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Database: UniProt
Entry: A0A101VR50_9FIRM
LinkDB: A0A101VR50_9FIRM
Original site: A0A101VR50_9FIRM 
ID   A0A101VR50_9FIRM        Unreviewed;       587 AA.
AC   A0A101VR50;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Phosphoglucomutase {ECO:0000256|ARBA:ARBA00039995};
DE   AltName: Full=Alpha-phosphoglucomutase {ECO:0000256|ARBA:ARBA00041467};
DE   AltName: Full=Glucose phosphomutase {ECO:0000256|ARBA:ARBA00041398};
GN   ORFNames=APF84_10015 {ECO:0000313|EMBL:KUO59258.1};
OS   Gracilibacter sp. BRH_c7a.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Gracilibacteraceae;
OC   Gracilibacter.
OX   NCBI_TaxID=1734398 {ECO:0000313|EMBL:KUO59258.1, ECO:0000313|Proteomes:UP000053404};
RN   [1] {ECO:0000313|EMBL:KUO59258.1, ECO:0000313|Proteomes:UP000053404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c7a {ECO:0000313|EMBL:KUO59258.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KUO59258.1}.
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DR   EMBL; LOEZ01000081; KUO59258.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101VR50; -.
DR   STRING; 1734398.APF84_10015; -.
DR   Proteomes; UP000053404; 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; 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   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}.
FT   DOMAIN          46..183
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          212..316
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          328..451
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   587 AA;  66051 MW;  C38EBEC837866B73 CRC64;
     MLIEDSVKEK FARWINNDCF DCATKDELLA LDDPSEIEDR FYTDLEFGTG GMRGIIGAGT
     NRMNKYVIRR LTQGLADTIK DHGEEACAKG VVIAHDPRRY SKEFALETAL VLAANGIKAY
     LFDSLRPVPE LSFAVRYLHT MAGVNITASH NPKEYNGYKV YWEDGGQIPP NKANIIVSKM
     SARESWEVEI SSETEARSNG FLVTIGEDID KAYLEQVKAQ LLYPELVADK GKMLKIVYSP
     LHGSGGMLIS RILKDTGFSS LFVVPEQKDP DTEFATVKSP NPEDPAAFEL ALTHAVQQNA
     DIVMASDPDA DRLGLYVKGD EGYYHRFNGN QIGVLLQYYI LSQRKKRGNL PDNAVVVKTV
     ASTDLGDAVA EKFGVKTVNV LVGFKYIGEQ IRDMEEKGWG TYQFGFEESF GYLAGTHARD
     KDAVVAAALL AEAALYYRQE ENKNLTDVLD EIHKMCGYYR DEQVALTYQG KAGKECIANI
     MNTLRKDKKI EIAGIPLKSR EDYYISRRQL IRENREEEID LPKANVLRFS FAEGGFVMAR
     PSGTEPKIRF YFCVKDDSPQ ALLETMKRVK EDFMGRIKEF LTIPYEQ
//
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