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P52410 (KASC1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

EC=2.3.1.41
Alternative name(s):
Beta-ketoacyl-ACP synthase I
Short name=KAS I
Gene names
Name:KAS1
Ordered Locus Names:At5g46290
ORF Names:MPL12.7
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids By similarity.

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Subcellular location

Plastidchloroplast stroma Ref.6 Ref.7 Ref.8 Ref.9.

Sequence similarities

Belongs to the beta-ketoacyl-ACP synthases family.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentChloroplast
Plastid
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchloroplast stroma

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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P52410-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P52410-2)

The sequence of this isoform differs from the canonical sequence as follows:
     198-252: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4646Chloroplast Potential
Chain47 – 4734273-oxoacyl-[acyl-carrier-protein] synthase I, chloroplastic
PRO_0000000586

Sites

Active site2241 By similarity

Natural variations

Alternative sequence198 – 25255Missing in isoform 2.
VSP_040746

Experimental info

Sequence conflict741F → C in AAC49118. Ref.1
Sequence conflict238 – 2392IR → NH in AAC49118. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 27, 2002. Version 2.
Checksum: 38CA54382419411C

FASTA47350,413
        10         20         30         40         50         60 
MQALQSSSLR ASPPNPLRLP SNRQSHQLIT NARPLRRQQR SFISASASTV SAPKRETDPK 

        70         80         90        100        110        120 
KRVVITGMGL VSVFGNDVDA YYEKLLSGES GISLIDRFDA SKFPTRFGGQ IRGFSSEGYI 

       130        140        150        160        170        180 
DGKNERRLDD CLKYCIVAGK KALESANLGG DKLNTIDKRK AGVLVGTGMG GLTVFSEGVQ 

       190        200        210        220        230        240 
NLIEKGHRRI SPFFIPYAIT NMGSALLAID LGLMGPNYSI STACATSNYC FYAAANHIRR 

       250        260        270        280        290        300 
GEADMMIAGG TEAAIIPIGL GGFVACRALS QRNDDPQTAS RPWDKARDGF VMGEGAGVLV 

       310        320        330        340        350        360 
MESLEHAMKR GAPIVAEYLG GAVNCDAHHM TDPRADGLGV SSCIERCLED AGVSPEEVNY 

       370        380        390        400        410        420 
INAHATSTLA GDLAEINAIK KVFKSTSGIK INATKSMIGH CLGAAGGLEA IATVKAINTG 

       430        440        450        460        470 
WLHPSINQFN PEQAVDFDTV PNEKKQHEVD VAISNSFGFG GHNSVVAFSA FKP 

« Hide

Isoform 2 [UniParc].

Checksum: 1B656C5985A93752
Show »

FASTA41844,730

References

« Hide 'large scale' references
[1]"Isolation of an Arabidopsis cDNA encoding 3-ketoacyl-acyl carrier protein synthase I.1."
Millar A.A., Kunst L.
Plant Gene Register PGR95-027
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones."
Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N., Tabata S.
DNA Res. 5:131-145(1998) [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] (ISOFORM 1).
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]"Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis."
Froehlich J.E., Wilkerson C.G., Ray W.K., McAndrew R.S., Osteryoung K.W., Gage D.A., Phinney B.S.
J. Proteome Res. 2:413-425(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"The oligomeric stromal proteome of Arabidopsis thaliana chloroplasts."
Peltier J.-B., Cai Y., Sun Q., Zabrouskov V., Giacomelli L., Rudella A., Ytterberg A.J., Rutschow H., van Wijk K.J.
Mol. Cell. Proteomics 5:114-133(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"Sorting signals, N-terminal modifications and abundance of the chloroplast proteome."
Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., van Wijk K.J.
PLoS ONE 3:E1994-E1994(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]"AT_CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins."
Ferro M., Brugiere S., Salvi D., Seigneurin-Berny D., Court M., Moyet L., Ramus C., Miras S., Mellal M., Le Gall S., Kieffer-Jaquinod S., Bruley C., Garin J., Joyard J., Masselon C., Rolland N.
Mol. Cell. Proteomics 9:1063-1084(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U24177 mRNA. Translation: AAC49118.1.
AB010698 Genomic DNA. Translation: BAB11084.1.
CP002688 Genomic DNA. Translation: AED95363.1.
CP002688 Genomic DNA. Translation: AED95364.1.
AY037261 mRNA. Translation: AAK59862.1.
AY094005 mRNA. Translation: AAM16266.1.
AY123979 mRNA. Translation: AAM74493.1.
AY087843 mRNA. Translation: AAM65396.1.
RefSeqNP_001032018.1. NM_001036941.1.
NP_199441.1. NM_123998.2.
UniGeneAt.9183.

3D structure databases

ProteinModelPortalP52410.
SMRP52410. Positions 60-471.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT5G46290.1-P.

Proteomic databases

PaxDbP52410.
PRIDEP52410.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G46290.1; AT5G46290.1; AT5G46290. [P52410-1]
GeneID834671.
KEGGath:AT5G46290.

Organism-specific databases

TAIRAT5G46290.

Phylogenomic databases

eggNOGCOG0304.
HOGENOMHOG000060166.
InParanoidP52410.
KOK09458.
PhylomeDBP52410.
ProtClustDBCLSN2715653.

Enzyme and pathway databases

BioCycARA:AT5G46290-MONOMER.
ARA:GQT-472-MONOMER.
ARA:GQT-473-MONOMER.
MetaCyc:AT5G46290-MONOMER.

Gene expression databases

GenevestigatorP52410.

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]
SUPFAMSSF53901. SSF53901. 2 hits.
TIGRFAMsTIGR03150. fabF. 1 hit.
PROSITEPS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKASC1_ARATH
AccessionPrimary (citable) accession number: P52410
Secondary accession number(s): Q2V312, Q9FL32
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: March 27, 2002
Last modified: April 16, 2014
This is version 114 of the entry and version 2 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names