ID   PGM_NEIGO               Reviewed;         460 AA.
AC   P40390;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Phosphoglucomutase;
DE            Short=PGM;
DE            EC=5.4.2.2;
DE   AltName: Full=Glucose phosphomutase;
GN   Name=pgm;
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1291;
RX   PubMed=8157643; DOI=10.1016/s0021-9258(19)78105-8;
RA   Zhou D., Stephens D.S., Gibson B.W., Engstrom J.J., McAllister C.F.,
RA   Lee F.K.N., Apicella M.A.;
RT   "Lipooligosaccharide biosynthesis in pathogenic Neisseria. Cloning,
RT   identification, and characterization of the phosphoglucomutase gene.";
RL   J. Biol. Chem. 269:11162-11169(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1291;
RX   PubMed=8188595; DOI=10.1128/jb.176.10.2930-2937.1994;
RA   Sandlin R.C., Stein D.C.;
RT   "Role of phosphoglucomutase in lipooligosaccharide biosynthesis in
RT   Neisseria gonorrhoeae.";
RL   J. Bacteriol. 176:2930-2937(1994).
CC   -!- FUNCTION: This enzyme participates in both the breakdown and synthesis
CC       of glucose.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC         Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC         EC=5.4.2.2;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR   EMBL; U02489; AAA20588.1; -; Genomic_DNA.
DR   EMBL; L23426; AAA20399.1; -; Unassigned_DNA.
DR   PIR; A53614; A53614.
DR   RefSeq; WP_003687793.1; NZ_SURI01000001.1.
DR   AlphaFoldDB; P40390; -.
DR   SMR; P40390; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
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   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   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Glucose metabolism; Isomerase;
KW   Magnesium; Metal-binding; Phosphoprotein.
FT   CHAIN           1..460
FT                   /note="Phosphoglucomutase"
FT                   /id="PRO_0000147810"
FT   ACT_SITE        103
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         103..104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         103
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         239
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         241
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         243..244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         243
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         303
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         322..324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
SQ   SEQUENCE   460 AA;  49466 MW;  24AB77C7B8AE6391 CRC64;
     MASITRDIFK AYDIRGIVGK TLTDDAAYFI GRAIAAKAAE KGIARIALGR DGRLSGPELM
     EHIQRGLTDS GISVLNVGMV TTPMLYFAAV NECGGSGVMI TGSHNPPDYN GFKMMLGGDT
     LAGEAIQELL AIVEKDGFVA ADKQGSVTEK DISGAYHDHI VGHVKLKRPI NIAIDAGNGV
     GGAFAGKLYK GLGNEVTELF CEVDGNFPNH HPDPSKPENL QDLIAALKNG DAEIGLAFDG
     DADRLGVVTK DGNIIYPDRQ LMLFAQDVLN RNPGAKVIFD VKSTRLLAPW IKEHGGEAIM
     EKTGHSFIKS AMKKTGALVA GEMSGHVFFK ERWFGFDDGL YAGARLLEIL SASDNPSEVL
     DNLPQSISTP ELNISLPEGS NGHQVIEELA AKAEFEGATE IITIDGLRVE FPDGFGLMRA
     SNTTPILVLR FEADTQAAIE RIQNRFKAVI ESNPHLIWPL