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LOCUS WP_004151349 170 aa linear BCT 02-MAR-2025 ACCESSION WP_004151349 VERSION WP_004151349.1 KEYWORDS RefSeq. SOURCE Klebsiella ORGANISM Klebsiella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group. REFERENCE 1 (residues 1 to 170) AUTHORS Romao,M.J., Turk,D., Gomis-Ruth,F.X., Huber,R., Schumacher,G., Mollering,H. and Russmann,L. TITLE Crystal structure analysis, refinement and enzymatic reaction mechanism of N-carbamoylsarcosine amidohydrolase from Arthrobacter sp. at 2.0 A resolution JOURNAL J Mol Biol 226 (4), 1111-1130 (1992) PUBMED 1381445 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 :: NF013053.6 Evidence Source :: EMBL-EBI Source Identifier :: PF00857.25 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..170 /organism="Klebsiella" /db_xref="taxon:570" Protein 1..170 /product="isochorismatase family protein" /calculated_mol_wt=18461 Region 1..141 /region_name="cysteine_hydrolases" /note="Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine amidohydrolase), involved in creatine metabolism and nicotinamidase, converting nicotinamide to nicotinic acid and ammonia in the pyridine nucleotide cycle. It...; cl00220" /db_xref="CDD:444760" Site order(4,69,102) /site_type="active" /note="catalytic triad [active]" /db_xref="CDD:238245" Site 97..98 /site_type="active" /note="conserved cis-peptide bond [active]" /db_xref="CDD:238245" ORIGIN 1 mvvdmqngvf atprlarerc vaqinrlvra adkvifiqhd eaggleagse gfallpeleq 61 pagalyvtkt acdafyhtsl aqvldehdiq qfvicgcatd ycldttikng asrgyvivia 121 edahttadrp aaqaatliah ynevwrtlti pgnplqvkpt etilhawqqn