MULTISPECIES: carbon-nitrogen hydrolase family protein

LOCUS       WP_016960798             272 aa            linear   BCT 01-JAN-2025
            [Enterovibrio].
ACCESSION   WP_016960798
VERSION     WP_016960798.1
KEYWORDS    RefSeq.
SOURCE      Enterovibrio
  ORGANISM  Enterovibrio
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Brenner,C.
  TITLE     Catalysis in the nitrilase superfamily
  JOURNAL   Curr Opin Struct Biol 12 (6), 775-782 (2002)
   PUBMED   12504683
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Pace,H.C. and Brenner,C.
  TITLE     The nitrilase superfamily: classification, structure and function
  JOURNAL   Genome Biol 2 (1), REVIEWS0001 (2001)
   PUBMED   11380987
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 10166075
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Enterovibrio"
                     /db_xref="taxon:188143"
     Protein         1..272
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30048
     Region          3..264
                     /region_name="nit"
                     /note="Nit1, Nit 2, and related proteins, and the
                     Nit1-like domain of NitFhit (class 10 nitrilases);
                     cd07572"
                     /db_xref="CDD:143596"
     Site            order(41,95,112,116,129,154..155,157..158,179)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143596"
     Site            order(41,112,154)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143596"
     Site            order(113..114,135..137,155,158..162,164..165,187..188,
                     191..192,194..196,198..199,229,259..260,263..264)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143596"
ORIGIN      
        1 mtkfgvvqmn sgvnaednld vlesqlkhlq aqgarliltp enalvfgrke dyekyaeelg
       61 hgplqkrlse lafelgiwlv mgsfpirnhd gtlsttclvy daagnlrasy eklhmfdvdi
      121 adnhrsyres dtfragenla lvdtpfgmlg lsicydirfp qlyaalrqrg adiivvpaaf
      181 tkvtgaahwe vllraraiet qcwvlaaaqc gehqggrety ghsmiidpwg qvacelnnni
      241 gtawadvdla snsairskmp llqhaqlqcv mk