KCS15_ARATH
ID KCS15_ARATH Reviewed; 451 AA.
AC Q9SUY9; Q8LFQ2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=3-ketoacyl-CoA synthase 15 {ECO:0000303|PubMed:18465198};
DE Short=KCS-15 {ECO:0000303|PubMed:18465198};
DE EC=2.3.1.199 {ECO:0000305};
DE AltName: Full=Very long-chain fatty acid condensing enzyme 15 {ECO:0000303|PubMed:18465198};
DE Short=VLCFA condensing enzyme 15 {ECO:0000303|PubMed:18465198};
GN Name=KCS15 {ECO:0000303|PubMed:18465198};
GN OrderedLocusNames=At3g52160 {ECO:0000312|Araport:AT3G52160};
GN ORFNames=F4F15.270 {ECO:0000312|EMBL:CAB41336.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-451.
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 [5]
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 [6]
RP GENE FAMILY, NOMENCLATURE, 3D-STRUCTURE MODELING, AND TISSUE SPECIFICITY.
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: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers.
CC {ECO:0000269|PubMed:18465198}.
CC -!- INDUCTION: Repressed by herbicides such as flufenacet and benfuresate.
CC {ECO:0000269|PubMed:12916765}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM61287.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ446759; ABE66011.1; -; mRNA.
DR EMBL; AL049711; CAB41336.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78906.1; -; Genomic_DNA.
DR EMBL; AY084713; AAM61287.1; ALT_INIT; mRNA.
DR PIR; T49095; T49095.
DR RefSeq; NP_190784.1; NM_115076.4.
DR AlphaFoldDB; Q9SUY9; -.
DR SMR; Q9SUY9; -.
DR BioGRID; 9699; 5.
DR IntAct; Q9SUY9; 5.
DR STRING; 3702.AT3G52160.1; -.
DR PaxDb; Q9SUY9; -.
DR PRIDE; Q9SUY9; -.
DR EnsemblPlants; AT3G52160.1; AT3G52160.1; AT3G52160.
DR GeneID; 824381; -.
DR Gramene; AT3G52160.1; AT3G52160.1; AT3G52160.
DR KEGG; ath:AT3G52160; -.
DR Araport; AT3G52160; -.
DR TAIR; locus:2083825; AT3G52160.
DR eggNOG; ENOG502QV8E; Eukaryota.
DR HOGENOM; CLU_013238_2_1_1; -.
DR InParanoid; Q9SUY9; -.
DR OrthoDB; 801187at2759; -.
DR PhylomeDB; Q9SUY9; -.
DR BioCyc; ARA:AT3G52160-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9SUY9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SUY9; baseline and differential.
DR Genevisible; Q9SUY9; 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 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; 2.
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..451
FT /note="3-ketoacyl-CoA synthase 15"
FT /id="PRO_0000249107"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 82..366
FT /note="FAE"
FT /evidence="ECO:0000255"
FT ACT_SITE 224
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 303
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 356
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 393
FT /evidence="ECO:0000250|UniProtKB:Q38860"
SQ SEQUENCE 451 AA; 51109 MW; 008254970E11E40F CRC64;
MEKEATKMVN GGVKSKSPKG SPDFLGYNLR YVKLGYIYLL SLSRTFCFFL PPLLLLFIFV
SRFLPILAFP LSTFFILLIY HYLTPSSVFL LDFSCYRPPD HLKITKSDFI ELAMKSGNFN
ETAIELQRKV LDQSGIGEES YMPRVVFKPG HRVNLRDGRE EAAMVIFGAI DELLAATKIN
VKHIKILVLN CGVLNTTPSL SAMVINHYKL RHNTESYNLG GMGCSAGVIA IDLAKDLLNA
HQGSYALVVS TEIVSFTWYS GNDVALLPPN CFFRMGAAAV MLSSRRIDRW RAKYQLMQLV
RTHKGMEDTS YKSIELREDR DGKQGLYVSR DVMEVGRHAL KANIATLGRL EPSFEHICVL
ASSKKVLDDI HKDLKLTEEN MEASRRTLER FGNTSSSSIW YELAYLEHKA KMKRGDRVWQ
IGFGSGFKCN SVVWKALKNI DPPRHNNPWN L
