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LOCUS WP_003113413 339 aa linear BCT 24-DEC-2024 ACCESSION WP_003113413 VERSION WP_003113413.1 KEYWORDS RefSeq. SOURCE Pseudomonas ORGANISM Pseudomonas Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae. REFERENCE 1 (residues 1 to 339) AUTHORS Anderson,M.S., Eveland,S.S. and Price,N.P. TITLE Conserved cytoplasmic motifs that distinguish sub-groups of the polyprenol phosphate:N-acetylhexosamine-1-phosphate transferase family JOURNAL FEMS Microbiol Lett 191 (2), 169-175 (2000) PUBMED 11024259 REFERENCE 2 (residues 1 to 339) AUTHORS Lehrman,M.A. TITLE A family of UDP-GlcNAc/MurNAc: polyisoprenol-P GlcNAc/MurNAc-1-P transferases JOURNAL Glycobiology 4 (6), 768-771 (1994) PUBMED 7734839 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 :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 10160628 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..339 /organism="Pseudomonas" /db_xref="taxon:286" Protein 1..339 /product="MraY family glycosyltransferase" /EC_number="2.-.-.-" /GO_function="GO:0016780 - phosphotransferase activity, for other substituted phosphate groups [Evidence IEA]" /GO_function="GO:0046872 - metal ion binding [Evidence IEA]" /GO_process="GO:0009252 - peptidoglycan biosynthetic process [Evidence IEA]" /calculated_mol_wt=36295 Region 31..287 /region_name="GT_WbpL_WbcO_like" /note="The members of this subfamily catalyze the formation of a phosphodiester bond between a membrane-associated undecaprenyl-phosphate (Und-P) molecule and N-acetylhexosamine 1-phosphate, which is usually donated by a soluble UDP-N-acetylhexosamine precursor; cd06854" /db_xref="CDD:133464" Site 92..93 /site_type="other" /note="Mg++ binding site [ion binding]" /db_xref="CDD:133464" Site 209..212 /site_type="active" /note="putative catalytic motif [active]" /db_xref="CDD:133464" Site order(258,269..272) /site_type="other" /note="putative substrate binding site [chemical binding]" /db_xref="CDD:133464" ORIGIN 1 mmiwmiaclv vllfsfvatw glrryalatk lmdvpnarss hsqptprggg vaivlvflaa 61 lvwmlsagsi sggwggamlg agsgvallgf lddhghiaar wrllghfsaa iwillwtggf 121 ppldvvghav dlgwlghvla vfylvwvlnl ynfmdgidgi asveaigvcv ggaliywltg 181 hvamvgipll lacavagfli wnfpparifm gdagsgflgm vigalaiqaa wtapslfwcw 241 lillgvfivd atytlirria rgekfyeahr shayqfasrr yashlrvtlg vlaintlwll 301 plalmvalgw isgfigilva yaplcllavg ykagsleks