ID   GLMM_COXBN              Reviewed;         446 AA.
AC   A9KGE3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=CBUD_1438;
OS   Coxiella burnetii (strain Dugway 5J108-111).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=434922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dugway 5J108-111;
RX   PubMed=19047403; DOI=10.1128/iai.01141-08;
RA   Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA   Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA   Heinzen R.A.;
RT   "Comparative genomics reveal extensive transposon-mediated genomic
RT   plasticity and diversity among potential effector proteins within the genus
RT   Coxiella.";
RL   Infect. Immun. 77:642-656(2009).
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; CP000733; ABS77805.1; -; Genomic_DNA.
DR   RefSeq; WP_011997086.1; NC_009727.1.
DR   AlphaFoldDB; A9KGE3; -.
DR   SMR; A9KGE3; -.
DR   EnsemblBacteria; ABS77805; ABS77805; CBUD_1438.
DR   KEGG; cbd:CBUD_1438; -.
DR   HOGENOM; CLU_016950_7_0_6; -.
DR   OMA; PHNPEPL; -.
DR   OrthoDB; 1265792at2; -.
DR   Proteomes; UP000008555; 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; 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.
PE   3: Inferred from homology;
KW   Isomerase; Magnesium; Metal-binding; Phosphoprotein.
FT   CHAIN           1..446
FT                   /note="Phosphoglucosamine mutase"
FT                   /id="PRO_1000087763"
FT   ACT_SITE        101
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   BINDING         101
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         240
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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   MOD_RES         101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
SQ   SEQUENCE   446 AA;  48103 MW;  F4BAECB5436331EC CRC64;
     MQKKYFGTDG IRGKVGNSLI NAEFMLKLGW AVGRVLANSH SATVLIGKDT RISGYMIESA
     LQAGLSAAGV NIKLTGPMPT PAIAYLTNSV RADAGIVISA SHNHYPDNGV KFFNKDGFKL
     SDELELAIEK QIDKPMKTVV ADRLGKAARM NEAHGRYIEF CKSTFPSNLT LKGLKIVVDC
     ANGAAYAVAP SIFHELGAEV VAIADDPDGF NINQTCGATD TAHLQEMVVK HNADVGIAFD
     GDGDRLIMVD HHGLRVDGDE LLCIMAIDRF YLKENAPLGV VGTIMSNLGL EQTLKRHHIA
     FERSPVGDRY VLDLMQQKGW FLGGESSGHI VDLGFTTTGD GVITALQILR IMQQAEKPLA
     DLKKVMVKNP QVLINVPIKG ILDIAQNPNI KKAITEAEKQ LNGAGRILLR PSGTEPVIRV
     MVEGSDEGIV RQTAEMLAAA VQQSTL