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Database: UniProt
Entry: A0A373LLL5_9FIRM
LinkDB: A0A373LLL5_9FIRM
Original site: A0A373LLL5_9FIRM 
ID   A0A373LLL5_9FIRM        Unreviewed;       578 AA.
AC   A0A373LLL5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=DW006_08000 {ECO:0000313|EMBL:RGF50588.1};
OS   Eubacterium sp. AF36-5BH.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=2293108 {ECO:0000313|EMBL:RGF50588.1, ECO:0000313|Proteomes:UP000262191};
RN   [1] {ECO:0000313|EMBL:RGF50588.1, ECO:0000313|Proteomes:UP000262191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF36-5BH {ECO:0000313|EMBL:RGF50588.1,
RC   ECO:0000313|Proteomes:UP000262191};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) 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:RGF50588.1}.
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DR   EMBL; QTVG01000006; RGF50588.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A373LLL5; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000262191; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000262191}.
FT   DOMAIN          43..179
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          207..312
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          326..452
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   578 AA;  64701 MW;  4A6BE99A34152D73 CRC64;
     MDYRELYNEW LTNPYFDDNT KKELEAIEND DKEIEDRFYK ELEFGTAGLR GVIGAGTNRM
     NIYTVRKATQ GLANYIIKMH GEDKGVAIAY DSRHMSPEFA DEAALCLNAN GIKAYVFDSL
     RPTPELSFAV RELKCIAGIN VTASHNPAEY NGYKVYWEDG AQITPPHDVG IMDAVAALKD
     YNKVKTMDKD QAVADGLYIQ IGKEVDDKYI EILKTQVKNP DAIKEVQKDI KIVYTPLHGT
     GNIPVRRVLK ELGFENVYVV KEQELPDGDF PTVGYPNPES AKAFELAVKL GNEVGADLLL
     ATDPDADRLG VYVKGSKPGT YHILTGNMSG CLLAEYEISQ LKEKGQLPSD GAFIKSIVST
     NLANDIAKYY NINLFEVLTG FKYIGEKMLD FEVNHTGTYV FGFEESYGCL IGTHARDKDA
     IVASMALCEA AAYYKTKGMS LWDKMKEMYE RYGYWSDGVQ SIELKGKEGI EKIQNTLEKL
     RENVPTTVDN YKVLSVRDYL ADTVTNMETG DVTTTGLPKS NVLYLDLSEC AWVCIRPSGT
     EPKLKFYYGV KGENFDDSKA KLADLGSYMI NMVNEMLK
//
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