ID   KASC1_HORVU             Reviewed;         462 AA.
AC   P23902;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase I, chloroplastic;
DE            EC=2.3.1.41;
DE   AltName: Full=Beta-ketoacyl-ACP synthase I;
DE            Short=KAS I;
DE   Flags: Precursor;
GN   Name=KAS12;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Bonus;
RX   PubMed=2034657; DOI=10.1073/pnas.88.10.4114;
RA   Siggaard-Andersen M., Kauppinen S., von Wettstein-Knowles P.;
RT   "Primary structure of a cerulenin-binding beta-ketoacyl-[acyl carrier
RT   protein] synthase from barley chloroplasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:4114-4118(1991).
CC   -!- FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis
CC       by the addition to an acyl acceptor of two carbons from malonyl-ACP.
CC       Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty
CC       acids.
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;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000305}.
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DR   EMBL; M60410; AAA32968.1; -; mRNA.
DR   PIR; A39356; A39356.
DR   AlphaFoldDB; P23902; -.
DR   SMR; P23902; -.
DR   PRIDE; P23902; -.
DR   EnsemblPlants; HORVU.MOREX.r2.2HG0141350.1.mrna1; HORVU.MOREX.r2.2HG0141350.1.mrna1; HORVU.MOREX.r2.2HG0141350.1.
DR   Gramene; HORVU.MOREX.r2.2HG0141350.1.mrna1; HORVU.MOREX.r2.2HG0141350.1.mrna1; HORVU.MOREX.r2.2HG0141350.1.
DR   ExpressionAtlas; P23902; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; 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-KW.
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   PANTHER; PTHR11712; PTHR11712; 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; SSF53901; 2.
DR   TIGRFAMs; TIGR03150; fabF; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Chloroplast; Direct protein sequencing;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Plastid; Transferase; Transit peptide.
FT   TRANSIT         1..35
FT                   /note="Chloroplast"
FT   CHAIN           36..462
FT                   /note="3-oxoacyl-[acyl-carrier-protein] synthase I,
FT                   chloroplastic"
FT                   /id="PRO_0000000587"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        213
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
SQ   SEQUENCE   462 AA;  49016 MW;  BDFA3622263A7764 CRC64;
     MHAHAAHALG LRVPPPAFPR RRARPRRRPA AAVLATSAAP QRETDPRKRV VITGMGLASV
     FGSDVDTFYD RLLAGESGVG PIDRFDASSF PTRFAGQIRG FSSEGYIDGK NDRRLDDCIR
     YCILSGKKAL ESAGLGAGSD AHVKLDVGRA GVLVGTGMGG LSVFSDGVQN LIEKGYRKIS
     PFFIPYAITN MGSALLAIDV GFMGPNYSIS TACATSNYCF YAAANHIRRG EADIIVAGGT
     EAAIIPIGLG GFVACRALSQ RNDDPITACR PWDKERDGFV MGEGAGVLVM ESLEHAMKRD
     APIIAEYLGG AVNCDAYHMT DPRADGLGVS SCITMSLRDA GVAPEEVNYI NAHATSTLAG
     DLAEVRAIKQ VFKNPSEIKI NSTKSMIGHC LGAAGGLEAI ATIKSITTGW VHPTINQFNP
     EPEVDFDTVA NEKKQHEVNV GISNSFGFGG HNSVVVFAPF KP