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Q9D404 (OXSM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion Potential
Chain28 – 4594323-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
PRO_0000232661

Amino acid modifications

Modified residue1091N6-acetyllysine; alternate Ref.3
Modified residue1091N6-succinyllysine; alternate Ref.2
Modified residue1131N6-succinyllysine Ref.2
Modified residue1741N6-acetyllysine; alternate Ref.3
Modified residue1741N6-succinyllysine; alternate Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9D404 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 47F9733FBBF08BE1

FASTA45948,628
        10         20         30         40         50         60 
MLSKCLQHFL KATISHPYPA SYSWLISKHR FYGTVPAAML RRRVVITGIG LVTPLGVGTQ 

        70         80         90        100        110        120 
LVWDRLLRGE SGIVSVVGDE YKNIPCSVAA YVPRGPHEGQ FNEENFVSKS DAKSMSSSTI 

       130        140        150        160        170        180 
MAVGAAELAL KDSGWHPKRE ADQVATGVAI GMGMVPLEVI SETALLFQTK GYNKVSPFFV 

       190        200        210        220        230        240 
PKILINMAAG QVSIRYKLKG PNHSVSTACT TGAHAVGDSF RFIAHGDADV MVAGGTDSCI 

       250        260        270        280        290        300 
SPLSLAGFSR ARALSSNPDP KLACRPFHPE RDGFVMGEGA AVLVLEEHEH AVQRGARIYA 

       310        320        330        340        350        360 
EILGYGLSGD AGHITAPDPE GEGALRCMAA AVKDAGVSPE QISYVNAHAT STPLGDAAEN 

       370        380        390        400        410        420 
RAIKRLFRDH ACALAISSTK GATGHLLGAA GAVEATFTAL ACYHQKLPPT LNLDCTEPEF 

       430        440        450 
DLNYVPLESQ EWKAEGRCIG LTNSFGFGGT NATLCIAGM 

« Hide

References

[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. expand/collapse author list , 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(2005) [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(2013) [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(2013) [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK016905 mRNA. Translation: BAB30490.1.
AK083617 mRNA. Translation: BAC38969.1.
AK084829 mRNA. Translation: BAC39286.1.
CCDSCCDS26831.1.
RefSeqNP_081971.1. NM_027695.3.
XP_006518163.1. XM_006518100.1.
XP_006518164.1. XM_006518101.1.
XP_006518165.1. XM_006518102.1.
XP_006518166.1. XM_006518103.1.
UniGeneMm.197960.

3D structure databases

ProteinModelPortalQ9D404.
SMRQ9D404. Positions 40-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9D404. 2 interactions.
MINTMINT-4126973.

PTM databases

PhosphoSiteQ9D404.

Proteomic databases

MaxQBQ9D404.
PaxDbQ9D404.
PRIDEQ9D404.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022311; ENSMUSP00000022311; ENSMUSG00000021786.
ENSMUST00000112624; ENSMUSP00000108243; ENSMUSG00000021786.
ENSMUST00000112625; ENSMUSP00000108244; ENSMUSG00000021786.
GeneID71147.
KEGGmmu:71147.
UCSCuc007sgw.1. mouse.

Organism-specific databases

CTD54995.
MGIMGI:1918397. Oxsm.

Phylogenomic databases

eggNOGCOG0304.
GeneTreeENSGT00530000063309.
HOGENOMHOG000060166.
HOVERGENHBG082096.
InParanoidQ9D404.
KOK09458.
OMAWMEPKEQ.
OrthoDBEOG77DJ5Z.
PhylomeDBQ9D404.

Enzyme and pathway databases

UniPathwayUPA00094.

Gene expression databases

ArrayExpressQ9D404.
BgeeQ9D404.
CleanExMM_OXSM.
GenevestigatorQ9D404.

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

ChiTaRSOXSM. mouse.
NextBio333127.
PROQ9D404.
SOURCESearch...

Entry information

Entry nameOXSM_MOUSE
AccessionPrimary (citable) accession number: Q9D404
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 98 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot