ID   GLMM_NATTJ              Reviewed;         442 AA.
AC   B2A4R9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=Nther_0242;
OS   Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 /
OS   JW/NM-WN-LF).
OC   Bacteria; Firmicutes; Clostridia; Natranaerobiales; Natranaerobiaceae;
OC   Natranaerobius.
OX   NCBI_TaxID=457570;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.;
RT   "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-
RT   LF.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001034; ACB83841.1; -; Genomic_DNA.
DR   RefSeq; WP_012446730.1; NC_010718.1.
DR   AlphaFoldDB; B2A4R9; -.
DR   SMR; B2A4R9; -.
DR   STRING; 457570.Nther_0242; -.
DR   PRIDE; B2A4R9; -.
DR   EnsemblBacteria; ACB83841; ACB83841; Nther_0242.
DR   KEGG; nth:Nther_0242; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_7_0_9; -.
DR   OMA; PHNPEPL; -.
DR   OrthoDB; 1265792at2; -.
DR   Proteomes; UP000001683; 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; Reference proteome.
FT   CHAIN           1..442
FT                   /note="Phosphoglucosamine mutase"
FT                   /id="PRO_1000201121"
FT   ACT_SITE        98
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   BINDING         98
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         236
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   BINDING         238
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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   MOD_RES         98
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
SQ   SEQUENCE   442 AA;  48032 MW;  A2C8F93EF7A381F6 CRC64;
     MPKLFGTDGV RGVANEDLTP ELCLKIGRAA GEYLKSYGDT VLVGRDTRLS GTMLEAALSA
     GLASVGLKVE RLGIVTTPAV AFLASREDVA GGAMISASHN PVPDNGVKFF DNKGYKLAES
     HEEQIENYLE KELSRPTGTD IGKVLPENNK LIENYIQELI DKYPLDLSNY KIVLDCAYGA
     TYQIAPRLFK KLGAEIIPLH AENRGEKINV ECGSTNPELT SRTVVEEGAD LGFSFDGDGD
     RIIALDEEGN QVNGDKIMAI LAKDMKSRGE LKNDKLIATV MSNLGLKLAL KELGIALEET
     KVGDRNVLNR MREQDCVLGG EQSGHIINLQ DNTTGDGVLT GLKLMKVLID TGQSLKQLAS
     IMEELPQLLV NVKVSNKDSA INSQKVQEEK SKVEKQLGSK GRVLIRPSGT EPVIRVMVEG
     ENRETLHEVA NHLTQVIKKA AE