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Protein

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

Gene

Oxsm

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein 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: HGNC

GO - Biological processi

  1. acyl-CoA metabolic process Source: HGNC
  2. medium-chain fatty acid biosynthetic process Source: HGNC
  3. short-chain fatty acid biosynthetic process Source: HGNC
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1918397. Oxsm.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. mitochondrion Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727MitochondrionSequence AnalysisAdd
BLAST
Chaini28 – 4594323-oxoacyl-[acyl-carrier-protein] synthase, mitochondrialPRO_0000232661Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei109 – 1091N6-acetyllysine; alternate1 Publication
Modified residuei109 – 1091N6-succinyllysine; alternate1 Publication
Modified residuei113 – 1131N6-succinyllysine1 Publication
Modified residuei174 – 1741N6-acetyllysine; alternate1 Publication
Modified residuei174 – 1741N6-succinyllysine; alternate1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9D404.
PaxDbiQ9D404.
PRIDEiQ9D404.

PTM databases

PhosphoSiteiQ9D404.

Expressioni

Gene expression databases

BgeeiQ9D404.
CleanExiMM_OXSM.
ExpressionAtlasiQ9D404. baseline and differential.
GenevestigatoriQ9D404.

Interactioni

Protein-protein interaction databases

IntActiQ9D404. 2 interactions.
MINTiMINT-4126973.

Structurei

3D structure databases

ProteinModelPortaliQ9D404.
SMRiQ9D404. Positions 40-459.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0304.
GeneTreeiENSGT00530000063309.
HOGENOMiHOG000060166.
HOVERGENiHBG082096.
InParanoidiQ9D404.
KOiK09458.
OMAiQKASRPY.
OrthoDBiEOG77DJ5Z.
PhylomeDBiQ9D404.

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.

Q9D404-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSKCLQHFL KATISHPYPA SYSWLISKHR FYGTVPAAML RRRVVITGIG
60 70 80 90 100
LVTPLGVGTQ LVWDRLLRGE SGIVSVVGDE YKNIPCSVAA YVPRGPHEGQ
110 120 130 140 150
FNEENFVSKS DAKSMSSSTI MAVGAAELAL KDSGWHPKRE ADQVATGVAI
160 170 180 190 200
GMGMVPLEVI SETALLFQTK GYNKVSPFFV PKILINMAAG QVSIRYKLKG
210 220 230 240 250
PNHSVSTACT TGAHAVGDSF RFIAHGDADV MVAGGTDSCI SPLSLAGFSR
260 270 280 290 300
ARALSSNPDP KLACRPFHPE RDGFVMGEGA AVLVLEEHEH AVQRGARIYA
310 320 330 340 350
EILGYGLSGD AGHITAPDPE GEGALRCMAA AVKDAGVSPE QISYVNAHAT
360 370 380 390 400
STPLGDAAEN RAIKRLFRDH ACALAISSTK GATGHLLGAA GAVEATFTAL
410 420 430 440 450
ACYHQKLPPT LNLDCTEPEF DLNYVPLESQ EWKAEGRCIG LTNSFGFGGT

NATLCIAGM
Length:459
Mass (Da):48,628
Last modified:June 1, 2001 - v1
Checksum:i47F9733FBBF08BE1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK016905 mRNA. Translation: BAB30490.1.
AK083617 mRNA. Translation: BAC38969.1.
AK084829 mRNA. Translation: BAC39286.1.
CCDSiCCDS26831.1.
RefSeqiNP_081971.1. NM_027695.3.
XP_006518163.1. XM_006518100.2.
XP_006518164.1. XM_006518101.2.
XP_006518165.1. XM_006518102.2.
XP_006518166.1. XM_006518103.2.
UniGeneiMm.197960.

Genome annotation databases

EnsembliENSMUST00000022311; ENSMUSP00000022311; ENSMUSG00000021786.
ENSMUST00000112624; ENSMUSP00000108243; ENSMUSG00000021786.
ENSMUST00000112625; ENSMUSP00000108244; ENSMUSG00000021786.
GeneIDi71147.
KEGGimmu:71147.
UCSCiuc007sgw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK016905 mRNA. Translation: BAB30490.1.
AK083617 mRNA. Translation: BAC38969.1.
AK084829 mRNA. Translation: BAC39286.1.
CCDSiCCDS26831.1.
RefSeqiNP_081971.1. NM_027695.3.
XP_006518163.1. XM_006518100.2.
XP_006518164.1. XM_006518101.2.
XP_006518165.1. XM_006518102.2.
XP_006518166.1. XM_006518103.2.
UniGeneiMm.197960.

3D structure databases

ProteinModelPortaliQ9D404.
SMRiQ9D404. Positions 40-459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D404. 2 interactions.
MINTiMINT-4126973.

PTM databases

PhosphoSiteiQ9D404.

Proteomic databases

MaxQBiQ9D404.
PaxDbiQ9D404.
PRIDEiQ9D404.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022311; ENSMUSP00000022311; ENSMUSG00000021786.
ENSMUST00000112624; ENSMUSP00000108243; ENSMUSG00000021786.
ENSMUST00000112625; ENSMUSP00000108244; ENSMUSG00000021786.
GeneIDi71147.
KEGGimmu:71147.
UCSCiuc007sgw.1. mouse.

Organism-specific databases

CTDi54995.
MGIiMGI:1918397. Oxsm.

Phylogenomic databases

eggNOGiCOG0304.
GeneTreeiENSGT00530000063309.
HOGENOMiHOG000060166.
HOVERGENiHBG082096.
InParanoidiQ9D404.
KOiK09458.
OMAiQKASRPY.
OrthoDBiEOG77DJ5Z.
PhylomeDBiQ9D404.

Enzyme and pathway databases

UniPathwayiUPA00094.

Miscellaneous databases

ChiTaRSiOxsm. mouse.
NextBioi333127.
PROiQ9D404.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D404.
CleanExiMM_OXSM.
ExpressionAtlasiQ9D404. baseline and differential.
GenevestigatoriQ9D404.

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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo, Heart and Testis.
  2. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-109; LYS-113 AND LYS-174, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  3. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-109 AND LYS-174, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiOXSM_MOUSE
AccessioniPrimary (citable) accession number: Q9D404
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: June 1, 2001
Last modified: April 1, 2015
This is version 104 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.