ID   PGCA_STAES              Reviewed;         546 AA.
AC   Q8CN38;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=SE_2042;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
CC   -!- FUNCTION: Catalyzes the interconversion between glucose-6-phosphate and
CC       alpha-glucose-1-phosphate. This is the first step in the biosynthesis
CC       of diglucosyl-diacylglycerol (Glc2-DAG), i.e. a glycolipid found in the
CC       membrane, which is also used as a membrane anchor for lipoteichoic acid
CC       (LTA) (By similarity). {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR   EMBL; AE015929; AAO05683.1; -; Genomic_DNA.
DR   RefSeq; NP_765597.1; NC_004461.1.
DR   RefSeq; WP_002484958.1; NZ_WBME01000003.1.
DR   AlphaFoldDB; Q8CN38; -.
DR   SMR; Q8CN38; -.
DR   STRING; 176280.SE_2042; -.
DR   EnsemblBacteria; AAO05683; AAO05683; SE_2042.
DR   KEGG; sep:SE_2042; -.
DR   PATRIC; fig|176280.10.peg.1995; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_0_0_9; -.
DR   OMA; PQDNGYK; -.
DR   UniPathway; UPA00894; -.
DR   Proteomes; UP000001411; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
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   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   3: Inferred from homology;
KW   Carbohydrate metabolism; Glucose metabolism; Isomerase; Magnesium;
KW   Metal-binding; Phosphoprotein.
FT   CHAIN           1..546
FT                   /note="Phosphoglucomutase"
FT                   /id="PRO_0000308346"
FT   ACT_SITE        135
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         290
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         292
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   546 AA;  60899 MW;  AAE01A6922EC88EC CRC64;
     MKNNWIDVLD ESLVKDFYNN QTSEEQQEGL NTTLSFGTAG IRGKFGLGEG RLNKFTVSKV
     ALGFAHYLTS SIAHPVVVIH YDTRHLSPEF AQIIANILAS LDIKVYLADT YRTTPDLSFA
     VRYLQADAGV MITASHNPKD YNGIKVYGED GAQLSTDDSA RLSTYIDKLG HPLHINLPSL
     TTEQQSLIHS VPSEVREDYF KNVQDLVGTI PQSDLKVVFT SLHGTSVPVV PDILSSLNFN
     QFELVASQCE PDSDFSSVAS ANPEDHKAFD QSIELANLID ADLLIGTDPD ADRLGIVERD
     AEGNIYYYNG NQIGALLLNY RIKQTEGLPN RIMFQSIVSG GLAKSLAQYH NVNFKEVLTG
     FKYIAAEIRH LSPEQNFIFG YEESYGFLAR PFVRDKDAIQ IVPLMIKYAA ELKNEGRMLK
     DELEDITRNV GNFNDKLFSH TFEGTQGKAK IENIMTQFRS ETPTEMCGLK VIAIEDFETG
     KKTDLQNDEV SDITLPKANV IKIYFNEGFI ALRPSGTEPK IKLYVSLSCD HFDVIAQKIN
     DAIFNS