MULTISPECIES: hydrolase [Enterobacterales].

LOCUS       WP_002890357             213 aa            linear   BCT 20-OCT-2023
ACCESSION   WP_002890357
VERSION     WP_002890357.1
KEYWORDS    RefSeq.
SOURCE      Enterobacterales
  ORGANISM  Enterobacterales
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Colovos,C., Cascio,D. and Yeates,T.O.
  TITLE     The 1.8 A crystal structure of the ycaC gene product from
            Escherichia coli reveals an octameric hydrolase of unknown
            specificity
  JOURNAL   Structure 6 (10), 1329-1337 (1998)
   PUBMED   9782055
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10099061
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Enterobacterales"
                     /db_xref="taxon:91347"
     Protein         1..213
                     /product="hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=23517
     Region          13..172
                     /region_name="YcaC_related"
                     /note="YcaC related amidohydrolases; E.coli YcaC is an
                     homooctameric hydrolase with unknown specificity. Despite
                     its weak sequence similarity, it is structurally related
                     to other amidohydrolases and shares conserved active site
                     residues with them; cd01012"
                     /db_xref="CDD:238494"
     Site            order(18,83,116)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238494"
     Site            order(21,24,70)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238494"
     Site            111..112
                     /site_type="active"
                     /note="conserved cis-peptide bond [active]"
                     /db_xref="CDD:238494"
ORIGIN      
        1 msirelldpt nsalifidhq pqmsfgvani drqtlknntv alakagkifn vpviytsvet
       61 ksfsgyiwpe llavhpdvkp iertsmnswe ddafvaavka tgrkklvisa lwtevcltfp
      121 almaleagye vyvvtdtsgg tsvdahersi drmvqagavp vtwqqvlley qrdwsrkaty
      181 davmdlvreh sgaygmgvdy aytmvhgape rka