MULTISPECIES: phosphoglucomutase

LOCUS       WP_005049438             546 aa            linear   BCT 17-NOV-2023
            (alpha-D-glucose-1,6-bisphosphate-dependent) [Shigella].
ACCESSION   WP_005049438
VERSION     WP_005049438.1
KEYWORDS    RefSeq.
SOURCE      Shigella
  ORGANISM  Shigella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Kvam,C., Olsvik,E.S., McKinley-McKee,J. and Saether,O.
  TITLE     Studies on recombinant Acetobacter xylinum alpha-phosphoglucomutase
  JOURNAL   Biochem J 326 (Pt 1), 197-203 (1997)
   PUBMED   9337869
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 :: TIGR01132.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Shigella"
                     /db_xref="taxon:620"
     gene            1..546
                     /gene="pgm"
     Protein         1..546
                     /product="phosphoglucomutase
                     (alpha-D-glucose-1,6-bisphosphate-dependent)"
                     /EC_number="5.4.2.2"
                     /GO_function="GO:0004614 - phosphoglucomutase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=58246
     Region          2..544
                     /region_name="pgm"
                     /note="phosphoglucomutase, alpha-D-glucose
                     phosphate-specific; TIGR01132"
                     /db_xref="CDD:273459"
     Site            order(43,45,48,146..148,156,304,306,308..309,350,371..373,
                     390,392,394,507,509..511,516)
                     /site_type="active"
                     /db_xref="CDD:100094"
     Site            order(45,146,309,350,371,373,390,392,394,507,509..511,516)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100094"
     Site            order(146,304,306,308)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:100094"
ORIGIN      
        1 maihnragqp aqqsdlinva qltaqyyvlk peagnaehav kfgtsghrgs aarhsfneph
       61 ilaiaqaiae erakngitgp cyvgkdthal sepafisvle vlaangvdvi vqenngftpt
      121 pavsnailvh nkkggpladg ivitpshnpp edggikynpp nggpadtnvt kvvedkanal
      181 madglkgvkr isldeamasg yvkeqdlvqp fvegladivd maaiqkaglt lgvdplggsg
      241 ieywkrigey ynlnltivnd qvdqtfrfmh ldkdgairmd cssecamagl lalrdkfdla
      301 fandpdydrh givtpaglmn pnhylavain ylfqhrpqwg kdvavgktlv ssamidrvvn
      361 dlgrklvevp vgfkwfvdgl fdgsfgfgge esagasflrf dgtpwstdkd giimcllaae
      421 itavtgknpq ehynelakrf gapsynrlqa aatsaqkaal sklspemvsa stlagdpita
      481 rltaapgnga sigglkvmtd ngwfaarpsg tedaykiyce sflgeehrkq iekeaveivs
      541 evlkna