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   16-JUN-2009, entry version 24.
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).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W.,
RA   Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC8325 genome.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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
RT   anchoring in Staphylococcus aureus.";
RL   J. Bacteriol. 189:2521-2530(2007).
CC   -!- FUNCTION: Catalyzes the interconversion between glucose-6-
CC       phosphate and alpha-glucose-1-phosphate (Probable). This is the
CC       first step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-
CC       DAG), i.e. the predominant glycolipid found in the S.aureus
CC       membrane, which is also used as a membrane anchor for lipoteichoic
CC       acid (LTA).
CC   -!- CATALYTIC ACTIVITY: Alpha-D-glucose 1-phosphate = alpha-D-glucose
CC       6-phosphate.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol
CC       biosynthesis.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000253; ABD31796.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_501252.1; -.
DR   GeneID; 3921447; -.
DR   GenomeReviews; CP000253_GR; SAOUHSC_02793.
DR   KEGG; sao:SAOUHSC_02793; -.
DR   HOGENOM; Q2FVC1; -.
DR   BioCyc; SAUR93061:SAOUHSC_02793-MON; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:EC.
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; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; A-D-PHexomutase_N.
DR   Gene3D; G3DSA:3.40.120.10; A-D-PHexomutase_a/b/a-I/II/III; 3.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF00408; PGM_PMM_IV; 1.
DR   PRINTS; PR00509; PGMPMM.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Complete proteome; Glucose metabolism;
KW   Isomerase; Magnesium; Metal-binding; Phosphoprotein.
FT   CHAIN         1    552       Phosphoglucomutase.
FT                                /FTId=PRO_0000308336.
FT   ACT_SITE    143    143       Phosphoserine intermediate (By
FT                                similarity).
FT   METAL       143    143       Magnesium; via phosphate group (By
FT                                similarity).
FT   METAL       295    295       Magnesium (By similarity).
FT   METAL       297    297       Magnesium (By similarity).
FT   METAL       299    299       Magnesium (By similarity).
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
//