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 16-JUN-2009, entry version 30. 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; Bacillales; Staphylococcus. OX NCBI_TaxID=279808; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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., RA Lee J.C., 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- CC phosphate and alpha-glucose-1-phosphate. This is the first step in CC the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG), i.e. a CC glycolipid found in the membrane, which is also used as a membrane CC anchor for lipoteichoic acid (LTA) (By similarity). 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; AP006716; BAE03610.1; -; Genomic_DNA. DR RefSeq; YP_252216.1; -. DR GeneID; 3483980; -. DR GenomeReviews; AP006716_GR; SH0301. DR KEGG; sha:SH0301; -. DR NMPDR; fig|279808.3.peg.313; -. DR HOGENOM; Q4L9R5; -. DR OMA; Q4L9R5; PKIKCYY. DR BioCyc; SHAE279808:SH0301-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 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; KW Isomerase; Magnesium; Metal-binding; Phosphoprotein. FT CHAIN 1 548 Phosphoglucomutase. FT /FTId=PRO_0000308347. FT ACT_SITE 135 135 Phosphoserine intermediate (By FT similarity). FT METAL 135 135 Magnesium; via phosphate group (By FT similarity). FT METAL 288 288 Magnesium (By similarity). FT METAL 290 290 Magnesium (By similarity). FT METAL 292 292 Magnesium (By similarity). 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 //