OXSM_HUMAN
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 03-AUG-2022, entry version 164.
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 C10-[acyl-
CC 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; 53.
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; Q9NWU1; -.
DR PeptideAtlas; Q9NWU1; -.
DR PRIDE; Q9NWU1; -.
DR ProteomicsDB; 82980; -. [Q9NWU1-1]
DR ProteomicsDB; 82981; -. [Q9NWU1-2]
DR Antibodypedia; 11437; 214 antibodies from 21 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 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; QIGHCLG; -.
DR PhylomeDB; Q9NWU1; -.
DR BioCyc; MetaCyc:HS07707-MON; -.
DR BRENDA; 2.3.1.41; 2681.
DR PathwayCommons; Q9NWU1; -.
DR SABIO-RK; Q9NWU1; -.
DR SignaLink; Q9NWU1; -.
DR UniPathway; UPA00094; -.
DR BioGRID-ORCS; 54995; 124 hits in 1086 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 187 other tissues.
DR ExpressionAtlas; Q9NWU1; baseline and differential.
DR Genevisible; Q9NWU1; HS.
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 PANTHER; PTHR11712; PTHR11712; 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; SSF53901; 2.
DR TIGRFAMs; TIGR03150; fabF; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
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 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
