MULTISPECIES: aspartate--ammonia ligase [Klebsiella].

LOCUS       WP_002882514             330 aa            linear   BCT 04-JUN-2024
ACCESSION   WP_002882514
VERSION     WP_002882514.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
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="Klebsiella"
                     /db_xref="taxon:570"
     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=36681
     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 rqleeklgli evqapilsrv gdgtqdnlsg cekavqvkvk
       61 tlpdaqfevv hslakwkrqt lgqhdfsage glythmkalr pdedrltpih svyvdqwdwe
      121 rvmgdeerhv gtlkatveai yagikatela vsqefgltpf lpeqihfvhs qellsrypel
      181 dakgreraia kelgavflig iggkladgkr hdvrapdydd wstevsegfa glngdilvwn
      241 pvledafeis smgirvdaea lkrqlaltgd edrlklewhq allrgempqt igggigqsrl
      301 tmlllqldhi gqvqcgvwpa qvresvsall