ID W5MI44_LEPOC Unreviewed; 612 AA.
AC W5MI44;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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|Ensembl:ENSLOCP00000008053.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000008053.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000008053.1}
RP IDENTIFICATION.
RG Ensembl;
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}.
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DR EMBL; AHAT01015964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MI44; -.
DR STRING; 7918.ENSLOCP00000008053; -.
DR Ensembl; ENSLOCT00000008063.1; ENSLOCP00000008053.1; ENSLOCG00000006665.1.
DR eggNOG; KOG0027; Eukaryota.
DR eggNOG; KOG0625; Eukaryota.
DR GeneTree; ENSGT00940000155542; -.
DR InParanoid; W5MI44; -.
DR Proteomes; UP000018468; Linkage group LG10.
DR Bgee; ENSLOCG00000006665; Expressed in muscle tissue and 13 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR CDD; cd00051; EFh; 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 Gene3D; 1.10.238.10; EF-hand; 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; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR045244; PGM.
DR PANTHER; PTHR22573:SF37; PHOSPHOGLUCOMUTASE-1; 1.
DR PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 1.
DR Pfam; PF13499; EF-hand_7; 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; SSF47473; EF-hand; 1.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 85..120
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 612 AA; 67642 MW; 3E1B532161233246 CRC64;
MTSYTAPVAG SHSEEGTFYR NCRAAYVAVF RSSLVNISSK EELCLVLQQA GRNPSRKVLG
KYWTPRTTKL NFDDFCEILK KEKPTEESDL IKAFRTIDLN SDGYVTHSEL FKVLTSRGEK
MSPEEVNRIF SVADTSQNGT GDHSKIGRLV IGQNGILSTP AVSCIIRKIK AIGGIILTAS
HNPGGPNGDF GIKFNISNGG PAPEAVTDKI FQISKTIEEY AICPDLKVDL TTIGKQQFDL
ENKFKPFTVE IIDSVESYAN MLRNIFDFAA LKELLSGQNQ LKIRIDAMHG VVGPYVKKIL
CEELGSPANS AVNCVPLEDF GGHHPDPNLT YAADLVETMK GGEYDFGAAF DGDGDRNMVL
GKHGFFVNPS DSVAVIAANI FSIPYFQHTG VRGFARSMPT SGALDNVAKA TKITLYETPT
GWKFFGNLMD ANKLSLCGEE SFGTGSDHIR EKDGLWAVLA WLSIIAARKQ SVEDILKEHW
QKYGRNFFTR YDYEEVDSDS ASKMMKDLEA MMLDRAFIGQ KFSVGDKTYT VERADNFEYS
DSVDGSISRN QGLRIIFSDG SRVIFRLSGT GSAGATVRLY IDSYEKDPQK IYQDPQVSLG
YNCLESKLIH CL
//
