ID A0A0J1DE09_9BURK Unreviewed; 214 AA.
AC A0A0J1DE09;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Beta-phosphoglucomutase {ECO:0000313|EMBL:KLU37310.1};
DE EC=5.4.2.6 {ECO:0000313|EMBL:KLU37310.1};
GN ORFNames=AB595_08515 {ECO:0000313|EMBL:KLU37310.1};
OS Massilia sp. WF1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1406431 {ECO:0000313|EMBL:KLU37310.1, ECO:0000313|Proteomes:UP000036336};
RN [1] {ECO:0000313|Proteomes:UP000036336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF1 {ECO:0000313|Proteomes:UP000036336};
RA Lou J., Gu H., Wang H., Xu J.;
RT "High quality genome sequence of a efficient PHE-degrading Massilia sp.
RT strain WF1, isolated from a polycyclic aromatic hydrocarbons (PAHs)
RT contaminated soil.";
RL Submitted (JUN-2015) 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:KLU37310.1}.
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DR EMBL; LELH02000009; KLU37310.1; -; Genomic_DNA.
DR RefSeq; WP_047824259.1; NZ_LELH02000009.1.
DR AlphaFoldDB; A0A0J1DE09; -.
DR PATRIC; fig|1406431.3.peg.5123; -.
DR Proteomes; UP000036336; 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 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 Isomerase {ECO:0000313|EMBL:KLU37310.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR610972-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR610972-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000036336}.
FT ACT_SITE 11
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-1"
FT ACT_SITE 13
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-1"
FT BINDING 11..13
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 27
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 46..51
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 116..120
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
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 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 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT SITE 116
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 147
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 214 AA; 23098 MW; 232E450A7A73CD26 CRC64;
MSSRFKAVVF DLDGVITDTA RFHYLAWKRL ADGIGAPFDE AFNEELKGVD RMGSLELILA
RAPRSYTAQE KLRLADAKNA HYQELVATMT PDDLLPGALR ALEQVRAAGL KIGLASVSKN
AFTVLDRLGI RDRFDDVVDA ATIANSKPHP EIFLTAASHL GIAPADCLGV EDAAAGVASI
KDAGMRAVGV GDPQILARAD YIIPSMREFR LGDY
//
