ID GLMM_STRZP Reviewed; 450 AA. AC C1CLQ9; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 04-NOV-2026, entry version 78. DE RecName: Full=Phosphoglucosamine mutase {ECO:0000255|HAMAP-Rule:MF_01554}; DE EC=5.4.2.10 {ECO:0000255|HAMAP-Rule:MF_01554}; GN Name=glmM {ECO:0000255|HAMAP-Rule:MF_01554}; GN OrderedLocusNames=SPP_1583; OS Streptococcus pneumoniae (strain P1031). OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=488223; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P1031; RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107; RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J., RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R., RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D., RA Rappuoli R., Moxon E.R., Masignani V.; RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and RT closely related species."; RL Genome Biol. 11:R107.1-R107.19(2010). CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to CC glucosamine-1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01554}. CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate; CC Xref=Rhea:RHEA:23424, ChEBI:CHEBI:58516, ChEBI:CHEBI:58725; CC EC=5.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01554}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01554}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01554}; CC -!- PTM: Activated by phosphorylation. {ECO:0000255|HAMAP-Rule:MF_01554}. CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. CC {ECO:0000255|HAMAP-Rule:MF_01554}. 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; CP000920; ACO21953.1; -; Genomic_DNA. DR RefSeq; WP_000521410.1; NC_012467.1. DR AlphaFoldDB; C1CLQ9; -. DR SMR; C1CLQ9; -. DR KEGG; spp:SPP_1583; -. DR HOGENOM; CLU_016950_7_0_9; -. DR OMA; AAAHIFM; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004615; F:phosphomannomutase activity; IEA:TreeGrafter. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:TreeGrafter. DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:TreeGrafter. DR CDD; cd05802; GlmM; 1. DR FunFam; 3.30.310.50:FF:000001; Phosphoglucosamine mutase; 1. DR FunFam; 3.40.120.10:FF:000001; Phosphoglucosamine mutase; 1. DR FunFam; 3.40.120.10:FF:000002; Phosphoglucosamine mutase; 1. DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3. DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1. DR HAMAP; MF_01554_B; GlmM_B; 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; IPR036900; A-D-PHexomutase_C_sf. DR InterPro; IPR016066; A-D-PHexomutase_CS. DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF. DR InterPro; IPR006352; GlmM_bact. DR InterPro; IPR050060; Phosphoglucosamine_mutase. DR NCBIfam; TIGR01455; glmM; 1. DR PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1. DR PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 1. 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 SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1. DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3. DR PROSITE; PS00710; PGM_PMM; 1. PE 3: Inferred from homology; KW Isomerase; Magnesium; Metal-binding; Phosphoprotein. FT CHAIN 1..450 FT /note="Phosphoglucosamine mutase" FT /id="PRO_1000185388" FT ACT_SITE 101 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554" FT BINDING 101 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="via phosphate group" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554" FT BINDING 240 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554" FT BINDING 242 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554" FT BINDING 244 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554" FT MOD_RES 101 FT /note="Phosphoserine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554" SQ SEQUENCE 450 AA; 48124 MW; 4966FDEFAAD7AFE8 CRC64; MGKYFGTDGV RGEANLELTP ELAFKLGRFG GYVLSQHETE APKVFVGRDT RISGEMLESA LVAGLLSVGI HVYKLGVLAT PAVAYLVETE GASAGVMISA SHNPALDNGI KFFGGDGFKL DDEKEAEIEA LLDAEEDTLP RPSAEGLGIL VDYPEGLRKY EGYLVSTGTP LDGMKVALDT ANGAASTSAR QIFADLGAQL TVIGETPDGL NINLNVGSTH PEALQEVVKE SGSAIGLAFD GDSDRLIAVD ENGDIVDGDK IMYIIGKYLS EKGQLAQNTI VTTVMSNLGF HKALNREGIN KAVTAVGDRY VVEEMRKSGY NLGGEQSGHV ILMDYNTTGD GQLSAVQLTK IMKETGKSLS ELAAEVTIYP QKLVNIRVEN VMKEKAMEVP AIKAIIEKME EEMAGNGRIL VRPSGTEPLL RVMAEAPTTE EVDYYVDTIT DVVRAEIGID //