Q9NWU1 (OXSM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
EC=2.3.1.41

Alternative name(s):
Beta-ketoacyl-ACP synthase

Gene names

Name:

OXSM

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	459 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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]

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transit peptide
Molecular function	Acyltransferase Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acyl-CoA metabolic process Inferred from direct assay Ref.4. Source: HGNC medium-chain fatty acid biosynthetic process Inferred from direct assay Ref.4. Source: HGNC short-chain fatty acid biosynthetic process Inferred from direct assay Ref.4. Source: HGNC
Cellular_component	mitochondrion Inferred from direct assay. Source: LIFEdb
Molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from direct assay Ref.4. Source: HGNC
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 27

27

Mitochondrion Potential

Chain

28 – 459

432

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

PRO_0000232660

Amino acid modifications

Modified residue

174

1

N6-acetyllysine Ref.5

Natural variations

Alternative sequence

229 – 311

83

Missing in isoform 2.

VSP_041671

Natural variant

106

1

F → I in a breast cancer sample; somatic mutation. Ref.9

VAR_036064

Secondary structure

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459

Helix Strand Turn

Details...

Beta strand

38 – 41

4

Beta strand

44 – 53

10

Beta strand

56 – 58

3

Helix

59 – 67

9

Beta strand

73 – 75

3

Helix

79 – 81

3

Beta strand

88 – 90

3

Beta strand

94 – 97

4

Helix

103 – 105

3

Helix

109 – 112

4

Helix

117 – 133

17

Helix

140 – 144

5

Beta strand

146 – 153

8

Helix

157 – 170

14

Helix

172 – 174

3

Helix

179 – 182

4

Helix

187 – 196

10

Helix

208 – 210

3

Helix

211 – 225

15

Beta strand

229 – 237

9

Helix

242 – 250

9

Turn

260 – 262

3

Beta strand

279 – 287

9

Helix

288 – 293

6

Beta strand

300 – 309

10

Beta strand

314 – 316

3

Helix

322 – 335

14

Helix

339 – 341

3

Beta strand

344 – 346

3

Helix

353 – 367

15

Helix

368 – 372

5

Beta strand

374 – 377

4

Helix

380 – 383

4

Helix

387 – 389

3

Helix

390 – 404

15

Beta strand

426 – 428

3

Beta strand

435 – 437

3

Beta strand

439 – 446

8

Turn

447 – 449

3

Beta strand

450 – 457

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: B2EF550CD354F18C	FASTA	459	48,843
	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
	Isoform 2 [UniParc]. Checksum: B9470D089DE7CF7D	FASTA	376	40,035
	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 RFIAHGDAGH ITAPDPEGEG 250 260 270 280 290 300 ALRCMAAALK DAGVQPEEIS YINAHATSTP LGDAAENKAI KHLFKDHAYA LAVSSTKGAT 310 320 330 340 350 360 GHLLGAAGAV EAAFTTLACY YQKLPPTLNL DCSEPEFDLN YVPLKAQEWK TEKRFIGLTN 370 SFGFGGTNAT LCIAGL

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY.
[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. , 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.

IPI

IPI00016637.
IPI00922369.

RefSeq

NP_001138863.1. NM_001145391.1.
NP_060367.1. NM_017897.2.

UniGene

Hs.55781.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C9H	X-ray	1.80	A	39-459	[»]
2IWY	X-ray	2.06	A/B	38-459	[»]
2IWZ	X-ray	1.65	A/B	38-459	[»]

ProteinModelPortal

Q9NWU1.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000280701.

PTM databases

PhosphoSite

Q9NWU1.

Polymorphism databases

DMDM

74753030.

Proteomic databases

PaxDb

Q9NWU1.

PeptideAtlas

Q9NWU1.

PRIDE

Q9NWU1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000280701; ENSP00000280701; ENSG00000151093.
ENST00000420173; ENSP00000411303; ENSG00000151093.

GeneID

54995.

KEGG

hsa:54995.

UCSC

uc003cdn.3. human.

Organism-specific databases

CTD

54995.

GeneCards

GC03P025824.

HGNC

HGNC:26063. OXSM.

HPA

HPA021293.
HPA021300.
HPA021337.

MIM

610324. gene.

neXtProt

NX_Q9NWU1.

PharmGKB

PA142671214.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0304.

HOGENOM

HOG000060166.

HOVERGEN

HBG082096.

InParanoid

Q9NWU1.

KO

K09458.

OMA

MSSPTIM.

PhylomeDB

Q9NWU1.

Enzyme and pathway databases

BRENDA

2.3.1.41. 2681.

SABIO-RK

Q9NWU1.

UniPathway

UPA00094.

Gene expression databases

ArrayExpress

Q9NWU1.

Bgee

Q9NWU1.

CleanEx

HS_OXSM.

Genevestigator

Q9NWU1.

GermOnline

ENSG00000151093. Homo sapiens.

Family and domain databases

Gene3D

3.40.47.10. 2 hits.

InterPro

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]

Pfam

PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]

PIRSF

PIRSF000447. KAS_II. 1 hit.

SUPFAM

SSF53901. Thiolase-like. 2 hits.

TIGRFAMs

TIGR03150. fabF. 1 hit.

PROSITE

PS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9NWU1.

GenomeRNAi

54995.

NextBio

58306.

SOURCE

Search...

Entry information

Entry name

OXSM_HUMAN

Accession

Primary (citable) accession number: Q9NWU1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2006
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.