ID   PGCA_STAS1              Reviewed;         552 AA.
AC   Q49WH7;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=SSP1737;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE18882.1; -; Genomic_DNA.
DR   RefSeq; WP_011303449.1; NZ_MTGA01000039.1.
DR   AlphaFoldDB; Q49WH7; -.
DR   SMR; Q49WH7; -.
DR   STRING; 342451.SSP1737; -.
DR   PRIDE; Q49WH7; -.
DR   EnsemblBacteria; BAE18882; BAE18882; SSP1737.
DR   KEGG; ssp:SSP1737; -.
DR   PATRIC; fig|342451.11.peg.1735; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_0_0_9; -.
DR   OMA; PQDNGYK; -.
DR   OrthoDB; 637615at2; -.
DR   UniPathway; UPA00894; -.
DR   Proteomes; UP000006371; 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..552
FT                   /note="Phosphoglucomutase"
FT                   /id="PRO_0000308348"
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         289
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         291
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         293
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   552 AA;  62077 MW;  886FB7BAE51C97DF CRC64;
     MKALWLENIN ESLVKDFYET QTEEEQNAGF EGVLSFGTAG IRSTFGLGPA RLNAFTVRKV
     ALGLAQYLNH NVDDASVVIH FDTRFLSKAF SQEMASVLAN NGITAIISDN YKSTPELSFA
     VRHLQVNAGI MITASHNPKN YNGIKIYNEK GGQLLPEASE QLSEYINSIE TPLNIEKGDF
     NAFVENGKIK YMSNEVTESY KKEVKSLVGS IDAHDAKVIL TSLHGTSLPL VSDILTELDY
     HNFVIEKEQS EPNGNFPTVA IANPEDEAAF TLGKQLADKT DAQLIIATDP DADRLGFIER
     YGDNDFRYFN GNEIGLLLMK LRFQDLTEDS TPQYMIKSIV TSELAERLAT SLNVEVNDVL
     TGFKFISDLI EHKQKDDDKQ LLLAFEESHG YLAQPISRDK DAIQMVPLLV KYKNLLDKNG
     ITFKETIEDI YENIGYFKDR TLAPTFEGKA GVKKIESIMS QFRNEQVFSI CGMDVLKIED
     YHVGEVRDMI TGHTEKLTLP KTNLIRFIFE NGFIALRPSG TEPKIKLYFS LEVENIDEIT
     QQFEANYINN IV