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
