ID A0A0F3KKH6_9NEIS Unreviewed; 413 AA.
AC A0A0F3KKH6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 2 {ECO:0000256|ARBA:ARBA00014657, ECO:0000256|PIRNR:PIRNR000447};
DE EC=2.3.1.179 {ECO:0000256|ARBA:ARBA00012356, ECO:0000256|PIRNR:PIRNR000447};
GN ORFNames=DLM_2855 {ECO:0000313|EMBL:BBF86456.1};
OS Aquitalea magnusonii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Aquitalea.
OX NCBI_TaxID=332411 {ECO:0000313|EMBL:BBF86456.1, ECO:0000313|Proteomes:UP000198290};
RN [1] {ECO:0000313|Proteomes:UP000198290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3 {ECO:0000313|Proteomes:UP000198290};
RX PubMed=28293292; DOI=10.1186/s13068-017-0746-8;
RA Ishizawa H., Kuroda M., Morikawa M., Ike M.;
RT "Evaluation of environmental bacterial communities as a factor affecting
RT the growth of duckweed Lemna minor.";
RL Biotechnol. Biofuels 10:62-62(2017).
RN [2] {ECO:0000313|EMBL:BBF86456.1, ECO:0000313|Proteomes:UP000198290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3 {ECO:0000313|EMBL:BBF86456.1,
RC ECO:0000313|Proteomes:UP000198290};
RX DOI=10.1128/genomea.00812-17;
RA Ishizawa H., Kuroda M., Ike M.;
RT "Draft genome sequence of Aquitalea magnusonii strain H3, a plant growth-
RT promoting bacterium of duckweed Lemna minor.";
RL Genome Announc 5 0:0-0(2017).
RN [3] {ECO:0000313|Proteomes:UP000198290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3 {ECO:0000313|Proteomes:UP000198290};
RX DOI=10.1016/j.plaphy.2017.08.006;
RA Ishizawa H., Kuroda M., Morikawa M., Ike M.;
RT "Differential oxidative and antioxidative response of duckweed Lemna minor
RT toward plant growth promoting/inhibiting bacteria.";
RL Plant Physiol. Biochem. 118:0-0(2017).
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:0000256|PIRNR:PIRNR000447}.
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:0000256|PIRNR:PIRNR000447};
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:0000256|PIRNR:PIRNR000447};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194, ECO:0000256|PIRNR:PIRNR000447}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467,
CC ECO:0000256|PIRNR:PIRNR000447, ECO:0000256|RuleBase:RU003694}.
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DR EMBL; AP018823; BBF86456.1; -; Genomic_DNA.
DR RefSeq; WP_045846174.1; NZ_AP018823.1.
DR STRING; 332411.VI06_07565; -.
DR KEGG; amah:DLM_2855; -.
DR OrthoDB; 9808669at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000198290; 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; -; 2.
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 NCBIfam; TIGR03150; fabF; 1.
DR PANTHER; PTHR11712:SF336; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11712; POLYKETIDE SYNTHASE-RELATED; 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; Thiolase-like; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|PIRNR:PIRNR000447};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW ECO:0000256|PIRNR:PIRNR000447};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|PIRNR:PIRNR000447};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Transferase {ECO:0000256|PIRNR:PIRNR000447, ECO:0000256|RuleBase:RU003694}.
SQ SEQUENCE 413 AA; 43054 MW; F2EDEFE9B373C43F CRC64;
MSKRRVVVTG LGHISPVGND VATGWANLLA GKSGIGKVTR FDASDLNCQI AGEVKDFDIS
AYISPKEARR SDLFIHYGIA AALQAVADAG LDDVADLDKT RVGVNIGSGI GGLPLIEETG
VAVQENGIRK IGPFFIPGSL INLIAGHVSI LKGYQGPSYG IVSACTTGAH CIGDAARMIQ
YGDADVMVAG GAEGAISKLG MGGFAAMKAL STRNDDPETA SRPWDKGRDG FVMGEGAGVL
VLEEYEHAVK RGARIYAELI GFGMSSDAHH ITAPNADGPA RGVQNALRDA RINPDQVQYV
NAHGTSTPLG DANETSALKI AFGDHAKKLV VNSTKSMTGH LLGGAGGVEA IYSILALYNQ
VSPPTINLHE QDVEAGCDLD YVANTARDMK IDIAISNSFG FGGTNGTLVF KRM
//
