Latest update: September 24, 2018


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 / PR
Domain Bacteria
PhylumProteobacteria
ClassificationFamily: Pseudomonadaceae
Order: Pseudomonadales
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)208964
Genome Information
Gene BankAE004091
EMBLAE004091
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 EL, Preston A, Field RA, Lam JS. 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. 2008 Sep 15;190(18):6060-9.

Authors Westman EL, Preston A, Field RA, Lam JS
Research groups1 University of Guelph, Department of Molecular and Cellular Biology, Guelph, Ontario, Canada.
Corresponding Author Lam JS
Contacts1 University of Guelph, Department of Molecular and Cellular Biology, Guelph, Ontario, Canada.
Reference Larkin A, Imperiali B. 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. 2009 May 22;48(23):5446-55.

Authors Larkin A, Imperiali B
Research groups1 Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge,Massachusetts 02139, USA.
Corresponding Author Imperiali B
Contacts1 Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge,Massachusetts 02139, USA.
Reference Westman EL, McNally DJ, Charchoglyan A, Brewer D, Field RA, Lam JS. 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. 2009 Mar 12.

Authors Westman EL, McNally DJ, Charchoglyan A, Brewer D, Field RA, Lam JS
Research groups1 Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario N1G 2W1, Canada.
Corresponding AuthorLam JS
Contacts1 Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario N1G 2W1, Canada.
Reference Thoden JB, Holden HM. Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2, 3-diacetamido-2, 3-dideoxy-D-mannuronic acid. Biochemistry. 2010 Aug 19;49(36):7939-48.

Authors Thoden JB, Holden HM.
Research groups1 Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
Corresponding AuthorHolden HM.
Contacts1 Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.