ID I6T8Y4_ENTHA Unreviewed; 221 AA.
AC I6T8Y4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Beta-phosphoglucomutase {ECO:0000313|EMBL:AFM69659.1};
GN OrderedLocusNames=EHR_03435 {ECO:0000313|EMBL:AFM69659.1};
OS Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 /
OS NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=768486 {ECO:0000313|EMBL:AFM69659.1, ECO:0000313|Proteomes:UP000002895};
RN [1] {ECO:0000313|EMBL:AFM69659.1, ECO:0000313|Proteomes:UP000002895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB
RC 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R
RC {ECO:0000313|Proteomes:UP000002895};
RX PubMed=22933757; DOI=10.1128/JB.01075-12;
RA Gaechter T., Wunderlin C., Schmidheini T., Solioz M.;
RT "Genome sequence of Enterococcus hirae (Streptococcus faecalis) ATCC 9790,
RT a model organism for the study of ion transport, bioenergetics, and copper
RT homeostasis.";
RL J. Bacteriol. 194:5126-5127(2012).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR610972-3};
CC Note=Binds 2 magnesium ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR610972-3};
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DR EMBL; CP003504; AFM69659.1; -; Genomic_DNA.
DR RefSeq; WP_010736920.1; NZ_KB946222.1.
DR AlphaFoldDB; I6T8Y4; -.
DR KEGG; ehr:EHR_03435; -.
DR PATRIC; fig|768486.10.peg.302; -.
DR eggNOG; COG0637; Bacteria.
DR HOGENOM; CLU_045011_13_3_9; -.
DR OrthoDB; 9797743at2; -.
DR Proteomes; UP000002895; Chromosome.
DR GO; GO:0008801; F:beta-phosphoglucomutase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd02598; HAD_BPGM; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR010976; B-phosphoglucomutase_hydrolase.
DR InterPro; IPR010972; Beta-phosphoglucomutase.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR NCBIfam; TIGR01990; bPGM; 1.
DR NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR NCBIfam; TIGR02009; PGMB-YQAB-SF; 1.
DR PANTHER; PTHR46193; 6-PHOSPHOGLUCONATE PHOSPHATASE; 1.
DR PANTHER; PTHR46193:SF22; HEXITOL PHOSPHATASE B; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SFLD; SFLDF00046; beta-phosphoglucomutase; 1.
DR SFLD; SFLDG01135; C1.5.6:_HAD__Beta-PGM__Phospha; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 4: Predicted;
KW Magnesium {ECO:0000256|PIRSR:PIRSR610972-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR610972-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000002895}.
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-1"
FT ACT_SITE 10
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-1"
FT BINDING 8..10
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 24
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 43..48
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 115..119
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT SITE 115
FT /note="Important for catalytic activity and assists the
FT phosphoryl transfer reaction to Asp8 by balancing charge
FT and orienting the reacting groups"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-4"
FT SITE 146
FT /note="Important for catalytic activity and assists the
FT phosphoryl transfer reaction to Asp8 by balancing charge
FT and orienting the reacting groups"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-4"
SQ SEQUENCE 221 AA; 24501 MW; AB5080A217ED36F5 CRC64;
MFKGVLFDLD GVITDTAEFH YRAWKKLGQE IGVPIDRTFN EQLKGVSRED SLRLLLSYGQ
KESEFSPQEF QELAHRKNEY YLEMIQAITP TDVFPGILPL LEELRANKIK IALASASKNG
PFLLAKMALT PFFDAIADPA TIKLGKPAPD IFLLAAKEIG LSPQECIGIE DAQSGIKAIR
ASGAFPIGVG RIEDLGKDIP VVPDTTCLTL DYLKNEWTQY V
//
