ID C7MEW4_BRAFD Unreviewed; 448 AA. AC C7MEW4; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 04-NOV-2026, entry version 89. DE RecName: Full=Phosphoglucosamine mutase {ECO:0000256|ARBA:ARBA00068193, ECO:0000256|HAMAP-Rule:MF_01554}; DE EC=5.4.2.10 {ECO:0000256|ARBA:ARBA00066330, ECO:0000256|HAMAP-Rule:MF_01554}; GN Name=glmM {ECO:0000256|HAMAP-Rule:MF_01554}; GN OrderedLocusNames=Bfae_23210 {ECO:0000313|EMBL:ACU86114.1}; OS Brachybacterium faecium (strain ATCC 43885 / DSM 4810 / JCM 11609 / LMG OS 19847 / NBRC 14762 / NCIMB 9860 / 6-10). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales; OC Dermabacteraceae; Brachybacterium. OX NCBI_TaxID=446465 {ECO:0000313|EMBL:ACU86114.1, ECO:0000313|Proteomes:UP000001919}; RN [1] {ECO:0000313|EMBL:ACU86114.1, ECO:0000313|Proteomes:UP000001919} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43885 / DSM 4810 / JCM 11609 / LMG 19847 / NBRC 14762 / RC NCIMB 9860 / 6-10 {ECO:0000313|Proteomes:UP000001919}; RX PubMed=21304631; DOI=10.4056/sigs.492; RA Lapidus A., Pukall R., Labuttii K., Copeland A., Del Rio T.G., Nolan M., RA Chen F., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., RA Rohde M., Goker M., Pati A., Ivanova N., Mavrommatis K., Chen A., RA Palaniappan K., D'haeseleer P., Chain P., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Brachybacterium faecium type strain RT (Schefferle 6-10)."; RL Stand. Genomic Sci. 1:3-11(2009). 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|ARBA:ARBA00050364, CC ECO:0000256|HAMAP-Rule:MF_01554, ECO:0000256|RuleBase:RU004327}; 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-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; CP001643; ACU86114.1; -; Genomic_DNA. DR AlphaFoldDB; C7MEW4; -. DR STRING; 446465.Bfae_23210; -. DR KEGG; bfa:Bfae_23210; -. DR PATRIC; fig|446465.5.peg.2295; -. DR eggNOG; COG1109; Bacteria. DR HOGENOM; CLU_016950_7_0_11; -. DR OMA; AAAHIFM; -. DR OrthoDB; 9803322at2; -. DR Proteomes; UP000001919; 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 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 {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}; Reference proteome {ECO:0000313|Proteomes:UP000001919}. FT DOMAIN 3..137 FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha" FT /evidence="ECO:0000259|Pfam:PF02878" FT DOMAIN 158..254 FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha" FT /evidence="ECO:0000259|Pfam:PF02879" FT DOMAIN 258..367 FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha" FT /evidence="ECO:0000259|Pfam:PF02880" FT DOMAIN 374..439 FT /note="Alpha-D-phosphohexomutase C-terminal" FT /evidence="ECO:0000259|Pfam:PF00408" FT ACT_SITE 104 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554" FT BINDING 104 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 241 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554" FT BINDING 243 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554" FT BINDING 245 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554" FT MOD_RES 104 FT /note="Phosphoserine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554" SQ SEQUENCE 448 AA; 46653 MW; 7979C5E033471297 CRC64; MARLFGTDGV RGRANGDITA ELAVELSVGA AHVLGTLGAF GGTRPRAIVA RDTRPSGDFL SAAVSAGLAS AGVDVLDAEV LPTPGLAHLV RSTGADLGVM ISASHNPAPD NGIKFFARGG TKLPDEVENA IEARLGEEWD RPEGTDVGTI TRYEGAIDAY VEHLVATLDR SLEGLTVVAD CANGAASITG PEALRRAGAT VHVIGDLSDG GLINDGVGST HLGPLQAAVR ERGADIGVAF DGDADRCLAV DADGEIIDGD QIMAILALDL KERGKLHDDT LVVTVMSNLG LKLAMKEHGI VLGQTGVGDR YVLEEMNLGG YSIGGEQSGH VIIAEHATTG DGELTALHLL QRMAETGRTA RELKNVMTRL PQALINVKDV DKAKATIDRG VSDAIEAAEK ELGEAGRVLL RPSGTEPVVR VMVEAPTDEQ AHEIAERLAV VVRERVGL //