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Information on EC 1.1.1.22 - UDP-glucose 6-dehydrogenase and Organism(s) Haloferax volcanii and UniProt Accession D4GYH5

for references in articles please use BRENDA:EC1.1.1.22
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IUBMB Comments
Also acts on UDP-alpha-D-2-deoxyglucose.
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Select one or more organisms in this record:
This record set is specific for:
Haloferax volcanii
UNIPROT: D4GYH5
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The taxonomic range for the selected organisms is: Haloferax volcanii
Synonyms
udp-glucose dehydrogenase, udpgdh, udpgd, uridine diphosphoglucose dehydrogenase, udpglucose dehydrogenase, udp-gdh, udp-glc dehydrogenase, udpg dehydrogenase, udp-glcdh, udp-d-glucose dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenase, uridine diphosphoglucose
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HVO_1531
Sugarless protein
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UDP-alpha-D-glucose:NAD oxidoreductase
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UDP-D-glucose dehydrogenase
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UDP-Glc dehydrogenase
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UDP-Glc DH
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UDP-GlcDH
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UDP-glucose dehydrogenase
300612
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UDPG dehydrogenase
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UDPG:NAD oxidoreductase
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UDPGDH
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UDPGlc dehydrogenase
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UDPglucose dehydrogenase
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UDPglucose:NAD+ oxidoreductase
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uridine diphosphate D-glucose dehydrogenase
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uridine diphosphate glucose dehydrogenase
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uridine diphosphoglucose dehydrogenase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-glucose:NAD+ 6-oxidoreductase
Also acts on UDP-alpha-D-2-deoxyglucose.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-26-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
UDP-alpha-D-mannose + 2 NAD+ + H2O
UDP-alpha-D-mannuronate + 2 NADH + 2 H+
show the reaction diagram
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme
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?
UDP-D-galactose + 2 NAD+ + H2O
UDP-alpha-D-galacturonate + 2 NADH + 2 H+
show the reaction diagram
while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme
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?
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
UDP-alpha-D-glucose + 2 NAD+ + H2O
UDP-alpha-D-glucuronate + 2 NADH + 2 H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.2
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assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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the organism grows optimally in 1.7-2.5 M NaCl
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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in the Haloferax volcanii archaeal glycosylation pathway, Agl, responsible for the assembly and attachment of an Asn-linked pentasaccharide, enzyme AglM acts as a UDP-glucose dehydrogenase, converting UDP-glucose into UDP-glucuronic acid
physiological function
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enzyme AglM can be functionally replaced by another UDP-glucose dehydrogenase, VNG1048G, in vivo
malfunction
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Haloferax volcanii cells deleted of HVO_1531 present a modified S-layer
physiological function
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the enzyme is involved in protein N-glycosylation
additional information
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Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
550000
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gel filtration at 2 M NaCl
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
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12 * 47000, about, SDS-PAGE
additional information
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sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
recombinant CBD- and poly-His-tagged enzyme by ultracentrifugation and nickel affinity chromatography
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
gene aglM, recombinant expression of CBD-tagged and C-terminally poly-His-tagged enzyme
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yurist-Doutsch, S.; Magidovich, H.; Ventura, V.V.; Hitchen, P.G.; Dell, A.; Eichler, J.
N-glycosylation in Archaea: on the coordinated actions of Haloferax volcanii AglF and AglM
Mol. Microbiol.
75
1047-1058
2010
Haloferax volcanii (D4GYH5), Haloferax volcanii, Haloferax volcanii DSM 3757 (D4GYH5)
Manually annotated by BRENDA team
Kandiba, L.; Eichler, J.
AglM and VNG1048G, two haloarchaeal UDP-glucose dehydrogenases, show different salt-related behaviors
Life
6
pii: E31
2016
Halobacterium salinarum, Halobacterium salinarum (Q9HQQ9), Halobacterium salinarum ATCC 700922 (Q9HQQ9), Haloferax volcanii (D4GYH5), Haloferax volcanii, Haloferax volcanii ATCC 29605 (D4GYH5)
Manually annotated by BRENDA team
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