ID   PGCA_STAHJ              Reviewed;         548 AA.
AC   Q4L9R5;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=SH0301;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(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}.
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; AP006716; BAE03610.1; -; Genomic_DNA.
DR   RefSeq; WP_011274630.1; NC_007168.1.
DR   AlphaFoldDB; Q4L9R5; -.
DR   SMR; Q4L9R5; -.
DR   STRING; 279808.SH0301; -.
DR   EnsemblBacteria; BAE03610; BAE03610; SH0301.
DR   KEGG; sha:SH0301; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_0_0_9; -.
DR   OMA; PQDNGYK; -.
DR   OrthoDB; 637615at2; -.
DR   UniPathway; UPA00894; -.
DR   Proteomes; UP000000543; 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..548
FT                   /note="Phosphoglucomutase"
FT                   /id="PRO_0000308347"
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   548 AA;  62002 MW;  30DDFD65916EA473 CRC64;
     MKDNWMKYKD DSLVASFYDS QTTTFQEQGF ETELAFGTAG IRGQFGLGPG RLNRYTIQRL
     ALGIANYLKD KEDNPSIVIH YDIRHLSSEF AHIITQILTS KGIKVYLADV YKTTPQLSFA
     VRYLQTSAGI MITASHNPKD YNGIKVYGAD GAQLDEDTSL EVAQYINNLG NPLELNIDLN
     QELIEKNTFD LQEAVYDSYI NEITNLIGDI PQSDLKVVYT SLHGTGVPII PDVLKHLNFQ
     NVSLVELQCE LDPNFSSVKS ANPEEREAFD LAIQQAHDLE ANLIIATDPD VDRMGFVERD
     TNGQTYYFGG SEIGALLIKY LLEYTNVPNH SVVIQSIVSG ELGKRLAQQH EVTVKEVLIG
     FKHIAKAIRE LDDTESFLFA YEESYGYLAD DFVRDKDAIQ IVPLIIKYTS ILKNEGKTLH
     DALKEIHREV GQYRDKPMSK VFEGREGQQQ INALMDKLRR NIPDVIAGLK VIAVEDYETL
     KRNYKEDNTE EAISLPQANV IRILFKEGFI ALRPSGTEPK LKFYLSLNVD NFEQVSQDIY
     NYIFGDTE