FABB_PSEAB
ID FABB_PSEAB Reviewed; 405 AA.
AC Q02K94;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 1 {ECO:0000250|UniProtKB:P0A953};
DE EC=2.3.1.41 {ECO:0000250|UniProtKB:P0A953};
DE AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase I {ECO:0000250|UniProtKB:P0A953};
DE AltName: Full=Beta-ketoacyl-ACP synthase I {ECO:0000250|UniProtKB:P0A953};
DE Short=KAS I {ECO:0000250|UniProtKB:P0A953};
GN Name=fabB; OrderedLocusNames=PA14_43690;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=UCBPP-PA14;
RX PubMed=25096199; DOI=10.1007/s00216-014-8045-8;
RA Ouidir T., Jarnier F., Cosette P., Jouenne T., Hardouin J.;
RT "Potential of liquid-isoelectric-focusing protein fractionation to improve
RT phosphoprotein characterization of Pseudomonas aeruginosa PA14.";
RL Anal. Bioanal. Chem. 406:6297-6309(2014).
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 also use
CC unsaturated fatty acids. Catalyzes a key reaction in unsaturated fatty
CC acid (UFA) synthesis, the elongation of the cis-3-decenoyl-ACP produced
CC by FabA. {ECO:0000250|UniProtKB:P0A953}.
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 EC=2.3.1.41; Evidence={ECO:0000250|UniProtKB:P0A953};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837;
CC Evidence={ECO:0000250|UniProtKB:P0A953};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3Z)-decenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(5Z)-
CC dodecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:54940, Rhea:RHEA-
CC COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9927, Rhea:RHEA-
CC COMP:14042, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78798, ChEBI:CHEBI:138410;
CC Evidence={ECO:0000250|UniProtKB:P0A953};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54941;
CC Evidence={ECO:0000250|UniProtKB:P0A953};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:P0A953}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0A953}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A953}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000305}.
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DR EMBL; CP000438; ABJ10790.1; -; Genomic_DNA.
DR RefSeq; WP_003087471.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02K94; -.
DR SMR; Q02K94; -.
DR PRIDE; Q02K94; -.
DR EnsemblBacteria; ABJ10790; ABJ10790; PA14_43690.
DR KEGG; pau:PA14_43690; -.
DR HOGENOM; CLU_000022_69_2_6; -.
DR OMA; YAYLSMQ; -.
DR BioCyc; PAER208963:G1G74-3665-MON; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000653; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; -; 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 SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Transferase.
FT CHAIN 1..405
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase 1"
FT /id="PRO_0000431475"
FT ACT_SITE 161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
SQ SEQUENCE 405 AA; 42879 MW; E5D6F98464E2A022 CRC64;
MRRVVITGLG IVSCLGNDKD TVSANLRAGR PGIRFNPSYA EMGLRSHVSG SVDLNLEELI
DRKVFRFMGD AAAYAYLAME QAIKDSGLTP EQISNPRTGL IAGSGGASTL NQMEAIDTLR
EKGVKRIGPY RVTRTMGSTV SACLATPFQI KGVNYSISSA CATSAHCIGQ AMEQIQLGKQ
DVVFAGGGEE EHWSQSCLFD AMGALSTQYN ETPEKASRAY DAKRDGFVIA GGGGMVVVEE
LEHALKRGAK IYAEIVGYGA TSDGYDMVAP SGEGAIRCMQ QALATVDAPI DYLNTHGTST
PVGDVAEIRG VREVFGDKAP AISSTKSLSG HSLGAAGVHE AIYCLLMMEG GFIAGSANID
ELDPEVADLP ILRETRENAK LDTVMSNSFG FGGTNATLVL KRWQG
