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Q9D404

- OXSM_MOUSE

UniProt

Q9D404 - OXSM_MOUSE

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Protein
3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
Gene
Oxsm
Organism
Mus musculus (Mouse)
Status
Reviewed - 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: Chromosome 14

Organism-specific databases

MGIiMGI:1918397. Oxsm.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrion Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727Mitochondrion Reviewed prediction
Add
BLAST
Chaini28 – 4594323-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
PRO_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

ArrayExpressiQ9D404.
BgeeiQ9D404.
CleanExiMM_OXSM.
GenevestigatoriQ9D404.

Interactioni

Protein-protein interaction databases

IntActiQ9D404. 2 interactions.
MINTiMINT-4126973.

Structurei

3D structure databases

ProteinModelPortaliQ9D404.
SMRiQ9D404. Positions 40-459.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0304.
GeneTreeiENSGT00530000063309.
HOGENOMiHOG000060166.
HOVERGENiHBG082096.
InParanoidiQ9D404.
KOiK09458.
OMAiWMEPKEQ.
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

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MLSKCLQHFL KATISHPYPA SYSWLISKHR FYGTVPAAML RRRVVITGIG    50
LVTPLGVGTQ LVWDRLLRGE SGIVSVVGDE YKNIPCSVAA YVPRGPHEGQ 100
FNEENFVSKS DAKSMSSSTI MAVGAAELAL KDSGWHPKRE ADQVATGVAI 150
GMGMVPLEVI SETALLFQTK GYNKVSPFFV PKILINMAAG QVSIRYKLKG 200
PNHSVSTACT TGAHAVGDSF RFIAHGDADV MVAGGTDSCI SPLSLAGFSR 250
ARALSSNPDP KLACRPFHPE RDGFVMGEGA AVLVLEEHEH AVQRGARIYA 300
EILGYGLSGD AGHITAPDPE GEGALRCMAA AVKDAGVSPE QISYVNAHAT 350
STPLGDAAEN RAIKRLFRDH ACALAISSTK GATGHLLGAA GAVEATFTAL 400
ACYHQKLPPT LNLDCTEPEF DLNYVPLESQ EWKAEGRCIG LTNSFGFGGT 450
NATLCIAGM 459
Length:459
Mass (Da):48,628
Last modified:June 1, 2001 - v1
Checksum:i47F9733FBBF08BE1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006518100.1.
XP_006518164.1. XM_006518101.1.
XP_006518165.1. XM_006518102.1.
XP_006518166.1. XM_006518103.1.
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:
EMBL
GenBank
DDBJ
Links Updated
AK016905 mRNA. Translation: BAB30490.1 .
AK083617 mRNA. Translation: BAC38969.1 .
AK084829 mRNA. Translation: BAC39286.1 .
CCDSi CCDS26831.1.
RefSeqi NP_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.
UniGenei Mm.197960.

3D structure databases

ProteinModelPortali Q9D404.
SMRi Q9D404. Positions 40-459.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9D404. 2 interactions.
MINTi MINT-4126973.

PTM databases

PhosphoSitei Q9D404.

Proteomic databases

MaxQBi Q9D404.
PaxDbi Q9D404.
PRIDEi Q9D404.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022311 ; ENSMUSP00000022311 ; ENSMUSG00000021786 .
ENSMUST00000112624 ; ENSMUSP00000108243 ; ENSMUSG00000021786 .
ENSMUST00000112625 ; ENSMUSP00000108244 ; ENSMUSG00000021786 .
GeneIDi 71147.
KEGGi mmu:71147.
UCSCi uc007sgw.1. mouse.

Organism-specific databases

CTDi 54995.
MGIi MGI:1918397. Oxsm.

Phylogenomic databases

eggNOGi COG0304.
GeneTreei ENSGT00530000063309.
HOGENOMi HOG000060166.
HOVERGENi HBG082096.
InParanoidi Q9D404.
KOi K09458.
OMAi WMEPKEQ.
OrthoDBi EOG77DJ5Z.
PhylomeDBi Q9D404.

Enzyme and pathway databases

UniPathwayi UPA00094 .

Miscellaneous databases

ChiTaRSi OXSM. mouse.
NextBioi 333127.
PROi Q9D404.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9D404.
Bgeei Q9D404.
CleanExi MM_OXSM.
Genevestigatori Q9D404.

Family and domain databases

Gene3Di 3.40.47.10. 2 hits.
InterProi IPR017568. 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 ]
Pfami PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000447. KAS_II. 1 hit.
SUPFAMi SSF53901. SSF53901. 2 hits.
TIGRFAMsi TIGR03150. fabF. 1 hit.
PROSITEi PS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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.

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: July 9, 2014
This is version 98 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

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