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Q9NWU1 (OXSM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Ref.4

Catalytic activity

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

Enzyme regulation

Inhibited by cerulenin. Ref.4

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subcellular location

Mitochondrion Ref.4.

Tissue specificity

Widely expressed. Higher expression in heart, skeletal muscle, liver and kidney which contain high levels of active mitochondria. Ref.4

Sequence similarities

Belongs to the beta-ketoacyl-ACP synthases family.

Biophysicochemical properties

Kinetic parameters:

The highest catalytic efficiency is observed for C10-[acyl-carrier-protein].

KM=3.9 µM for C4-[acyl-carrier-protein] Ref.4

KM=1.9 µM for C6-[acyl-carrier-protein]

KM=10.9 µM for C8-[acyl-carrier-protein]

KM=1.8 µM for C10-[acyl-carrier-protein]

KM=9.5 µM for C12-[acyl-carrier-protein]

KM=50.8 µM for C14-[acyl-carrier-protein]

Vmax=129 nmol/min/mg enzyme toward C4-[acyl-carrier-protein]

Vmax=241 nmol/min/mg enzyme toward C6-[acyl-carrier-protein]

Vmax=271 nmol/min/mg enzyme toward C8-[acyl-carrier-protein]

Vmax=364 nmol/min/mg enzyme toward C10-[acyl-carrier-protein]

Vmax=1045 nmol/min/mg enzyme toward C12-[acyl-carrier-protein]

Vmax=115 nmol/min/mg enzyme toward C14-[acyl-carrier-protein]

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NWU1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9NWU1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     229-311: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion Potential
Chain28 – 4594323-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
PRO_0000232660

Amino acid modifications

Modified residue1091N6-acetyllysine; alternate By similarity
Modified residue1091N6-succinyllysine; alternate By similarity
Modified residue1131N6-succinyllysine By similarity
Modified residue1741N6-acetyllysine; alternate Ref.5
Modified residue1741N6-succinyllysine; alternate By similarity

Natural variations

Alternative sequence229 – 31183Missing in isoform 2.
VSP_041671
Natural variant1061F → I in a breast cancer sample; somatic mutation. Ref.9
VAR_036064

Secondary structure

.......................................................................... 459
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: B2EF550CD354F18C

FASTA45948,843
        10         20         30         40         50         60 
MSNCLQNFLK ITSTRLLCSR LCQQLRSKRK FFGTVPISRL HRRVVITGIG LVTPLGVGTH 

        70         80         90        100        110        120 
LVWDRLIGGE SGIVSLVGEE YKSIPCSVAA YVPRGSDEGQ FNEQNFVSKS DIKSMSSPTI 

       130        140        150        160        170        180 
MAIGAAELAM KDSGWHPQSE ADQVATGVAI GMGMIPLEVV SETALNFQTK GYNKVSPFFV 

       190        200        210        220        230        240 
PKILVNMAAG QVSIRYKLKG PNHAVSTACT TGAHAVGDSF RFIAHGDADV MVAGGTDSCI 

       250        260        270        280        290        300 
SPLSLAGFSR ARALSTNSDP KLACRPFHPK RDGFVMGEGA AVLVLEEYEH AVQRRARIYA 

       310        320        330        340        350        360 
EVLGYGLSGD AGHITAPDPE GEGALRCMAA ALKDAGVQPE EISYINAHAT STPLGDAAEN 

       370        380        390        400        410        420 
KAIKHLFKDH AYALAVSSTK GATGHLLGAA GAVEAAFTTL ACYYQKLPPT LNLDCSEPEF 

       430        440        450 
DLNYVPLKAQ EWKTEKRFIG LTNSFGFGGT NATLCIAGL 

« Hide

Isoform 2 [UniParc].

Checksum: B9470D089DE7CF7D
Show »

FASTA37640,035

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Carcinoma.
[2]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta.
[4]"Cloning, expression, and characterization of the human mitochondrial beta-ketoacyl synthase. Complementation of the yeast CEM1 knock-out strain."
Zhang L., Joshi A.K., Hofmann J., Schweizer E., Smith S.
J. Biol. Chem. 280:12422-12429(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[5]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-174, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Structure of mitochondrial beta-ketoacyl synthase."
Bunkoczi G., Wu X., Smee C., Gileadi O., Arrowsmith C., Edwards A., Sundstrom M., Weigelt J., von Delft F., Oppermann U.
Submitted (DEC-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 39-459.
[8]"Structure of the human beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase."
Christensen C.E., Kragelund B.B., von Wettstein-Knowles P., Henriksen A.
Protein Sci. 16:261-272(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 38-459.
[9]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-106.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK000611 mRNA. Translation: BAA91286.1.
AK225260 mRNA. No translation available.
AC092798 Genomic DNA. No translation available.
BC008202 mRNA. Translation: AAH08202.1.
RefSeqNP_001138863.1. NM_001145391.1.
NP_060367.1. NM_017897.2.
UniGeneHs.55781.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C9HX-ray1.80A39-459[»]
2IWYX-ray2.06A/B38-459[»]
2IWZX-ray1.65A/B38-459[»]
ProteinModelPortalQ9NWU1.
SMRQ9NWU1. Positions 38-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120328. 2 interactions.
STRING9606.ENSP00000280701.

PTM databases

PhosphoSiteQ9NWU1.

Polymorphism databases

DMDM74753030.

Proteomic databases

PaxDbQ9NWU1.
PeptideAtlasQ9NWU1.
PRIDEQ9NWU1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000280701; ENSP00000280701; ENSG00000151093. [Q9NWU1-1]
ENST00000420173; ENSP00000411303; ENSG00000151093. [Q9NWU1-2]
GeneID54995.
KEGGhsa:54995.
UCSCuc003cdn.3. human. [Q9NWU1-1]
uc010hfh.3. human. [Q9NWU1-2]

Organism-specific databases

CTD54995.
GeneCardsGC03P025824.
HGNCHGNC:26063. OXSM.
HPAHPA021293.
HPA021300.
HPA021337.
MIM610324. gene.
neXtProtNX_Q9NWU1.
PharmGKBPA142671214.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0304.
HOGENOMHOG000060166.
HOVERGENHBG082096.
InParanoidQ9NWU1.
KOK09458.
OMAWMEPKEQ.
PhylomeDBQ9NWU1.

Enzyme and pathway databases

BRENDA2.3.1.41. 2681.
SABIO-RKQ9NWU1.
UniPathwayUPA00094.

Gene expression databases

ArrayExpressQ9NWU1.
BgeeQ9NWU1.
CleanExHS_OXSM.
GenevestigatorQ9NWU1.

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

EvolutionaryTraceQ9NWU1.
GenomeRNAi54995.
NextBio58306.
PROQ9NWU1.
SOURCESearch...

Entry information

Entry nameOXSM_HUMAN
AccessionPrimary (citable) accession number: Q9NWU1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: October 1, 2000
Last modified: March 19, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM