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 16-JUN-2009, entry version 27. 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 / OS DSM 20229). OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=342451; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16135568; DOI=10.1073/pnas.0502950102; RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., RA Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., RA 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- 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; AP008934; BAE18882.1; -; Genomic_DNA. DR RefSeq; YP_301827.1; -. DR GeneID; 3616646; -. DR GenomeReviews; AP008934_GR; SSP1737. DR KEGG; ssp:SSP1737; -. DR NMPDR; fig|342451.4.peg.1790; -. DR HOGENOM; Q49WH7; -. DR OMA; Q49WH7; IGEDVDM. DR BioCyc; SSAP342451:SSP1737-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 1 552 Phosphoglucomutase. FT /FTId=PRO_0000308348. FT ACT_SITE 135 135 Phosphoserine intermediate (By FT similarity). FT METAL 135 135 Magnesium; via phosphate group (By FT similarity). FT METAL 289 289 Magnesium (By similarity). FT METAL 291 291 Magnesium (By similarity). FT METAL 293 293 Magnesium (By similarity). 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 //