MULTISPECIES: hydrolase [Pseudomonas].

LOCUS       WP_003100571             180 aa            linear   BCT 20-NOV-2023
ACCESSION   WP_003100571
VERSION     WP_003100571.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 180)
  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..180
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..180
                     /product="hydrolase"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=19761
     Region          9..164
                     /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(14,76,108)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238494"
     Site            order(17,20,63)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238494"
     Site            103..104
                     /site_type="active"
                     /note="conserved cis-peptide bond [active]"
                     /db_xref="CDD:238494"
ORIGIN      
        1 mliraatstl lvvdiqerll paiddgpalv eysqwllrva raldvpvlas eqyskglgpt
       61 vaalrdelep tqilekldfs aaadgallra pggdrrqfvv cgseahvcvl qtvldllgrg
      121 revfvveeai gsrrpsdkal avermrqaga mivsremvaf ewmeragsdr freisrnfir