ID   GLMM_CAMLR              Reviewed;         445 AA.
AC   B9KE78;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=Cla_1567;
OS   Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=306263;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM2100 / D67 / ATCC BAA-1060;
RX   PubMed=18713059; DOI=10.1089/fpd.2008.0101;
RA   Miller W.G., Wang G., Binnewies T.T., Parker C.T.;
RT   "The complete genome sequence and analysis of the human pathogen
RT   Campylobacter lari.";
RL   Foodborne Pathog. Dis. 5:371-386(2008).
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; CP000932; ACM64866.1; -; Genomic_DNA.
DR   RefSeq; WP_012662248.1; NC_012039.1.
DR   AlphaFoldDB; B9KE78; -.
DR   SMR; B9KE78; -.
DR   STRING; 306263.Cla_1567; -.
DR   EnsemblBacteria; ACM64866; ACM64866; CLA_1567.
DR   GeneID; 7411136; -.
DR   KEGG; cla:CLA_1567; -.
DR   PATRIC; fig|306263.5.peg.1545; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_7_0_7; -.
DR   OMA; PHNPEPL; -.
DR   OrthoDB; 1265792at2; -.
DR   Proteomes; UP000007727; 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; 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   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..445
FT                   /note="Phosphoglucosamine mutase"
FT                   /id="PRO_1000185357"
FT   ACT_SITE        99
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   BINDING         99
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         99
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
SQ   SEQUENCE   445 AA;  48927 MW;  0E1293910AE25BF8 CRC64;
     MKLFGTDGVR GKAGEFLDSF LAMRLAMAAG IYFKDKALTN NILVGKDTRR SGYMIENAIV
     SGLTSIGYNV IEIGPMPTPA IAFLTEDMRC DAGIMISASH NPYYDNGIKF FDAHGNKLDE
     QAEAKIEEIY FNDKLIEEAR TTKSQIGQAK RIDDVIGRYI VSIKNSFPKE LTLKSLRVVL
     DVAHGASYKV APTVFRELGA DVIVINDKPN GLNINENCGA LHPLNLALEV KKFRADVGFA
     FDGDADRLVV VDEKGEVAHG DSLLGVLALF LKKQGKLKSS VVSTIMSNGA LKEFLTKYKI
     PHETCNVGDK YVLEKLKECG GNFGGEQSGH IIFSDYAKTG DGLVAALQFS ALMLSEAKSA
     SEILNQVKPY PQLLHNLKIS EKKDLSKLAG LEELKKDLEK KGIASLFRYS GTENLIRLLL
     EAKDIKLLEK EMKVVESFFM KVLNA