UniProt functional annotation for Q8L3X9



	UniProt functional annotation for Q8L3X9

UniProt code: Q8L3X9.

Organism: Arabidopsis thaliana (Mouse-ear cress).

Taxonomy: Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.

Function: Catalyzes all the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Able to elongate saturated acyl chains from 4 to at least 16 carbons. Uses malonyl-CoA but not acetyl-CoA as primer substrate. When expressed in a heterologous system, reveals a bimodal distribution of products, with peaks at C8 and C14-C16. The major product of the reaction (octanoyl-ACP) is required for the lipoylation of essential mitochondrial proteins. {ECO:0000269|PubMed:17616510}.

Catalytic activity: Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651; EC=2.3.1.41;

Activity regulation: Inhibited by cerulenin.

Pathway: Lipid metabolism; fatty acid biosynthesis.

Subunit: Homodimer. {ECO:0000269|PubMed:15527780}.

Subcellular location: Mitochondrion {ECO:0000269|PubMed:14660674}.

Tissue specificity: Expressed at the same level in leaves, roots and flowers. {ECO:0000269|PubMed:14660674}.

Disruption phenotype: Slow growth and bleached leaf phenotype when grown under ambient air, but normal growth under CO(2)-enriched air. Highly prevents lipoylation of the H-protein subunit of the glycine decarboxylase (GDC) in leaves, but has only a limited effect on the lipoylation of the E2 subunits of pyruvate dehydrogenase (PDH) and alpha-ketoacid dehydrogenase (KGDH) complexes in leaves and even no effect in roots. {ECO:0000269|PubMed:17616510}.

Miscellaneous: Mitochondrial protein lipoylation in leaves does not exclusively depend on the lipoate biosynthesis by KAS and may occur independently of this pathway in roots. {ECO:0000305|PubMed:17616510}.

Similarity: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. {ECO:0000305}.

Sequence caution: Sequence=AAD25826.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Arabidopsis thaliana (Mouse-ear cress).
Taxonomy:		Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.



Function:		Catalyzes all the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Able to elongate saturated acyl chains from 4 to at least 16 carbons. Uses malonyl-CoA but not acetyl-CoA as primer substrate. When expressed in a heterologous system, reveals a bimodal distribution of products, with peaks at C8 and C14-C16. The major product of the reaction (octanoyl-ACP) is required for the lipoylation of essential mitochondrial proteins. {ECO:0000269\|PubMed:17616510}.


Catalytic activity:		Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651; EC=2.3.1.41;
Activity regulation:		Inhibited by cerulenin.
Pathway:		Lipid metabolism; fatty acid biosynthesis.
Subunit:		Homodimer. {ECO:0000269\|PubMed:15527780}.
Subcellular location:		Mitochondrion {ECO:0000269\|PubMed:14660674}.
Tissue specificity:		Expressed at the same level in leaves, roots and flowers. {ECO:0000269\|PubMed:14660674}.
Disruption phenotype:		Slow growth and bleached leaf phenotype when grown under ambient air, but normal growth under CO(2)-enriched air. Highly prevents lipoylation of the H-protein subunit of the glycine decarboxylase (GDC) in leaves, but has only a limited effect on the lipoylation of the E2 subunits of pyruvate dehydrogenase (PDH) and alpha-ketoacid dehydrogenase (KGDH) complexes in leaves and even no effect in roots. {ECO:0000269\|PubMed:17616510}.
Miscellaneous:		Mitochondrial protein lipoylation in leaves does not exclusively depend on the lipoate biosynthesis by KAS and may occur independently of this pathway in roots. {ECO:0000305\|PubMed:17616510}.
Similarity:		Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. {ECO:0000305}.
Sequence caution:		Sequence=AAD25826.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};