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Protein

3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial

Gene

KAS

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Enzyme regulationi

Inhibited by cerulenin.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei209 – 2091PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciARA:AT2G04540-MONOMER.
MetaCyc:AT2G04540-MONOMER.
BRENDAi2.3.1.41. 399.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial (EC:2.3.1.41)
Alternative name(s):
Beta-ketoacyl-ACP synthase
mtKAS
Gene namesi
Name:KAS
Ordered Locus Names:At2g04540
ORF Names:T1O3.5
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G04540.

Subcellular locationi

  • Mitochondrion 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2828MitochondrionSequence AnalysisAdd
BLAST
Chaini29 – 4614333-oxoacyl-[acyl-carrier-protein] synthase, mitochondrialPRO_0000000588Add
BLAST

Proteomic databases

PaxDbiQ8L3X9.
PRIDEiQ8L3X9.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriQ8L3X9.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi3702.AT2G04540.1-P.

Structurei

Secondary structure

1
461
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 4210Combined sources
Beta strandi45 – 473Combined sources
Helixi48 – 569Combined sources
Beta strandi62 – 643Combined sources
Helixi67 – 704Combined sources
Helixi77 – 859Combined sources
Beta strandi91 – 933Combined sources
Beta strandi97 – 1004Combined sources
Helixi106 – 1094Combined sources
Helixi117 – 13216Combined sources
Helixi140 – 1445Combined sources
Beta strandi146 – 1549Combined sources
Helixi157 – 16812Combined sources
Helixi172 – 1743Combined sources
Helixi179 – 1835Combined sources
Helixi187 – 19610Combined sources
Helixi208 – 2103Combined sources
Helixi211 – 22515Combined sources
Beta strandi229 – 2379Combined sources
Helixi242 – 2509Combined sources
Turni257 – 2604Combined sources
Helixi262 – 2643Combined sources
Beta strandi281 – 2899Combined sources
Helixi290 – 2956Combined sources
Beta strandi302 – 31110Combined sources
Helixi324 – 33714Combined sources
Helixi341 – 3433Combined sources
Beta strandi346 – 3483Combined sources
Helixi355 – 36915Combined sources
Helixi371 – 3744Combined sources
Beta strandi378 – 3814Combined sources
Helixi384 – 3874Combined sources
Helixi391 – 3933Combined sources
Helixi394 – 40815Combined sources
Beta strandi418 – 4203Combined sources
Beta strandi426 – 4283Combined sources
Beta strandi440 – 4489Combined sources
Turni449 – 4513Combined sources
Beta strandi452 – 4598Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W0IX-ray2.10A/B31-461[»]
2IX4X-ray1.95A/B31-461[»]
ProteinModelPortaliQ8L3X9.
SMRiQ8L3X9. Positions 31-461.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8L3X9.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi139 – 1446Poly-Glu

Sequence similaritiesi

Belongs to the beta-ketoacyl-ACP synthases family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0304.
HOGENOMiHOG000060166.
InParanoidiQ8L3X9.
KOiK09458.
OMAiQKASRPY.
PhylomeDBiQ8L3X9.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
InterProiIPR017568. 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]
PfamiPF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000447. KAS_II. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR03150. fabF. 1 hit.
PROSITEiPS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8L3X9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSNLRRHL SASRLRLNRF ISTSSSYHSH RRVVVTGLGM VTPLGRGVET
60 70 80 90 100
TWRRLIDGEC GIRGLTLDDL KMKSFDEETK LYTFDQLSSK VAAFVPYGSN
110 120 130 140 150
PGEFDEALWL NSKAVANFIG YAVCAADEAL RDAEWLPTEE EEKERTGVSI
160 170 180 190 200
GGGIGSICDI VEAAQLICEK RLRRLSPFFI PKILVNMASG HVSMKYGFQG
210 220 230 240 250
PNHAAVTACA TGAHSIGDAT RMIQFGDADV MVAGGTESSI DALSVAGFSR
260 270 280 290 300
SRALSTKFNS SPQEASRPFD CDRDGFVIGE GSGVIVLEEY EHAKRRGAKI
310 320 330 340 350
YAELCGYGMS GDAHHITQPP EDGKGAVLAM TRALRQSGLC PNQIDYVNAH
360 370 380 390 400
ATSTPIGDAV EARAIKTVFS EHATSGTLAF SSTKGATGHL LGAAGAVEAI
410 420 430 440 450
FSILAIHHGV APMTLNVKNP DPIFDKRFMP LTTSKKMLVR TAMSNSFGFG
460
GTNASLLFAS I
Length:461
Mass (Da):49,379
Last modified:October 1, 2002 - v1
Checksum:iD9B02B19F5A5FB45
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiF84458.
RefSeqiNP_178533.2. NM_126485.3.
UniGeneiAt.41299.

Genome annotation databases

EnsemblPlantsiAT2G04540.1; AT2G04540.1; AT2G04540.
GeneIDi814996.
KEGGiath:AT2G04540.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiF84458.
RefSeqiNP_178533.2. NM_126485.3.
UniGeneiAt.41299.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W0IX-ray2.10A/B31-461[»]
2IX4X-ray1.95A/B31-461[»]
ProteinModelPortaliQ8L3X9.
SMRiQ8L3X9. Positions 31-461.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT2G04540.1-P.

Proteomic databases

PaxDbiQ8L3X9.
PRIDEiQ8L3X9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G04540.1; AT2G04540.1; AT2G04540.
GeneIDi814996.
KEGGiath:AT2G04540.

Organism-specific databases

TAIRiAT2G04540.

Phylogenomic databases

eggNOGiCOG0304.
HOGENOMiHOG000060166.
InParanoidiQ8L3X9.
KOiK09458.
OMAiQKASRPY.
PhylomeDBiQ8L3X9.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciARA:AT2G04540-MONOMER.
MetaCyc:AT2G04540-MONOMER.
BRENDAi2.3.1.41. 399.

Miscellaneous databases

EvolutionaryTraceiQ8L3X9.
PROiQ8L3X9.

Gene expression databases

GenevestigatoriQ8L3X9.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
InterProiIPR017568. 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]
PfamiPF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000447. KAS_II. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR03150. fabF. 1 hit.
PROSITEiPS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.

Entry informationi

Entry nameiKASM_ARATH
AccessioniPrimary (citable) accession number: Q8L3X9
Secondary accession number(s): Q9SJB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: October 1, 2002
Last modified: January 7, 2015
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.