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Database: UniProt
Entry: G7SH86_STRSU
LinkDB: G7SH86_STRSU
Original site: G7SH86_STRSU 
ID   G7SH86_STRSU            Unreviewed;       572 AA.
AC   G7SH86;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 53.
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=SSUD12_1118 {ECO:0000313|EMBL:AER19418.1};
OS   Streptococcus suis D12.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1004952 {ECO:0000313|EMBL:AER19418.1, ECO:0000313|Proteomes:UP000008845};
RN   [1] {ECO:0000313|EMBL:AER19418.1, ECO:0000313|Proteomes:UP000008845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D12 {ECO:0000313|EMBL:AER19418.1};
RX   PubMed=22026465; DOI=10.1186/1471-2164-12-523;
RA   Zhang A., Yang M., Hu P., Wu J., Chen B., Hua Y., Yu J., Chen H., Xiao J.,
RA   Jin M.;
RT   "Comparative Genomic Analysis of Streptococcus suis reveals significant
RT   genomic diversity among different serotypes.";
RL   BMC Genomics 12:523-523(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; CP002644; AER19418.1; -; Genomic_DNA.
DR   RefSeq; WP_014638080.1; NC_017621.1.
DR   AlphaFoldDB; G7SH86; -.
DR   KEGG; ssk:SSUD12_1118; -.
DR   PATRIC; fig|1004952.3.peg.1094; -.
DR   HOGENOM; CLU_016950_0_0_9; -.
DR   Proteomes; UP000008845; Chromosome.
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; 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};
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..180
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          209..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          509..548
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   572 AA;  63023 MW;  00FE74224A7C5017 CRC64;
     MTYQETYQTW LDFTDLPDYL REELVAMDEK TKEDAFYTNL EFGTAGMRGY IGAGTNRINV
     FVVRQATEGL AKLVESKGEE AKKRGVAIAY DSRHFSPEFA FESAQVLAAH GIKSYVFESL
     RPTPELSFAV RHYNAIAGIM VTASHNPKEF NGYKVYGEDG GQMPPADADA LTNFIRAIDN
     PFAVELADLE ASKENGLITV LGEETDLKYL EELKDLNINP ELIAEYGKDM KIVYTPLHGT
     GEMLARRALA QAGFESVQVV EAQATADPDF STVASPNPES QAAFALAEEL GREVGADVLL
     ATDPDADRVG VEVRQADGSY WNLSGNQIGA IIAKYILEAH KQAGTLPANA ALAKSIVSTE
     LVTKIAESYG ATMFNVLTGF KFIAEKIQEF EEKHNYTYMF GFEESFGYLI KPFVRDKDAI
     QAVLIVAEIA AYYRSRGMTL ADGIDEIFKE YGYFAEKTIS VTLSGKDGAE QIKAIMAKFR
     NNSPAQFNAT DIAVFEDFAL QTKTDKDGNV EKLTTPPSDV LKYTLADDSW FAVRPSGTEP
     KIKFYIATVG ETLAEAEEKI ANIEKEINDF VG
//
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