UniProt functional annotation for Q93ZN9



	UniProt functional annotation for Q93ZN9

UniProt code: Q93ZN9.

Organism: Arabidopsis thaliana (Mouse-ear cress).

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

Function: Required for lysine biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate, a reaction that requires three enzymes in E.coli. Not active with meso- diaminopimelate, lysine or ornithine as substrates. {ECO:0000269|PubMed:16361515, ECO:0000269|PubMed:17583737, ECO:0000269|PubMed:18952095, ECO:0000269|PubMed:21435399}.

Catalytic activity: Reaction=(2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)- 2,3,4,5-tetrahydrodipicolinate + H(+) + H2O + L-glutamate; Xref=Rhea:RHEA:23988, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:16845, ChEBI:CHEBI:29985, ChEBI:CHEBI:57609; EC=2.6.1.83; Evidence={ECO:0000269|PubMed:16361515, ECO:0000269|PubMed:17583737};

Cofactor: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:17583737, ECO:0000269|PubMed:18952095};

Biophysicochemical properties: Kinetic parameters: KM=47 uM for LL-2,6-diaminopimelate {ECO:0000269|PubMed:17583737}; KM=67 uM for LL-2,6-diaminopimelate {ECO:0000269|PubMed:16361515}; KM=8.7 mM for 2-oxoglutarate {ECO:0000269|PubMed:16361515}; KM=38 uM for L-2,3,4,5-tetrahydrodipicolinate {ECO:0000269|PubMed:16361515}; KM=1.9 mM for glutamatic acid {ECO:0000269|PubMed:16361515}; Vmax=22.3 umol/min/mg enzyme for the forward reaction {ECO:0000269|PubMed:16361515}; Vmax=0.38 umol/min/mg enzyme for the reverse reaction {ECO:0000269|PubMed:16361515}; pH dependence: Optimum pH is 7.9 in Tris buffer and 7.6 in HEPES buffer. {ECO:0000269|PubMed:16361515}; Temperature dependence: Optimum temperature is 36 degrees Celsius. {ECO:0000269|PubMed:16361515};

Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route): step 1/1.

Subunit: Homodimer. {ECO:0000269|PubMed:17583737, ECO:0000269|PubMed:18952095}.

Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:14729919}.

Tissue specificity: Highly expressed in seedlings, roots, stems, flowers and leaves. Lower expression in siliques. {ECO:0000269|PubMed:14729919}.

Developmental stage: Down-regulated during senescence. {ECO:0000269|PubMed:14729919}.

Induction: Not induced by pathogen infection, but down-regulated by dark treatment. {ECO:0000269|PubMed:14729919}.

Disruption phenotype: Embryonic lethality. {ECO:0000269|PubMed:14729919}.

Miscellaneous: The expected covalent binding of pyridoxal phosphate by Lys-305 has not been observed in the 3D-structure.

Similarity: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. LL-diaminopimelate aminotransferase subfamily. {ECO:0000305}.

Sequence caution: Sequence=CAA20581.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; Sequence=CAB80085.1; 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:		Required for lysine biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate, a reaction that requires three enzymes in E.coli. Not active with meso- diaminopimelate, lysine or ornithine as substrates. {ECO:0000269\|PubMed:16361515, ECO:0000269\|PubMed:17583737, ECO:0000269\|PubMed:18952095, ECO:0000269\|PubMed:21435399}.


Catalytic activity:		Reaction=(2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)- 2,3,4,5-tetrahydrodipicolinate + H(+) + H2O + L-glutamate; Xref=Rhea:RHEA:23988, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:16845, ChEBI:CHEBI:29985, ChEBI:CHEBI:57609; EC=2.6.1.83; Evidence={ECO:0000269\|PubMed:16361515, ECO:0000269\|PubMed:17583737};
Cofactor:		Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269\|PubMed:17583737, ECO:0000269\|PubMed:18952095};
Biophysicochemical properties:		Kinetic parameters: KM=47 uM for LL-2,6-diaminopimelate {ECO:0000269\|PubMed:17583737}; KM=67 uM for LL-2,6-diaminopimelate {ECO:0000269\|PubMed:16361515}; KM=8.7 mM for 2-oxoglutarate {ECO:0000269\|PubMed:16361515}; KM=38 uM for L-2,3,4,5-tetrahydrodipicolinate {ECO:0000269\|PubMed:16361515}; KM=1.9 mM for glutamatic acid {ECO:0000269\|PubMed:16361515}; Vmax=22.3 umol/min/mg enzyme for the forward reaction {ECO:0000269\|PubMed:16361515}; Vmax=0.38 umol/min/mg enzyme for the reverse reaction {ECO:0000269\|PubMed:16361515}; pH dependence: Optimum pH is 7.9 in Tris buffer and 7.6 in HEPES buffer. {ECO:0000269\|PubMed:16361515}; Temperature dependence: Optimum temperature is 36 degrees Celsius. {ECO:0000269\|PubMed:16361515};
Pathway:		Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route): step 1/1.
Subunit:		Homodimer. {ECO:0000269\|PubMed:17583737, ECO:0000269\|PubMed:18952095}.
Subcellular location:		Plastid, chloroplast {ECO:0000269\|PubMed:14729919}.
Tissue specificity:		Highly expressed in seedlings, roots, stems, flowers and leaves. Lower expression in siliques. {ECO:0000269\|PubMed:14729919}.
Developmental stage:		Down-regulated during senescence. {ECO:0000269\|PubMed:14729919}.
Induction:		Not induced by pathogen infection, but down-regulated by dark treatment. {ECO:0000269\|PubMed:14729919}.
Disruption phenotype:		Embryonic lethality. {ECO:0000269\|PubMed:14729919}.
Miscellaneous:		The expected covalent binding of pyridoxal phosphate by Lys-305 has not been observed in the 3D-structure.
Similarity:		Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. LL-diaminopimelate aminotransferase subfamily. {ECO:0000305}.
Sequence caution:		Sequence=CAA20581.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; Sequence=CAB80085.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};