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Database: UniProt
Entry: C0JPQ2_OENOE
LinkDB: C0JPQ2_OENOE
Original site: C0JPQ2_OENOE 
ID   C0JPQ2_OENOE            Unreviewed;       177 AA.
AC   C0JPQ2;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 34.
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};
DE   Flags: Fragment;
GN   Name=pgm {ECO:0000313|EMBL:ACN56509.1};
OS   Oenococcus oeni (Leuconostoc oenos).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Oenococcus.
OX   NCBI_TaxID=1247 {ECO:0000313|EMBL:ACN56509.1};
RN   [1] {ECO:0000313|EMBL:ACN56509.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=19114515; DOI=10.1128/AEM.02563-08;
RA   Bilhere E., Lucas P.M., Claisse O., Lonvaud-Funel A.;
RT   "Multilocus sequence typing of Oenococcus oeni: detection of two
RT   subpopulations shaped by intergenic recombination.";
RL   Appl. Environ. Microbiol. 75:1291-1300(2009).
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}.
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DR   EMBL; FJ403350; ACN56509.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0JPQ2; -.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 2.
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; 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   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 2.
PE   3: Inferred from homology;
FT   DOMAIN          2..58
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          83..176
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACN56509.1"
FT   NON_TER         177
FT                   /evidence="ECO:0000313|EMBL:ACN56509.1"
SQ   SEQUENCE   177 AA;  19618 MW;  446FD8AA50C23A30 CRC64;
     GPHPTPELSF AVMHLHTYAG IMITASHNSK EYNGYKLYGE DGGQLPPKPA DEIVRERQEV
     TDIFHIKKVA GGIKKIGSEI DKEYLNQVKT IPINRDLIKK WGDKLTISFT PLHGAGGDLG
     SKALKEAGFN KILTVKEQFK PDGTFPTVKY PNPEFYEVFK ISESYGADVE LAVDPDS
//
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