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KASC1_ARATH
ID   KASC1_ARATH             Reviewed;         473 AA.
AC   P52410; Q2V312; Q9FL32;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 2.
DT   03-AUG-2022, entry version 157.
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=KAS1; OrderedLocusNames=At5g46290; ORFNames=MPL12.7;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Millar A.A., Kunst L.;
RT   "Isolation of an Arabidopsis cDNA encoding 3-ketoacyl-acyl carrier protein
RT   synthase I.1.";
RL   (er) Plant Gene Register PGR95-027(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA   Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT   features of the regions of 1,381,565 bp covered by twenty one physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:131-145(1998).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA   Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT   "Multidimensional protein identification technology (MudPIT) analysis of
RT   ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA   Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA   van Wijk K.J.;
RT   "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT   proteome.";
RL   PLoS ONE 3:E1994-E1994(2008).
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 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000269|PubMed:18431481}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P52410-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P52410-2; Sequence=VSP_040746;
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000305}.
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DR   EMBL; U24177; AAC49118.1; -; mRNA.
DR   EMBL; AB010698; BAB11084.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95363.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95364.1; -; Genomic_DNA.
DR   EMBL; AY037261; AAK59862.1; -; mRNA.
DR   EMBL; AY094005; AAM16266.1; -; mRNA.
DR   EMBL; AY123979; AAM74493.1; -; mRNA.
DR   EMBL; AY087843; AAM65396.1; -; mRNA.
DR   RefSeq; NP_001032018.1; NM_001036941.1. [P52410-2]
DR   RefSeq; NP_199441.1; NM_123998.3. [P52410-1]
DR   AlphaFoldDB; P52410; -.
DR   SMR; P52410; -.
DR   BioGRID; 19920; 1.
DR   STRING; 3702.AT5G46290.3; -.
DR   PaxDb; P52410; -.
DR   PRIDE; P52410; -.
DR   ProteomicsDB; 250616; -. [P52410-1]
DR   EnsemblPlants; AT5G46290.1; AT5G46290.1; AT5G46290. [P52410-1]
DR   EnsemblPlants; AT5G46290.2; AT5G46290.2; AT5G46290. [P52410-2]
DR   GeneID; 834671; -.
DR   Gramene; AT5G46290.1; AT5G46290.1; AT5G46290. [P52410-1]
DR   Gramene; AT5G46290.2; AT5G46290.2; AT5G46290. [P52410-2]
DR   KEGG; ath:AT5G46290; -.
DR   Araport; AT5G46290; -.
DR   eggNOG; KOG1394; Eukaryota.
DR   HOGENOM; CLU_000022_69_2_1; -.
DR   InParanoid; P52410; -.
DR   OMA; QICTNAR; -.
DR   PhylomeDB; P52410; -.
DR   BioCyc; ARA:AT5G46290-MON; -.
DR   BioCyc; MetaCyc:AT5G46290-MON; -.
DR   BRENDA; 2.3.1.41; 399.
DR   PRO; PR:P52410; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; P52410; baseline and differential.
DR   Genevisible; P52410; AT.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IBA:GO_Central.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
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   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; Alternative splicing; Chloroplast;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Plastid; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..46
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           47..473
FT                   /note="3-oxoacyl-[acyl-carrier-protein] synthase I,
FT                   chloroplastic"
FT                   /id="PRO_0000000586"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        224
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   VAR_SEQ         198..252
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_040746"
FT   CONFLICT        74
FT                   /note="F -> C (in Ref. 1; AAC49118)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        238..239
FT                   /note="IR -> NH (in Ref. 1; AAC49118)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   473 AA;  50413 MW;  38CA54382419411C CRC64;
     MQALQSSSLR ASPPNPLRLP SNRQSHQLIT NARPLRRQQR SFISASASTV SAPKRETDPK
     KRVVITGMGL VSVFGNDVDA YYEKLLSGES GISLIDRFDA SKFPTRFGGQ IRGFSSEGYI
     DGKNERRLDD CLKYCIVAGK KALESANLGG DKLNTIDKRK AGVLVGTGMG GLTVFSEGVQ
     NLIEKGHRRI SPFFIPYAIT NMGSALLAID LGLMGPNYSI STACATSNYC FYAAANHIRR
     GEADMMIAGG TEAAIIPIGL GGFVACRALS QRNDDPQTAS RPWDKARDGF VMGEGAGVLV
     MESLEHAMKR GAPIVAEYLG GAVNCDAHHM TDPRADGLGV SSCIERCLED AGVSPEEVNY
     INAHATSTLA GDLAEINAIK KVFKSTSGIK INATKSMIGH CLGAAGGLEA IATVKAINTG
     WLHPSINQFN PEQAVDFDTV PNEKKQHEVD VAISNSFGFG GHNSVVAFSA FKP
 
 
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