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LOCUS WP_000595487 305 aa linear BCT 06-NOV-2024 [Salmonella]. ACCESSION WP_000595487 VERSION WP_000595487.1 KEYWORDS RefSeq. SOURCE Salmonella ORGANISM Salmonella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 305) AUTHORS Jackman,J.E., Raetz,C.R. and Fierke,C.A. TITLE UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme JOURNAL Biochemistry 38 (6), 1902-1911 (1999) PUBMED 10026271 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 :: TIGR00325.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..305 /organism="Salmonella" /db_xref="taxon:590" gene 1..305 /gene="lpxC" Protein 1..305 /product="UDP-3-O-acyl-N-acetylglucosamine deacetylase" /EC_number="3.5.1.108" /GO_function="GO:0103117 - UDP-3-O-acyl-N-acetylglucosamine deacetylase activity [Evidence IEA]" /GO_process="GO:0009245 - lipid A biosynthetic process [Evidence IEA]" /calculated_mol_wt=33854 Region 2..301 /region_name="lpxC" /note="UDP-3-0-acyl N-acetylglucosamine deacetylase; TIGR00325" /db_xref="CDD:273014" ORIGIN 1 mikqrtlkri vqatgvglht gkkvtltlrp apantgviyr rtdlnppvdf padaksvrdt 61 mlctclvneh dvristvehl naalaglgid nivievnape ipimdgsaap fvyllldagi 121 delncakkfv riketvrved gdkwaefrpy ngftldftid fnhpaidsss qryamnfsad 181 afmrqisrar tfgfmrdiey lqsrglclgg sfdcaivvdd yrvlnedglr fedefvrhkm 241 ldaigdlfmc ghniigafta yksghalnnk llqavlakqe awefvtfqdd aelplafkap 301 stvla