ID   GLMM_SYNY3              Reviewed;         481 AA.
AC   P73648;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 127.
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=sll1758;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA17693.1; -; Genomic_DNA.
DR   PIR; S77135; S77135.
DR   AlphaFoldDB; P73648; -.
DR   SMR; P73648; -.
DR   STRING; 1148.1652774; -.
DR   PaxDb; P73648; -.
DR   EnsemblBacteria; BAA17693; BAA17693; BAA17693.
DR   KEGG; syn:sll1758; -.
DR   eggNOG; COG1109; Bacteria.
DR   InParanoid; P73648; -.
DR   OMA; PHNPEPL; -.
DR   PhylomeDB; P73648; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008966; F:phosphoglucosamine mutase activity; IBA:GO_Central.
DR   GO; GO:0004615; F:phosphomannomutase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..481
FT                   /note="Phosphoglucosamine mutase"
FT                   /id="PRO_0000147988"
FT   ACT_SITE        128
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   BINDING         128
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         269
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   BINDING         271
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   BINDING         273
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   MOD_RES         128
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
SQ   SEQUENCE   481 AA;  51677 MW;  AE9727ACA808ECC6 CRC64;
     MVASPIHSRG LDLPLPSTMG EFGLSLPRSP LFGTDGIRGK AGELLTAPLA LSLGFWAGQV
     LREQTDTAGP VIIGQDSRLS SDMLANAMAA GLNSAGVEVW QLGLCPTPCV AYLTRKTAAI
     GGIMISASHN PPEDNGIKFF DHQGLKLPKS LATAIEAGLR GQNQTSGLNA SQWGRSYGQP
     HRVQYYQDFL LGSLPQPLNF QGLKVVLDLA WGASVNLAPH IFRSLGAEVI ALHDLADGSQ
     INVDCGSTHL HRLQRAVRET GADLGFAFDG DADRVMAVDA QGRPVDGDYI LFLWGKTLQE
     SNHLPDNLIV GTVMANLAFE RAWEKLGGKL IRTAVGDQNV QAQMWETGAM LGGEQSGHII
     CHHHSYSGDG LQAALHLATL VQKSGLSLSE LLSESFQPYP QILRNVRVLD RERRLHWQEC
     APLQQAIATA EKSMGTTGRI LVRASGTEPL IRVMVEAACA ETAAHWSDQL TSTVQCHLGD
     S