ID GLMM_METPP Reviewed; 457 AA. AC A2SF93; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 06-MAR-2007, sequence version 1. DT 22-SEP-2009, entry version 24. DE RecName: Full=Phosphoglucosamine mutase; DE EC=5.4.2.10; GN Name=glmM; OrderedLocusNames=Mpe_A1270; OS Methylibium petroleiphilum (strain PM1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Methylibium. OX NCBI_TaxID=420662; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17158667; DOI=10.1128/JB.01259-06; RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., RA Hristova K.R.; RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta- RT proteobacterium Methylibium petroleiphilum PM1."; RL J. Bacteriol. 189:1931-1945(2007). CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to CC glucosamine-1-phosphate (By similarity). CC -!- CATALYTIC ACTIVITY: Alpha-D-glucosamine 1-phosphate = D- CC glucosamine 6-phosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity). CC -!- PTM: Activated by phosphorylation (By similarity). CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000555; ABM94232.1; -; Genomic_DNA. DR RefSeq; YP_001020467.1; -. DR STRING; A2SF93; -. DR GeneID; 4785847; -. DR GenomeReviews; CP000555_GR; Mpe_A1270. DR KEGG; mpt:Mpe_A1270; -. DR NMPDR; fig|279263.3.peg.1595; -. DR OMA; A2SF93; AHAVGRV. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR HAMAP; MF_01554; -; 1. 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 InterPro; IPR006352; GlmM. 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; PF02880; PGM_PMM_III; 1. DR Pfam; PF00408; PGM_PMM_IV; 1. DR PRINTS; PR00509; PGMPMM. DR TIGRFAMs; TIGR01455; glmM; 1. DR PROSITE; PS00710; PGM_PMM; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Magnesium; Metal-binding; KW Phosphoprotein. FT CHAIN 1 457 Phosphoglucosamine mutase. FT /FTId=PRO_0000301337. FT ACT_SITE 106 106 Phosphoserine intermediate (By FT similarity). FT METAL 106 106 Magnesium; via phosphate group (By FT similarity). FT METAL 245 245 Magnesium (By similarity). FT METAL 247 247 Magnesium (By similarity). FT METAL 249 249 Magnesium (By similarity). FT MOD_RES 106 106 Phosphoserine (By similarity). SQ SEQUENCE 457 AA; 48254 MW; 7D2E75174F8E010B CRC64; MSRTYFGTDG IRGAVGQAPI TPDFVLRLGH AVGRVLKSQQ TSPASRPTVL IGKDTRISGY MLESALEAGF ASAGVDVLLT GPLPTPGVAY LTRALRLSLG VVISASHNPY GDNGIKFFSA KGEKLPDSWE QQVEATVEEA AQWVDSSGLG KARRLDDAQG RYIEFCKSTV AGELSLKGLK LVVDGAHGAA YQVAPAVFHE LGAEVISIGC NPNGLNINDG FGATHPEALV SAVQAHQADY GIALDGDADR LQLVDATGRL YNGDELLYLM TLDRLAAEPS EDAAPSRVGV PGVVGTLMTN LAVEQALAAR GVAFVRAKVG DRYVLEELLA RGWQLGGEGS GHLIALDKHT TGDGLVSALQ VLQAVVRSGR TLAQLLEGLT LFPQVLLNVR LQPGQDWKAS AALAEAQRES LAELGERGRI LIRPSGTEPL LRVMVEASDA ALAQRCAQRM ADAVRRA //