KCS13_ARATH
ID KCS13_ARATH Reviewed; 466 AA.
AC Q9ZUZ0; Q9FR50;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=3-ketoacyl-CoA synthase 13 {ECO:0000303|PubMed:18465198};
DE Short=KCS-13 {ECO:0000303|PubMed:18465198};
DE EC=2.3.1.199 {ECO:0000305};
DE AltName: Full=Protein HIGH CARBON DIOXIDE {ECO:0000303|PubMed:11130071};
DE AltName: Full=Very long-chain fatty acid condensing enzyme 13 {ECO:0000303|PubMed:18465198};
DE Short=VLCFA condensing enzyme 13 {ECO:0000303|PubMed:18465198};
DE Flags: Precursor;
GN Name=HIC {ECO:0000303|PubMed:11130071};
GN Synonyms=KCS13 {ECO:0000303|PubMed:18465198};
GN OrderedLocusNames=At2g46720 {ECO:0000312|Araport:AT2G46720};
GN ORFNames=T3A4.10 {ECO:0000312|EMBL:AAC69929.1};
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 [GENOMIC DNA / MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. C24, and cv. Columbia;
RX PubMed=11130071; DOI=10.1038/35047071;
RA Gray J.E., Holroyd G.H., van der Lee F.M., Bahrami A.R., Sijmons P.C.,
RA Woodward F.I., Schuch W., Hetherington A.M.;
RT "The HIC signalling pathway links CO2 perception to stomatal development.";
RL Nature 408:713-716(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 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, 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 -!- FUNCTION: Contributes to cuticular wax and suberin biosynthesis (By
CC similarity). Regulates negatively the stomatal development in elevated
CC CO(2) conditions. {ECO:0000250, ECO:0000269|PubMed:11130071}.
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 and 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}.
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DR EMBL; AF188484; AAG24644.1; -; mRNA.
DR EMBL; AF188485; AAG24645.1; -; Genomic_DNA.
DR EMBL; AC005819; AAC69929.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10745.1; -; Genomic_DNA.
DR PIR; D84906; D84906.
DR RefSeq; NP_182195.1; NM_130237.3.
DR AlphaFoldDB; Q9ZUZ0; -.
DR SMR; Q9ZUZ0; -.
DR STRING; 3702.AT2G46720.1; -.
DR PaxDb; Q9ZUZ0; -.
DR PRIDE; Q9ZUZ0; -.
DR ProteomicsDB; 247316; -.
DR EnsemblPlants; AT2G46720.1; AT2G46720.1; AT2G46720.
DR GeneID; 819284; -.
DR Gramene; AT2G46720.1; AT2G46720.1; AT2G46720.
DR KEGG; ath:AT2G46720; -.
DR Araport; AT2G46720; -.
DR TAIR; locus:2062775; AT2G46720.
DR eggNOG; ENOG502QPKZ; Eukaryota.
DR HOGENOM; CLU_013238_2_1_1; -.
DR InParanoid; Q9ZUZ0; -.
DR OMA; GDSIHKY; -.
DR OrthoDB; 801187at2759; -.
DR PhylomeDB; Q9ZUZ0; -.
DR BioCyc; ARA:AT2G46720-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q9ZUZ0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUZ0; baseline and differential.
DR Genevisible; Q9ZUZ0; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..466
FT /note="3-ketoacyl-CoA synthase 13"
FT /id="PRO_0000249105"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 52..341
FT /note="FAE"
FT /evidence="ECO:0000255"
FT ACT_SITE 196
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 275
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 359
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 363
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 392
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 396
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT CONFLICT 36
FT /note="F -> Y (in Ref. 1; AAG24644)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 52176 MW; CDE55A737A288D46 CRC64;
MFIAMADFKI LLLILILISL FELDLLHFHH DFFSPFPVKI GLLLISIFFY AYSTTRSKPV
YLVDFSCHQP TDSCKISSET FFNMAKGAQL YTDETIQFMT RILNRSGLGD DTYSPRCMLT
SPPTPSMYEA RHESELVIFG ALNSLFKKTG IEPREVGIFI VNCSLFNPNP SLSSMIVNRY
KLKTDVKTYN LSGMGCSAGA ISVDLATNLL KANPNTYAVI VSTENMTLSM YRGNDRSMLV
PNCLFRVGGA AVMLSNRSQD RVRSKYELTH IVRTHKGSSD KHYTCAEQKE DSKGIVGVAL
SKELTVVAGD SLKTNLTALG PLVLPLSEKL RFILFLVKSK LFRLKVSPYV PDFKLCFKHF
CIHAGGRALL DAVEKGLGLS EFDLEPSRMT LHRFGNTSSS SLWYELAYVE AKCRVKRGDR
VWQLAFGSGF KCNSIVWRAL RTIPANESLV GNPWGDSVHK YPVHVT
