ID V7HW45_9LACO Unreviewed; 222 AA.
AC V7HW45;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Beta-phosphoglucomutase {ECO:0000313|EMBL:ETA73495.1};
GN ORFNames=LEQ_1629c {ECO:0000313|EMBL:ETA73495.1};
OS Ligilactobacillus equi DPC 6820.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1392007 {ECO:0000313|EMBL:ETA73495.1, ECO:0000313|Proteomes:UP000018559};
RN [1] {ECO:0000313|EMBL:ETA73495.1, ECO:0000313|Proteomes:UP000018559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DPC 6820 {ECO:0000313|EMBL:ETA73495.1,
RC ECO:0000313|Proteomes:UP000018559};
RX PubMed=24435863;
RA O'Donnell M.M., Harris H.M., O'Toole P.W., Ross R.P.;
RT "The Genome of the Predominant Equine Lactobacillus Species, Lactobacillus
RT equi, Is Reflective of Its Lifestyle Adaptations to an Herbivorous Host.";
RL Genome Announc. 2:e01155-e01113(2014).
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETA73495.1}.
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DR EMBL; AWWH01000179; ETA73495.1; -; Genomic_DNA.
DR RefSeq; WP_023860292.1; NZ_AWWH01000179.1.
DR AlphaFoldDB; V7HW45; -.
DR PATRIC; fig|1392007.3.peg.1703; -.
DR Proteomes; UP000018559; Unassembled WGS sequence.
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 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:UP000018559}.
FT ACT_SITE 7
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-1"
FT ACT_SITE 9
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-1"
FT BINDING 7..9
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 23
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; 23949 MW; D2B252BA4C9D4BCF CRC64;
MQAAVFDLDG VVTDTAKFHF QAWSKLAKEE FNLDLPASFE TNLKGISRTE SLEAILKFGD
LLDKYSKEEV QNLANKKNDY YVEAISKLTK EDILPGISKL LTDLKANGVK LAVASASKNA
PFILEKLGLA HVFDAVADPA KVKAGKPAPD IFLAGAKAVG VAPNQCVGVE DAVAGVSAIK
AADMVAVAVG DKNELRQADC VVPTTRNFTY QLFSDVFDRY HK
//
