class II glutamine amidotransferase [Escherichia coli].

LOCUS       WP_001301698             255 aa            linear   BCT 01-APR-2023
ACCESSION   WP_001301698
VERSION     WP_001301698.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Zalkin,H. and Smith,J.L.
  TITLE     Enzymes utilizing glutamine as an amide donor
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 72, 87-144 (1998)
   PUBMED   9559052
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Zalkin,H.
  TITLE     The amidotransferases
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 66, 203-309 (1993)
   PUBMED   8430515
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 11206994
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..255
                     /product="class II glutamine amidotransferase"
                     /EC_number="2.4.2.-"
                     /GO_function="GO:0016740 - transferase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006541 - glutamine metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28530
     Region          1..252
                     /region_name="GATase_4"
                     /note="Glutamine amidotransferases class-II; pfam13230"
                     /db_xref="CDD:433047"
     Site            order(2,79,108..110,129)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238889"
     Site            order(47,50..51,96,120..121,142)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:238889"
ORIGIN      
        1 mcellgmsan vptdicfsft glvqrgggtg phkdgwgitf yegkgcrtfk dpqpsfnspi
       61 aklvqdypik scsvvahirq anrgevalen thpftrelwg rnwtyahngq ltgyksletg
      121 nfrpvgktds ekafcwllyk ltqryprtpg nmaavfkyia sladelrqkg vfnmllsdgr
      181 yvmaycstnl hwitrrapfg vatlldqdve idfssqttpn dvvtviatqp ltgnetwqki
      241 mpgewrlfcl gervv