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Database: UniProt
Entry: Q836Y8_ENTFA
LinkDB: Q836Y8_ENTFA
Original site: Q836Y8_ENTFA 
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
//
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