2-oxoglutaramate amidase [Escherichia coli].

LOCUS       WP_001118031             256 aa            linear   BCT 10-JUL-2019
ACCESSION   WP_001118031
VERSION     WP_001118031.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Peracchi,A., Veiga-da-Cunha,M., Kuhara,T., Ellens,K.W., Paczia,N.,
            Stroobant,V., Seliga,A.K., Marlaire,S., Jaisson,S., Bommer,G.T.,
            Sun,J., Huebner,K., Linster,C.L., Cooper,A.J.L. and Van
            Schaftingen,E.
  TITLE     Nit1 is a metabolite repair enzyme that hydrolyzes deaminated
            glutathione
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 114 (16), E3233-E3242 (2017)
   PUBMED   28373563
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  :: BlastRule
            Evidence Accession :: NBR007568
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..256
                     /gene="yafV"
     Protein         1..256
                     /product="2-oxoglutaramate amidase"
                     /EC_number="3.5.1.111"
                     /calculated_mol_wt=28820
     Region          1..256
                     /region_name="PRK10438"
                     /note="C-N hydrolase family amidase; Provisional"
                     /db_xref="CDD:182461"
     Site            order(42,48,107,111,116,141..142,144..145,164..165)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143599"
     Site            order(42,107,141)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143599"
     Site            order(108..109,113,142,145..149,151,171..172,175..176,
                     178..180,182..183,211,213..221,225,227..228,230,243..246,
                     248..253)
                     /site_type="other"
                     /note="multimer interface [polypeptide binding]"
                     /db_xref="CDD:143599"
     Site            order(108..109,113,142,145..149,151,171..172,175..176,
                     178..180,182..183,213..215,243..246,248..253)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:143599"
ORIGIN      
        1 mpglkitllq qplvwmdgpa nlrhfdrqle gitgrdvivl pemftsgfam eaaasslaqd
       61 dvvnwmtaka qqcnaliags valqtesgsv nrfllvepgg tvhfydkrhl frmadehlhy
      121 kagnarvive wrgwrilplv cydlrfpvws rnlndydlai yvanwpaprs lhwqalltar
      181 aienqayvag cnrvgsdgng chyrgdsrvi npqgeiiata dahqatrida elsmvalrey
      241 rekfpawrda defrlr