ID A0A0E0VSY8_STAA5 Unreviewed; 451 AA. AC A0A0E0VSY8; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-NOV-2018, entry version 19. DE RecName: Full=Phosphoglucosamine mutase {ECO:0000256|HAMAP-Rule:MF_01554, ECO:0000256|RuleBase:RU004327, ECO:0000256|SAAS:SAAS00358419}; DE EC=5.4.2.10 {ECO:0000256|HAMAP-Rule:MF_01554, ECO:0000256|RuleBase:RU004327, ECO:0000256|SAAS:SAAS00378212}; 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 RT Staphylococcus aureus ST398 clone with distinct genomic and cell RT 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, ECO:0000256|SAAS:SAAS00566919}. CC -!- CATALYTIC ACTIVITY: Alpha-D-glucosamine 1-phosphate = D- CC glucosamine 6-phosphate. {ECO:0000256|HAMAP-Rule:MF_01554, CC ECO:0000256|RuleBase:RU004327, ECO:0000256|SAAS:SAAS00378185}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01554}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01554}; CC -!- PTM: Activated by phosphorylation. {ECO:0000256|HAMAP- CC Rule:MF_01554}. CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. CC {ECO:0000256|HAMAP-Rule:MF_01554, ECO:0000256|RuleBase:RU004326, CC ECO:0000256|SAAS:SAAS00551227}. 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 ProteinModelPortal; A0A0E0VSY8; -. DR SMR; A0A0E0VSY8; -. DR EnsemblBacteria; AFH70408; AFH70408; ST398NM01_2216. DR KEGG; sud:ST398NM01_2216; -. DR PATRIC; fig|1155084.3.peg.1953; -. DR KO; K03431; -. DR OrthoDB; POG091H02H5; -. 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 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 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; SSF53738; SSF53738; 3. DR SUPFAM; SSF55957; SSF55957; 1. DR TIGRFAMs; TIGR01455; glmM; 1. DR PROSITE; PS00710; PGM_PMM; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005003}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01554, KW ECO:0000256|RuleBase:RU004327, ECO:0000256|SAAS:SAAS01085081, KW ECO:0000313|EMBL:AFH70408.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01554, KW ECO:0000256|RuleBase:RU004326, ECO:0000256|SAAS:SAAS00042171}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01554, KW ECO:0000256|RuleBase:RU004326, ECO:0000256|SAAS:SAAS00042289}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01554}. FT DOMAIN 3 136 PGM_PMM_I. {ECO:0000259|Pfam:PF02878}. FT DOMAIN 160 255 PGM_PMM_II. {ECO:0000259|Pfam:PF02879}. FT DOMAIN 259 371 PGM_PMM_III. {ECO:0000259|Pfam:PF02880}. FT DOMAIN 375 443 PGM_PMM_IV. {ECO:0000259|Pfam:PF00408}. FT ACT_SITE 102 102 Phosphoserine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01554}. FT METAL 102 102 Magnesium; via phosphate group. FT {ECO:0000256|HAMAP-Rule:MF_01554}. FT METAL 242 242 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01554}. FT METAL 244 244 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01554}. FT METAL 246 246 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_01554}. FT MOD_RES 102 102 Phosphoserine. {ECO:0000256|HAMAP-Rule: FT 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 //