ID   GLMM_SYNE7              Reviewed;         472 AA.
AC   Q31LA7;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
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};
GN   OrderedLocusNames=Synpcc7942_2132;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) 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; CP000100; ABB58162.1; -; Genomic_DNA.
DR   RefSeq; WP_011378332.1; NC_007604.1.
DR   AlphaFoldDB; Q31LA7; -.
DR   SMR; Q31LA7; -.
DR   STRING; 1140.Synpcc7942_2132; -.
DR   PRIDE; Q31LA7; -.
DR   EnsemblBacteria; ABB58162; ABB58162; Synpcc7942_2132.
DR   KEGG; syf:Synpcc7942_2132; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_7_0_3; -.
DR   OMA; PHNPEPL; -.
DR   OrthoDB; 1265792at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_2132-MON; -.
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..472
FT                   /note="Phosphoglucosamine mutase"
FT                   /id="PRO_0000305685"
FT   ACT_SITE        123
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   BINDING         123
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         262
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   BINDING         264
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   BINDING         266
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   MOD_RES         123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
SQ   SEQUENCE   472 AA;  50439 MW;  05B400C3A276D5DD CRC64;
     MVSATRWETA IEVTPWIAAI AEQVPLFGTD GIRGRVGEHL TAPLAQQVGF WTGQVLRQAG
     GDRGPVVVGQ DSRNSSNMLA MALSSGLAAA GVEVLHLGLC PTPGVAYLTH HSEAIGGVMI
     SASHNPPGDN GIKVFGADGS KLDRQLQAAI EAGLRGQQTS LPATTWGQHY YQPQLADHYQ
     AAIAQSLGQR ANLQGLKIVL DLAWGAAALL APRLFRELGA EVIALHDLPD GNQINVNCGS
     THLARLQAAV LEQGADMGFA FDGDADRVLA VDGRGRSVDG DHILFLWGRE LEQQQQLPGQ
     AIVTTVMANL GFERAWQAVG GEFVRTAVGD QYVQAEMQAR GAMLGGEQSG HILCRHYALT
     GDGTLTAAHV AALVQASGVS LADLVDQSFR PYPQLLRNVR VEDRDRRCNW QNCAALTQAI
     AAAETDMGDR GRVLVRASGT EPLLRIMVEA EEAQQVEHWT THLVQVAESH LL