ID   GLMM_CORGB              Reviewed;         447 AA.
AC   A4QBS5;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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}; OrderedLocusNames=cgR_0701;
OS   Corynebacterium glutamicum (strain R).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=340322;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R;
RX   PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA   Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA   Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT   "Comparative analysis of the Corynebacterium glutamicum group and complete
RT   genome sequence of strain R.";
RL   Microbiology 153:1042-1058(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;
CC         Evidence={ECO:0000255|HAMAP-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}.
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DR   EMBL; AP009044; BAF53672.1; -; Genomic_DNA.
DR   RefSeq; WP_003854539.1; NC_009342.1.
DR   AlphaFoldDB; A4QBS5; -.
DR   SMR; A4QBS5; -.
DR   EnsemblBacteria; BAF53672; BAF53672; cgR_0701.
DR   GeneID; 58309494; -.
DR   KEGG; cgt:cgR_0701; -.
DR   HOGENOM; CLU_016950_7_0_11; -.
DR   OMA; PHNPEPL; -.
DR   PhylomeDB; A4QBS5; -.
DR   Proteomes; UP000006698; 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   Isomerase; Magnesium; Metal-binding; Phosphoprotein.
FT   CHAIN           1..447
FT                   /note="Phosphoglucosamine mutase"
FT                   /id="PRO_0000301305"
FT   ACT_SITE        104
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000255|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: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   BINDING         245
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   BINDING         247
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   MOD_RES         104
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
SQ   SEQUENCE   447 AA;  46445 MW;  935440E7BE929323 CRC64;
     MTRLFGTDGV RGLANEVLTA PLALKLGAAA AHVLTAEKRV DGRRPVAIVG RDPRVSGEML
     AAALSAGMAS QGVDVIRVGV IPTPAVAFLT DDYGADMGVM ISASHNPMPD NGIKFFSAGG
     HKLPDHVEDE IERVMDSLPA EGPTGHGVGR VIEEATDAQD RYLEHLKEAV PTSLEGIKIV
     VDAANGAASV VAPKAYEAAG ATVIAIHNKP DSYNINMDCG STHIDQVQAA VLKHGADLGL
     AHDGDADRCL AVDKDGNLID GDQIMAMLAI AMKENGELRK NTLVGTVMSN LGLKIAMDEA
     GITLRTTKVG DRYVLEDLNA GGFSLGGEQS GHIVLPDHGT TGDGTLTGLS IMARMAETGK
     SLGELAQAMT VLPQVLINVP VSDKSTIVSH PSVVAAIAEA EAELGSTGRV LLRASGTEEL
     FRVMVEAGDK EQARRIAGRL SAVVAEV