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LOCUS WP_003113426 191 aa linear BCT 17-AUG-2020 N-acetyltransferase [Pseudomonas]. ACCESSION WP_003113426 VERSION WP_003113426.1 KEYWORDS RefSeq. SOURCE Pseudomonas ORGANISM Pseudomonas Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae. REFERENCE 1 (residues 1 to 191) AUTHORS Larkin,A. and Imperiali,B. TITLE 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 JOURNAL Biochemistry 48 (23), 5446-5455 (2009) PUBMED 19348502 REFERENCE 2 (residues 1 to 191) AUTHORS Westman,E.L., McNally,D.J., Charchoglyan,A., Brewer,D., Field,R.A. and Lam,J.S. TITLE 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 J. Biol. Chem. 284 (18), 11854-11862 (2009) PUBMED 19282284 REFERENCE 3 (residues 1 to 191) AUTHORS Wenzel,C.Q., Daniels,C., Keates,R.A., Brewer,D. and Lam,J.S. TITLE Evidence that WbpD is an N-acetyltransferase belonging to the hexapeptide acyltransferase superfamily and an important protein for O-antigen biosynthesis in Pseudomonas aeruginosa PAO1 JOURNAL Mol. Microbiol. 57 (5), 1288-1303 (2005) PUBMED 16102001 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: BlastRule Evidence Accession :: NBR012425 Evidence Source :: NCBI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..191 /organism="Pseudomonas" /db_xref="taxon:286" gene 1..191 /gene="wbpD" Protein 1..191 /product="UDP-2-acetamido-3-amino-2, 3-dideoxy-D-glucuronate N-acetyltransferase" /EC_number="2.3.1.201" /calculated_mol_wt=20431 Region 35..153 /region_name="LbH_WxcM_N_like" /note="WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization...; cd03358" /db_xref="CDD:100048" Site order(56,58,66,74,76,82,88..90,107,109,112,131,147) /site_type="other" /note="putative trimer interface [polypeptide binding]" /db_xref="CDD:100048" Site order(58,60,88,90,109,111..112,117,129..130,135..136, 145..146,148) /site_type="active" /note="putative active site [active]" /db_xref="CDD:100048" Site order(58,60,88) /site_type="other" /note="putative substrate binding site [chemical binding]" /db_xref="CDD:100048" Site order(88,90,109,111..112,117,127,129..130,135..136,143, 145..146,148,152) /site_type="other" /note="putative CoA binding site [chemical binding]" /db_xref="CDD:100048" ORIGIN 1 msyyqhpsai vddgaqigsd srvwhfvhic agarigagvs lgqnvfvgnk vvigdrckiq 61 nnvsvydnvt leegvfcgps mvftnvynpr slierkdqyr ntlvkkgatl ganctivcgv 121 tigeyafvga gavinknvps yalmvgvpar qigwmsefge qlqlneqgea vcshsgaryv 181 lngkilskvd v