ID   PGCA_STAA8              Reviewed;         552 AA.
AC   Q2FVC1;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Phosphoglucomutase;
DE            Short=PGM;
DE            EC=5.4.2.2;
DE   AltName: Full=Alpha-phosphoglucomutase;
DE   AltName: Full=Glucose phosphomutase;
GN   Name=pgcA; OrderedLocusNames=SAOUHSC_02793;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   FUNCTION IN GLYCOLIPID AND LTA BIOSYNTHESIS, AND PATHWAY.
RX   PubMed=17209021; DOI=10.1128/jb.01683-06;
RA   Gruendling A., Schneewind O.;
RT   "Genes required for glycolipid synthesis and lipoteichoic acid anchoring in
RT   Staphylococcus aureus.";
RL   J. Bacteriol. 189:2521-2530(2007).
CC   -!- FUNCTION: Catalyzes the interconversion between glucose-6-phosphate and
CC       alpha-glucose-1-phosphate (Probable). This is the first step in the
CC       biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG), i.e. the
CC       predominant glycolipid found in the S.aureus membrane, which is also
CC       used as a membrane anchor for lipoteichoic acid (LTA).
CC       {ECO:0000269|PubMed:17209021, ECO:0000305}.
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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis.
CC       {ECO:0000269|PubMed:17209021}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD31796.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000253; ABD31796.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_501252.1; NC_007795.1.
DR   AlphaFoldDB; Q2FVC1; -.
DR   SMR; Q2FVC1; -.
DR   STRING; 1280.SAXN108_2739; -.
DR   PRIDE; Q2FVC1; -.
DR   EnsemblBacteria; ABD31796; ABD31796; SAOUHSC_02793.
DR   GeneID; 3921447; -.
DR   KEGG; sao:SAOUHSC_02793; -.
DR   PATRIC; fig|93061.5.peg.2525; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_0_0_9; -.
DR   UniPathway; UPA00894; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008973; F:phosphopentomutase activity; IBA:GO_Central.
DR   GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IBA:GO_Central.
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   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; SSF53738; SSF53738; 3.
DR   SUPFAM; SSF55957; SSF55957; 1.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glucose metabolism; Isomerase; Magnesium;
KW   Metal-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..552
FT                   /note="Phosphoglucomutase"
FT                   /id="PRO_0000308336"
FT   ACT_SITE        143
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         297
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   552 AA;  62377 MW;  BBD3821D6991CB3A CRC64;
     MKGCLATMDK ELWIERANDS LVKHFYEQQS DIEQREGFES KLTFGTAGIR GKFGLGEGRL
     NKFTIEKLAL GLARYLNAQT NSPTIVIHYD IRHLSTEFAQ IIANVLANHQ ITVYLPDTYK
     TTPELSFAVR NLNTTAGIMI TASHNPKDYN GIKVYGSDGA QLSTDASELA SRYIEEVGDP
     LQIDIPISKQ NTSYIKPFPK SVTDDYMKHI QNMIGYIPKS DLQVVFTSLH GTSVPIVPEL
     LQSLNFNQFN LVEAQCKPDP NFSSVQSANP EDHRAFDQAV ELANKSHADL LISTDPDADR
     LGIAERDAHG HITYFNGNQI GALLLNYRIQ QTSQLRHRLM IQSIVSSELT KSLARYNNVE
     YKEVLTGFKF IAQEIRQLDD HQNMIFAFEE SYGFLSEPFV RDKDAVQIVP LIIKYASELK
     LYGKTLKDEL EQIYQTVGRH EDTLFSHTLE GFEGKKKINA IMTKFRSNPP QEIQGLKVKA
     IEDYLTSEVY HLDKDTTSQI NSPKSNVIRV LFDEGFIALR PSGTEPKIKL YVSLKCPNFD
     DVAQKINAMI FS