ID A0A150LCY3_9BACI Unreviewed; 229 AA.
AC A0A150LCY3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Beta-phosphoglucomutase {ECO:0000313|EMBL:KYD10124.1};
DE EC=5.4.2.6 {ECO:0000313|EMBL:KYD10124.1};
GN ORFNames=B4135_3603 {ECO:0000313|EMBL:KYD10124.1};
OS Caldibacillus debilis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus.
OX NCBI_TaxID=301148 {ECO:0000313|EMBL:KYD10124.1, ECO:0000313|Proteomes:UP000075683};
RN [1] {ECO:0000313|EMBL:KYD10124.1, ECO:0000313|Proteomes:UP000075683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4135 {ECO:0000313|EMBL:KYD10124.1,
RC ECO:0000313|Proteomes:UP000075683};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT Foods.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:KYD10124.1}.
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DR EMBL; LQYT01000121; KYD10124.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150LCY3; -.
DR STRING; 301148.B4135_3603; -.
DR PATRIC; fig|301148.3.peg.1646; -.
DR OrthoDB; 9797743at2; -.
DR Proteomes; UP000075683; Unassembled WGS sequence.
DR GO; GO:0008801; F:beta-phosphoglucomutase activity; IEA:UniProtKB-EC.
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; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:KYD10124.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR610972-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR610972-3}.
FT ACT_SITE 10
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-1"
FT ACT_SITE 12
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-1"
FT BINDING 10..12
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
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 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 26
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 45..50
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 117..121
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT SITE 117
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 148
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 229 AA; 25564 MW; 1A8959BABD2C5392 CRC64;
MTKPKLFIFD LDGVITDTAE FHFLAWKQLA EELGITIDRR FNEELKGISR MESLEKILAL
DPALQGMPLE EKKRLAEKKN DHYKELIRTI TPDHILPGVE PLIKRIKEEG ILLALGSASK
NAPAVLQRLG LYEDFDFIVD PAKVKKGKPD PEIFTKAADH FRVPYSACVG VEDSAAGIEA
INRAGMFSVG VGAADVLSAS AYIVPDTSRL DFDRIVEKFN RAWEVEPSR
//
