KCS5_ARATH
ID KCS5_ARATH Reviewed; 492 AA.
AC Q9C6L5; Q84W57; Q8L8L0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=3-ketoacyl-CoA synthase 5 {ECO:0000303|PubMed:18465198};
DE Short=KCS-5 {ECO:0000303|PubMed:18465198};
DE EC=2.3.1.199 {ECO:0000305};
DE AltName: Full=Eceriferum 60 {ECO:0000303|PubMed:11041893};
DE AltName: Full=Very long-chain fatty acid condensing enzyme 5 {ECO:0000303|PubMed:18465198};
DE Short=VLCFA condensing enzyme 5 {ECO:0000303|PubMed:18465198};
GN Name=KCS5 {ECO:0000303|PubMed:18465198};
GN Synonyms=CER60 {ECO:0000303|PubMed:11041893};
GN OrderedLocusNames=At1g25450 {ECO:0000312|Araport:AT1G25450};
GN ORFNames=F2J7.9 {ECO:0000312|EMBL:AAG50800.1};
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 [MRNA].
RX PubMed=11041893; DOI=10.2307/3871209;
RA Fiebig A., Mayfield J.A., Miley N.L., Chau S., Fischer R.L., Preuss D.;
RT "Alterations in CER6, a gene identical to CUT1, differentially affect long-
RT chain lipid content on the surface of pollen and stems.";
RL Plant Cell 12:2001-2008(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) 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, SUBCELLULAR LOCATION, 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 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).
RN [9]
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: Mediates mostly the synthesis of VLCFAs from 26 to 30 carbons
CC in length (e.g. C20:1, C26, C28, C30). {ECO:0000269|PubMed:15277688}.
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 -!- ACTIVITY REGULATION: Inhibited by K3 herbicides such as alachlor,
CC allidochlor, anilofos, cafenstrole and flufenacet (PubMed:15277688).
CC Strongly inhibited by metazachlor and mefluidide (PubMed:22284369).
CC {ECO:0000269|PubMed:15277688, ECO:0000269|PubMed:22284369}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15277688}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:15277688}.
CC -!- TISSUE SPECIFICITY: Expressed in siliques, flowers, leaves and
CC seedlings. {ECO:0000269|PubMed:18465198}.
CC -!- INDUCTION: Repressed by herbicides such as flufenacet and benfuresate
CC (PubMed:12916765). Down-regulated by darkness, low temperature, salt,
CC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC079281; AAG50800.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30626.1; -; Genomic_DNA.
DR EMBL; BT004205; AAO42223.1; -; mRNA.
DR EMBL; AY088928; AAM67234.1; -; mRNA.
DR PIR; F86384; F86384.
DR RefSeq; NP_173916.1; NM_102356.4.
DR AlphaFoldDB; Q9C6L5; -.
DR SMR; Q9C6L5; -.
DR BioGRID; 24368; 1.
DR STRING; 3702.AT1G25450.1; -.
DR ChEMBL; CHEMBL2242737; -.
DR PaxDb; Q9C6L5; -.
DR PRIDE; Q9C6L5; -.
DR ProteomicsDB; 247273; -.
DR EnsemblPlants; AT1G25450.1; AT1G25450.1; AT1G25450.
DR GeneID; 839131; -.
DR Gramene; AT1G25450.1; AT1G25450.1; AT1G25450.
DR KEGG; ath:AT1G25450; -.
DR Araport; AT1G25450; -.
DR TAIR; locus:2031260; AT1G25450.
DR eggNOG; ENOG502QPKZ; Eukaryota.
DR HOGENOM; CLU_013238_2_2_1; -.
DR InParanoid; Q9C6L5; -.
DR OMA; WKSNRTI; -.
DR OrthoDB; 801187at2759; -.
DR PhylomeDB; Q9C6L5; -.
DR BioCyc; ARA:AT1G25450-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9C6L5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C6L5; baseline and differential.
DR Genevisible; Q9C6L5; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0048868; P:pollen tube development; IMP:TAIR.
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 2: Evidence at transcript level;
KW Acyltransferase; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..492
FT /note="3-ketoacyl-CoA synthase 5"
FT /id="PRO_0000249097"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 76..365
FT /note="FAE"
FT /evidence="ECO:0000255"
FT ACT_SITE 220
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 299
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 383
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 387
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 416
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 420
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT CONFLICT 232
FT /note="D -> N (in Ref. 5; AAM67234)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="F -> S (in Ref. 4; AAO42223)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 55653 MW; 42D21D34E4A0DDEC CRC64;
MSDFSSSVKL KYVKLGYQYL INNFLTLLLI PVIATVAIEL LRMGPEEILS VLNSLHFELL
HILCSSFLII FVSTVYFMSK PRTVYLVDYS CYKPPVTCRV PFSSFMEHSR LILKDNPKSV
EFQMRILERS GLGEETCLPP AIHYIPPTPT MESARNEAQM VIFTAMEDLF KNTGLKPKDI
DILIVNCSLF SPTPSLSAMI INKYKLRSNI KSYNLSGMGC SASLISVDVA RDLLQVHPNS
NAIIISTEII TPNYYKGNER AMLLPNCLFR MGGAAILLSN RRSDRWRAKY KLCHLVRTHR
GADDKSYNCV MEQEDKNGNV GINLSKDLMT IAGEALKANI TTIGPLVLPA SEQLLFLSSL
IGRKIFNPKW KPYIPDFKQA FEHFCIHAGG RAVIDELQKN LQLSGEHVEA SRMTLHRFGN
TSSSSLWYEL SYIEAQGRMK RNDRVWQIAF GSGFKCNSAV WKCNRTIKTP TDGAWSDCIE
RYPVFIPEVV KL
