Reviewed, UniProtKB/Swiss-Prot Q38860 (KCS18_ARATH)

Names and origin

Protein names

Recommended name:
    3-ketoacyl-CoA synthase 18
      Short name=KCS-18
    EC=2.3.1.-
    EC=2.3.1.119
Alternative name(s):
    Very long-chain fatty acid condensing enzyme 18
      Short name=VLCFA condensing enzyme 18
    Protein FATTY ACID ELONGATION 1

Gene names

Name:	FAE1
Synonyms:	KCS18
Ordered Locus Names:	At4g34520
ORF Names:	T4L20.100

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	506 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Contributes to fatty acids elongation and stockage in developing seeds. Active on both saturated and mono-unsaturated acyl-CoAs of 16 and 18 carbons. Required for the elongation of C18 to C20 and of C20 to C22 fatty acids. Mediates also the synthesis of VLCFAs from 20 to 26 carbons in length (e.g. C20:1, C20, C22:1, C22, C24:1, C24, C26). Ref.1 Ref.3 Ref.4 Ref.5 Ref.9 Ref.10
Catalytic activity	Stearoyl-CoA + malonyl-CoA + 2 NAD(P)H = icosanoyl-CoA + CO2 + CoA + 2 NAD(P)+ + H2O.
Enzyme regulation	Inhibited by K3 herbicides such as allidochlor, cafenstrole and flufenacet. Ref.9
Pathway	Lipid metabolism; fatty acid biosynthesis.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Tissue specificity	Expressed specifically in seeds, especially in embryos. Ref.1 Ref.7
Developmental stage	Accumulates in upper part of roots, hypocotyls and cotyledons of developing embryo. Levels increase in early stages (torpedo, 4 days after flowering) and decrease during late stages of embryo development. Ref.7
Induction	Repressed by herbicides such as flufenacet and benfuresate. Ref.8
Sequence similarities	Belongs to the chalcone/stilbene synthases family. Contains 1 FAE (fatty acid elongase) domain.

Ontologies

Keywords
Cellular component	Membrane
Domain	Transmembrane
Ligand	NAD NADP
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	fatty acid elongase activity Ref.6 Inferred from direct assay. Source: TAIR icosanoyl-CoA synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 506	506	3-ketoacyl-CoA synthase 18		PRO_0000249110
Regions
	Transmembrane	13 – 33	21	Potential
	Transmembrane	52 – 72	21	Potential
	Domain	69 – 368	300	FAE
Sites
	Active site	223	1	Ref.6
	Active site	302	1	Ref.6
	Active site	387	1	Ref.6
	Active site	391	1	Ref.6
	Active site	420	1	Ref.6
	Active site	424	1	By similarity
Experimental info
	Mutagenesis	84	1	C → A or S: Normal activity. Ref.6
	Mutagenesis	223	1	C → A: Loss of activity. Ref.6
	Mutagenesis	223	1	C → S: Normal activity. Ref.6
	Mutagenesis	270	1	C → A: Normal activity. Ref.6
	Mutagenesis	270	1	C → S: Reduced activity. Ref.6
	Mutagenesis	302	1	H → A or K: Loss of activity. Ref.6
	Mutagenesis	312	1	C → A: Normal activity. Ref.6
	Mutagenesis	312	1	C → S: Reduced activity. Ref.6
	Mutagenesis	387	1	H → A or K: Loss of activity. Ref.6
	Mutagenesis	389	1	C → A or S: Normal activity. Ref.6
	Mutagenesis	391	1	H → A or K: Loss of activity. Ref.6
	Mutagenesis	420	1	H → A or K: Loss of activity. Ref.6
	Mutagenesis	460	1	C → A or S: Normal activity. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q38860-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 4516D0EF8E453D18	FASTA	506	56,264
	10 20 30 40 50 60 MTSVNVKLLY RYVLTNFFNL CLFPLTAFLA GKASRLTIND LHNFLSYLQH NLITVTLLFA 70 80 90 100 110 120 FTVFGLVLYI VTRPNPVYLV DYSCYLPPPH LKVSVSKVMD IFYQIRKADT SSRNVACDDP 130 140 150 160 170 180 SSLDFLRKIQ ERSGLGDETY SPEGLIHVPP RKTFAASREE TEKVIIGALE NLFENTKVNP 190 200 210 220 230 240 REIGILVVNS SMFNPTPSLS AMVVNTFKLR SNIKSFNLGG MGCSAGVIAI DLAKDLLHVH 250 260 270 280 290 300 KNTYALVVST ENITQGIYAG ENRSMMVSNC LFRVGGAAIL LSNKSGDRRR SKYKLVHTVR 310 320 330 340 350 360 THTGADDKSF RCVQQEDDES GKIGVCLSKD ITNVAGTTLT KNIATLGPLI LPLSEKFLFF 370 380 390 400 410 420 ATFVAKKLLK DKIKHYYVPD FKLAVDHFCI HAGGRAVIDE LEKNLGLSPI DVEASRSTLH 430 440 450 460 470 480 RFGNTSSSSI WYELAYIEAK GRMKKGNKAW QIALGSGFKC NSAVWVALRN VKASANSPWQ 490 500 HCIDRYPVKI DSDLSKSKTH VQNGRS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Directed tagging of the Arabidopsis FATTY ACID ELONGATION1 (FAE1) gene with the maize transposon activator." James D.W. Jr., Lim E., Keller J., Plooy I., Ralston E., Dooner H.K. Plant Cell 7:309-319(1995) [PubMed: 7734965] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY. Strain: cv. Wassilewskija.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Mutants of Arabidopsis with alterations in seed lipid fatty acid composition." Lemieux B., Miquel M., Somerville C., Browse J. Theor. Appl. Genet. 80:234-240(1990) [Agricola: IND90051597] Cited for: FUNCTION.
[4]	"Isolation of EMS-induced mutants in Arabidopsis altered in seed fatty acid composition." James D.W. Jr., Dooner H.K. Theor. Appl. Genet. 80:241-245(1990) [Agricola: IND90051598] Cited for: FUNCTION.
[5]	"Very-long-chain fatty acid biosynthesis is controlled through the expression and specificity of the condensing enzyme." Millar A.A., Kunst L. Plant J. 12:121-131(1997) [PubMed: 9263455] [Abstract] Cited for: FUNCTION.
[6]	"Active-site residues of a plant membrane-bound fatty acid elongase beta-ketoacyl-CoA synthase, FAE1 KCS." Ghanevati M., Jaworski J.G. Biochim. Biophys. Acta 1530:77-85(2001) [PubMed: 11341960] [Abstract] Cited for: ACTIVE SITES, MUTAGENESIS OF CYS-84; CYS-223; CYS-270; HIS-302; CYS-312; HIS-387; CYS-389; HIS-391; HIS-420 AND CYS-460.
[7]	"Expression of the FAE1 gene and FAE1 promoter activity in developing seeds of Arabidopsis thaliana." Rossak M., Smith M., Kunst L. Plant Mol. Biol. 46:717-725(2001) [PubMed: 11575726] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[8]	"Flufenacet herbicide treatment phenocopies the fiddlehead mutant in Arabidopsis thaliana." Lechelt-Kunze C., Meissner R.C., Drewes M., Tietjen K. Pest Manag. Sci. 59:847-856(2003) [PubMed: 12916765] [Abstract] Cited for: INDUCTION, GENE FAMILY.
[9]	"Specific and differential inhibition of very-long-chain fatty acid elongases from Arabidopsis thaliana by different herbicides." Trenkamp S., Martin W., Tietjen K. Proc. Natl. Acad. Sci. U.S.A. 101:11903-11908(2004) [PubMed: 15277688] [Abstract] Cited for: FUNCTION, ENZYME REGULATION.
[10]	"Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases." Blacklock B.J., Jaworski J.G. Biochem. Biophys. Res. Commun. 346:583-590(2006) [PubMed: 16765910] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U29142 Genomic DNA. Translation: AAA70154.1. AL023094 Genomic DNA. Translation: CAA18831.1. AL161585 Genomic DNA. Translation: CAB80169.1.
IPI	IPI00519188.
PIR	T05272.
RefSeq	NP_195178.1.
UniGene	At.26989
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q38860.
Genome annotation databases
GeneID	829603.
GenomeReviews	Gene locus AT4G34520 in contig CT486007_GR.
KEGG	ath:AT4G34520.
NMPDR	fig|3702.1.peg.21524.
Organism-specific databases
TAIR	At4g34520.
Enzyme and pathway databases
BRENDA	2.3.1.119. 302.
Gene expression databases
ArrayExpress	Q38860.
Genevestigator	Q38860.
GermOnline	AT4G34520. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR012392. 3-ktacl-CoA_syn. IPR012328. Chalcone/stilbene_synth_C. IPR013601. FAE1_typ3_polyketide_synth. IPR016038. Thiolase-like_subgr. [Graphical view]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
Pfam	PF02797. Chal_sti_synt_C. 1 hit. PF08392. FAE1_CUT1_RppA. 1 hit. [Graphical view]
PIRSF	PIRSF036417. 3-ktacl-CoA_syn. 1 hit.
ProtoNet	Search...

Entry information

Entry name

KCS18_ARATH

Accession

Primary (citable) accession number: Q38860

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	November 1, 1996
Last modified:	October 13, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)