phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent)

LOCUS       WP_001302267             546 aa            linear   BCT 22-MAR-2021
            [Escherichia coli].
ACCESSION   WP_001302267
VERSION     WP_001302267.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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="Escherichia coli"
                     /db_xref="taxon:562"
     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=58204
     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 kvvedranal
      181 madglkgvkr isldeamasg hvkeqdlvqp fvegladivd maaiqkaglt lgvdplggsg
      241 ieywkrigey ynlnltivnd qvdqtfrfmh ldkdgairmd cssecamagl lalrdkfdla
      301 fandpdydrh givtpaglmn pnhylavain ylfqhrpqwg kavavgktlv ssamidrvvn
      361 dlgrklvevp vgfkwfvdgl fdgsfgfgge esagasflrf dgtpwstdkd giimcllaae
      421 itavtgknpq ehynelakrf gapsynrlqa aatsaqkaal sklspemvsa stlagdpita
      481 rltaapgnga sigglkvmtd ngwfaarpsg tedaykiyce sflgeehrkq iekeaveivs
      541 evlkna