UniProt functional annotation for P04964



	UniProt functional annotation for P04964

UniProt code: P04964.

Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025).

Taxonomy: Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; Corynebacterium.

Function: Catalyzes the reversible NADPH-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L- tetrahydrodipicolinate, to generate the meso compound, D,L-2,6- diaminopimelate. Probably plays a role in lysine biosynthesis. Exhibits a high substrate specificity for meso-2,6-diaminopimelate, since L,L- 2,6-diaminopimelate, D,D-2,6-diaminopimelate, L-glutamate, L-alanine, L-leucine, L-valine, L-aspartate, L-threonine, L-homoserine, L- methionine, L-lysine, L-serine, L-phenylalanine, L-tyrosine, L- tryptophan, L-ornithine, L-histidine, L-arginine, D-glutamate, and D- alanine are not substrates for the oxidative deamination reaction. Can use NAD(+) only poorly since the activity observed in the presence of NAD(+) is about 3% of that with NADP(+). {ECO:0000269|PubMed:8865347, ECO:0000269|Ref.4}.

Catalytic activity: Reaction=H2O + meso-2,6-diaminoheptanedioate + NADP(+) = (S)-2-amino-6- oxoheptanedioate + H(+) + NADPH + NH4(+); Xref=Rhea:RHEA:13561, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57783, ChEBI:CHEBI:57791, ChEBI:CHEBI:58349, ChEBI:CHEBI:58556; EC=1.4.1.16; Evidence={ECO:0000269|PubMed:8865347, ECO:0000269|Ref.4};

Activity regulation: L,L-2,6-diaminopimelate and D,D-2,6- diaminopimelate competitively inhibit the oxidative deamination of meso-2,6-diaminopimelate. The enzyme is also inhibited by L-cysteine, and by p-chloromercuribenzoate, iodoacetic acid and HgCl(2) in vitro. {ECO:0000269|Ref.4}.

Biophysicochemical properties: Kinetic parameters: KM=3.1 mM for meso-2,6-diaminoheptanedioate {ECO:0000269|Ref.4}; KM=0.12 mM for NADP(+) {ECO:0000269|Ref.4}; KM=0.13 mM for NADPH {ECO:0000269|Ref.4}; KM=0.28 mM for L-2-amino-6-oxoheptanedioate {ECO:0000269|Ref.4}; KM=36 mM for ammonia {ECO:0000269|Ref.4}; pH dependence: Optimum pH is about 9.8 for the oxidative deamination of meso- diaminopimelate and 7.9 for the reductive amination of L-2-amino-6- oxopimelate. {ECO:0000269|Ref.4};

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

Subunit: Homodimer. {ECO:0000269|PubMed:11106178, ECO:0000269|PubMed:8865347, ECO:0000269|PubMed:8885833, ECO:0000269|PubMed:9521647, ECO:0000269|Ref.4}.

Domain: Is composed of three domains: a dinucleotide binding domain, a dimerization domain, and a substrate-binding domain. {ECO:0000269|PubMed:8885833}.

Mass spectrometry: Mass=35198; Method=Electrospray; Evidence={ECO:0000269|PubMed:8865347};

Similarity: Belongs to the diaminopimelate dehydrogenase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025).
Taxonomy:		Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; Corynebacterium.



Function:		Catalyzes the reversible NADPH-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L- tetrahydrodipicolinate, to generate the meso compound, D,L-2,6- diaminopimelate. Probably plays a role in lysine biosynthesis. Exhibits a high substrate specificity for meso-2,6-diaminopimelate, since L,L- 2,6-diaminopimelate, D,D-2,6-diaminopimelate, L-glutamate, L-alanine, L-leucine, L-valine, L-aspartate, L-threonine, L-homoserine, L- methionine, L-lysine, L-serine, L-phenylalanine, L-tyrosine, L- tryptophan, L-ornithine, L-histidine, L-arginine, D-glutamate, and D- alanine are not substrates for the oxidative deamination reaction. Can use NAD(+) only poorly since the activity observed in the presence of NAD(+) is about 3% of that with NADP(+). {ECO:0000269\|PubMed:8865347, ECO:0000269\|Ref.4}.


Catalytic activity:		Reaction=H2O + meso-2,6-diaminoheptanedioate + NADP(+) = (S)-2-amino-6- oxoheptanedioate + H(+) + NADPH + NH4(+); Xref=Rhea:RHEA:13561, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57783, ChEBI:CHEBI:57791, ChEBI:CHEBI:58349, ChEBI:CHEBI:58556; EC=1.4.1.16; Evidence={ECO:0000269\|PubMed:8865347, ECO:0000269\|Ref.4};
Activity regulation:		L,L-2,6-diaminopimelate and D,D-2,6- diaminopimelate competitively inhibit the oxidative deamination of meso-2,6-diaminopimelate. The enzyme is also inhibited by L-cysteine, and by p-chloromercuribenzoate, iodoacetic acid and HgCl(2) in vitro. {ECO:0000269\|Ref.4}.
Biophysicochemical properties:		Kinetic parameters: KM=3.1 mM for meso-2,6-diaminoheptanedioate {ECO:0000269\|Ref.4}; KM=0.12 mM for NADP(+) {ECO:0000269\|Ref.4}; KM=0.13 mM for NADPH {ECO:0000269\|Ref.4}; KM=0.28 mM for L-2-amino-6-oxoheptanedioate {ECO:0000269\|Ref.4}; KM=36 mM for ammonia {ECO:0000269\|Ref.4}; pH dependence: Optimum pH is about 9.8 for the oxidative deamination of meso- diaminopimelate and 7.9 for the reductive amination of L-2-amino-6- oxopimelate. {ECO:0000269\|Ref.4};
Pathway:		Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate: step 1/1.
Subunit:		Homodimer. {ECO:0000269\|PubMed:11106178, ECO:0000269\|PubMed:8865347, ECO:0000269\|PubMed:8885833, ECO:0000269\|PubMed:9521647, ECO:0000269\|Ref.4}.
Domain:		Is composed of three domains: a dinucleotide binding domain, a dimerization domain, and a substrate-binding domain. {ECO:0000269\|PubMed:8885833}.
Mass spectrometry:		Mass=35198; Method=Electrospray; Evidence={ECO:0000269\|PubMed:8865347};
Similarity:		Belongs to the diaminopimelate dehydrogenase family. {ECO:0000305}.