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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//