ID A0A287DGJ8_ICTTR Unreviewed; 580 AA.
AC A0A287DGJ8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Phosphoglucomutase 1 {ECO:0000313|Ensembl:ENSSTOP00000032660.1};
GN Name=PGM1 {ECO:0000313|Ensembl:ENSSTOP00000032660.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000032660.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000032660.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
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DR EMBL; AGTP01094937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005337772.1; XM_005337715.2.
DR AlphaFoldDB; A0A287DGJ8; -.
DR STRING; 43179.ENSSTOP00000032660; -.
DR Ensembl; ENSSTOT00000033399.1; ENSSTOP00000032660.1; ENSSTOG00000007561.3.
DR GeneTree; ENSGT00940000155542; -.
DR InParanoid; A0A287DGJ8; -.
DR OrthoDB; 5476118at2759; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:Ensembl.
DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
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:SF60; 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 Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215}.
FT DOMAIN 33..175
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 212..317
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 325..438
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 580 AA; 63812 MW; C5AD00C51FB3E455 CRC64;
MSDFEEWISG TYRKMEEGPL PLLTFATAPY HDQKPGTSGL RKKAYYFEAK PCYLENFIQS
IFFSIDLKDR QGSSLVVGGD GRYFNKSAIE TIVQMAAANG IGRLVIGQNG ILSTPAVSCI
IRKIKAIGGI ILTASHNPGG PNGDFGIKFN ISNGGPAPEA ITDKIFQISK TIEEYAICPD
LKVDLGVLGK QQFDLENKFK PFTVEIVDSV EAYATMLRNI FDFNALKELL SGPNRLKIRI
DAMHGVVGPY VKKILCEELG APANSAVNCV PLEDFGGHHP DPNLTYAADL VETMKSGEHD
FGAAFDGDGD RNMILGKHGF FVNPSDSVAV IAANIFSIPY FQQTGVRGFA RSMPTSGALD
RVANATKIAL YETPTGWKFF GNLMDASKLS LCGEESFGTG SDHIREKDGL WAVLAWLSIL
ATRKQSVEDI LKDHWQKYGR NFFTRYDYEE VEAEGANKMM KDLETLMFDR SFVGKQFSAN
DKVYTVEKAD NFEYSDPVDG SISRNQGLRL IFADGSRIIF RLSGTGSAGA TIRLYIDSYE
KDVAKINQDP QVMLAPLISI ALKVSQLQER TGRTAPTVIT
//
