KCS17_ARATH
ID KCS17_ARATH Reviewed; 487 AA.
AC O65677;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=3-ketoacyl-CoA synthase 17 {ECO:0000303|PubMed:18465198};
DE Short=KCS-17 {ECO:0000303|PubMed:18465198};
DE EC=2.3.1.199 {ECO:0000269|PubMed:16765910};
DE AltName: Full=Very long-chain fatty acid condensing enzyme 17 {ECO:0000303|PubMed:18465198};
DE Short=VLCFA condensing enzyme 17 {ECO:0000303|PubMed:18465198};
GN Name=KCS17 {ECO:0000303|PubMed:18465198};
GN Synonyms=KCS2 {ECO:0000303|PubMed:12916765};
GN OrderedLocusNames=At4g34510 {ECO:0000312|Araport:AT4G34510};
GN ORFNames=T4L20.90 {ECO:0000312|EMBL:CAA18830.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 FUNCTION, 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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=16765910; DOI=10.1016/j.bbrc.2006.05.162;
RA Blacklock B.J., Jaworski J.G.;
RT "Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases.";
RL Biochem. Biophys. Res. Commun. 346:583-590(2006).
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).
RN [7]
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: Active on saturated acyl-CoAs up to C22. Mediates the
CC synthesis of VLCFAs from 20 to 26 carbons in length (e.g. C20:1, C20,
CC C24, C26). {ECO:0000269|PubMed:15277688, ECO:0000269|PubMed:16765910}.
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:0000269|PubMed:16765910};
CC -!- ACTIVITY REGULATION: Inhibited by K3 herbicides such as alachlor,
CC allidochlor, anilofos, cafenstrole, fentrazamide and flufenacet
CC (PubMed:15277688). Strongly inhibited by metazachlor (PubMed:22284369).
CC {ECO:0000269|PubMed:15277688, ECO:0000269|PubMed:22284369}.
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}.
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DR EMBL; AL023094; CAA18830.1; -; Genomic_DNA.
DR EMBL; AL161585; CAB80168.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86387.1; -; Genomic_DNA.
DR PIR; T05271; T05271.
DR RefSeq; NP_195177.1; NM_119616.3.
DR AlphaFoldDB; O65677; -.
DR SMR; O65677; -.
DR STRING; 3702.AT4G34510.1; -.
DR ChEMBL; CHEMBL2242738; -.
DR PaxDb; O65677; -.
DR PRIDE; O65677; -.
DR ProteomicsDB; 247269; -.
DR EnsemblPlants; AT4G34510.1; AT4G34510.1; AT4G34510.
DR GeneID; 829602; -.
DR Gramene; AT4G34510.1; AT4G34510.1; AT4G34510.
DR KEGG; ath:AT4G34510; -.
DR Araport; AT4G34510; -.
DR TAIR; locus:2139579; AT4G34510.
DR eggNOG; ENOG502QPKZ; Eukaryota.
DR HOGENOM; CLU_013238_2_1_1; -.
DR InParanoid; O65677; -.
DR OMA; EYCIHRY; -.
DR OrthoDB; 801187at2759; -.
DR PhylomeDB; O65677; -.
DR BioCyc; ARA:AT4G34510-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:O65677; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65677; baseline and differential.
DR Genevisible; O65677; 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 1: Evidence at protein level;
KW Acyltransferase; Membrane; NAD; NADP; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..487
FT /note="3-ketoacyl-CoA synthase 17"
FT /id="PRO_0000249094"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 74..363
FT /note="FAE"
FT /evidence="ECO:0000255"
FT ACT_SITE 218
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 297
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 382
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 386
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 415
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 419
FT /evidence="ECO:0000250|UniProtKB:Q38860"
SQ SEQUENCE 487 AA; 54912 MW; 70847625895E3256 CRC64;
MDANGGPVQI RTQNYVKLGY HYLITHFFKL MFLPLMAVLF MNVSLLSLNH LQLYYNSTGF
IFVITLAIVG SIVFFMSRPR SIYLLDYSCY LPPSSQKVSY QKFMNNSSLI QDFSETSLEF
QRKILIRSGL GEETYLPDSI HSIPPRPTMA AAREEAEQVI FGALDNLFEN TKINPREIGV
LVVNCSLFNP TPSLSAMIVN KYKLRGNIKS FNLGGMGCSA GVIAVDLASD MLQIHRNTFA
LVVSTENITQ NWYFGNKKAM LIPNCLFRVG GSAVLLSNKP LDRKRSKYKL VHTVRTHKGS
DENAFNCVYQ EQDECLKTGV SLSKDLMAIA GEALKTNITS LGPLVLPISE QILFFATFVA
KRLFNDKKKK PYIPDFKLAL DHFCIHAGGR AVIDELEKSL KLSPKHVEAS RMTLHRFGNT
SSSSIWYELA YTEAKGRMRK GNRVWQIAFG SGFKCNSAVW VALRNVEPSV NNPWEHCIHR
YPVKIDL
