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Q0VCA7 (OXSM_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 65. 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·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
Gene names
Name:OXSM
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May play a role in the biosynthesis of lipoic acid as well as longer chain fatty acids required for optimal mitochondrial function By similarity.

Catalytic activity

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

Enzyme regulation

Inhibited by cerulenin By similarity.

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the beta-ketoacyl-ACP synthases family.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical termComplete 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 – 4604323-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
PRO_0000310304

Amino acid modifications

Modified residue1101N6-acetyllysine; alternate By similarity
Modified residue1101N6-succinyllysine; alternate By similarity
Modified residue1141N6-succinyllysine By similarity
Modified residue1751N6-acetyllysine; alternate By similarity
Modified residue1751N6-succinyllysine; alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0VCA7 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 34D49F1E15BD27B3

FASTA46048,617
        10         20         30         40         50         60 
MLSDGLQIFL RITKCHLIHA RSCQRLVNER RFLATAPAPG LRRRVVITGI GLVTPLGVGT 

        70         80         90        100        110        120 
QLVWDRLVRG ESGIVSLVGD EYQSIPCSVA AYVPRGCDEG QFNEQNFVPK SDTKSMSPPT 

       130        140        150        160        170        180 
VMAIAAAELA LKDAGWHPQS EADQAATGVA IGMGMVPLEV ISETALTFQT KGYSKVSPFF 

       190        200        210        220        230        240 
VPKILVNMAS GQVSIRHKLK GPNHAVSTAC TTGAHAVGDS FRFVAHGDAD VMVAGGTDSC 

       250        260        270        280        290        300 
ISPLSLAGFA RARALSTNTD PKSACRPFHP QRDGFVMGEG AAVLVLEEHR HALRRGARVY 

       310        320        330        340        350        360 
AEIVGYGLSG DAGHITAPDP GGEGAFRCMA AAVKDAGIQP EEVSYINAHA TSTPLGDAAE 

       370        380        390        400        410        420 
NKAIKQLFKD HAHVLAVSST KGATGHLLGT AGAAEAAFTA LACYHRKLPP TLNLDCTEPH 

       430        440        450        460 
FDLNYVPLKA QEWKAENRRI ALTNSFGFGG TNATLCIAGM 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Thymus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC120268 mRNA. Translation: AAI20269.1.
RefSeqNP_001069092.1. NM_001075624.2.
UniGeneBt.21584.

3D structure databases

ProteinModelPortalQ0VCA7.
SMRQ0VCA7. Positions 41-460.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000009250.

Proteomic databases

PRIDEQ0VCA7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID513530.
KEGGbta:513530.

Organism-specific databases

CTD54995.

Phylogenomic databases

eggNOGCOG0304.
HOGENOMHOG000060166.
HOVERGENHBG082096.
InParanoidQ0VCA7.
KOK09458.

Enzyme and pathway databases

UniPathwayUPA00094.

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

NextBio20870896.

Entry information

Entry nameOXSM_BOVIN
AccessionPrimary (citable) accession number: Q0VCA7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: September 5, 2006
Last modified: March 19, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways