ID GLMM_LIGS1 Reviewed; 450 AA. AC Q1WSZ9; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2006, sequence version 1. DT 28-JAN-2026, entry version 102. 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=LSL_1144; OS Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius). OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Ligilactobacillus. OX NCBI_TaxID=362948; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCC118; RX PubMed=16617113; DOI=10.1073/pnas.0511060103; RA Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P., RA Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K., RA Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.; RT "Multireplicon genome architecture of Lactobacillus salivarius."; RL Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006). 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; CP000233; ABD99952.1; -; Genomic_DNA. DR RefSeq; WP_003700589.1; NC_007929.1. DR AlphaFoldDB; Q1WSZ9; -. DR SMR; Q1WSZ9; -. DR STRING; 362948.LSL_1144; -. DR KEGG; lsl:LSL_1144; -. DR PATRIC; fig|362948.14.peg.1218; -. DR HOGENOM; CLU_016950_7_0_9; -. DR OrthoDB; 9806956at2; -. DR Proteomes; UP000006559; Chromosome. 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 NCBIfam; NF008139; PRK10887.1; 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; Reference proteome. FT CHAIN 1..450 FT /note="Phosphoglucosamine mutase" FT /id="PRO_0000305647" 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 241 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554" FT BINDING 243 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554" FT BINDING 245 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; 48571 MW; E69399029F7CAA74 CRC64; MKYFGTDGVR GIANETLSPE LAFKLGRCGG YVLTQHASNK PARVLVARDT RISGQMLEQA LIAGLLSVGI EVFSLGVMTT PGVAYLVRLQ DADAGIMISA SHNPVQDNGI KFFGSDGYKL SDEKEEEIEA LLESDEDTLP RPSAEGLGTL SDYREGALKY TQFLEQTIPD DLEGMHIAVD GANGSTSALV SRLFADLGAD FDTMATNPDG LNINKGVGST HPEALAKFVV EKGAQVGVAF DGDGDRCIAV DENGEIVDGD KIMFICGKYL SERGRLKKDT IVTTVMSNIG LYKAMKENNL NSVQTKVGDR YVVEAMRKDG YNVGGEQSGH VVFLDFNTTG DGMLTALQLL NVIKQTGKKL SELAAEVKTY PQELVNIKVT DKKAALDNEK IKEAIAKVEE KMAGDGRVLV RPSGTEDLLR VMAEAKTQEL VHDYVMEIAD VVEAEMGVNE //