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LOCUS WP_010989627 377 aa linear BCT 03-JUN-2024 monocytogenes]. ACCESSION WP_010989627 VERSION WP_010989627.1 KEYWORDS RefSeq. SOURCE Listeria monocytogenes ORGANISM Listeria monocytogenes Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria. REFERENCE 1 (residues 1 to 377) AUTHORS Hall,R.S., Brown,S., Fedorov,A.A., Fedorov,E.V., Xu,C., Babbitt,P.C., Almo,S.C. and Raushel,F.M. TITLE Structural diversity within the mononuclear and binuclear active sites of N-acetyl-D-glucosamine-6-phosphate deacetylase JOURNAL Biochemistry 46 (27), 7953-7962 (2007) PUBMED 17567048 REFERENCE 2 (residues 1 to 377) AUTHORS Hall,R.S., Xiang,D.F., Xu,C. and Raushel,F.M. TITLE N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation via a single divalent metal ion JOURNAL Biochemistry 46 (27), 7942-7952 (2007) PUBMED 17567047 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 :: HMM Evidence Accession :: TIGR00221.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..377 /organism="Listeria monocytogenes" /db_xref="taxon:1639" gene 1..377 /gene="nagA" Protein 1..377 /product="N-acetylglucosamine-6-phosphate deacetylase" /EC_number="3.5.1.25" /GO_function="GO:0008448 - N-acetylglucosamine-6-phosphate deacetylase activity [Evidence IEA]" /GO_process="GO:0006044 - N-acetylglucosamine metabolic process [Evidence IEA]" /calculated_mol_wt=41283 Region 4..373 /region_name="NagA" /note="N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to...; cd00854" /db_xref="CDD:238434" Site order(62,64,129,140,195,213,216..217,248,271,304) /site_type="active" /db_xref="CDD:238434" Site order(215,221,223..224,226,233..234,247..250,252..253, 255..256,259) /site_type="other" /note="dimer interface [polypeptide binding]" /db_xref="CDD:238434" ORIGIN 1 mankvitnat iytgkgvlen afvrfdkqil evgsmadfqa dkaeevidak gqklvpgfid 61 vhshggysfd amdadpealr kqvngmlneg ittyfpttmt qsheniekal kvinevaqte 121 pviggihleg pfvskvfkga qpeeyiqapd lelfkkwfdi sggliklvty apehdtsadf 181 enlcfelgvv psighsndvr ehlktskath athlynachr mthrepgvpg hvllergina 241 elivdgihvh pdmvklayqm kgpehlciit dsmrakgmpe gkselggqtv ivkdkqarle 301 dgtlagsvlt yddgfrnmik ftgcsveeav lmssgnqare fnltqkgaie agkdadfnll 361 dedlhitaty sfgkkhs