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Information on EC 4.1.1.86 - diaminobutyrate decarboxylase and Organism(s) Acinetobacter baumannii and UniProt Accession Q43908

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.86 diaminobutyrate decarboxylase
IUBMB Comments
A pyridoxal-phosphate protein that requires a divalent cation for activity . N4-Acetyl-L-2,4-diaminobutanoate, 2,3-diaminopropanoate, ornithine and lysine are not substrates. Found in the proteobacteria Haemophilus influenzae and Acinetobacter baumannii. In the latter, this enzyme is cotranscribed with the dat gene that encodes EC 2.6.1.76, diaminobutyrate---2-oxoglutarate transaminase, which can supply the substrate for this enzyme.
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This record set is specific for:
Acinetobacter baumannii
UNIPROT: Q43908
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Word Map
The taxonomic range for the selected organisms is: Acinetobacter baumannii
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
daba dc, l-2,4-diaminobutyrate decarboxylase, daba decarboxylase, daba-dc, l-2,4-diaminobutyric acid decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-2,4-diaminobutyrate decarboxylase
-
L-2,4-diaminobutyrate decarboxylase
-
-
L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase
-
additional information
the enzyme belongs to the subgroup II of the aminotransferases
SYSTEMATIC NAME
IUBMB Comments
L-2,4-diaminobutanoate carboxy-lyase (propane-1,3-diamine-forming)
A pyridoxal-phosphate protein that requires a divalent cation for activity [1]. N4-Acetyl-L-2,4-diaminobutanoate, 2,3-diaminopropanoate, ornithine and lysine are not substrates. Found in the proteobacteria Haemophilus influenzae and Acinetobacter baumannii. In the latter, this enzyme is cotranscribed with the dat gene that encodes EC 2.6.1.76, diaminobutyrate---2-oxoglutarate transaminase, which can supply the substrate for this enzyme.
CAS REGISTRY NUMBER
COMMENTARY hide
110277-62-8
-
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
propylamine + CO2
show the reaction diagram
-
-
-
?
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
L-2,4-diaminobutanoate + 2-oxoglutarate
L-aspartic beta-semialdehyde + L-glutamic acid
show the reaction diagram
the enzyme is highly specific for 2-oxoglutarate
-
-
r
L-lysine
1,5-diaminopentane + CO2
show the reaction diagram
-
-
-
?
L-ornithine
1,4-diaminobutane + CO2
show the reaction diagram
low activity
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-2,4-diaminobutanoate
propane-1,3-diamine + CO2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.012
-
recombinant enzyme in Escherichia coli
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
maximal growth temperature of the organism is 44°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2
amino acid sequence calculation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DDC_ACIBA
510
0
56244
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53000
x * 53000, recombinant enzyme, SDS-PAGE
47423
x * 47423, DNA sequence calculation
53000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 53000, recombinant enzyme, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain HB101
recombinant enzyme from Escherichia coli strain HB101 to homogeneity by ammonium sulfate fractionation, ion exchange chromatography, gel filtration, and hydroxylapatite chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain HB101
DNA sequence determination and analysis, promoter determination, restriction mapping, functional expression in Escherichia coli strain XL1-Blue
-
gene dat, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain HB101
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ikai, H.; Yamamoto, S.
Identification and analysis of a gene encoding L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase involved in the 1,3-diaminopropane production pathway in Acinetobacter baumannii
J. Bacteriol.
179
5118-5125
1997
Acinetobacter baumannii (P56744), Acinetobacter baumannii
Manually annotated by BRENDA team
Ikai, H.; Yamamoto, S.
Sequence analysis of the gene encoding a novel L-2,4-diaminobutyrate decarboxylase of Acinetobacter baumannii: similarity to the group II amino acid decarboxylases
Arch. Microbiol.
166
128-131
1996
Acinetobacter baumannii (Q43908), Acinetobacter baumannii
Manually annotated by BRENDA team
Yamamoto, S.; Ikai, H.; Uesugi, T.; Horie, A.; Hirai, Y.
Occurrence and antigenic heterogeneity of L-2,4-diaminobutyrate decarboxylase in Acinetobacter species
Biol. Pharm. Bull.
18
454-456
1995
Acinetobacter baumannii, Acinetobacter baumannii ATCC 19606, Acinetobacter calcoaceticus
Manually annotated by BRENDA team
Ikai, H.; Yamamoto, S.
Cloning and expression in Escherichia coli of the gene encoding a novel L-2,4-diaminobutyrate decarboxylase of Acinetobacter baumannii
FEMS Microbiol. Lett.
124
225-228
1994
Acinetobacter baumannii, Acinetobacter baumannii ATCC 19606
Manually annotated by BRENDA team