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Protein

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

Gene

OXSM

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

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

Enzyme regulationi

Inhibited by cerulenin.By similarity

Pathwayi

GO - Molecular functioni

  1. 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-UniPathway
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

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
Gene namesi
Name:OXSM
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Unplaced

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2828MitochondrionSequence AnalysisAdd
BLAST
Chaini29 – 4604323-oxoacyl-[acyl-carrier-protein] synthase, mitochondrialPRO_0000310304Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei110 – 1101N6-acetyllysine; alternateBy similarity
Modified residuei110 – 1101N6-succinyllysine; alternateBy similarity
Modified residuei114 – 1141N6-succinyllysineBy similarity
Modified residuei175 – 1751N6-acetyllysine; alternateBy similarity
Modified residuei175 – 1751N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ0VCA7.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000009250.

Structurei

3D structure databases

ProteinModelPortaliQ0VCA7.
SMRiQ0VCA7. Positions 41-460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0304.
HOGENOMiHOG000060166.
HOVERGENiHBG082096.
InParanoidiQ0VCA7.
KOiK09458.

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.

Q0VCA7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSDGLQIFL RITKCHLIHA RSCQRLVNER RFLATAPAPG LRRRVVITGI
60 70 80 90 100
GLVTPLGVGT QLVWDRLVRG ESGIVSLVGD EYQSIPCSVA AYVPRGCDEG
110 120 130 140 150
QFNEQNFVPK SDTKSMSPPT VMAIAAAELA LKDAGWHPQS EADQAATGVA
160 170 180 190 200
IGMGMVPLEV ISETALTFQT KGYSKVSPFF VPKILVNMAS GQVSIRHKLK
210 220 230 240 250
GPNHAVSTAC TTGAHAVGDS FRFVAHGDAD VMVAGGTDSC ISPLSLAGFA
260 270 280 290 300
RARALSTNTD PKSACRPFHP QRDGFVMGEG AAVLVLEEHR HALRRGARVY
310 320 330 340 350
AEIVGYGLSG DAGHITAPDP GGEGAFRCMA AAVKDAGIQP EEVSYINAHA
360 370 380 390 400
TSTPLGDAAE NKAIKQLFKD HAHVLAVSST KGATGHLLGT AGAAEAAFTA
410 420 430 440 450
LACYHRKLPP TLNLDCTEPH FDLNYVPLKA QEWKAENRRI ALTNSFGFGG
460
TNATLCIAGM
Length:460
Mass (Da):48,617
Last modified:September 4, 2006 - v1
Checksum:i34D49F1E15BD27B3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC120268 mRNA. Translation: AAI20269.1.
RefSeqiNP_001069092.1. NM_001075624.2.
UniGeneiBt.21584.

Genome annotation databases

GeneIDi513530.
KEGGibta:513530.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC120268 mRNA. Translation: AAI20269.1.
RefSeqiNP_001069092.1. NM_001075624.2.
UniGeneiBt.21584.

3D structure databases

ProteinModelPortaliQ0VCA7.
SMRiQ0VCA7. Positions 41-460.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000009250.

Proteomic databases

PRIDEiQ0VCA7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi513530.
KEGGibta:513530.

Organism-specific databases

CTDi54995.

Phylogenomic databases

eggNOGiCOG0304.
HOGENOMiHOG000060166.
HOVERGENiHBG082096.
InParanoidiQ0VCA7.
KOiK09458.

Enzyme and pathway databases

UniPathwayiUPA00094.

Miscellaneous databases

NextBioi20870896.

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

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

Entry informationi

Entry nameiOXSM_BOVIN
AccessioniPrimary (citable) accession number: Q0VCA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 12, 2007
Last sequence update: September 4, 2006
Last modified: March 3, 2015
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.