KCS1_ARATH
ID KCS1_ARATH Reviewed; 528 AA.
AC Q9MAM3; Q56YX9; Q9ZTK3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=3-ketoacyl-CoA synthase 1 {ECO:0000303|PubMed:10074711};
DE Short=KCS-1 {ECO:0000303|PubMed:10074711};
DE EC=2.3.1.199 {ECO:0000269|PubMed:10074711, ECO:0000269|PubMed:16765910};
DE AltName: Full=Very long-chain fatty acid condensing enzyme 1 {ECO:0000303|PubMed:10074711};
DE Short=VLCFA condensing enzyme 1 {ECO:0000303|PubMed:10074711};
GN Name=KCS1 {ECO:0000303|PubMed:10074711}; Synonyms=EL1;
GN OrderedLocusNames=At1g01120 {ECO:0000312|Araport:AT1G01120};
GN ORFNames=T25K16.11 {ECO:0000312|EMBL:AAF26470.1};
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=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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-528, FUNCTION, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=10074711; DOI=10.1046/j.1365-313x.1999.00352.x;
RA Todd J., Post-Beittenmiller D., Jaworski J.G.;
RT "KCS1 encodes a fatty acid elongase 3-ketoacyl-CoA synthase affecting wax
RT biosynthesis in Arabidopsis thaliana.";
RL Plant J. 17:119-130(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 400-528.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=15277688; DOI=10.1073/pnas.0404600101;
RA Trenkamp S., Martin W., Tietjen K.;
RT "Specific and differential inhibition of very-long-chain fatty acid
RT elongases from Arabidopsis thaliana by different herbicides.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11903-11908(2004).
RN [8]
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 [9]
RP GENE FAMILY, NOMENCLATURE, 3D-STRUCTURE MODELING, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND 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).
RN [10]
RP ACTIVITY REGULATION.
RX PubMed=22284369; DOI=10.1016/j.phytochem.2011.12.023;
RA Tresch S., Heilmann M., Christiansen N., Looser R., Grossmann K.;
RT "Inhibition of saturated very-long-chain fatty acid biosynthesis by
RT mefluidide and perfluidone, selective inhibitors of 3-ketoacyl-CoA
RT synthases.";
RL Phytochemistry 76:162-171(2012).
CC -!- FUNCTION: Contributes to cuticular wax and suberin biosynthesis.
CC Involved in both decarbonylation and acyl-reduction wax synthesis
CC pathways. Elongase condensing enzyme mostly active with saturated fatty
CC acids, especially with 16:0, 16:1, 18:0, and 20:0. Mediates the
CC synthesis of VLCFAs from 20 to 26 carbons in length (e.g. C20:1, C20,
CC C22, C24 and C26). {ECO:0000269|PubMed:10074711,
CC ECO:0000269|PubMed:15277688, 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:10074711,
CC ECO:0000269|PubMed:16765910};
CC -!- ACTIVITY REGULATION: Inhibited by K3 herbicides such as alachlor,
CC allidochlor, anilofos, cafenstrole, fentrazamide and flufenacet
CC (PubMed:15277688). Strongly inhibited by metazachlor and mefluidide
CC (PubMed:22284369). {ECO:0000269|PubMed:15277688,
CC ECO:0000269|PubMed:22284369}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18465198}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:10074711). Expressed in
CC siliques, flowers, leaves and stems. Barely detected in roots
CC (PubMed:18465198). {ECO:0000269|PubMed:10074711,
CC ECO:0000269|PubMed:18465198}.
CC -!- INDUCTION: Repressed by herbicides such as flufenacet and benfuresate
CC (PubMed:12916765). Down-regulated by darkness and low temperature, and
CC up-regulated by salt, drought and osmotic stress (PubMed:18465198).
CC {ECO:0000269|PubMed:12916765, ECO:0000269|PubMed:18465198}.
CC -!- DISRUPTION PHENOTYPE: Plants have thinner stems with an altered wax
CC composition, and are more sensitive to dehydration.
CC {ECO:0000269|PubMed:10074711}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD95286.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC007323; AAF26470.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27241.1; -; Genomic_DNA.
DR EMBL; AY074285; AAL66982.1; -; mRNA.
DR EMBL; AY096568; AAM20218.1; -; mRNA.
DR EMBL; AF053345; AAC99312.1; -; Genomic_DNA.
DR EMBL; AK221191; BAD95286.1; ALT_INIT; mRNA.
DR PIR; F86141; F86141.
DR RefSeq; NP_171620.2; NM_099994.4.
DR AlphaFoldDB; Q9MAM3; -.
DR SMR; Q9MAM3; -.
DR BioGRID; 24630; 7.
DR IntAct; Q9MAM3; 1.
DR STRING; 3702.AT1G01120.1; -.
DR ChEMBL; CHEMBL2242739; -.
DR iPTMnet; Q9MAM3; -.
DR PaxDb; Q9MAM3; -.
DR PRIDE; Q9MAM3; -.
DR ProteomicsDB; 230174; -.
DR EnsemblPlants; AT1G01120.1; AT1G01120.1; AT1G01120.
DR GeneID; 839395; -.
DR Gramene; AT1G01120.1; AT1G01120.1; AT1G01120.
DR KEGG; ath:AT1G01120; -.
DR Araport; AT1G01120; -.
DR TAIR; locus:2200955; AT1G01120.
DR eggNOG; ENOG502QPKZ; Eukaryota.
DR HOGENOM; CLU_013238_2_1_1; -.
DR InParanoid; Q9MAM3; -.
DR OMA; MEPSRCT; -.
DR OrthoDB; 801187at2759; -.
DR PhylomeDB; Q9MAM3; -.
DR BioCyc; ARA:AT1G01120-MON; -.
DR BioCyc; MetaCyc:AT1G01120-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9MAM3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MAM3; baseline and differential.
DR Genevisible; Q9MAM3; AT.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS:TAIR.
DR GO; GO:0009922; F:fatty acid elongase activity; IDA:TAIR.
DR GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0070417; P:cellular response to cold; IGI:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IMP:TAIR.
DR GO; GO:0010025; P:wax biosynthetic process; IDA: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; Endoplasmic reticulum; Membrane; NAD; NADP;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..528
FT /note="3-ketoacyl-CoA synthase 1"
FT /id="PRO_0000249093"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 114..403
FT /note="FAE"
FT /evidence="ECO:0000255"
FT ACT_SITE 258
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 337
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 421
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 425
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 454
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 458
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT CONFLICT 467
FT /note="E -> G (in Ref. 5; BAD95286)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 59276 MW; DEA6CBF18692A33B CRC64;
MERTNSIEMD RERLTAEMAF RDSSSAVIRI RRRLPDLLTS VKLKYVKLGL HNSCNVTTIL
FFLIILPLTG TVLVQLTGLT FDTFSELWSN QAVQLDTATR LTCLVFLSFV LTLYVANRSK
PVYLVDFSCY KPEDERKISV DSFLTMTEEN GSFTDDTVQF QQRISNRAGL GDETYLPRGI
TSTPPKLNMS EARAEAEAVM FGALDSLFEK TGIKPAEVGI LIVNCSLFNP TPSLSAMIVN
HYKMREDIKS YNLGGMGCSA GLISIDLANN LLKANPNSYA VVVSTENITL NWYFGNDRSM
LLCNCIFRMG GAAILLSNRR QDRKKSKYSL VNVVRTHKGS DDKNYNCVYQ KEDERGTIGV
SLARELMSVA GDALKTNITT LGPMVLPLSE QLMFLISLVK RKMFKLKVKP YIPDFKLAFE
HFCIHAGGRA VLDEVQKNLD LKDWHMEPSR MTLHRFGNTS SSSLWYEMAY TEAKGRVKAG
DRLWQIAFGS GFKCNSAVWK ALRPVSTEEM TGNAWAGSID QYPVKVVQ
