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Database: UniProt
Entry: E4NAT3_KITSK
LinkDB: E4NAT3_KITSK
Original site: E4NAT3_KITSK 
ID   E4NAT3_KITSK            Unreviewed;       422 AA.
AC   E4NAT3;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
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=fabF2 {ECO:0000313|EMBL:BAJ28314.1};
GN   OrderedLocusNames=KSE_25000 {ECO:0000313|EMBL:BAJ28314.1};
OS   Kitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304
OS   / NBRC 14216 / KM-6054) (Streptomyces setae).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=452652 {ECO:0000313|EMBL:BAJ28314.1, ECO:0000313|Proteomes:UP000007076};
RN   [1] {ECO:0000313|EMBL:BAJ28314.1, ECO:0000313|Proteomes:UP000007076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 /
RC   KM-6054 {ECO:0000313|Proteomes:UP000007076};
RX   PubMed=21059706; DOI=10.1093/dnares/dsq026;
RA   Ichikawa N., Oguchi A., Ikeda H., Ishikawa J., Kitani S., Watanabe Y.,
RA   Nakamura S., Katano Y., Kishi E., Sasagawa M., Ankai A., Fukui S.,
RA   Hashimoto Y., Kamata S., Otoguro M., Tanikawa S., Nihira T., Horinouchi S.,
RA   Ohnishi Y., Hayakawa M., Kuzuyama T., Arisawa A., Nomoto F., Miura H.,
RA   Takahashi Y., Fujita N.;
RT   "Genome sequence of Kitasatospora setae NBRC 14216T: an evolutionary
RT   snapshot of the family Streptomycetaceae.";
RL   DNA Res. 17:393-406(2010).
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; AP010968; BAJ28314.1; -; Genomic_DNA.
DR   RefSeq; WP_014135628.1; NC_016109.1.
DR   AlphaFoldDB; E4NAT3; -.
DR   STRING; 452652.KSE_25000; -.
DR   KEGG; ksk:KSE_25000; -.
DR   PATRIC; fig|452652.3.peg.2504; -.
DR   eggNOG; COG0304; Bacteria.
DR   HOGENOM; CLU_000022_69_2_11; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000007076; 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; -; 1.
DR   InterPro; IPR017568; 3-oxoacyl-ACP_synth-2.
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   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; 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   Reference proteome {ECO:0000313|Proteomes:UP000007076};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000447, ECO:0000256|RuleBase:RU003694}.
FT   DOMAIN          5..421
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   ACT_SITE        171
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000447-1"
SQ   SEQUENCE   422 AA;  43968 MW;  78F6831A3C947AF8 CRC64;
     MTAENRTVVV TGIGAFTPLG GDAATFWEGL LAGRSGVRAL TEEWAADLPV RIAARVAVEP
     GEILPRPLAR KLDRSAQFAL IAAREAWKDA GYQAPATDES NALAPERLGA VIASGIGGVT
     TLLDQYDVLK EQGVRKVSPH TVPMLMPNSP AANVGLEVGA RAGVHTPVSA CASGAEAIGY
     AIEMIRTGRA DVVVAGGTEA AIHPLPIVAF SNMMAMSKNN DDPQHASRPY DKGRDGFVLG
     EGAGVVVLES AEHAAARGAR VYCEAVGQGL SSDAHHIAQP EPTGAGVARA IDDLFARNEL
     DRSEVVHVNA HATSTPQGDT AEIKALRRTL GEHLDHVAIS ATKSMTGHLL GGAGGIETVA
     TVLALYNRIA PPTVNVVDLD DDIDADIVRD EARKLPVEGR IAALNNSFGF GGHNVVLAFR
     TV
//
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