Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P23902 (KASC1_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 I, chloroplastic

EC=2.3.1.41
Alternative name(s):
Beta-ketoacyl-ACP synthase I
Short name=KAS I
Gene names
Name:KAS12
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Catalytic activity

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

Subunit structure

Homodimer.

Subcellular location

Plastidchloroplast.

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
   DomainTransit peptide
   Molecular functionAcyltransferase
Transferase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchloroplast

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 – 3535Chloroplast
Chain36 – 4624273-oxoacyl-[acyl-carrier-protein] synthase I, chloroplastic
PRO_0000000587

Sites

Active site2131 By similarity

Sequences

Sequence LengthMass (Da)Tools
P23902 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: BDFA3622263A7764

FASTA46249,016
        10         20         30         40         50         60 
MHAHAAHALG LRVPPPAFPR RRARPRRRPA AAVLATSAAP QRETDPRKRV VITGMGLASV 

        70         80         90        100        110        120 
FGSDVDTFYD RLLAGESGVG PIDRFDASSF PTRFAGQIRG FSSEGYIDGK NDRRLDDCIR 

       130        140        150        160        170        180 
YCILSGKKAL ESAGLGAGSD AHVKLDVGRA GVLVGTGMGG LSVFSDGVQN LIEKGYRKIS 

       190        200        210        220        230        240 
PFFIPYAITN MGSALLAIDV GFMGPNYSIS TACATSNYCF YAAANHIRRG EADIIVAGGT 

       250        260        270        280        290        300 
EAAIIPIGLG GFVACRALSQ RNDDPITACR PWDKERDGFV MGEGAGVLVM ESLEHAMKRD 

       310        320        330        340        350        360 
APIIAEYLGG AVNCDAYHMT DPRADGLGVS SCITMSLRDA GVAPEEVNYI NAHATSTLAG 

       370        380        390        400        410        420 
DLAEVRAIKQ VFKNPSEIKI NSTKSMIGHC LGAAGGLEAI ATIKSITTGW VHPTINQFNP 

       430        440        450        460 
EPEVDFDTVA NEKKQHEVNV GISNSFGFGG HNSVVVFAPF KP 

« Hide

References

[1]"Primary structure of a cerulenin-binding beta-ketoacyl-[acyl carrier protein] synthase from barley chloroplasts."
Siggaard-Andersen M., Kauppinen S., von Wettstein-Knowles P.
Proc. Natl. Acad. Sci. U.S.A. 88:4114-4118(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: cv. Bonus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60410 mRNA. Translation: AAA32968.1.
PIRA39356.
UniGeneHv.115.

3D structure databases

ProteinModelPortalP23902.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP23902.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP23902.

Gene expression databases

GenevestigatorP23902.

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...

Entry information

Entry nameKASC1_HORVU
AccessionPrimary (citable) accession number: P23902
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: October 16, 2013
This is version 78 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