ProGTNC9 (WbpE)

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ProGT ID ProGTNC9 (WbpE)
Organism Information
Organism NamePseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRRS 101 / PAO1)
Domain Bacteria
Classification Phylum : Proteobacteria
Class : Gammaproteobacteria
Orders : Pseudomonadales
Family : Pseudomanadaceae
Genus : Pseudomonas
Species : aeruginosa
Strain : ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRRS 101 / PAO1
Taxonomic ID (NCBI)208964
Genome Information
Gene BankAE004091.2
EMBLAE004091.2
Gene Information
Gene NamewbpE 
NCBI Gene ID882653
Protein information
Protein NameWbpE 
UniProtKB/ SwissProt IDQ9HZ76
NCBI Ref SeqWP_003113425.1
UniProtKB Sequence>sp|Q9HZ76|WBPE_PSEAE UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronate aminotransferase OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=wbpE PE=1 SV=1 MIEFIDLKNQQARIKDKIDAGIQRVLRHGQYILGPEVTELEDRLADFVGAKYCISCANGT DALQIVQMALGVGPGDEVITPGFTYVATAETVALLGAKPVYVDIDPRTYNLDPQLLEAAI TPRTKAIIPVSLYGQCADFDAINAIASKYGIPVIEDAAQSFGASYKGKRSCNLSTVACTS FFPSKPLGCYGDGGAIFTNDDELATAIRQIARHGQDRRYHHIRVGVNSRLDTLQAAILLP KLEIFEEEIALRQKVAAEYDLSLKQVGIGTPFIEVNNISVYAQYTVRMDNRESVQASLKA AGVPTAVHYPIPLNKQPAVADEKAKLPVGDKAATQVMSLPMHPYLDTASIKIICAALTN
EMBL CDSAAG06543
Sequence length359 AA
String208964.PA3155
PDB ID (Structural Information)3NU7, 3NU8, 3NUB, 3NYS, 3NYT, 3NYU
Glycosylation Information
EC Number (BRENDA)2.6.1.98
Acceptor Substrate SpecificityUDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate
ProductUDP-2-acetamido-2-deoxy-D-ribo-hex-3-uluronate
Function in Glycosylation pathway1) Catalyzes the amination of UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronic acid (UDP-3-oxo-D-GlcNAcA) to UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronic acid (UDP-GlcNAc3NA), using L-glutamate as the preferred amine donor.
Litrature
Year Of Validation2008 
Reference Westman, E.L., Preston, A., Field, R.A. and Lam, J.S., 2008. Biosynthesis of a rare di-N-acetylated sugar in the lipopolysaccharides of both Pseudomonas aeruginosa and Bordetella pertussis occurs via an identical scheme despite different gene clusters. Journal of bacteriology, 190(18), pp.6060-6069.

Corresponding Author1 University of Guelph, Department of Molecular and Cellular Biology, Guelph, Ontario, Canada.
Reference Larkin, A. and Imperiali, B., 2009. Biosynthesis of UDP-GlcNAc (3NAc) A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1. Biochemistry, 48(23), pp.5446-5455.

Corresponding Author1 Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge,Massachusetts 02139, USA.
Reference Westman, E.L., McNally, D.J., Charchoglyan, A., Brewer, D., Field, R.A. and Lam, J.S., 2009. Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway for the biosynthesis of UDP-2, 3-diacetamido-2, 3-dideoxy-D-mannuronic acid in Pseudomonas aeruginosa. Journal of Biological Chemistry, 284(18), pp.11854-11862.

Corresponding Author1 Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario N1G 2W1, Canada.
Reference Thoden, J.B. and Holden, H.M., 2010. Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2, 3-diacetamido-2, 3-dideoxy-D-mannuronic acid. Biochemistry, 49(36), pp.7939-7948.

Corresponding Author1 Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.