ID A0A1U7QA35_MESAU Unreviewed; 562 AA.
AC A0A1U7QA35;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Phosphoglucomutase-1 {ECO:0000256|ARBA:ARBA00040178};
DE EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
DE AltName: Full=Glucose phosphomutase 1 {ECO:0000256|ARBA:ARBA00043051};
GN Name=Pgm1 {ECO:0000313|RefSeq:XP_005074388.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005074388.1};
RN [1] {ECO:0000313|RefSeq:XP_005074388.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: This enzyme participates in both the breakdown and synthesis
CC of glucose. {ECO:0000256|ARBA:ARBA00003488}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
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DR RefSeq; XP_005074388.1; XM_005074331.2.
DR AlphaFoldDB; A0A1U7QA35; -.
DR GeneID; 101835247; -.
DR KEGG; maua:101835247; -.
DR CTD; 5236; -.
DR eggNOG; KOG0625; Eukaryota.
DR OrthoDB; 5476118at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03085; PGM1; 1.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR045244; PGM.
DR PANTHER; PTHR22573:SF37; PHOSPHOGLUCOMUTASE-1; 1.
DR PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706}.
FT DOMAIN 15..157
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 194..299
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 307..420
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 562 AA; 61448 MW; 1A062BB6A6872A23 CRC64;
MVKIVTVKTQ AYPDQKPGTS GLRKRVKVFQ SNANYAENFI QSIVSTVEPA LRQEATLVVG
GDGRFYMTEA IQLIVRIAAA NGIGRLVIGQ NGILSTPAVS CIIRKIKAIG GIILTASHNP
GGPNGDFGIK FNISNGGPAP EAITDKIFQI SKTIEEYAIC PDLKVDLSVL GKQQFDLENK
FKPFTVEIVD SVEAYATMLR NIFDFNALKE LLSGPNRLKI RIDAMHGVVG PYVKKILCEE
LGAPANSAVN CVPLEDFGGH HPDPNLTYAA ELVETMKSGE HDFGAAFDGD GDRNMILGKH
GFFVNPSDSV AVIAANIFSI PYFQQTGVRG FARSMPTSGA LDRVANATKI ALYETPTGWK
FFGNLMDASK LSLCGEESFG TGSDHIREKD GLWAVLAWLS ILATRKQSVE DILKDHWQKF
GRNFFTRYDY EEVEAEGANK MMKDLEALML DRSFVGKQFS ANDKVYTVEK ADNFEYSDPV
DGSVSRNQGL RLIFADGSRI IFRLSGTGSA GATIRLYIDS YEKDAAKINQ DPQVMLAPLI
SIALKVSQLQ ERTGRTAPTV IT
//
