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LOCUS WP_012551094 305 aa linear BCT 06-NOV-2024 [Aliivibrio]. ACCESSION WP_012551094 VERSION WP_012551094.1 KEYWORDS RefSeq. SOURCE Aliivibrio ORGANISM Aliivibrio Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae. 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="Aliivibrio" /db_xref="taxon:511678" 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=33885 Region 2..280 /region_name="LpxC" /note="UDP-3-O-acyl-N-acetylglucosamine deacetylase [Cell wall/membrane/envelope biogenesis]; COG0774" /db_xref="CDD:440537" ORIGIN 1 mirqrtlksi vqmtgvglhs grkvtltlrp aaantgviyr rtdlnppvdf padpesvrdt 61 mlctalvndd gvristvehl naalagvgid nvvievdape ipimdgsasp fvyllqsagi 121 eelntakkfi rikkpvried gdkwaeirpy ngfrldftid fnhpaiesdd qklvfefssq 181 sfikdisrar tfgfmrdiey lqsqnlclgg sfdcaivldd yrilnedglr fenefvthkv 241 ldavgdlymc ghsilgelsa yksghalnnq llravladqe awewttiede kdspvafmqp 301 gmvla