ID A0A0E0VSY8_STAA5 Unreviewed; 451 AA. AC A0A0E0VSY8; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 22-FEB-2023, entry version 31. DE RecName: Full=Phosphoglucosamine mutase {ECO:0000256|HAMAP-Rule:MF_01554, ECO:0000256|RuleBase:RU004327}; DE EC=5.4.2.10 {ECO:0000256|HAMAP-Rule:MF_01554, ECO:0000256|RuleBase:RU004327}; GN Name=glmM {ECO:0000256|HAMAP-Rule:MF_01554}; GN ORFNames=ST398NM01_2216 {ECO:0000313|EMBL:AFH70408.1}; OS Staphylococcus aureus subsp. aureus 71193. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=1155084 {ECO:0000313|EMBL:AFH70408.1, ECO:0000313|Proteomes:UP000005003}; RN [1] {ECO:0000313|EMBL:AFH70408.1, ECO:0000313|Proteomes:UP000005003} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=71193 {ECO:0000313|EMBL:AFH70408.1}; RX PubMed=22375071; RA Uhlemann A.C., Porcella S.F., Trivedi S., Sullivan S.B., Hafer C., RA Kennedy A.D., Barbian K.D., McCarthy A.J., Street C., Hirschberg D.L., RA Lipkin W.I., Lindsay J.A., DeLeo F.R., Lowy F.D.; RT "Identification of a highly transmissible animal-independent Staphylococcus RT aureus ST398 clone with distinct genomic and cell adhesion properties."; RL MBio 3:e00027-12(2012). CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to CC glucosamine-1-phosphate. {ECO:0000256|HAMAP-Rule:MF_01554, CC ECO:0000256|RuleBase:RU004327}. 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:0000256|HAMAP-Rule:MF_01554, CC ECO:0000256|RuleBase:RU004327}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01554}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01554}; CC -!- PTM: Activated by phosphorylation. {ECO:0000256|HAMAP-Rule:MF_01554}. CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|HAMAP-Rule:MF_01554, CC ECO:0000256|RuleBase:RU004326}. 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; CP003045; AFH70408.1; -; Genomic_DNA. DR RefSeq; WP_000521495.1; NC_017673.1. DR AlphaFoldDB; A0A0E0VSY8; -. DR SMR; A0A0E0VSY8; -. DR EnsemblBacteria; AFH70408; AFH70408; ST398NM01_2216. DR KEGG; sud:ST398NM01_2216; -. DR PATRIC; fig|1155084.3.peg.1953; -. DR HOGENOM; CLU_016950_7_0_9; -. DR Proteomes; UP000005003; Chromosome. 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:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd05802; GlmM; 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 PANTHER; PTHR42946:SF1; PHOSPHOGLUCOSAMINE MUTASE FAMILY PROTEIN; 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 TIGRFAMs; TIGR01455; glmM; 1. DR PROSITE; PS00710; PGM_PMM; 1. PE 3: Inferred from homology; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01554}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01554}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01554}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP- KW Rule:MF_01554}. FT DOMAIN 3..136 FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha" FT /evidence="ECO:0000259|Pfam:PF02878" FT DOMAIN 160..255 FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha" FT /evidence="ECO:0000259|Pfam:PF02879" FT DOMAIN 259..371 FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha" FT /evidence="ECO:0000259|Pfam:PF02880" FT DOMAIN 375..443 FT /note="Alpha-D-phosphohexomutase C-terminal" FT /evidence="ECO:0000259|Pfam:PF00408" FT ACT_SITE 102 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_01554" FT BINDING 242 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554" FT BINDING 244 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554" FT BINDING 246 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554" FT MOD_RES 102 FT /note="Phosphoserine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554" SQ SEQUENCE 451 AA; 49294 MW; A7330C90CA7F9CD8 CRC64; MGKYFGTDGV RGVANQELTP ELAFKLGRYG GYVLAHNKGE KHPRVLVGRD TRVSGEMLES ALIAGLISIG AEVMRLGIIS TPGVAYLTRD MGAELGVMIS ASHNPVADNG IKFFGSDGFK LSDEQENEIE ALLDQENPEL PRPVGNDIVH YSDYFEGAQK YLSYLKSTVD VNFEGLKIVL 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 //