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Q8L3X9 (KASM_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial

EC=2.3.1.41
Alternative name(s):
Beta-ketoacyl-ACP synthase
mtKAS
Gene names
Name:KAS
Ordered Locus Names:At2g04540
ORF Names:T1O3.5
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes all the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Able to elongate saturated acyl chains from 4 to at least 16 carbons. Uses malonyl-CoA but not acetyl-CoA as primer substrate. When expressed in a heterologous system, reveals a bimodal distribution of products, with peaks at C8 and C14-C16. The major product of the reaction (octanoyl-ACP) is required for the lipoylation of essential mitochondrial proteins. Ref.5

Catalytic activity

Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].

Enzyme regulation

Inhibited by cerulenin.

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Homodimer. Ref.6

Subcellular location

Mitochondrion Ref.1.

Tissue specificity

Expressed at the same level in leaves, roots and flowers. Ref.1

Disruption phenotype

Slow growth and bleached leaf phenotype when grown under ambient air, but normal growth under CO(2)-enriched air. Highly prevents lipoylation of the H-protein subunit of the glycine decarboxylase (GDC) in leaves, but has only a limited effect on the lipoylation of the E2 subunits of pyruvate dehydrogenase (PDH) and alpha-ketoacid dehydrogenase (KGDH) complexes in leaves and even no effect in roots. Ref.5

Miscellaneous

Mitochondrial protein lipoylation in leaves does not exclusively depend on the lipoate biosynthesis by KAS and may occur independently of this pathway in roots (Ref.5).

Sequence similarities

Belongs to the beta-ketoacyl-ACP synthases family.

Sequence caution

The sequence AAD25826.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionAcyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function3-oxoacyl-[acyl-carrier-protein] synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion Potential
Chain29 – 4614333-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
PRO_0000000588

Regions

Compositional bias139 – 1446Poly-Glu

Sites

Active site2091 By similarity

Secondary structure

......................................................................... 461
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8L3X9 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: D9B02B19F5A5FB45

FASTA46149,379
        10         20         30         40         50         60 
MATSNLRRHL SASRLRLNRF ISTSSSYHSH RRVVVTGLGM VTPLGRGVET TWRRLIDGEC 

        70         80         90        100        110        120 
GIRGLTLDDL KMKSFDEETK LYTFDQLSSK VAAFVPYGSN PGEFDEALWL NSKAVANFIG 

       130        140        150        160        170        180 
YAVCAADEAL RDAEWLPTEE EEKERTGVSI GGGIGSICDI VEAAQLICEK RLRRLSPFFI 

       190        200        210        220        230        240 
PKILVNMASG HVSMKYGFQG PNHAAVTACA TGAHSIGDAT RMIQFGDADV MVAGGTESSI 

       250        260        270        280        290        300 
DALSVAGFSR SRALSTKFNS SPQEASRPFD CDRDGFVIGE GSGVIVLEEY EHAKRRGAKI 

       310        320        330        340        350        360 
YAELCGYGMS GDAHHITQPP EDGKGAVLAM TRALRQSGLC PNQIDYVNAH ATSTPIGDAV 

       370        380        390        400        410        420 
EARAIKTVFS EHATSGTLAF SSTKGATGHL LGAAGAVEAI FSILAIHHGV APMTLNVKNP 

       430        440        450        460 
DPIFDKRFMP LTTSKKMLVR TAMSNSFGFG GTNASLLFAS I 

« Hide

References

« Hide 'large scale' references
[1]"Identification and molecular characterization of the beta-ketoacyl-[acyl carrier-protein] synthase component of the Arabidopsis mitochondrial fatty acid synthase."
Yasuno R., von Wettstein-Knowles P., Wada H.
J. Biol. Chem. 279:8242-8251(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Mitochondrial protein lipoylation does not exclusively depend on the mtKAS pathway of de novo fatty acid synthesis in Arabidopsis."
Ewald R., Kolukisaoglu U., Bauwe U., Mikkat S., Bauwe H.
Plant Physiol. 145:41-48(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[6]"Structure of the mitochondrial beta-ketoacyl-[acyl carrier-protein] synthase from Arabidopsis and its role in fatty acid synthesis."
Olsen J.G., Rasmussen A.V., von Wettstein-Knowles P., Henriksen A.
FEBS Lett. 577:170-174(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 31-461, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB073746 mRNA. Translation: BAB91181.1.
AC006951 Genomic DNA. Translation: AAD25826.1. Sequence problems.
CP002685 Genomic DNA. Translation: AEC05844.1.
AY099587 mRNA. Translation: AAM20439.1.
AY128832 mRNA. Translation: AAM91232.1.
PIRF84458.
RefSeqNP_178533.2. NM_126485.3.
UniGeneAt.41299.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W0IX-ray2.10A/B31-461[»]
2IX4X-ray1.95A/B31-461[»]
ProteinModelPortalQ8L3X9.
SMRQ8L3X9. Positions 31-461.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT2G04540.1-P.

Proteomic databases

PaxDbQ8L3X9.
PRIDEQ8L3X9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G04540.1; AT2G04540.1; AT2G04540.
GeneID814996.
KEGGath:AT2G04540.

Organism-specific databases

TAIRAT2G04540.

Phylogenomic databases

eggNOGCOG0304.
HOGENOMHOG000060166.
InParanoidQ8L3X9.
KOK09458.
OMAHAQKRNA.
PhylomeDBQ8L3X9.

Enzyme and pathway databases

BioCycARA:AT2G04540-MONOMER.
MetaCyc:AT2G04540-MONOMER.
BRENDA2.3.1.41. 399.
UniPathwayUPA00094.

Gene expression databases

GenevestigatorQ8L3X9.

Family and domain databases

Gene3D3.40.47.10. 2 hits.
InterProIPR017568. 3-oxoacyl-ACP_synth-2.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
PIRSFPIRSF000447. KAS_II. 1 hit.
SUPFAMSSF53901. SSF53901. 2 hits.
TIGRFAMsTIGR03150. fabF. 1 hit.
PROSITEPS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8L3X9.
PROQ8L3X9.

Entry information

Entry nameKASM_ARATH
AccessionPrimary (citable) accession number: Q8L3X9
Secondary accession number(s): Q9SJB7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: October 1, 2002
Last modified: May 14, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names