Due to scheduled maintenance work, this service may not be available on Monday January 22nd between 08.00 am and 9.00 am CEST.
To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https

ENZYME entry: EC

Accepted Name
UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase.
Reaction catalysed
UDP-N-acetyl-2-amino-2-deoxy-alpha-D-glucuronate + NAD(+) <=> UDP-2-acetamido-2-deoxy-alpha-D-ribo-hex-3-uluronate + NADH
  • This enzyme participates in the biosynthetic pathway for UDP-alpha-D- ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronic acid), an important precursor of B-band lipopolysaccharide.
  • The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the the enzyme catalyzing the next step the pathway (EC
  • The enzyme also possesses an EC activity, and utilizes the 2-oxoglutarate produced by EC to regenerate the tightly bound NAD(+).
  • The enzymes from Bordetella pertussis and Chromobacterium violaceum do not bind NAD(+) as tightly and do not require 2-oxoglutarate to function.
PRIAM enzyme-specific profiles1.1.1.335
KEGG Ligand Database for Enzyme Nomenclature1.1.1.335
IUBMB Enzyme Nomenclature1.1.1.335
MEDLINEFind literature relating to

View entry in original ENZYME format
View entry in raw text format (no links)

All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.1.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-