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Reviewed, UniProtKB/Swiss-Prot O65677 (KCS2_ARATH)

Last modified October 13, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Probable 3-ketoacyl-CoA synthase 2
      Short name=KCS-2
    EC=2.3.1.-
    EC=2.3.1.119
Alternative name(s):
    Very long-chain fatty acid condensing enzyme 2
      Short name=VLCFA condensing enzyme 2
Gene names
Name: KCS2
Ordered Locus Names: At4g34510
ORF Names: T4L20.90
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length487 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Active on saturated acyl-CoAs up to C22. Mediates the synthesis of VLCFAs from 20 to 26 carbons in length (e.g. C20:1, C20, C24, C26). Ref.3 Ref.4

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 alachlor, allidochlor, anilofos, cafenstrole, fentrazamide and flufenacet. Ref.3

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Induction

Repressed by herbicides such as flufenacet and benfuresate. Ref.2

Sequence similarities

Belongs to the chalcone/stilbene synthases family.

Contains 1 FAE (fatty acid elongase) domain.

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Ontologies

Keywords
   Cellular componentMembrane
   DomainTransmembrane
   LigandNAD
NADP
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionacyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

icosanoyl-CoA synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 487487Probable 3-ketoacyl-CoA synthase 2
PRO_0000249094

Regions

Transmembrane23 – 4321 Potential
Transmembrane57 – 7721 Potential
Domain74 – 363290FAE

Sites

Active site2181 By similarity
Active site2971 By similarity
Active site3821 By similarity
Active site3861 By similarity
Active site4151 By similarity
Active site4191 By similarity

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Sequences

Sequence LengthMass (Da)Tools
O65677-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 70847625895E3256

FASTA48754,912
        10         20         30         40         50         60 
MDANGGPVQI RTQNYVKLGY HYLITHFFKL MFLPLMAVLF MNVSLLSLNH LQLYYNSTGF 

        70         80         90        100        110        120 
IFVITLAIVG SIVFFMSRPR SIYLLDYSCY LPPSSQKVSY QKFMNNSSLI QDFSETSLEF 

       130        140        150        160        170        180 
QRKILIRSGL GEETYLPDSI HSIPPRPTMA AAREEAEQVI FGALDNLFEN TKINPREIGV 

       190        200        210        220        230        240 
LVVNCSLFNP TPSLSAMIVN KYKLRGNIKS FNLGGMGCSA GVIAVDLASD MLQIHRNTFA 

       250        260        270        280        290        300 
LVVSTENITQ NWYFGNKKAM LIPNCLFRVG GSAVLLSNKP LDRKRSKYKL VHTVRTHKGS 

       310        320        330        340        350        360 
DENAFNCVYQ EQDECLKTGV SLSKDLMAIA GEALKTNITS LGPLVLPISE QILFFATFVA 

       370        380        390        400        410        420 
KRLFNDKKKK PYIPDFKLAL DHFCIHAGGR AVIDELEKSL KLSPKHVEAS RMTLHRFGNT 

       430        440        450        460        470        480 
SSSSIWYELA YTEAKGRMRK GNRVWQIAFG SGFKCNSAVW VALRNVEPSV NNPWEHCIHR 


YPVKIDL

« Hide

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References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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.
[2]"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.
[3]"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.
[4]"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.

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Cross-references

Sequence databases

AL023094 Genomic DNA. Translation: CAA18830.1.
AL161585 Genomic DNA. Translation: CAB80168.1.
IPIIPI00541766.
PIRT05271.
RefSeqNP_195177.1.
UniGeneAt.27519

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID829602.
GenomeReviewsGene locus AT4G34510 in contig CT486007_GR.
KEGGath:AT4G34510.
NMPDRfig|3702.1.peg.21523.

Organism-specific databases

TAIRAt4g34510.

Enzyme and pathway databases

BRENDA2.3.1.119. 302.

Gene expression databases

ArrayExpressO65677.
GenevestigatorO65677.
GermOnlineAT4G34510. Arabidopsis thaliana.

Family and domain databases

InterProIPR012392. 3-ktacl-CoA_syn.
IPR012328. Chalcone/stilbene_synth_C.
IPR013601. FAE1_typ3_polyketide_synth.
IPR016038. Thiolase-like_subgr.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
PfamPF02797. Chal_sti_synt_C. 1 hit.
PF08392. FAE1_CUT1_RppA. 1 hit.
[Graphical view]
PIRSFPIRSF036417. 3-ktacl-CoA_syn. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameKCS2_ARATH
AccessionPrimary (citable) accession number: O65677
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: August 1, 1998
Last modified: October 13, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents