ID   PGM_KOMXY               Reviewed;         555 AA.
AC   P38569;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Phosphoglucomutase;
DE            Short=PGM;
DE            EC=5.4.2.2;
DE   AltName: Full=Glucose phosphomutase;
GN   Name=celB;
OS   Komagataeibacter xylinus (Gluconacetobacter xylinus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Komagataeibacter.
OX   NCBI_TaxID=28448;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23768 / DSM 2004 / NCIMB 7029 / B 4168;
RX   PubMed=8025683; DOI=10.1099/13500872-140-5-1183;
RA   Brautaset T., Standal R., Fjaervik E., Valla S.;
RT   "Nucleotide sequence and expression analysis of the Acetobacter xylinum
RT   phosphoglucomutase gene.";
RL   Microbiology 140:1183-1188(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   -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR   EMBL; L24077; AAA21561.1; -; Genomic_DNA.
DR   PIR; I39487; I39487.
DR   AlphaFoldDB; P38569; -.
DR   SMR; P38569; -.
DR   STRING; 1220579.GCA_001571345_02922; -.
DR   PRIDE; P38569; -.
DR   SABIO-RK; P38569; -.
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   CDD; cd05801; PGM_like3; 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; IPR045244; PGM.
DR   InterPro; IPR005852; PGM_a-D-Glc-sp.
DR   PANTHER; PTHR22573; PTHR22573; 1.
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   SUPFAM; SSF53738; SSF53738; 3.
DR   SUPFAM; SSF55957; SSF55957; 1.
DR   TIGRFAMs; TIGR01132; pgm; 1.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glucose metabolism; Isomerase; Magnesium;
KW   Metal-binding; Phosphoprotein.
FT   CHAIN           1..555
FT                   /note="Phosphoglucomutase"
FT                   /id="PRO_0000147807"
FT   ACT_SITE        148
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         148..149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         148
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         306
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         308
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         310..311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         310
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         393..395
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
SQ   SEQUENCE   555 AA;  59634 MW;  C67D1475AD4A9E8D CRC64;
     MPSISPFAGK PVDPDRLVNI DALLDAYYTR KPDPAIATQR VAFGTSGHRG SSLTTSFNEN
     HILSISQAIA DYRKGAGITG PLFIGIDTHA LSRPALKSAL EVFAANGVEV RIDAQDGYTP
     TPVISHAILT YNRDRSSDLA DGVVITPSHN PPEDGGYKYN PPHGGPADTD ITKVVETAAN
     DYMAKKMEGV KRVSFEDALK APTTKRHDYI TPYVDDLAAV VDMDVIRESG VSIGIDPLGG
     AAVDYWQPII DKYGINATIV SKEVDPTFRF MTADWDGQIR MDCSSPYAMA RLVGMKDKFD
     IAFANDTDAD RHGIVSGKYG LMNPNHYLAV AIEYLFNNRE NWNASAGVGK TVVSSSMIDR
     VAKEIGRKLV EVPVGFKWFV DGLYNGTLGF GGEESAGASF LRRAGTVWST DKDGIILGLL
     AAEITARTKR TPGAAYEDMT RRLGTPYYAR IDAPADPEQK AILKNLSPEQ IGMTELAGEP
     ILSTLTNAPG NGAAIGGLKV SAKDGWFAAR PSGTENVYKI YAESFKSAAH LKAIQTEAQD
     AISALFAKAA QKNAG