ID A0A1I7EX19_9FIRM Unreviewed; 550 AA.
AC A0A1I7EX19;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=SAMN05216508_10168 {ECO:0000313|EMBL:SFU28429.1};
OS Eubacterium pyruvativorans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=155865 {ECO:0000313|EMBL:SFU28429.1, ECO:0000313|Proteomes:UP000198817};
RN [1] {ECO:0000313|EMBL:SFU28429.1, ECO:0000313|Proteomes:UP000198817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KHGC13 {ECO:0000313|EMBL:SFU28429.1,
RC ECO:0000313|Proteomes:UP000198817};
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; FPBT01000001; SFU28429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7EX19; -.
DR STRING; 155865.SAMN05216515_10269; -.
DR Proteomes; UP000198817; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 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:UP000198817}.
FT DOMAIN 48..183
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 208..310
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 319..442
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 474..538
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 550 AA; 62625 MW; FD7E3F59087C199C CRC64;
MREMREHAEQ EYRRWLENTE DDSSMHAELL KLMGNDDEIF DAFYQDLSFG TSGLRGILGP
GTNRMNVYVV RRASQGIANY LKKHYDRPSV VIAYDTRKDS ELFAREAAAV FRGNKVKTHL
FGEVTPVSVL AFAIRQLKCS MGVMITASHN PKHYNGYKVY NSDGYQVIGQ EPEMILEEIG
RVDFFEGIHR KLDNGVMTVS TRVSEDFIRA ALKRPPHISP EAVNQLKTVY TPLHGTGLKY
VRSLFKNVGY SNYTVVRSQE YPDPAFHTCS TPNPEKILTY DEAFKVIDRE GGELIVATDP
DADRCGAALY HDGVRTIVTG NQLGLLMLDY LCHMEPPEPD QIVAKSIVTS PLVNQMARKY
GFKVVNNVPG FRYIGNILAR LDQAGQGNRF YLGFEESNSF LVNPFSHEKD GITAAMLIVE
IAAFHKAQGK DLIDRLNEIY EEFGRCVDKQ RNYFFSGAGG RRTMDQIMTY LRREVRTRLG
DKEVIRKVDY LRDTGLPKAD ALEFDFHDGS RLIIRPSGTE AKLKVYSFET DDFKSVERDM
VRIIERFSQV
//
