ID Q836Y8_ENTFA Unreviewed; 222 AA.
AC Q836Y8;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 109.
DE SubName: Full=Beta-phosphoglucomutase {ECO:0000313|EMBL:AAO80763.1};
GN Name=pgmB {ECO:0000313|EMBL:AAO80763.1};
GN OrderedLocusNames=EF_0956 {ECO:0000313|EMBL:AAO80763.1};
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185 {ECO:0000313|EMBL:AAO80763.1, ECO:0000313|Proteomes:UP000001415};
RN [1] {ECO:0000313|EMBL:AAO80763.1, ECO:0000313|Proteomes:UP000001415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583 {ECO:0000313|Proteomes:UP000001415};
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D.,
RA Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L., Brinkac L., Beanan M., Daugherty S., DeBoy R.T.,
RA Durkin S., Kolonay J., Madupu R., Nelson W., Vamathevan J., Tran B.,
RA Upton J., Hansen T., Shetty J., Khouri H., Utterback T., Radune D.,
RA Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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; AE016830; AAO80763.1; -; Genomic_DNA.
DR RefSeq; NP_814693.1; NC_004668.1.
DR RefSeq; WP_002355844.1; NZ_KE136527.1.
DR AlphaFoldDB; Q836Y8; -.
DR STRING; 226185.EF_0956; -.
DR DNASU; 1199844; -.
DR EnsemblBacteria; AAO80763; AAO80763; EF_0956.
DR GeneID; 60893291; -.
DR KEGG; efa:EF0956; -.
DR PATRIC; fig|226185.45.peg.3164; -.
DR eggNOG; COG0637; Bacteria.
DR HOGENOM; CLU_045011_13_3_9; -.
DR OMA; TQTAKVH; -.
DR Proteomes; UP000001415; 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:SF18; HEXITOL PHOSPHATASE B; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SFLD; SFLDF00046; beta-phosphoglucomutase; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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:UP000001415}.
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 222 AA; 24335 MW; 517520AFE4249C62 CRC64;
MFKGVLFDLD GVITDTAEFH YHAWKKLGNE IGISIDRVFN EQLKGVSRED SLQLLLKYGK
KEGTFSSEEF AQLAQRKNDY YLEMIQAITP EDVYPGILSL LTELREANIK IALASASKNG
PFLLEKMQLT PLFDAIANPA DVQAGKPAPD IFILAAKEID LTPAECLGIE DAKAGIQAIL
ASGAQPVGVG RKEELGEGLP IVPETSALTF DYLKKVWLDH EG
//