -.
DR PhylomeDB; Q9HU15; -.
DR BioCyc; MetaCyc:MON-17580; -.
DR BioCyc; PAER208964:G1FZ6-5291-MON; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IBA:GO_Central.
DR GO; GO:0033818; F:beta-ketoacyl-acyl-carrier-protein synthase III activity; IDA:CACAO.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IMP:CACAO.
DR GO; GO:0009245; P:lipid A biosynthetic process; IMP:CACAO.
DR GO; GO:0009372; P:quorum sensing; IMP:CACAO.
DR GO; GO:0019290; P:siderophore biosynthetic process; IMP:CACAO.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR000794; Beta-ketoacyl_synthase.
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; 2.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW Reference proteome; Transferase.
FT CHAIN 1..634
FT /note="Beta-ketoacyl-[acyl-carrier-protein] synthase FabY"
FT /id="PRO_0000433484"
FT ACT_SITE 281
FT /evidence="ECO:0000305|PubMed:25456814"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 23..28
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 35..48
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 69..82
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:4CW4"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 185..199
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 205..210
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:4CW4"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 233..238
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 258..266
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 283..296
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 301..309
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 314..322
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 329..336
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 361..369
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 370..376
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 381..389
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 404..420
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 422..428
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 439..456
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 460..464
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 467..470
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 474..476
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 477..491
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 527..534
FT /evidence="ECO:0007829|PDB:4CW4"
FT TURN 535..537
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 538..545
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 547..558
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 560..585
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 602..604
FT /evidence="ECO:0007829|PDB:4CW4"
FT STRAND 609..613
FT /evidence="ECO:0007829|PDB:4CW4"
FT HELIX 630..632
FT /evidence="ECO:0007829|PDB:4CW4"
SQ SEQUENCE 634 AA; 68764 MW; 008E69989B99A2D1 CRC64;
MSRLPVIVGF GGYNAAGRSS FHHGFRRMVI ESMDPQARQE TLAGLAVMMK LVKAEGGRYL
AEDGTPLSPE DIERRYAERI FASTLVRRIE PQYLDPDAVH WHKVLELSPA EGQALTFKAS
PKQLPEPLPA NWSIAPAEDG EVLVSIHERC EFKVDSYRAL TVKSAGQLPT GFEPGELYNS
RFHPRGLQMS VVAATDAIRS TGIDWKTIVD NVQPDEIAVF SGSIMSQLDD NGFGGLMQSR
LKGHRVSAKQ LPLGFNSMPT DFINAYVLGS VGMTGSITGA CATFLYNLQK GIDVITSGQA
RVVIVGNSEA PILPECIEGY SAMGALATEE GLRLIEGRDD VDFRRASRPF GENCGFTLAE
SSQYVVLMDD ELALRLGADI HGAVTDVFIN ADGFKKSISA PGPGNYLTVA KAVASAVQIV
GLDTVRHASF VHAHGSSTPA NRVTESEILD RVASAFGIDG WPVTAVKAYV GHSLATASAD
QLISALGTFK YGILPGIKTI DKVADDVHQQ RLSISNRDMR QDKPLEVCFI NSKGFGGNNA
SGVVLSPRIA EKMLRKRHGQ AAFAAYVEKR EQTRAAARAY DQRALQGDLE IIYNFGQDLI
DEHAIEVSAE QVTVPGFSQP LVYKKDARFS DMLD
