KCS11_ARATH
ID KCS11_ARATH Reviewed; 509 AA.
AC O48780;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=3-ketoacyl-CoA synthase 11 {ECO:0000303|PubMed:18465198};
DE Short=KCS-11 {ECO:0000303|PubMed:18465198};
DE EC=2.3.1.199 {ECO:0000269|PubMed:16765910};
DE AltName: Full=Very long-chain fatty acid condensing enzyme 11 {ECO:0000303|PubMed:18465198};
DE Short=VLCFA condensing enzyme 11 {ECO:0000303|PubMed:18465198};
GN Name=KCS11 {ECO:0000303|PubMed:18465198};
GN OrderedLocusNames=At2g26640 {ECO:0000312|Araport:AT2G26640};
GN ORFNames=F18A8.1 {ECO:0000312|EMBL:AAB95298.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
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 [4]
RP INDUCTION, AND GENE FAMILY.
RX PubMed=12916765; DOI=10.1002/ps.714;
RA Lechelt-Kunze C., Meissner R.C., Drewes M., Tietjen K.;
RT "Flufenacet herbicide treatment phenocopies the fiddlehead mutant in
RT Arabidopsis thaliana.";
RL Pest Manag. Sci. 59:847-856(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=16765910; DOI=10.1016/j.bbrc.2006.05.162;
RA Blacklock B.J., Jaworski J.G.;
RT "Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases.";
RL Biochem. Biophys. Res. Commun. 346:583-590(2006).
RN [6]
RP GENE FAMILY, NOMENCLATURE, 3D-STRUCTURE MODELING, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=18465198; DOI=10.1007/s11103-008-9339-z;
RA Joubes J., Raffaele S., Bourdenx B., Garcia C., Laroche-Traineau J.,
RA Moreau P., Domergue F., Lessire R.;
RT "The VLCFA elongase gene family in Arabidopsis thaliana: phylogenetic
RT analysis, 3D modelling and expression profiling.";
RL Plant Mol. Biol. 67:547-566(2008).
CC -!- FUNCTION: Active on both saturated and mono-unsaturated acyl chains C16
CC to C20. {ECO:0000269|PubMed:16765910}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-
CC chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736;
CC EC=2.3.1.199; Evidence={ECO:0000269|PubMed:16765910};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Only expressed in guard cells. Expressed in
CC siliques, flowers, leaves, stems, roots and seedlings
CC (PubMed:18465198). {ECO:0000269|PubMed:18465198}.
CC -!- INDUCTION: Repressed by herbicides such as flufenacet and benfuresate
CC (PubMed:12916765). Down-regulated by darkness and low temperature
CC (PubMed:18465198). {ECO:0000269|PubMed:12916765,
CC ECO:0000269|PubMed:18465198}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; AC003105; AAB95298.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07869.1; -; Genomic_DNA.
DR EMBL; BT003854; AAO41904.1; -; mRNA.
DR EMBL; BT005692; AAO64112.1; -; mRNA.
DR PIR; A84663; A84663.
DR RefSeq; NP_180232.1; NM_128221.6.
DR AlphaFoldDB; O48780; -.
DR SMR; O48780; -.
DR BioGRID; 2557; 1.
DR IntAct; O48780; 1.
DR STRING; 3702.AT2G26640.1; -.
DR PaxDb; O48780; -.
DR PRIDE; O48780; -.
DR ProteomicsDB; 247239; -.
DR EnsemblPlants; AT2G26640.1; AT2G26640.1; AT2G26640.
DR GeneID; 817205; -.
DR Gramene; AT2G26640.1; AT2G26640.1; AT2G26640.
DR KEGG; ath:AT2G26640; -.
DR Araport; AT2G26640; -.
DR TAIR; locus:2043849; AT2G26640.
DR eggNOG; ENOG502QPKZ; Eukaryota.
DR HOGENOM; CLU_013238_2_1_1; -.
DR InParanoid; O48780; -.
DR OMA; DIWEHLQ; -.
DR OrthoDB; 801187at2759; -.
DR PhylomeDB; O48780; -.
DR BioCyc; ARA:AT2G26640-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:O48780; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48780; baseline and differential.
DR Genevisible; O48780; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR012392; 3-ktacl-CoA_syn.
DR InterPro; IPR013747; ACP_syn_III_C.
DR InterPro; IPR013601; FAE1_typ3_polyketide_synth.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR31561; PTHR31561; 1.
DR Pfam; PF08541; ACP_syn_III_C; 1.
DR Pfam; PF08392; FAE1_CUT1_RppA; 1.
DR PIRSF; PIRSF036417; 3-ktacl-CoA_syn; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
PE 1: Evidence at protein level;
KW Acyltransferase; Membrane; NAD; NADP; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..509
FT /note="3-ketoacyl-CoA synthase 11"
FT /id="PRO_0000249103"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 92..381
FT /note="FAE"
FT /evidence="ECO:0000255"
FT ACT_SITE 236
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 315
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 399
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 403
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 436
FT /evidence="ECO:0000250|UniProtKB:Q38860"
SQ SEQUENCE 509 AA; 57815 MW; DB922BCB2B33662F CRC64;
MDVEQKKPLI ESSDRNLPDF KKSVKLKYVK LGYHYLITHG MYLFLSPLVL VIAAQISTFS
VTDLRSLWEH LQYNLISVVV CSMLLVFLMT IYFMTRPRPV YLVNFSCFKP DESRKCTKKI
FMDRSKLTGS FTEENLEFQR KILQRSGLGE STYLPEAVLN VPPNPCMKEA RKEAETVMFG
AIDELLAKTN VNPKDIGILI VNCSLFNPTP SLSAMVVNHY KLRGNILSYN LGGMGCSAGL
ISIDLAKHLL HSIPNTYAMV ISMENITLNW YFGNDRSKLV SNCLFRMGGA AILLSNKRWD
RRRSKYELVD TVRTHKGADD KCFGCITQEE DSASKIGVTL SKELMAVAGD ALKTNITTLG
PLVLPTSEQL LFFATLVGRK LFKMKIKPYI PDFKLAFEHF CIHAGGRAVL DELEKNLKLT
EWHMEPSRMT LYRFGNTSSS SLWYELAYSE AKGRIKKGDR IWQIAFGSGF KCNSSVWRAV
RSVNPKKEKN PWMDEIHEFP VEVPKVSTI
