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LOCUS WP_002898927 225 aa linear BCT 26-FEB-2025 ACCESSION WP_002898927 VERSION WP_002898927.1 KEYWORDS RefSeq. SOURCE Klebsiella ORGANISM Klebsiella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group. REFERENCE 1 (residues 1 to 225) 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..225 /organism="Klebsiella" /db_xref="taxon:570" Protein 1..225 /product="isochorismatase family protein" /calculated_mol_wt=23964 Region 20..180 /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(25,90,124) /site_type="active" /note="catalytic triad [active]" /db_xref="CDD:238494" Site 119..120 /site_type="active" /note="conserved cis-peptide bond [active]" /db_xref="CDD:238494" ORIGIN 1 mstpanfnga rpvidvndta mllidhqsgl fqtvgdmpmp elraraaala kmaslagipv 61 ittasvpqgp ngplipeihe naphakyiar kgeinawdnp efvaavkatg rktliiagti 121 tsvcmafpai aavadgykvf avidasgtys kmaqeitlar vvqagvvpmd taavaselqr 181 twnrpdaaew aevytkvfpa yqlliesysk aqdvvknneq ldsqr