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3-oxoacyl-[acyl-carrier-protein] synthase II, chloroplastic (EC 2.3.1.41) (Beta-ketoacyl-acyl-carrier-protein synthase II) (AtKAS2) (Beta-ketoacyl-ACP synthetase 2) (Protein FATTY ACID BIOSYNTHESIS 1)

 KASC2_ARATH             Reviewed;         541 AA.
Q9C9P4; Q8RXF5; Q945N5; Q9SSG8;
08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
28-MAR-2018, entry version 115.
RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase II, chloroplastic;
EC=2.3.1.41;
AltName: Full=Beta-ketoacyl-acyl-carrier-protein synthase II;
Short=AtKAS2;
Short=Beta-ketoacyl-ACP synthetase 2;
AltName: Full=Protein FATTY ACID BIOSYNTHESIS 1;
Flags: Precursor;
Name=KAS2; Synonyms=FAB1; OrderedLocusNames=At1g74960;
ORFNames=F25A4.7, F9E10.19;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF LEU-337.
STRAIN=cv. Wassilewskija;
PubMed=12148534; DOI=10.1046/j.1365-313X.2002.01253.x;
Carlsson A.S., LaBrie S.T., Kinney A.J., von Wettstein-Knowles P.,
Browse J.;
"A KAS2 cDNA complements the phenotypes of the Arabidopsis fab1 mutant
that differs in a single residue bordering the substrate binding
pocket.";
Plant J. 29:761-770(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LEU-337.
STRAIN=cv. Columbia;
PubMed=12232312; DOI=10.1104/pp.106.1.143;
Wu J., James D.W. Jr., Dooner H.K., Browse J.;
"A Mutant of Arabidopsis Deficient in the Elongation of Palmitic
Acid.";
Plant Physiol. 106:143-150(1994).
[6]
FUNCTION, AND MUTAGENESIS OF LEU-337.
STRAIN=cv. Columbia;
PubMed=12242349; DOI=10.1105/tpc.7.1.17;
Wu J., Browse J.;
"Elevated levels of high-melting-point phosphatidylglycerols do not
induce chilling sensitivity in an Arabidopsis mutant.";
Plant Cell 7:17-27(1995).
[7]
FUNCTION, AND MUTAGENESIS OF LEU-337.
STRAIN=cv. Columbia;
PubMed=9046588; DOI=10.1104/pp.113.2.347;
Wu J., Lightner J., Warwick N., Browse J.;
"Low-temperature damage and subsequent recovery of fab1 mutant
Arabidopsis exposed to 2 degrees C.";
Plant Physiol. 113:347-356(1997).
[8]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-337.
PubMed=17360594; DOI=10.1073/pnas.0611141104;
Pidkowich M.S., Nguyen H.T., Heilmann I., Ischebeck T., Shanklin J.;
"Modulating seed beta-ketoacyl-acyl carrier protein synthase II level
converts the composition of a temperate seed oil to that of a palm-
like tropical oil.";
Proc. Natl. Acad. Sci. U.S.A. 104:4742-4747(2007).
[9]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
STRAIN=cv. Columbia;
PubMed=18506098; DOI=10.1266/ggs.83.143;
Hakozaki H., Park J.-I., Endo M., Takada Y., Kazama T., Takeda Y.,
Suzuki G., Kawagishi-Kobayashi M., Watanabe M.;
"Expression and developmental function of the 3-ketoacyl-ACP synthase2
gene in Arabidopsis thaliana.";
Genes Genet. Syst. 83:143-152(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
PubMed=18431481; DOI=10.1371/journal.pone.0001994;
Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O.,
Sun Q., van Wijk K.J.;
"Sorting signals, N-terminal modifications and abundance of the
chloroplast proteome.";
PLoS ONE 3:E1994-E1994(2008).
-!- FUNCTION: Essential protein that catalyzes the condensation
reaction of fatty acid synthesis by the addition to an acyl
acceptor of two carbons from malonyl-ACP. Specific for elongation
from C-16 and C-16 to unsaturated C-18 fatty acids. Confers
resistance to low temperatures by maintaining chloroplast
membranes integrity. Involved in the regulation of fatty acids
ratios during seed metabolism. Required for embryo development,
especially at the transition from the globular to the heart stage.
{ECO:0000269|PubMed:12148534, ECO:0000269|PubMed:12232312,
ECO:0000269|PubMed:12242349, ECO:0000269|PubMed:17360594,
ECO:0000269|PubMed:18506098, ECO:0000269|PubMed:9046588}.
-!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + malonyl-[acyl-
carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) +
[acyl-carrier-protein]. {ECO:0000269|PubMed:12232312}.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
{ECO:0000269|PubMed:18431481}.
-!- TISSUE SPECIFICITY: Mostly expressed in siliques, and, to a lower
extent, in leaves, stems, flower buds, and flowers.
{ECO:0000269|PubMed:18506098}.
-!- DEVELOPMENTAL STAGE: First observed during the transition from the
late globular to the early heart embryo stages. Later observed
during heart, tropedo, and cotyledonary embryo stages. In
seedlings, observed in the shoot apex and stomatal guard cells. In
adult plants, expressed in inflorescences. In flowers, strongly
present in styles and pollen grains.
{ECO:0000269|PubMed:18506098}.
-!- DISRUPTION PHENOTYPE: Lethal when homozygous due to embryo
abortion before the torpedo stage. Converts temperate oilseed
composition (rich in unsaturated 18-carbon fatty acids) to that of
a palm-like tropical oil (enriched in saturated 16-carbon fatty
acids). {ECO:0000269|PubMed:17360594,
ECO:0000269|PubMed:18506098}.
-!- SIMILARITY: Belongs to the beta-ketoacyl-ACP synthases family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD55280.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAL06498.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAL06498.1; Type=Frameshift; Positions=38, 328; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF318307; AAK69603.1; -; mRNA.
EMBL; AC008263; AAD55280.1; ALT_SEQ; Genomic_DNA.
EMBL; AC013258; AAG51920.1; -; Genomic_DNA.
EMBL; CP002684; AEE35655.1; -; Genomic_DNA.
EMBL; CP002684; AEE35656.1; -; Genomic_DNA.
EMBL; CP002684; AEE35657.1; -; Genomic_DNA.
EMBL; AF412045; AAL06498.1; ALT_FRAME; mRNA.
EMBL; AF419598; AAL31930.1; -; mRNA.
EMBL; AY054196; AAL06857.1; -; mRNA.
EMBL; AY081285; AAL91174.1; -; mRNA.
EMBL; AY097344; AAM19860.1; -; mRNA.
PIR; D96779; D96779.
RefSeq; NP_001185400.1; NM_001198471.1.
RefSeq; NP_565097.1; NM_106154.4.
RefSeq; NP_849888.1; NM_179557.4.
UniGene; At.26097; -.
ProteinModelPortal; Q9C9P4; -.
SMR; Q9C9P4; -.
BioGrid; 29054; 1.
STRING; 3702.AT1G74960.1; -.
PaxDb; Q9C9P4; -.
PRIDE; Q9C9P4; -.
EnsemblPlants; AT1G74960.1; AT1G74960.1; AT1G74960.
EnsemblPlants; AT1G74960.2; AT1G74960.2; AT1G74960.
EnsemblPlants; AT1G74960.3; AT1G74960.3; AT1G74960.
GeneID; 843835; -.
Gramene; AT1G74960.1; AT1G74960.1; AT1G74960.
Gramene; AT1G74960.2; AT1G74960.2; AT1G74960.
Gramene; AT1G74960.3; AT1G74960.3; AT1G74960.
KEGG; ath:AT1G74960; -.
Araport; AT1G74960; -.
TAIR; locus:2027252; AT1G74960.
eggNOG; KOG1394; Eukaryota.
eggNOG; COG0304; LUCA.
HOGENOM; HOG000060166; -.
InParanoid; Q9C9P4; -.
KO; K09458; -.
OMA; EACMNIV; -.
OrthoDB; EOG093609PY; -.
PhylomeDB; Q9C9P4; -.
BioCyc; ARA:AT1G74960-MONOMER; -.
BioCyc; ARA:GQT-1583-MONOMER; -.
BioCyc; ARA:MONOMER-14118; -.
BioCyc; MetaCyc:MONOMER-14118; -.
BRENDA; 2.3.1.179; 399.
PRO; PR:Q9C9P4; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9C9P4; baseline and differential.
Genevisible; Q9C9P4; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0009536; C:plastid; ISS:TAIR.
GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IDA:TAIR.
GO; GO:0009631; P:cold acclimation; IMP:UniProtKB.
GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
GO; GO:0006633; P:fatty acid biosynthetic process; IDA:TAIR.
GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; TAS:TAIR.
Gene3D; 3.40.47.10; -; 2.
InterPro; IPR017568; 3-oxoacyl-ACP_synth-2.
InterPro; IPR018201; Ketoacyl_synth_AS.
InterPro; IPR014031; Ketoacyl_synth_C.
InterPro; IPR014030; Ketoacyl_synth_N.
InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
InterPro; IPR016039; Thiolase-like.
Pfam; PF00109; ketoacyl-synt; 1.
Pfam; PF02801; Ketoacyl-synt_C; 1.
SMART; SM00825; PKS_KS; 1.
SUPFAM; SSF53901; SSF53901; 2.
TIGRFAMs; TIGR03150; fabF; 1.
PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
1: Evidence at protein level;
Acyltransferase; Chloroplast; Complete proteome;
Developmental protein; Fatty acid biosynthesis; Fatty acid metabolism;
Lipid biosynthesis; Lipid metabolism; Plastid; Reference proteome;
Transferase; Transit peptide.
TRANSIT 1 103 Chloroplast. {ECO:0000255}.
CHAIN 104 541 3-oxoacyl-[acyl-carrier-protein] synthase
II, chloroplastic.
/FTId=PRO_0000406094.
ACT_SITE 292 292 {ECO:0000255|PROSITE-ProRule:PRU10022}.
MUTAGEN 337 337 L->F: In fab1; partial activity
deficience due to structural instability
and reduced substrate binding affinity,
resulting in increased levels of
saturated 16:0 but reduced levels of 18:0
fatty acids, particularly in
chloroplasts, and associated with damage
and death at continuous low temperature
(accompanied by chloroplast
degenerescence), but not after transient
chilling or freezing.
{ECO:0000269|PubMed:12148534,
ECO:0000269|PubMed:12232312,
ECO:0000269|PubMed:12242349,
ECO:0000269|PubMed:17360594,
ECO:0000269|PubMed:9046588}.
CONFLICT 472 472 A -> V (in Ref. 4; AAL91174).
{ECO:0000305}.
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


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