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Entry: F2QD93_STROU
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ID   F2QD93_STROU            Unreviewed;       572 AA.
AC   F2QD93;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
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   Name=pgmA {ECO:0000313|EMBL:CBZ00611.1};
GN   OrderedLocusNames=SOR_0952 {ECO:0000313|EMBL:CBZ00611.1};
OS   Streptococcus oralis (strain Uo5).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=927666 {ECO:0000313|EMBL:CBZ00611.1, ECO:0000313|Proteomes:UP000008131};
RN   [1] {ECO:0000313|EMBL:CBZ00611.1, ECO:0000313|Proteomes:UP000008131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Uo5 {ECO:0000313|EMBL:CBZ00611.1,
RC   ECO:0000313|Proteomes:UP000008131};
RX   PubMed=21460080; DOI=10.1128/JB.00321-11;
RA   Reichmann P., Nuhn M., Denapaite D., Bruckner R., Henrich B., Maurer P.,
RA   Rieger M., Klages S., Reinhard R., Hakenbeck R.;
RT   "Genome of Streptococcus oralis strain Uo5.";
RL   J. Bacteriol. 193:2888-2889(2011).
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; FR720602; CBZ00611.1; -; Genomic_DNA.
DR   RefSeq; WP_000222129.1; NC_015291.1.
DR   AlphaFoldDB; F2QD93; -.
DR   KEGG; sor:SOR_0952; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_0_0_9; -.
DR   Proteomes; UP000008131; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:RHEA.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:CBZ00611.1};
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}.
FT   DOMAIN          41..179
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          226..311
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          325..451
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          504..547
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   572 AA;  62720 MW;  2482EB542AE21500 CRC64;
     MTYQENYQKW VDFADLPDYL RQDLENMDEK TKEDAFYTNL EFGTAGMRGL IGAGTNRINI
     YVVRQATEGL ARLIESKGGN EKERGVAIAY DSRHFSPEFA FESAAVLAKH DIKSYVFESL
     RPTPELSFAV RHLNCFAGIM ITASHNPAPF NGYKVYGEDG GQMPPHDADA LTTYIRGIEN
     PFAVEVADVE AEKASGLIEV IGEAVDAEYL KEVKDVNINP ALIEEFGTDM KIVYTPLHGT
     GEMLARRALA QAGFDSVQVV EAQATADPDF STVKSPNPES QAAFALAEEL GRQVGADVLV
     ATDPDADRVG VEVLQKDGSY LNLSGNQIGA IMAKYILEAH KNAGTLPENA ALCKSIVSTD
     LVTKIAESYG ATMFNVLTGF KFIAEKIQEF EEKHNHTYMM GFEESFGYLI KPFVRDKDAI
     QAVLVVAELA AYYRSRGLTL ADGIEEIYKE YGYFAEKTIS VTLSGVDGAE QIKEIMAKFR
     NNAPKEWNTT AITIVEDFKA QTATAADGTV TNFTTPPSDV LKYTLADGSW IAVRPSGTEP
     KIKFYIAVVG ESNEDSQAKI ANIEAEINAF VK
//
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