ID PGM1_MACFA Reviewed; 562 AA. AC Q4R5E4; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 16-JUN-2009, entry version 30. DE RecName: Full=Phosphoglucomutase-1; DE Short=PGM 1; DE EC=5.4.2.2; DE AltName: Full=Glucose phosphomutase 1; GN Name=PGM1; ORFNames=QnpA-16101; OS Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Parietal cortex; RG International consortium for macaque cDNA sequencing and analysis; RT "DNA sequences of macaque genes expressed in brain or testis and its RT evolutionary implications."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This enzyme participates in both the breakdown and CC synthesis of glucose (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 -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). 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; AB169600; BAE01681.1; -; mRNA. DR SMR; Q4R5E4; 1-561, 2-562. DR HOVERGEN; Q4R5E4; -. DR BRENDA; 5.4.2.2; 3438. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; IPR005846; A-D-PHexomutase_a/b/a-III. 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; 2. 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 PROSITE; PS00710; PGM_PMM; 1. PE 2: Evidence at transcript level; KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; Isomerase; KW Magnesium; Metal-binding; Phosphoprotein. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 562 Phosphoglucomutase-1. FT /FTId=PRO_0000147777. FT ACT_SITE 117 117 Phosphoserine intermediate (By FT similarity). FT METAL 117 117 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). FT MOD_RES 115 115 Phosphothreonine (By similarity). FT MOD_RES 117 117 Phosphoserine (By similarity). FT MOD_RES 353 353 Phosphotyrosine (By similarity). SQ SEQUENCE 562 AA; 61487 MW; 4C134F265D8D6CCD CRC64; MVKIVTVKTQ AYPDQKPGTS GLRKRVKVFQ SSANYAENFI QSIISTVEPA QRQEATLVVG GDGRFYMKEA IQLIARIAAA NGIGRLVIGQ NGILSTPAVS CIIRKIKAIG GIILTASHNP GGPNGDFGIK FNISNGGPAP EAITDKIFQI SKTIEEYAIC PDLKVDLGVL GKQQFDLENK FEPFTVEIVD SVEAYATMLR NIFDFSALKE LLSGPNRLKI RIDAMHGVVG PYVKKILCEE LGAPANSAVN CVPLEDFGGH HPDPNLTYAA DLVETMKSGE HDFGAAFDGD GDRNMILGKH GFFVNPSDSV AVIAANIFSI PYFQQTGVRG FARSMPTSGA LDRVANATKI ALYETPTGWK FFGNLMDASK LSLCGEESFG TGSDHIREKD GLWAVLAWLS ILATRKQSVE DILKDHWQKY GRNFFTRYDY EEVEAEGANK MMKDLEALMF DRSFVGKQFS ANDKVYTVEK ADNFEYSDPV DGSISRNQGL RLIFTDGSRI IFRLSGTGSA GATIRLYIDS YEKDVAKINQ DPQVMLAPLI SIALKVSQLQ ERTGRSAPTV IT //