MULTISPECIES: aspartate--ammonia ligase [Shigella].

LOCUS       WP_000845131             330 aa            linear   BCT 04-JUN-2024
ACCESSION   WP_000845131
VERSION     WP_000845131.1
KEYWORDS    RefSeq.
SOURCE      Shigella
  ORGANISM  Shigella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
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  :: HMM
            Evidence Accession :: TIGR00669.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Shigella"
                     /db_xref="taxon:620"
     gene            1..330
                     /gene="asnA"
     Protein         1..330
                     /product="aspartate--ammonia ligase"
                     /EC_number="6.3.1.1"
                     /GO_component="GO:0005737 - cytoplasm [Evidence IEA]"
                     /GO_function="GO:0004071 - aspartate-ammonia ligase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006529 - asparagine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36512
     Region          1..330
                     /region_name="class_II_aaRS-like_core"
                     /note="Class II tRNA amino-acyl synthetase-like catalytic
                     core domain. Class II amino acyl-tRNA synthetases (aaRS)
                     share a common fold and generally attach an amino acid to
                     the 3' OH of ribose of the appropriate tRNA. PheRS is an
                     exception in that it attaches...; cl00268"
                     /db_xref="CDD:444800"
     Site            order(9..10,13,32..33,56,58,60,67,80,84,97,101..102,104,
                     313,317,323)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238350"
     Site            order(74,77,100,116,118,120,235,248,251,255,299)
                     /site_type="active"
                     /db_xref="CDD:238350"
ORIGIN      
        1 mktayiakqr qisfvkshfs rqleerlgli evqapilsrv gdgtqdnlsg cekavqvkvk
       61 alpdaqfevv hslakwkrqt lgqhdfsage glythmkalr pdedrlsplh svyvdqwdwe
      121 rvmgdgerql stlkstveai wagikateaa vneefglapf lpdqihfvhs qellsrypdl
      181 dakgreraia kdlgavflvg iggklsdghr hdvrapdydd wstpselgha glngdilvwn
      241 pvledafels smgirvdadt lkhqlaltgd edrlqlewhq allrgempqt igggigqsrl
      301 tmlllqlphi gqvqcgvwpa avresvpsll