ID   PGCA_STAEQ              Reviewed;         546 AA.
AC   Q5HLD2;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
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=SERP2055;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW52902.1; -; Genomic_DNA.
DR   RefSeq; WP_002501834.1; NC_002976.3.
DR   AlphaFoldDB; Q5HLD2; -.
DR   SMR; Q5HLD2; -.
DR   STRING; 176279.SERP2055; -.
DR   PRIDE; Q5HLD2; -.
DR   EnsemblBacteria; AAW52902; AAW52902; SERP2055.
DR   KEGG; ser:SERP2055; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_0_0_9; -.
DR   OMA; PQDNGYK; -.
DR   OrthoDB; 637615at2; -.
DR   UniPathway; UPA00894; -.
DR   Proteomes; UP000000531; 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; Reference proteome.
FT   CHAIN           1..546
FT                   /note="Phosphoglucomutase"
FT                   /id="PRO_0000308345"
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;  60851 MW;  DA1A1CE50ADF189A CRC64;
     MKNNWIDVLD ESLVKDFYNN QTSEEQQEGL NTTLSFGTAG IRGKFGLGEG RLNKFTVSKV
     ALGFAHYLTS SIAHPVVVIH YDTRHLSPEF AQIIANILAS HDIKVYLADT YRTTPDLSFA
     VRYLQADAGV MITASHNPKD YNGIKVYGED GAQLSTDASA QLSTYIDKLG HPLHINVPSL
     TTEQQSLIHS VPSEVREDYF KNVQDLVGTI PQSDLKVVFT SLHGTSVPIV 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