MULTISPECIES: methylaspartate mutase subunit S

LOCUS       WP_000710390             149 aa            linear   BCT 07-MAR-2022
            [Enterobacteriaceae].
ACCESSION   WP_000710390
VERSION     WP_000710390.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Zelder,O., Beatrix,B., Leutbecher,U. and Buckel,W.
  TITLE     Characterization of the coenzyme-B12-dependent glutamate mutase
            from Clostridium cochlearium produced in Escherichia coli
  JOURNAL   Eur J Biochem 226 (2), 577-585 (1994)
   PUBMED   7880251
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 :: NF002612.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK02261
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     gene            1..149
                     /gene="glmS"
     Protein         1..149
                     /product="methylaspartate mutase subunit S"
                     /EC_number="5.4.99.1"
                     /GO_function="GO:0050097 - methylaspartate mutase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=16299
     Region          1..137
                     /region_name="PRK02261"
                     /note="methylaspartate mutase subunit S; Provisional"
                     /db_xref="CDD:179400"
     Site            order(13..19,22,59..61,63..65,93,117,120,125)
                     /site_type="other"
                     /note="B12 binding site [chemical binding]"
                     /db_xref="CDD:239023"
     Site            order(13,15,17..18,21..22,25,37..40,64,66,68..70,93,
                     96..98,107,119)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:239023"
     Site            16
                     /site_type="other"
                     /note="cobalt ligand [ion binding]"
                     /db_xref="CDD:239023"
ORIGIN      
        1 mkkatlvigv igadchavgn kvldrvfsnh dfrvinlgvm vsqdeyidaa ietgadaivv
       61 ssiyghgdid clgmrercie rglgdillyv ggnlvvgkhd fadvetkfke mgfdrvfaps
      121 hdledvcqlm ahdinqrhdv dtrileeai