ID A0A1G8MZQ2_9BACI Unreviewed; 578 AA.
AC A0A1G8MZQ2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Phosphoglucomutase {ECO:0000256|ARBA:ARBA00039995};
DE EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
DE AltName: Full=Alpha-phosphoglucomutase {ECO:0000256|ARBA:ARBA00041467};
DE AltName: Full=Glucose phosphomutase {ECO:0000256|ARBA:ARBA00041398};
GN ORFNames=SAMN05216352_11148 {ECO:0000313|EMBL:SDI73471.1};
OS Alteribacillus bidgolensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacillus.
OX NCBI_TaxID=930129 {ECO:0000313|EMBL:SDI73471.1, ECO:0000313|Proteomes:UP000199017};
RN [1] {ECO:0000313|EMBL:SDI73471.1, ECO:0000313|Proteomes:UP000199017}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P4B,CCM 7963,CECT 7998,DSM 25260,IBRC-M 10614,KCTC 13821
RC {ECO:0000313|Proteomes:UP000199017};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005164}.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
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DR EMBL; FNDU01000011; SDI73471.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8MZQ2; -.
DR STRING; 930129.SAMN05216352_11148; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000199017; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR CDD; cd05799; PGM2; 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; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022526};
KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000199017}.
FT DOMAIN 43..181
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 210..314
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 326..453
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 520..553
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 578 AA; 65618 MW; 2E75EB0267B49854 CRC64;
MEWRKHWERW KKNIWLDQEL KKQLEQISMD EKQLEDSFYK YLEFGTGGMR GEIGPGTNRM
NKFTIRRAAE GLARFIEEHG EQAKSRGVVI AFDSRYHSKE FALETAFTLG AHKIQTYIFQ
ELRPTPELSY AVRKLKAFAG VVITASHNPP EYNGFKIYGD DGGQFPPEPA KAIIEKVEQV
EDELLVEAAE ENEMKASRLL KVIGEEIDEA YNDELQTISV NPELIQEKGE QVSIVFTPLH
GTANIPVSRV LETSGFSNVH IVKEQALPDP EFSTIKSPNP EEKAAFELAI NEGIKHDADV
LIATDPDADR VGVAVKGADT HYQLLTGNQT GALLLEYLLS ERKKKGFIPD NGVMLKTIVT
SEIGRVIAEN YGLKVMDTLT GFKFIGEKIK QFEKDGTYDF QFGYEESYGY LIGDFVRDKD
AVQAALLAAE MTLWYKDQGK TLYDGLIDIY EKYGYYLEDL DSLTLKGKEG AEKIYRLLKD
FRLNPPTSIS GKSITIIEDY QTSERSFIKG GKKEKIELPV SNVLKYIRED GAWFCIRPSG
TEPKVKFYFG VTEKNMESAE EHLLQLKMDV MAKVNQYI
//
