MULTISPECIES: isochorismatase family protein [Salmonella].

LOCUS       WP_000106461             226 aa            linear   BCT 26-FEB-2025
ACCESSION   WP_000106461
VERSION     WP_000106461.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 226)
  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..226
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     Protein         1..226
                     /product="isochorismatase family protein"
                     /calculated_mol_wt=24175
     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:238245"
     Site            119..120
                     /site_type="active"
                     /note="conserved cis-peptide bond [active]"
                     /db_xref="CDD:238245"
ORIGIN      
        1 mstpanfngq rpaidandav mllidhqsgl fqtvgdmpmp elraraaala kiatlcnmpv
       61 ittasvpqgp ngplipeiha naphaqyvar kgeinawdna dfvqavkatg rktliiagti
      121 tsvcmafpai savaegykvf avidasgtys kmaqeitmar vvqagvvpmd taavaselqr
      181 twnredaaew advytkifpa yqlliesytk aqevvknnel ldsqra