ID GLMM_RUTMC Reviewed; 441 AA. AC A1AVH5; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 28-JAN-2026, entry version 95. 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=Rmag_0138; OS Ruthia magnifica subsp. Calyptogena magnifica. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Candidatus Pseudothioglobaceae; Candidatus Ruthturnera. OX NCBI_TaxID=413404; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17303757; DOI=10.1126/science.1138438; RA Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J., RA Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M., RA Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.; RT "The Calyptogena magnifica chemoautotrophic symbiont genome."; RL Science 315:998-1000(2007). 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; CP000488; ABL01932.1; -; Genomic_DNA. DR RefSeq; WP_011737558.1; NC_008610.1. DR AlphaFoldDB; A1AVH5; -. DR SMR; A1AVH5; -. DR STRING; 413404.Rmag_0138; -. DR KEGG; rma:Rmag_0138; -. DR eggNOG; COG1109; Bacteria. DR HOGENOM; CLU_016950_7_0_6; -. DR OrthoDB; 9803322at2; -. DR Proteomes; UP000002587; 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; 3.40.120.10:FF:000001; Phosphoglucosamine mutase; 1. DR FunFam; 3.40.120.10:FF:000003; 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; 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. PE 3: Inferred from homology; KW Isomerase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome. FT CHAIN 1..441 FT /note="Phosphoglucosamine mutase" FT /id="PRO_0000305669" FT ACT_SITE 100 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554" FT BINDING 100 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 239 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" 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 MOD_RES 100 FT /note="Phosphoserine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554" SQ SEQUENCE 441 AA; 47935 MW; B962AF1CF3CE59B3 CRC64; MDNYFGTDGM RGKVGVEPIT ADFFLKLGWA VGSVLAKRAK ASVIIGKDTR VSGYLFESAL EAGFLSAGVD VGLLGPMPTP AVAYLTQTYN ASAGVVISAS HNNFQDNGVK FFSAKGLKLS SQYQSEIEKK LAETMISVGA DKIGKAYRYE QPLGRYIEFC KSTFDRTQSL LGLNIVIDCA NGATYHIAQS VFSELGANIN IINNTPDGFN INEHCGATDT KYLQQVVLES KADLGIAFDG DGDRLIMIDE NGELVDGDEL VFIIAKAWQS QGRLVNNTVV GTKMSNLGMH HALRDLDIKF IEADVGDRFV MEKMQKSGSI LGGEGSGHII CLNKTTSGDG IISALQVLEV LVKSQSSLAK LKQSMEKYPQ ILINVKTQAR INLKNYTKLQ RTQLAVEQTL GDESRVLIRV SGTEPLIRVM VEAKDKIIAQ QGAEKLSNIF K //