ID A0A150LE63_9BACI Unreviewed; 413 AA.
AC A0A150LE63;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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 Name=fabF {ECO:0000313|EMBL:REJ28043.1};
GN ORFNames=B4135_3429 {ECO:0000313|EMBL:KYD10628.1}, C6P37_09340
GN {ECO:0000313|EMBL:REJ28043.1};
OS Caldibacillus debilis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus.
OX NCBI_TaxID=301148 {ECO:0000313|EMBL:KYD10628.1, ECO:0000313|Proteomes:UP000075683};
RN [1] {ECO:0000313|EMBL:KYD10628.1, ECO:0000313|Proteomes:UP000075683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4135 {ECO:0000313|EMBL:KYD10628.1,
RC ECO:0000313|Proteomes:UP000075683};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT Foods.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:REJ28043.1, ECO:0000313|Proteomes:UP000257014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZCTH4_d {ECO:0000313|EMBL:REJ28043.1};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00023926,
CC 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|ARBA:ARBA00023971,
CC 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYD10628.1}.
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DR EMBL; LQYT01000117; KYD10628.1; -; Genomic_DNA.
DR EMBL; QEWE01000018; REJ28043.1; -; Genomic_DNA.
DR RefSeq; WP_020154812.1; NZ_QEWE01000018.1.
DR AlphaFoldDB; A0A150LE63; -.
DR STRING; 301148.B4135_3429; -.
DR PATRIC; fig|301148.3.peg.1408; -.
DR OrthoDB; 9808669at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000075683; Unassembled WGS sequence.
DR Proteomes; UP000257014; Unassembled WGS sequence.
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; -; 1.
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}.
FT DOMAIN 3..410
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT ACT_SITE 164
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000447-1"
SQ SEQUENCE 413 AA; 44035 MW; 2DAFCF67F6185426 CRC64;
MIKRRVVITG IGAVTPVGND AETAWQNIIR GKSGIGPLTR VNKDEFPAKV AAEVKDFNPE
DFLDKKDARK MDRFTHFAVA SALMAVKDAG LSIDESNAHR VGVWIGSGIG GMETYERQFE
TFLQRGYRRV SPFFVPMMIP DMAAGQVSIL LGAKGVNSCT VTACATGTNS IGDAFKVIQR
GDADVMITGG TEAPITKIAI AGFCANTALT TNPDPNTASR PFDKNRDGFV MGEGAGIVVL
EELNHALKRG AKIYAEIVGY GSTGDAYHIT APAPAGEGGA RAMKMALDDA GVSPEEVDYI
NAHGTSTEYN DKFETMAIKT VFGEHAYKIP VSSTKSMTGH LLGATGAVEA IFTALAIKEG
VIPPTMNYET PDPECDLDYV PNEARKKDVR VAISNSFGFG GHNATIVLKK FEP
//
