ProGTNC7 (WbpA)

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ProGT ID ProGTNC7 (WbpA)
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 NamewbpA 
NCBI Gene ID879921
Protein information
Protein NameWbpA 
UniProtKB/ SwissProt IDG3XD94
NCBI Ref SeqWP_003113429.1
UniProtKB Sequence>sp|G3XD94|UGND_PSEAE UDP-N-acetyl-D-glucosamine 6-dehydrogenase OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=wbpA PE=1 SV=1 MIDVNTVVEKFKSRQALIGIVGLGYVGLPLMLRYNAIGFDVLGIDIDDVKVDKLNAGQCY IEHIPQAKIAKARASGFEATTDFSRVSECDALILCVPTPLNKYREPDMSFVINTTDALKP YLRVGQVVSLESTTYPGTTEEELLPRVQEGGLVVGRDIYLVYSPEREDPGNPNFETRTIP KVIGGHTPQCLEVGIALYEQAIDRVVPVSSTKAAEMTKLLENIHRAVNIGLVNEMKIVAD RMGIDIFEVVDAAATKPFGFTPYYPGPGLGGHCIPIDPFYLTWKAREYGLHTRFIELSGE VNQAMPEYVLGKLMDGLNEAGRALKGSRVLVLGIAYKKNVDDMRESPSVEIMELIEAKGG MVAYSDPHVPVFPKMREHHFELSSEPLTAENLARFDAVVLATDHDKFDYELIKAEAKLVV DSRGKYRSPAAHIIKA
EMBL CDSAAC45852
Sequence length436 AA
Subcellular LocationMembrane (Integral component of membrane)
String208964.PA3159
Glycosylation Information
EC Number (BRENDA)1.1.1.336
Acceptor Substrate SpecificityUDP-N-acetyl-alpha-D-glucosamine
ProductUDP-2-acetamido-2-deoxy-alpha-D-glucuronate
Function in Glycosylation pathway1) Play important role in the C-6 dehydrogenation of UDP-D-GlcNAc to UDP-N-acetylglucosaminuronic acid (UDP-D-GlcNAcA).
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.