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Information on EC 1.1.1.290 - 4-phosphoerythronate dehydrogenase and Organism(s) Pseudomonas aeruginosa

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IUBMB Comments
This enzyme catalyses a step in a bacterial pathway for the biosynthesis of pyridoxal 5'-phosphate. The enzyme contains a tightly-bound NAD(H) cofactor that is not re-oxidized by free NAD+. In order to re-oxidize the cofactor and restore enzyme activity, the enzyme catalyses the reduction of a 2-oxo acid (such as 2-oxoglutarate, oxaloacetate, or pyruvate) to the respective (R)-hydroxy acid . cf. EC 1.1.1.399, 2-oxoglutarate reductase.
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This record set is specific for:
Pseudomonas aeruginosa
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
erythronate-4-phosphate dehydrogenase, 4-phosphoerythronate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-erythronate-4-phosphate dehydrogenase
-
erythronate-4-phosphate dehydrogenase
-
-
additional information
PdxB is a member of the D-isomer specific 2-hydroxyacid dehydrogenase superfamily
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-phospho-D-erythronate + NAD+ = (3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH + H+
show the reaction diagram
substrate recognition and catalytic mechanism, PdxB contains the conserved His254/Glu237/Arg208 triad
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
4-phospho-D-erythronate:NAD+ 2-oxidoreductase
This enzyme catalyses a step in a bacterial pathway for the biosynthesis of pyridoxal 5'-phosphate. The enzyme contains a tightly-bound NAD(H) cofactor that is not re-oxidized by free NAD+. In order to re-oxidize the cofactor and restore enzyme activity, the enzyme catalyses the reduction of a 2-oxo acid (such as 2-oxoglutarate, oxaloacetate, or pyruvate) to the respective (R)-hydroxy acid [6]. cf. EC 1.1.1.399, 2-oxoglutarate reductase.
CAS REGISTRY NUMBER
COMMENTARY hide
125858-75-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-phospho-D-erythronate + NAD+
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH
show the reaction diagram
erythronate-4-phosphate + NAD+
3-hydroxy-4-phospho-hydroxy-alpha-ketobutyrate + NADH
show the reaction diagram
-
-
-
-
?
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
4-phospho-D-erythronate + NAD+
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH
show the reaction diagram
the enzyme is involved in biosynthesis of pyridoxal-5'-phosphate
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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?
A0A0Q3G9I3_PSEAI
380
0
41030
TrEMBL
-
A0A8G6X860_PSEAI
380
0
41020
TrEMBL
-
A0A7M3AYW5_PSEAI
380
0
41041
TrEMBL
-
A0A643EGW7_PSEAI
380
0
40944
TrEMBL
-
A0A8G7LB04_PSEAI
380
0
40886
TrEMBL
-
A0A8G6ZK73_PSEAI
380
0
41046
TrEMBL
-
A0A8G7KV26_PSEAI
380
0
41052
TrEMBL
-
A0A8G4AEB6_PSEAI
380
0
40963
TrEMBL
-
A0A8G6Z6N0_PSEAI
380
0
41044
TrEMBL
-
A0A8G4HQW6_PSEAI
380
0
41030
TrEMBL
-
A0A367MG93_PSEAI
380
0
41032
TrEMBL
-
A0A8H2I331_PSEAI
380
0
41032
TrEMBL
-
A0A8G7PP46_PSEAI
380
0
41041
TrEMBL
-
A0A8G3TSH1_PSEAI
380
0
41132
TrEMBL
-
A0A8F9YBW9_PSEAI
380
0
40978
TrEMBL
-
A0A8G2W5M4_PSEAI
380
0
40992
TrEMBL
-
A0A8G4LPW1_PSEAI
380
0
41060
TrEMBL
-
A0A8G4FS13_PSEAI
380
0
40973
TrEMBL
-
A0A8G3ST38_PSEAI
380
0
41048
TrEMBL
-
A0A8G6ZZW8_PSEAI
380
0
41002
TrEMBL
-
A0A8G2TCR3_PSEAI
380
0
40949
TrEMBL
-
A0A8G2VWC4_PSEAI
380
0
40987
TrEMBL
-
A0A8G4UIZ2_PSEAI
380
0
41114
TrEMBL
-
A0A8G3J6S7_PSEAI
380
0
41072
TrEMBL
-
A0A8G2UY38_PSEAI
380
0
41105
TrEMBL
-
A0A8B5BP34_PSEAI
380
0
40952
TrEMBL
-
A0A8F9VF12_PSEAI
380
0
40964
TrEMBL
-
A0A8G3XG21_PSEAI
380
0
41025
TrEMBL
-
A0A509JBH5_PSEAI
380
0
41039
TrEMBL
-
A0A5F1BIN1_PSEAI
380
0
41030
TrEMBL
-
A0A8G3CP02_PSEAI
380
0
41011
TrEMBL
-
A0A8G6DMF7_PSEAI
380
0
41071
TrEMBL
-
A0A0A8RQ69_PSEAI
380
0
40891
TrEMBL
-
A0A8G2KFT1_PSEAI
380
0
41089
TrEMBL
-
A0A5R1B6A8_PSEAI
380
0
41002
TrEMBL
-
A0A8G4D040_PSEAI
380
0
40958
TrEMBL
-
A0A3N0EQC3_PSEAI
380
0
41061
TrEMBL
-
A0A8G4JEP6_PSEAI
380
0
41033
TrEMBL
-
A0A8G7GW79_PSEAI
380
0
41039
TrEMBL
-
A0A485HUK7_PSEAI
380
0
41029
TrEMBL
-
A0A8G7BNB6_PSEAI
380
0
41076
TrEMBL
-
A0A431XGR3_PSEAI
380
0
40912
TrEMBL
-
A0A8G6L526_PSEAI
380
0
41039
TrEMBL
-
A0A643IPC0_PSEAI
380
0
41078
TrEMBL
-
A0A8F9P1Y3_PSEAI
380
0
41028
TrEMBL
-
A0A2R3J365_PSEAI
380
0
41016
TrEMBL
-
A0A8G7M5K9_PSEAI
380
0
41051
TrEMBL
-
A0A8B5A7Z3_PSEAI
380
0
41058
TrEMBL
-
A0A5K1SGU4_PSEAI
380
0
41086
TrEMBL
-
A0A8G6NUA6_PSEAI
380
0
41074
TrEMBL
-
A0A8G5ZFF6_PSEAI
380
0
40967
TrEMBL
-
A0A8B5AMW1_PSEAI
380
0
41030
TrEMBL
-
A0A6B1Y3Z2_PSEAI
380
0
40930
TrEMBL
-
A0A6A9JP54_PSEAI
380
0
40974
TrEMBL
-
A0A8B4ZGB5_PSEAI
380
0
41043
TrEMBL
-
A0A8G5J7W6_PSEAI
380
0
41048
TrEMBL
-
A0A8F9PAY0_PSEAI
380
0
41017
TrEMBL
-
A0A8F9KTR0_PSEAI
380
0
40977
TrEMBL
-
A0A8G4KHB1_PSEAI
380
0
41058
TrEMBL
-
A0A8G3E6F3_PSEAI
380
0
41020
TrEMBL
-
A0A8G4ALC2_PSEAI
380
0
41082
TrEMBL
-
A0A8G2QS73_PSEAI
380
0
41039
TrEMBL
-
A0A8G7F6U9_PSEAI
380
0
41030
TrEMBL
-
A0A8G4YCF3_PSEAI
380
0
41053
TrEMBL
-
A0A8G2U1V0_PSEAI
380
0
40939
TrEMBL
-
A0A8F8RDY1_PSEAI
380
0
40961
TrEMBL
-
A0A8G6LHU8_PSEAI
380
0
40980
TrEMBL
-
A0A8G4B041_PSEAI
380
0
40992
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
83000
-
estimated by dynamic light-scattering analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer, each subunit consists of three structural domains: the lid domain, the nucleotide-binding domain, and the C-terminal dimerization domain with a unique fold responsible for the dimerization, crystal structure analysis, overview
homodimer
-
2 * 42 067, enzyme including a C-terminal tag, enzyme consists of two identical 380-residue subunits
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour diffusion at 24°C K using 0.7 M ammonium dihydrogen phosphate, 0.4 M ammonium tartrate, 0.1 M sodium citrate pH 5.6 and 10 mM cupric chloride
-
purified recombinant C-terminally His8-tagged and selenomethionine-labeled enzyme, subunit A is bound with NAD+ and a phosphate ion, while subunit B, with a more open active site cleft, is bound with NAD+ and L(+)-tartrate, cryoprotection by 30% glycerol, X-ray diffraction structure determination and analysis at 2.3 A resolution, asymmetric subunit conformation and strucure comparison, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
metal-chelate chromatography on Ni-NTA resin and size exclusion chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ha, J.Y.; Lee, J.H.; Kim, K.H.; Kim, D.J.; Lee, H.H.; Kim, H.K.; Yoon, H.J.; Suh, S.W.
Overexpression, crystallization and preliminary X-ray crystallographic analysis of erythronate-4-phosphate dehydrogenase from Pseudomonas aeruginosa
Acta Crystallogr. Sect. F
62
139-141
2006
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Ha, J.Y.; Lee, J.H.; Kim, K.H.; Kim, d.o..J.; Lee, H.H.; Kim, H.K.; Yoon, H.J.; Suh, S.W.
Crystal structure of D-erythronate-4-phosphate dehydrogenase complexed with NAD
J. Mol. Biol.
366
1294-1304
2007
Pseudomonas aeruginosa (Q9I3W9), Pseudomonas aeruginosa
Manually annotated by BRENDA team