KCS14_ARATH
ID KCS14_ARATH Reviewed; 459 AA.
AC Q9SS39;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable 3-ketoacyl-CoA synthase 14 {ECO:0000303|PubMed:18465198};
DE Short=KCS-14 {ECO:0000303|PubMed:18465198};
DE EC=2.3.1.199 {ECO:0000305};
DE AltName: Full=Very long-chain fatty acid condensing enzyme 14 {ECO:0000303|PubMed:18465198};
DE Short=VLCFA condensing enzyme 14 {ECO:0000303|PubMed:18465198};
DE Flags: Precursor;
GN Name=KCS14 {ECO:0000303|PubMed:18465198};
GN OrderedLocusNames=At3g10280 {ECO:0000312|Araport:AT3G10280};
GN ORFNames=F14P13.12 {ECO:0000312|EMBL:AAF02814.1};
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 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 [4]
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}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in siliques.
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}.
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DR EMBL; AC009400; AAF02814.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74883.1; -; Genomic_DNA.
DR RefSeq; NP_187639.1; NM_111863.2.
DR AlphaFoldDB; Q9SS39; -.
DR STRING; 3702.AT3G10280.1; -.
DR PaxDb; Q9SS39; -.
DR PRIDE; Q9SS39; -.
DR ProteomicsDB; 230172; -.
DR EnsemblPlants; AT3G10280.1; AT3G10280.1; AT3G10280.
DR GeneID; 820190; -.
DR Gramene; AT3G10280.1; AT3G10280.1; AT3G10280.
DR KEGG; ath:AT3G10280; -.
DR Araport; AT3G10280; -.
DR TAIR; locus:2076254; AT3G10280.
DR eggNOG; ENOG502QPKZ; Eukaryota.
DR HOGENOM; CLU_013238_2_1_1; -.
DR InParanoid; Q9SS39; -.
DR OMA; ILLCAYS; -.
DR OrthoDB; 801187at2759; -.
DR PhylomeDB; Q9SS39; -.
DR BioCyc; ARA:AT3G10280-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9SS39; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SS39; baseline and differential.
DR Genevisible; Q9SS39; 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; 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; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..459
FT /note="Probable 3-ketoacyl-CoA synthase 14"
FT /id="PRO_0000249106"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 52..334
FT /note="FAE"
FT /evidence="ECO:0000255"
FT ACT_SITE 268
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 352
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 356
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 385
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 389
FT /evidence="ECO:0000250|UniProtKB:Q38860"
SQ SEQUENCE 459 AA; 51626 MW; 1307C2E49C34C509 CRC64;
MFIAMADFKL LLLILILLSL FELDLLHFHH DFFSPFPVKI GLLLISIFFY AYSTTRSKPV
YLVDFSCHQP TDSCKISSET FFNMAKGAQL YTEETIQFMT RILNRSGLGD DTYSPRCMLT
SPPTPSMYEA RHESELVIFG ALNSLFKKTG IEPREVGIFI VNCSLFNPNP SLSSMIVNRY
KLKTDVKTYN LSGISVDLAT NLLKANPNTY AVIVSTENMT LSMYRGNDRS MLVPNCLFRV
GGAAVMLSNR SQDRVRSKYE LTHIVRTHKG SSDKHYTCAE QKEDSKGIVG VALSKELTVV
AGDTLKTNLT ALGPLVLPLS EKLRFILFLV KSKLFRLKVS PYVPDFKLCF KHFCIHAGGR
ALLDAVEKGL GLSEFDLEPS RMTLHRFGNT SSSSLWYELA YVEAKCRVKR GDRVWQLAFG
SGFKCNSIVW RALRTIPANE SLVGNPWGDS VHKYPVHVT
