KASC2_ARATH
ID KASC2_ARATH Reviewed; 541 AA.
AC Q9C9P4; Q8RXF5; Q945N5; Q9SSG8;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase II, chloroplastic;
DE EC=2.3.1.41;
DE AltName: Full=Beta-ketoacyl-acyl-carrier-protein synthase II;
DE Short=AtKAS2;
DE Short=Beta-ketoacyl-ACP synthetase 2;
DE AltName: Full=Protein FATTY ACID BIOSYNTHESIS 1;
DE Flags: Precursor;
GN Name=KAS2; Synonyms=FAB1; OrderedLocusNames=At1g74960;
GN ORFNames=F25A4.7, F9E10.19;
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], FUNCTION, AND MUTAGENESIS OF LEU-337.
RC STRAIN=cv. Wassilewskija;
RX PubMed=12148534; DOI=10.1046/j.1365-313x.2002.01253.x;
RA Carlsson A.S., LaBrie S.T., Kinney A.J., von Wettstein-Knowles P.,
RA Browse J.;
RT "A KAS2 cDNA complements the phenotypes of the Arabidopsis fab1 mutant that
RT differs in a single residue bordering the substrate binding pocket.";
RL Plant J. 29:761-770(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
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 FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LEU-337.
RC STRAIN=cv. Columbia;
RX PubMed=12232312; DOI=10.1104/pp.106.1.143;
RA Wu J., James D.W. Jr., Dooner H.K., Browse J.;
RT "A Mutant of Arabidopsis Deficient in the Elongation of Palmitic Acid.";
RL Plant Physiol. 106:143-150(1994).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF LEU-337.
RC STRAIN=cv. Columbia;
RX PubMed=12242349; DOI=10.2307/3869834;
RA Wu J., Browse J.;
RT "Elevated levels of high-melting-point phosphatidylglycerols do not induce
RT chilling sensitivity in an Arabidopsis mutant.";
RL Plant Cell 7:17-27(1995).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF LEU-337.
RC STRAIN=cv. Columbia;
RX PubMed=9046588; DOI=10.1104/pp.113.2.347;
RA Wu J., Lightner J., Warwick N., Browse J.;
RT "Low-temperature damage and subsequent recovery of fab1 mutant Arabidopsis
RT exposed to 2 degrees C.";
RL Plant Physiol. 113:347-356(1997).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-337.
RX PubMed=17360594; DOI=10.1073/pnas.0611141104;
RA Pidkowich M.S., Nguyen H.T., Heilmann I., Ischebeck T., Shanklin J.;
RT "Modulating seed beta-ketoacyl-acyl carrier protein synthase II level
RT converts the composition of a temperate seed oil to that of a palm-like
RT tropical oil.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:4742-4747(2007).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=18506098; DOI=10.1266/ggs.83.143;
RA Hakozaki H., Park J.-I., Endo M., Takada Y., Kazama T., Takeda Y.,
RA Suzuki G., Kawagishi-Kobayashi M., Watanabe M.;
RT "Expression and developmental function of the 3-ketoacyl-ACP synthase2 gene
RT in Arabidopsis thaliana.";
RL Genes Genet. Syst. 83:143-152(2008).
RN [10]
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: Essential protein that catalyzes the condensation reaction of
CC fatty acid synthesis by the addition to an acyl acceptor of two carbons
CC from malonyl-ACP. Specific for elongation from C-16 and C-16 to
CC unsaturated C-18 fatty acids. Confers resistance to low temperatures by
CC maintaining chloroplast membranes integrity. Involved in the regulation
CC of fatty acids ratios during seed metabolism. Required for embryo
CC development, especially at the transition from the globular to the
CC heart stage. {ECO:0000269|PubMed:12148534, ECO:0000269|PubMed:12232312,
CC ECO:0000269|PubMed:12242349, ECO:0000269|PubMed:17360594,
CC ECO:0000269|PubMed:18506098, ECO:0000269|PubMed:9046588}.
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; Evidence={ECO:0000269|PubMed:12232312};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:18431481}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in siliques, and, to a lower
CC extent, in leaves, stems, flower buds, and flowers.
CC {ECO:0000269|PubMed:18506098}.
CC -!- DEVELOPMENTAL STAGE: First observed during the transition from the late
CC globular to the early heart embryo stages. Later observed during heart,
CC tropedo, and cotyledonary embryo stages. In seedlings, observed in the
CC shoot apex and stomatal guard cells. In adult plants, expressed in
CC inflorescences. In flowers, strongly present in styles and pollen
CC grains. {ECO:0000269|PubMed:18506098}.
CC -!- DISRUPTION PHENOTYPE: Lethal when homozygous due to embryo abortion
CC before the torpedo stage. Converts temperate oilseed composition (rich
CC in unsaturated 18-carbon fatty acids) to that of a palm-like tropical
CC oil (enriched in saturated 16-carbon fatty acids).
CC {ECO:0000269|PubMed:17360594, ECO:0000269|PubMed:18506098}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD55280.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAL06498.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL06498.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF318307; AAK69603.1; -; mRNA.
DR EMBL; AC008263; AAD55280.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC013258; AAG51920.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35655.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35656.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35657.1; -; Genomic_DNA.
DR EMBL; AF412045; AAL06498.1; ALT_FRAME; mRNA.
DR EMBL; AF419598; AAL31930.1; -; mRNA.
DR EMBL; AY054196; AAL06857.1; -; mRNA.
DR EMBL; AY081285; AAL91174.1; -; mRNA.
DR EMBL; AY097344; AAM19860.1; -; mRNA.
DR PIR; D96779; D96779.
DR RefSeq; NP_001185400.1; NM_001198471.1.
DR RefSeq; NP_565097.1; NM_106154.4.
DR RefSeq; NP_849888.1; NM_179557.4.
DR AlphaFoldDB; Q9C9P4; -.
DR SMR; Q9C9P4; -.
DR BioGRID; 29054; 1.
DR STRING; 3702.AT1G74960.2; -.
DR PaxDb; Q9C9P4; -.
DR PRIDE; Q9C9P4; -.
DR ProteomicsDB; 250617; -.
DR EnsemblPlants; AT1G74960.1; AT1G74960.1; AT1G74960.
DR EnsemblPlants; AT1G74960.2; AT1G74960.2; AT1G74960.
DR EnsemblPlants; AT1G74960.3; AT1G74960.3; AT1G74960.
DR GeneID; 843835; -.
DR Gramene; AT1G74960.1; AT1G74960.1; AT1G74960.
DR Gramene; AT1G74960.2; AT1G74960.2; AT1G74960.
DR Gramene; AT1G74960.3; AT1G74960.3; AT1G74960.
DR KEGG; ath:AT1G74960; -.
DR Araport; AT1G74960; -.
DR TAIR; locus:2027252; AT1G74960.
DR eggNOG; KOG1394; Eukaryota.
DR HOGENOM; CLU_000022_69_1_1; -.
DR InParanoid; Q9C9P4; -.
DR OMA; CEEYYKS; -.
DR OrthoDB; 1014523at2759; -.
DR PhylomeDB; Q9C9P4; -.
DR BioCyc; ARA:MON-14118; -.
DR BioCyc; MetaCyc:MON-14118; -.
DR BRENDA; 2.3.1.179; 399.
DR PRO; PR:Q9C9P4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9P4; baseline and differential.
DR Genevisible; Q9C9P4; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009536; C:plastid; ISS:TAIR.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IDA:TAIR.
DR GO; GO:0009631; P:cold acclimation; IMP:UniProtKB.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:TAIR.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; TAS:TAIR.
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; Chloroplast; Developmental protein;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Plastid; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..103
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 104..541
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase II,
FT chloroplastic"
FT /id="PRO_0000406094"
FT ACT_SITE 292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MUTAGEN 337
FT /note="L->F: In fab1; partial activity deficiency due to
FT structural instability and reduced substrate binding
FT affinity, resulting in increased levels of saturated 16:0
FT but reduced levels of 18:0 fatty acids, particularly in
FT chloroplasts, and associated with damage and death at
FT continuous low temperature (accompanied by chloroplast
FT degenerescence), but not after transient chilling or
FT freezing."
FT /evidence="ECO:0000269|PubMed:12148534,
FT ECO:0000269|PubMed:12232312, ECO:0000269|PubMed:12242349,
FT ECO:0000269|PubMed:17360594, ECO:0000269|PubMed:9046588"
FT CONFLICT 472
FT /note="A -> V (in Ref. 4; AAL91174)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 57600 MW; CB4F87E7B0C82189 CRC64;
MVGASSSYAS PLCTWFVAAC MSVSHGGGDS RQAVALQSGG RSRRRRQLSK CSVASGSASI
QALVTSCLDF GPCTHYNNNN ALSSLFGSNS VSLNRNQRRL NRAASSGGAM AVMEMEKEAA
VNKKPPTEQR RVVVTGMGVE TSLGHDPHTF YENLLQGNSG ISQIENFDCS EFPTRIAGEI
KSFSTEGWVA PKLSKRMDKF MLYLLTAGKK ALADGGVTDE VMAEFDKTKC GVLIGSAMGG
MKVFYDAIEA LRISYKKMNP FCVPFATTNM GSAMLAMDLG WMGPNYSIST ACATSNFCIL
NSANHIIKGE ADVMLCGGSD AVIIPIGLGG FVACRALSQR NNDPTKASRP WDTNRDGFVM
GEGAGVLLLE ELEHAKKRGA TIYAEFLGGS FTCDAYHMTE PHPDGAGVIL CIERALASAG
ISKEQINYIN AHATSTHAGD IKEYQALAHC FGQNPELKVN STKSMIGHLL GAAGAVEAVA
TVQAIRTGWV HPNINLENPD SGVDTKLLVG PKKERLDIKA ALSNSFGFGG HNSSIIFAPY
K
