Information on EC 2.6.1.76 - diaminobutyrate-2-oxoglutarate transaminase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.6.1.76
-
RECOMMENDED NAME
GeneOntology No.
diaminobutyrate-2-oxoglutarate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-2,4-diaminobutanoate + 2-oxoglutarate = L-aspartate 4-semialdehyde + L-glutamate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ectoine biosynthesis
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norspermidine biosynthesis
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pyoverdine I biosynthesis
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rhizobactin 1021 biosynthesis
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threonine metabolism
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Glycine, serine and threonine metabolism
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Metabolic pathways
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
L-2,4-diaminobutanoate:2-oxoglutarate 4-aminotransferase
A pyridoxal-phosphate protein that requires potassium for activity [4]. In the proteobacterium Acinetobacter baumannii, this enzyme is cotranscribed with the neighbouring ddc gene that also encodes EC 4.1.1.86, diaminobutyrate decarboxylase. Differs from EC 2.6.1.46, diaminobutyrate---pyruvate transaminase, which has pyruvate as the amino-group acceptor. This is the first enzyme in the ectoine-biosynthesis pathway, the other enzymes involved being EC 2.3.1.178, diaminobutyrate acetyltransferase and EC 4.2.1.108, ectoine synthase [3,4].
CAS REGISTRY NUMBER
COMMENTARY hide
196622-96-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
3 ATCC 19004
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Manually annotated by BRENDA team
ATCC 17906
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Manually annotated by BRENDA team
ATCC 17909
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-
Manually annotated by BRENDA team
ATCC 17908
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-
Manually annotated by BRENDA team
ATCC 15309
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-
Manually annotated by BRENDA team
IAM13186
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Manually annotated by BRENDA team
Rd, types a, b, d, e, f
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-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-aminobutanoate + 2-oxoglutarate
? + L-glutamate
show the reaction diagram
beta-alanine + 2-oxoglutaric acid
?
show the reaction diagram
-
-
-
-
?
L-2,4-diaminobutanoate + 2-oxoglutarate
L-aspartate 4-semialdehyde + L-glutamate
show the reaction diagram
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
L-glutamic acid + L-aspartic beta-semialdehyde
show the reaction diagram
L-aspartate 4-semialdehyde + L-glutamate
L-2,4-diaminobutanoate + 2-oxoglutarate
show the reaction diagram
L-aspartate 4-semialdehyde + L-homoserine
L-2,4-diaminobutanoate + 2-oxoglutarate
show the reaction diagram
about 5% of the activity with L-glutamate
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-
r
L-glutamic acid + L-aspartic beta-semialdehyde
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
show the reaction diagram
L-lysine + oxaloacetic acid
?
show the reaction diagram
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-
-
-
?
L-ornithine + 2-oxoglutarate
? + L-glutamate
show the reaction diagram
L-ornithine + pyruvic acid
?
show the reaction diagram
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.46
2-oxoglutaric acid
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4.3
L-2,4-diaminobutyric acid
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4.5
L-aspartate 4-semialdehyde
pH 8.5, 25°C
9.1
L-glutamate
pH 8.5, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12
pH 8.5, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
isoelectric focussing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47420
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deduced from nucleotide sequence
49400
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predicted from amino acid sequence, gene HI0949
56200
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predicted from amino acid sequence, gene HI946
188000
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native enzyme, gel filtration
260000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
tetramer
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4 * 45000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, overexpressed in Escherichia coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Escherichia coli clone carrying the dat homolog of H. influenzae
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homologs of dat detected by PCR amplification
identification and analysis of the dat gene encoding L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase with Escherichia coli transformants
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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