ID GLMM_STAA3 Reviewed; 451 AA. AC Q2FEX1; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 02-SEP-2026, entry version 104. 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=SAUSA300_2111; OS Staphylococcus aureus (strain USA300). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=367830; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=USA300; RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7; RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G., RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F., RA Perdreau-Remington F.; RT "Complete genome sequence of USA300, an epidemic clone of community- RT acquired meticillin-resistant Staphylococcus aureus."; RL Lancet 367:731-739(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; CP000255; ABD21310.1; -; Genomic_DNA. DR RefSeq; WP_000521491.1; NZ_CP027476.1. DR AlphaFoldDB; Q2FEX1; -. DR SASBDB; Q2FEX1; -. DR SMR; Q2FEX1; -. DR KEGG; saa:SAUSA300_2111; -. DR HOGENOM; CLU_016950_7_0_9; -. DR OMA; SHNAMPD; -. DR Proteomes; UP000001939; 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..451 FT /note="Phosphoglucosamine mutase" FT /id="PRO_0000301385" FT ACT_SITE 102 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554" FT BINDING 102 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 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 BINDING 246 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554" FT MOD_RES 102 FT /note="Phosphoserine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554" SQ SEQUENCE 451 AA; 49266 MW; A164B280C4B9ABD8 CRC64; MGKYFGTDGV RGVANQELTP ELAFKLGRYG GYVLAHNKGE KHPRVLVGRD TRVSGEMLES ALIAGLISIG AEVMRLGIIS TPGVAYLTRD MGAELGVMIS ASHNPVADNG IKFFGSDGFK LSDEQENEIE ALLDQENPEL PRPVGNDIVH YSDYFEGAQK YLSYLKSTVD VNFEGLKIAL DGANGSTSSL APFLFGDLEA DTETIGCSPD GYNINEKCGS THPEKLAEKV VETESDFGLA FDGDGDRIIA VDENGQIVDG DQIMFIIGQE MHKNQELNND MIVSTVMSNL GFYKALEQEG IKSNKTKVGD RYVVEEMRRG NYNLGGEQSG HIVMMDYNTT GDGLLTGIQL ASVIKMTGKS LSELAGQMKK YPQSLINVRV TDKYRVEENV DVKEVMTKVE VEMNGEGRIL VRPSGTEPLV RVMVEAATDE DAERFAQQIA DVVQDKMGLD K //