MULTISPECIES: carbon-nitrogen hydrolase family protein

LOCUS       WP_003112739             282 aa            linear   BCT 31-DEC-2024
            [Pseudomonas].
ACCESSION   WP_003112739
VERSION     WP_003112739.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 282)
  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 282)
  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..282
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..282
                     /product="carbon-nitrogen hydrolase family protein"
                     /EC_number="3.5.-.-"
                     /GO_function="GO:0016787 - hydrolase activity [Evidence
                     IEA]"
                     /calculated_mol_wt=30593
     Region          3..269
                     /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(40,98,115,119,132,157..158,160..161,182)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143596"
     Site            order(40,115,157)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143596"
     Site            order(116..117,138..140,158,161..165,167..168,190..191,
                     194..195,197..199,201..202,232,262..263,266..267,269)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143596"
ORIGIN      
        1 msiaviqmvs qddvtanlaa arrlleqaae ggarlavlpe nfaamgrrdl aelgraearg
       61 ngpilpwlns aardlrlwiv agtlplppdg qpeakanacs llidehgerv arydklhlfd
      121 vdvadargry resddyafgq kivvadtpvg rlgltvcydl rfpelytalr eagaelitap
      181 saftavtgaa hwqvlvrara ietqcyllaa gqggvhprgr etfghsaivd pwgrvlaerp
      241 qgeavllavr daaeqadirr rmpvvahrrf fppaeprpar te