ID A0A841KSL1_9FIRM Unreviewed; 579 AA.
AC A0A841KSL1;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 13.
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=HNQ80_002483 {ECO:0000313|EMBL:MBB6216383.1};
OS Anaerosolibacter carboniphilus.
OC Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
OC Thermotaleaceae; Anaerosolibacter.
OX NCBI_TaxID=1417629 {ECO:0000313|EMBL:MBB6216383.1, ECO:0000313|Proteomes:UP000579281};
RN [1] {ECO:0000313|EMBL:MBB6216383.1, ECO:0000313|Proteomes:UP000579281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 103526 {ECO:0000313|EMBL:MBB6216383.1,
RC ECO:0000313|Proteomes:UP000579281};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:MBB6216383.1}.
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DR EMBL; JACHEN010000014; MBB6216383.1; -; Genomic_DNA.
DR RefSeq; WP_184310918.1; NZ_JACHEN010000014.1.
DR AlphaFoldDB; A0A841KSL1; -.
DR Proteomes; UP000579281; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0008973; F:phosphopentomutase activity; IEA:TreeGrafter.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:TreeGrafter.
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 2B-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, ECO:0000313|EMBL:MBB6216383.1};
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:UP000579281}.
FT DOMAIN 43..182
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 210..317
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 327..450
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 520..549
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 579 AA; 64887 MW; E12B47A91431FE6C CRC64;
MGYRESYIEW INSGYFDEDI RKELQAIEGN EKEIEDRFYR DLEFGTGGLR GVIGAGTNRM
NKYTVRRATQ GFAQYLLEEV GGARQKGVVI AYDSRHMSPE FAEEAALVMN GNGIKAYLFE
ALRTTPELSY AVRELGCAGG IVITASHNPP EYNGYKVYGE DGGQIIPDEA EKIINEIQGI
KDYSSVNYIT KEEALSQELL VMIGEEIDRK YIDRVKSLVL RDELIKETGK DVKIVYTPLH
GTGNMPVRRV LKELGFEKVW VVPEQENPDS NFSTVKSPNP EEHQAFTLAL ALADQVDADV
IIGTDPDCDR VGAVVRNKDG AYQILTGNQT GALLIDYVLS AMKEADSIPK NGLVIKTIVT
SEMGAKIAQS YGVDSLDTLT GFKFIGEKIK EFETSREKEF IFGYEESYGY LAGTFVRDKD
AVIASMLICE MAAYYKSKGM TLYDALIGLF ERYGYYQEGL ESITLKGKEG MEKIDEILSY
FRLNPLSHMN DQKICILKDY DHGKHVDLLI GETSDLTLPK SNVLHFTLED GSWFCIRPSG
TEPKVKIYFS VVGNSLDGAI QKLDELKREV MGLIRELID
//
