KCS3_ARATH
ID KCS3_ARATH Reviewed; 478 AA.
AC Q9LQP8;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=3-ketoacyl-CoA synthase 3 {ECO:0000303|PubMed:18465198};
DE Short=KCS-3 {ECO:0000303|PubMed:18465198};
DE EC=2.3.1.199 {ECO:0000305};
DE AltName: Full=Very long-chain fatty acid condensing enzyme 3 {ECO:0000303|PubMed:18465198};
DE Short=VLCFA condensing enzyme 3 {ECO:0000303|PubMed:18465198};
DE Flags: Precursor;
GN Name=KCS3 {ECO:0000303|PubMed:18465198};
GN OrderedLocusNames=At1g07720 {ECO:0000312|Araport:AT1G07720};
GN ORFNames=F24B9.18 {ECO:0000312|EMBL:AAF75082.1};
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 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 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).
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:0000305};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:18465198}.
CC -!- TISSUE SPECIFICITY: Expressed in siliques, leaves, stems and seedlings.
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 -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
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DR EMBL; AC007583; AAF75082.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28169.1; -; Genomic_DNA.
DR EMBL; AF428349; AAL16279.1; -; mRNA.
DR EMBL; AY062700; AAL32778.1; -; mRNA.
DR EMBL; AY128794; AAM91194.1; -; mRNA.
DR PIR; D86212; D86212.
DR RefSeq; NP_172251.1; NM_100646.3.
DR AlphaFoldDB; Q9LQP8; -.
DR SMR; Q9LQP8; -.
DR STRING; 3702.AT1G07720.1; -.
DR PaxDb; Q9LQP8; -.
DR ProteomicsDB; 230176; -.
DR EnsemblPlants; AT1G07720.1; AT1G07720.1; AT1G07720.
DR GeneID; 837286; -.
DR Gramene; AT1G07720.1; AT1G07720.1; AT1G07720.
DR KEGG; ath:AT1G07720; -.
DR Araport; AT1G07720; -.
DR TAIR; locus:2026600; AT1G07720.
DR eggNOG; ENOG502QPV6; Eukaryota.
DR HOGENOM; CLU_013238_3_1_1; -.
DR InParanoid; Q9LQP8; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9LQP8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQP8; baseline and differential.
DR Genevisible; Q9LQP8; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Reference proteome; Signal;
KW Transferase.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..478
FT /note="3-ketoacyl-CoA synthase 3"
FT /id="PRO_0000249095"
FT DOMAIN 26..313
FT /note="FAE"
FT /evidence="ECO:0000255"
FT ACT_SITE 168
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 247
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 345
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 349
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 378
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 382
FT /evidence="ECO:0000250|UniProtKB:Q38860"
SQ SEQUENCE 478 AA; 54335 MW; A6EB0BE5C305D809 CRC64;
MDLLVMLLSL LVSYLIFKIW KRIDSKRDQN CYILDYQCHK PSDDRMVNTQ FSGDIILRNK
HLRLNEYKFL LKAIVSSGIG EQTYAPRLFF EGREQRPTLQ DGLSEMEEFY IDTIEKVLKR
NKISPSEIDI LVVNVSMLNS TPSLSARIIN HYKMREDIKV FNLTAMGCSA SVISIDIVKN
IFKTYKNKLA LVVTSESLSP NWYSGNNRSM ILANCLFRSG GCAVLLTNKR SLSRRAMFKL
RCLVRTHHGA RDDSFNACVQ KEDELGHIGV HLDKTLPKAA TRAFIDNLKV ITPKILPVTE
LLRFMLCLLL KKLRSSPSKG STNVTQAAPK AGVKAGINFK TGIDHFCIHT GGKAVIDAIG
YSLDLNEYDL EPARMTLHRF GNTSASSLWY VLGYMEAKKR LKRGDRVFMI SFGAGFKCNS
CVWEVVRDLN VGEAVGNVWN HCINQYPPKS ILNPFFEKYG WIHEEEDPDT FKMPEGFM
