PGM_RHIRD
ID PGM_RHIRD Reviewed; 542 AA.
AC P39671;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Phosphoglucomutase;
DE Short=PGM;
DE EC=5.4.2.2;
DE AltName: Full=Glucose phosphomutase;
GN Name=pgm; Synonyms=exoC, pscA;
OS Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS radiobacter).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=358;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A348;
RX PubMed=7959036; DOI=10.1016/0378-1119(94)90869-9;
RA Uttaro A.D., Ugalde R.A.;
RT "A chromosomal cluster of genes encoding ADP-glucose synthetase, glycogen
RT synthase and phosphoglucomutase in Agrobacterium tumefaciens.";
RL Gene 150:117-122(1994).
RN [2]
RP CHARACTERIZATION.
RX PubMed=2307661; DOI=10.1128/jb.172.3.1640-1646.1990;
RA Uttaro A.D., Cangelosi G.A., Geremia R.A., Nester E.W., Ugalde R.A.;
RT "Biochemical characterization of avirulent exoC mutants of Agrobacterium
RT tumefaciens.";
RL J. Bacteriol. 172:1640-1646(1990).
CC -!- FUNCTION: This enzyme participates in both the breakdown and synthesis
CC of glucose. Required for the synthesis of capsular polysaccharide and
CC normal lipopolysaccharide.
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; AF033856; AAD03475.1; -; Genomic_DNA.
DR AlphaFoldDB; P39671; -.
DR SMR; P39671; -.
DR STRING; 1082932.ATCR1_20058; -.
DR eggNOG; COG0033; Bacteria.
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 InterPro; IPR045244; PGM.
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 PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glucose metabolism; Isomerase; Magnesium;
KW Metal-binding; Phosphoprotein.
FT CHAIN 1..542
FT /note="Phosphoglucomutase"
FT /id="PRO_0000147808"
FT ACT_SITE 112
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 17
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 21
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 112..113
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 278
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 280..281
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 362..364
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 375
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 495
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
SQ SEQUENCE 542 AA; 57802 MW; F40AD8ED482E905D CRC64;
MIKTIKTTPY QDQKPGTSGL RKKVPVFAQE NYAENFIQSI FDALEGFEGQ TLVIGGDGRY
YNREVIQKAI KMAAAAGFGK VLVGQGGILS TPAASNVIRK YKAFGGIVLS ASHNPGGPTE
DFGIKYNIGN GGPAPEKITD AIYARSKVID SYKISDAADI DLDKIGSFKV DELTVDVIDP
VADYAALMEE LFDFGAIRSL IAGGFKVVVD SMSAVTGPYA VEILEKRLGA PKGSVRNATP
LPDFGGHHPD PNLVHAKELY DDVMSPEGPD FGAASDGDGD RNMVVGKGMF VTPSDSLAII
AANAKLAPGY AAGISGIARS MPTSAAADRV AEKLGLGMYE TPTGWKFFGN LMDAGKVTIC
GEESFGTGSN HVREKDGLWA VLYWLNIVAA RKESVKDIVT KHWAEYGRNY YSRHDYEEVD
SDAANTLVAI LREKLATLPG TSYGNLKVAA ADDFAYHDPV DQSVSKNQGI RILFEGGSRI
VLRLSGTGTA GATLRLYVER YEPDAARHGI ETQSALADLI SVADTIAGIK AHTADSEPTV
IT
