KASM_ARATH
ID KASM_ARATH Reviewed; 461 AA.
AC Q8L3X9; Q9SJB7;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial;
DE EC=2.3.1.41;
DE AltName: Full=Beta-ketoacyl-ACP synthase;
DE AltName: Full=mtKAS;
DE Flags: Precursor;
GN Name=KAS; OrderedLocusNames=At2g04540; ORFNames=T1O3.5;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=14660674; DOI=10.1074/jbc.m308894200;
RA Yasuno R., von Wettstein-Knowles P., Wada H.;
RT "Identification and molecular characterization of the beta-ketoacyl-[acyl
RT carrier-protein] synthase component of the Arabidopsis mitochondrial fatty
RT acid synthase.";
RL J. Biol. Chem. 279:8242-8251(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17616510; DOI=10.1104/pp.107.104000;
RA Ewald R., Kolukisaoglu U., Bauwe U., Mikkat S., Bauwe H.;
RT "Mitochondrial protein lipoylation does not exclusively depend on the mtKAS
RT pathway of de novo fatty acid synthesis in Arabidopsis.";
RL Plant Physiol. 145:41-48(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 31-461, AND SUBUNIT.
RX PubMed=15527780; DOI=10.1016/j.febslet.2004.10.007;
RA Olsen J.G., Rasmussen A.V., von Wettstein-Knowles P., Henriksen A.;
RT "Structure of the mitochondrial beta-ketoacyl-[acyl carrier-protein]
RT synthase from Arabidopsis and its role in fatty acid synthesis.";
RL FEBS Lett. 577:170-174(2004).
CC -!- FUNCTION: Catalyzes all the condensation reaction of fatty acid
CC synthesis by the addition to an acyl acceptor of two carbons from
CC malonyl-ACP. Able to elongate saturated acyl chains from 4 to at least
CC 16 carbons. Uses malonyl-CoA but not acetyl-CoA as primer substrate.
CC When expressed in a heterologous system, reveals a bimodal distribution
CC of products, with peaks at C8 and C14-C16. The major product of the
CC reaction (octanoyl-ACP) is required for the lipoylation of essential
CC mitochondrial proteins. {ECO:0000269|PubMed:17616510}.
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;
CC -!- ACTIVITY REGULATION: Inhibited by cerulenin.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15527780}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14660674}.
CC -!- TISSUE SPECIFICITY: Expressed at the same level in leaves, roots and
CC flowers. {ECO:0000269|PubMed:14660674}.
CC -!- DISRUPTION PHENOTYPE: Slow growth and bleached leaf phenotype when
CC grown under ambient air, but normal growth under CO(2)-enriched air.
CC Highly prevents lipoylation of the H-protein subunit of the glycine
CC decarboxylase (GDC) in leaves, but has only a limited effect on the
CC lipoylation of the E2 subunits of pyruvate dehydrogenase (PDH) and
CC alpha-ketoacid dehydrogenase (KGDH) complexes in leaves and even no
CC effect in roots. {ECO:0000269|PubMed:17616510}.
CC -!- MISCELLANEOUS: Mitochondrial protein lipoylation in leaves does not
CC exclusively depend on the lipoate biosynthesis by KAS and may occur
CC independently of this pathway in roots. {ECO:0000305|PubMed:17616510}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25826.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB073746; BAB91181.1; -; mRNA.
DR EMBL; AC006951; AAD25826.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC05844.1; -; Genomic_DNA.
DR EMBL; AY099587; AAM20439.1; -; mRNA.
DR EMBL; AY128832; AAM91232.1; -; mRNA.
DR PIR; F84458; F84458.
DR RefSeq; NP_178533.2; NM_126485.4.
DR PDB; 1W0I; X-ray; 2.10 A; A/B=31-461.
DR PDB; 2IX4; X-ray; 1.95 A; A/B=31-461.
DR PDBsum; 1W0I; -.
DR PDBsum; 2IX4; -.
DR AlphaFoldDB; Q8L3X9; -.
DR SMR; Q8L3X9; -.
DR STRING; 3702.AT2G04540.1; -.
DR iPTMnet; Q8L3X9; -.
DR PaxDb; Q8L3X9; -.
DR PRIDE; Q8L3X9; -.
DR ProteomicsDB; 232273; -.
DR EnsemblPlants; AT2G04540.1; AT2G04540.1; AT2G04540.
DR GeneID; 814996; -.
DR Gramene; AT2G04540.1; AT2G04540.1; AT2G04540.
DR KEGG; ath:AT2G04540; -.
DR Araport; AT2G04540; -.
DR TAIR; locus:2058359; AT2G04540.
DR eggNOG; KOG1394; Eukaryota.
DR HOGENOM; CLU_000022_69_2_1; -.
DR InParanoid; Q8L3X9; -.
DR OMA; QIGHCLG; -.
DR OrthoDB; 1014523at2759; -.
DR PhylomeDB; Q8L3X9; -.
DR BioCyc; ARA:AT2G04540-MON; -.
DR BioCyc; MetaCyc:AT2G04540-MON; -.
DR BRENDA; 2.3.1.41; 399.
DR UniPathway; UPA00094; -.
DR EvolutionaryTrace; Q8L3X9; -.
DR PRO; PR:Q8L3X9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8L3X9; baseline and differential.
DR Genevisible; Q8L3X9; AT.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0010027; P:thylakoid membrane organization; IMP:TAIR.
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; Acyltransferase; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Mitochondrion;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 29..461
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase,
FT mitochondrial"
FT /id="PRO_0000000588"
FT ACT_SITE 209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT STRAND 33..42
FT /evidence="ECO:0007829|PDB:2IX4"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:2IX4"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:2IX4"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:2IX4"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 117..132
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:2IX4"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 179..183
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 211..225
FT /evidence="ECO:0007829|PDB:2IX4"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 242..250
FT /evidence="ECO:0007829|PDB:2IX4"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:2IX4"
FT STRAND 281..289
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 290..295
FT /evidence="ECO:0007829|PDB:2IX4"
FT STRAND 302..311
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 324..337
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:2IX4"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 355..369
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 371..374
FT /evidence="ECO:0007829|PDB:2IX4"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:2IX4"
FT HELIX 394..408
FT /evidence="ECO:0007829|PDB:2IX4"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:2IX4"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:2IX4"
FT STRAND 440..448
FT /evidence="ECO:0007829|PDB:2IX4"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:2IX4"
FT STRAND 452..459
FT /evidence="ECO:0007829|PDB:2IX4"
SQ SEQUENCE 461 AA; 49379 MW; D9B02B19F5A5FB45 CRC64;
MATSNLRRHL SASRLRLNRF ISTSSSYHSH RRVVVTGLGM VTPLGRGVET TWRRLIDGEC
GIRGLTLDDL KMKSFDEETK LYTFDQLSSK VAAFVPYGSN PGEFDEALWL NSKAVANFIG
YAVCAADEAL RDAEWLPTEE EEKERTGVSI GGGIGSICDI VEAAQLICEK RLRRLSPFFI
PKILVNMASG HVSMKYGFQG PNHAAVTACA TGAHSIGDAT RMIQFGDADV MVAGGTESSI
DALSVAGFSR SRALSTKFNS SPQEASRPFD CDRDGFVIGE GSGVIVLEEY EHAKRRGAKI
YAELCGYGMS GDAHHITQPP EDGKGAVLAM TRALRQSGLC PNQIDYVNAH ATSTPIGDAV
EARAIKTVFS EHATSGTLAF SSTKGATGHL LGAAGAVEAI FSILAIHHGV APMTLNVKNP
DPIFDKRFMP LTTSKKMLVR TAMSNSFGFG GTNASLLFAS I
