P38652
uniprot
P38652
canonical
amino_acid_sequence
MVKIVTVKTQAYPDQKPGTSGLRKRVKVFQGNANYAENFIQSIVSTVEPALRQEATLVVGGDGRFYMTEAIQLIVRIAAANGIGRLVIGQNGILSTPAVSCIIRKIKAIGGIILTASHNPGGPNGDFGIKFNISNGGPAPEAITDKIFQISKTIEEYAICPDLKVDLGVLGKQQFDLENKFKPFTVEIVDSVEAYATMLRNIFDFNALKELLSGPNRLKIRIDAMHGVVGPYVKKILCEELGAPANSAVNCVPLEDFGGHHPDPNLTYAADLVETMKSGEHDFGAAFDGDGDRNMILGKHGFFVNPSDSVAVIAANIFSIPYFQQTGVRGFARSMPTSGALDRVANATKIASYETPTGWKFFGNLMDASKLSLCGEESFGTGSDHIREKDGLWAVLAWLSILATRKQRVEDILKDHWQKFGRNFFTRYDYEEVEAEGANKMMKDLEALMLDRSFVGKQFSANDKVYTVEKADNFEYSDPVDGSISKNQGLRLIFADGSRIIFRLSGTGSAGATIRLYIDSYEKDAAKINQDPQVMLAPLISIALKVSQLQERTGRTAPTVIT
uniprot
proteins
ec_number
5.4.2.2
uniprot
proteins
function
FUNCTION: Catalyzes the reversible isomerization of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate (PubMed:8224913). The mechanism proceeds via the intermediate compound alpha-D-glucose 1,6-bisphosphate (Probable). This enzyme participates in both the breakdown and synthesis of glucose (By similarity). {ECO:0000250|UniProtKB:P36871, ECO:0000269|PubMed:8224913, ECO:0000305|PubMed:8224913}.
uniprot
proteins
mass_dalton
61403
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-467 by PAK1 significantly enhances enzymatic activity. {ECO:0000250|UniProtKB:P36871}.
uniprot
proteins
protein_family
Phosphohexose mutase family
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
8224913
uniprot
proteins
sequence_length
562
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm.
uniprot
proteins