ID   OXSM_HUMAN              Reviewed;         459 AA.
AC   Q9NWU1;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial {ECO:0000305};
DE            EC=2.3.1.41 {ECO:0000269|PubMed:15668256};
DE   AltName: Full=Beta-ketoacyl-ACP synthase;
DE   Flags: Precursor;
GN   Name=OXSM {ECO:0000312|HGNC:HGNC:26063};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Carcinoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY,
RP   ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=15668256; DOI=10.1074/jbc.m413686200;
RA   Zhang L., Joshi A.K., Hofmann J., Schweizer E., Smith S.;
RT   "Cloning, expression, and characterization of the human mitochondrial beta-
RT   ketoacyl synthase. Complementation of the yeast CEM1 knock-out strain.";
RL   J. Biol. Chem. 280:12422-12429(2005).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-174, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 39-459.
RA   Bunkoczi G., Wu X., Smee C., Gileadi O., Arrowsmith C., Edwards A.,
RA   Sundstrom M., Weigelt J., von Delft F., Oppermann U.;
RT   "Structure of mitochondrial beta-ketoacyl synthase.";
RL   Submitted (DEC-2005) to the PDB data bank.
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 38-459.
RX   PubMed=17242430; DOI=10.1110/ps.062473707;
RA   Christensen C.E., Kragelund B.B., von Wettstein-Knowles P., Henriksen A.;
RT   "Structure of the human beta-ketoacyl [ACP] synthase from the mitochondrial
RT   type II fatty acid synthase.";
RL   Protein Sci. 16:261-272(2007).
RN   [9]
RP   VARIANT [LARGE SCALE ANALYSIS] ILE-106.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: May play a role in the biosynthesis of lipoic acid as well as
CC       longer chain fatty acids required for optimal mitochondrial function.
CC       {ECO:0000269|PubMed:15668256}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC         + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC         EC=2.3.1.41; Evidence={ECO:0000269|PubMed:15668256};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837;
CC         Evidence={ECO:0000305|PubMed:15668256};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=butanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxohexanoyl-[ACP] +
CC         CO2 + holo-[ACP]; Xref=Rhea:RHEA:41820, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9628, Rhea:RHEA-COMP:9629, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78454, ChEBI:CHEBI:78456;
CC         Evidence={ECO:0000269|PubMed:15668256};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41821;
CC         Evidence={ECO:0000305|PubMed:15668256};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hexanoyl-[ACP] + malonyl-[ACP] = 3-oxooctanoyl-[ACP] +
CC         CO2 + holo-[ACP]; Xref=Rhea:RHEA:41836, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9632, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78459, ChEBI:CHEBI:78460;
CC         Evidence={ECO:0000269|PubMed:15668256};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41837;
CC         Evidence={ECO:0000305|PubMed:15668256};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + malonyl-[ACP] + octanoyl-[ACP] = 3-oxodecanoyl-[ACP] +
CC         CO2 + holo-[ACP]; Xref=Rhea:RHEA:41852, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78463, ChEBI:CHEBI:78464;
CC         Evidence={ECO:0000269|PubMed:15668256};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41853;
CC         Evidence={ECO:0000305|PubMed:15668256};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=decanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxododecanoyl-[ACP]
CC         + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41868, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9640, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78468, ChEBI:CHEBI:78469;
CC         Evidence={ECO:0000269|PubMed:15668256};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41869;
CC         Evidence={ECO:0000305|PubMed:15668256};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dodecanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxotetradecanoyl-
CC         [ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41884, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:65264, ChEBI:CHEBI:78449, ChEBI:CHEBI:78473;
CC         Evidence={ECO:0000269|PubMed:15668256};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41885;
CC         Evidence={ECO:0000305|PubMed:15668256};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + malonyl-[ACP] + tetradecanoyl-[ACP] = 3-
CC         oxohexadecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41900,
CC         Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9649,
CC         Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78477,
CC         ChEBI:CHEBI:78478; Evidence={ECO:0000269|PubMed:15668256};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41901;
CC         Evidence={ECO:0000305|PubMed:15668256};
CC   -!- ACTIVITY REGULATION: Inhibited by cerulenin.
CC       {ECO:0000269|PubMed:15668256}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.9 uM for C4-[acyl-carrier-protein]
CC         {ECO:0000269|PubMed:15668256};
CC         KM=1.9 uM for C6-[acyl-carrier-protein]
CC         {ECO:0000269|PubMed:15668256};
CC         KM=10.9 uM for C8-[acyl-carrier-protein]
CC         {ECO:0000269|PubMed:15668256};
CC         KM=1.8 uM for C10-[acyl-carrier-protein]
CC         {ECO:0000269|PubMed:15668256};
CC         KM=9.5 uM for C12-[acyl-carrier-protein]
CC         {ECO:0000269|PubMed:15668256};
CC         KM=50.8 uM for C14-[acyl-carrier-protein]
CC         {ECO:0000269|PubMed:15668256};
CC         Vmax=129 nmol/min/mg enzyme toward C4-[acyl-carrier-protein]
CC         {ECO:0000269|PubMed:15668256};
CC         Vmax=241 nmol/min/mg enzyme toward C6-[acyl-carrier-protein]
CC         {ECO:0000269|PubMed:15668256};
CC         Vmax=271 nmol/min/mg enzyme toward C8-[acyl-carrier-protein]
CC         {ECO:0000269|PubMed:15668256};
CC         Vmax=364 nmol/min/mg enzyme toward C10-[acyl-carrier-protein]
CC         {ECO:0000269|PubMed:15668256};
CC         Vmax=1045 nmol/min/mg enzyme toward C12-[acyl-carrier-protein]
CC         {ECO:0000269|PubMed:15668256};
CC         Vmax=115 nmol/min/mg enzyme toward C14-[acyl-carrier-protein]
CC         {ECO:0000269|PubMed:15668256};
CC         Note=The highest catalytic efficiency is observed for
CC         C10-[acyl-carrier-protein].;
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15668256}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NWU1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NWU1-2; Sequence=VSP_041671;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Higher expression in heart,
CC       skeletal muscle, liver and kidney which contain high levels of active
CC       mitochondria. {ECO:0000269|PubMed:15668256}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000305}.
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DR   EMBL; AK000611; BAA91286.1; -; mRNA.
DR   EMBL; AK225260; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC092798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC008202; AAH08202.1; -; mRNA.
DR   CCDS; CCDS2643.1; -. [Q9NWU1-1]
DR   CCDS; CCDS46780.1; -. [Q9NWU1-2]
DR   RefSeq; NP_001138863.1; NM_001145391.1. [Q9NWU1-2]
DR   RefSeq; NP_060367.1; NM_017897.2. [Q9NWU1-1]
DR   RefSeq; XP_006713279.1; XM_006713216.3. [Q9NWU1-1]
DR   RefSeq; XP_016862202.1; XM_017006713.1.
DR   PDB; 2C9H; X-ray; 1.80 A; A=39-459.
DR   PDB; 2IWY; X-ray; 2.06 A; A/B=38-459.
DR   PDB; 2IWZ; X-ray; 1.65 A; A/B=38-459.
DR   PDBsum; 2C9H; -.
DR   PDBsum; 2IWY; -.
DR   PDBsum; 2IWZ; -.
DR   AlphaFoldDB; Q9NWU1; -.
DR   SMR; Q9NWU1; -.
DR   BioGRID; 120328; 57.
DR   IntAct; Q9NWU1; 10.
DR   MINT; Q9NWU1; -.
DR   STRING; 9606.ENSP00000280701; -.
DR   SwissLipids; SLP:000001258; -.
DR   iPTMnet; Q9NWU1; -.
DR   PhosphoSitePlus; Q9NWU1; -.
DR   SwissPalm; Q9NWU1; -.
DR   BioMuta; OXSM; -.
DR   DMDM; 74753030; -.
DR   EPD; Q9NWU1; -.
DR   jPOST; Q9NWU1; -.
DR   MassIVE; Q9NWU1; -.
DR   MaxQB; Q9NWU1; -.
DR   PaxDb; 9606-ENSP00000280701; -.
DR   PeptideAtlas; Q9NWU1; -.
DR   ProteomicsDB; 82980; -. [Q9NWU1-1]
DR   ProteomicsDB; 82981; -. [Q9NWU1-2]
DR   Pumba; Q9NWU1; -.
DR   Antibodypedia; 11437; 243 antibodies from 22 providers.
DR   DNASU; 54995; -.
DR   Ensembl; ENST00000280701.8; ENSP00000280701.3; ENSG00000151093.8. [Q9NWU1-1]
DR   Ensembl; ENST00000420173.2; ENSP00000411303.2; ENSG00000151093.8. [Q9NWU1-2]
DR   GeneID; 54995; -.
DR   KEGG; hsa:54995; -.
DR   MANE-Select; ENST00000280701.8; ENSP00000280701.3; NM_017897.3; NP_060367.1.
DR   UCSC; uc003cdn.4; human. [Q9NWU1-1]
DR   AGR; HGNC:26063; -.
DR   CTD; 54995; -.
DR   DisGeNET; 54995; -.
DR   GeneCards; OXSM; -.
DR   HGNC; HGNC:26063; OXSM.
DR   HPA; ENSG00000151093; Low tissue specificity.
DR   MIM; 610324; gene.
DR   neXtProt; NX_Q9NWU1; -.
DR   OpenTargets; ENSG00000151093; -.
DR   PharmGKB; PA142671214; -.
DR   VEuPathDB; HostDB:ENSG00000151093; -.
DR   eggNOG; KOG1394; Eukaryota.
DR   GeneTree; ENSGT00940000157768; -.
DR   HOGENOM; CLU_000022_69_2_1; -.
DR   InParanoid; Q9NWU1; -.
DR   OMA; ESTICPV; -.
DR   OrthoDB; 546841at2759; -.
DR   PhylomeDB; Q9NWU1; -.
DR   BioCyc; MetaCyc:HS07707-MONOMER; -.
DR   BRENDA; 2.3.1.41; 2681.
DR   PathwayCommons; Q9NWU1; -.
DR   SABIO-RK; Q9NWU1; -.
DR   SignaLink; Q9NWU1; -.
DR   UniPathway; UPA00094; -.
DR   BioGRID-ORCS; 54995; 139 hits in 1167 CRISPR screens.
DR   ChiTaRS; OXSM; human.
DR   EvolutionaryTrace; Q9NWU1; -.
DR   GenomeRNAi; 54995; -.
DR   Pharos; Q9NWU1; Tbio.
DR   PRO; PR:Q9NWU1; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9NWU1; Protein.
DR   Bgee; ENSG00000151093; Expressed in right lobe of liver and 189 other cell types or tissues.
DR   ExpressionAtlas; Q9NWU1; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IDA:HGNC-UCL.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; IDA:HGNC-UCL.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0051792; P:medium-chain fatty acid biosynthetic process; IDA:HGNC-UCL.
DR   GO; GO:0051790; P:short-chain fatty acid biosynthetic process; IDA:HGNC-UCL.
DR   CDD; cd00834; KAS_I_II; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR017568; 3-oxoacyl-ACP_synth-2.
DR   InterPro; IPR000794; Beta-ketoacyl_synthase.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR03150; fabF; 1.
DR   PANTHER; PTHR11712:SF336; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11712; POLYKETIDE SYNTHASE-RELATED; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   PIRSF; PIRSF000447; KAS_II; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   Genevisible; Q9NWU1; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Acyltransferase; Alternative splicing;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Mitochondrion; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..27
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..459
FT                   /note="3-oxoacyl-[acyl-carrier-protein] synthase,
FT                   mitochondrial"
FT                   /id="PRO_0000232660"
FT   DOMAIN          41..458
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        209
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        348
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        385
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   MOD_RES         109
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D404"
FT   MOD_RES         109
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D404"
FT   MOD_RES         113
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D404"
FT   MOD_RES         174
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         174
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D404"
FT   VAR_SEQ         229..311
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_041671"
FT   VARIANT         106
FT                   /note="F -> I (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036064"
FT   STRAND          38..41
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   STRAND          44..53
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           59..67
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   STRAND          73..75
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   STRAND          88..90
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   STRAND          94..97
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           103..105
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           109..112
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           117..133
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           140..144
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   STRAND          146..153
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           157..170
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           172..174
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           179..182
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           187..196
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           208..210
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           211..225
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   STRAND          229..237
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           242..250
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   TURN            260..262
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   STRAND          279..287
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           288..293
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   STRAND          300..309
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   STRAND          314..316
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           322..335
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           339..341
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   STRAND          344..346
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           353..367
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           368..372
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   STRAND          374..377
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           380..383
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           387..389
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   HELIX           390..404
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   STRAND          426..428
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   STRAND          435..437
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   STRAND          439..446
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   TURN            447..449
FT                   /evidence="ECO:0007829|PDB:2IWZ"
FT   STRAND          450..457
FT                   /evidence="ECO:0007829|PDB:2IWZ"
SQ   SEQUENCE   459 AA;  48843 MW;  B2EF550CD354F18C CRC64;
     MSNCLQNFLK ITSTRLLCSR LCQQLRSKRK FFGTVPISRL HRRVVITGIG LVTPLGVGTH
     LVWDRLIGGE SGIVSLVGEE YKSIPCSVAA YVPRGSDEGQ FNEQNFVSKS DIKSMSSPTI
     MAIGAAELAM KDSGWHPQSE ADQVATGVAI GMGMIPLEVV SETALNFQTK GYNKVSPFFV
     PKILVNMAAG QVSIRYKLKG PNHAVSTACT TGAHAVGDSF RFIAHGDADV MVAGGTDSCI
     SPLSLAGFSR ARALSTNSDP KLACRPFHPK RDGFVMGEGA AVLVLEEYEH AVQRRARIYA
     EVLGYGLSGD AGHITAPDPE GEGALRCMAA ALKDAGVQPE EISYINAHAT STPLGDAAEN
     KAIKHLFKDH AYALAVSSTK GATGHLLGAA GAVEAAFTTL ACYYQKLPPT LNLDCSEPEF
     DLNYVPLKAQ EWKTEKRFIG LTNSFGFGGT NATLCIAGL
//