Top Level Name

  ⌊ Superfamily (core) Haloacid Dehalogenase

    ⌊ Subgroup C1.5: HAD, Beta-PGM, Phosphatase Like

  C1.5.6: HAD, Beta-PGM, Phosphatase Like

     ⌊ Family beta-phosphoglucomutase

  ⌊ FunctionalDomain beta-phosphoglucomutase (ID 2262)

Superfamily Assignment Evidence Code(s) FSM
Family Assignment Evidence Code CFM
This entry was last updated onJan. 14, 2017

References to Other Databases

Genbank

SpeciesGIAccessionModel
Lactococcus lactis 502661210 WP_012897250.1 (RefSeq) MB URP
Lactococcus lactis subsp. lactis 736044825 AJA56351.1 (Genbank) MB URP
Lactococcus lactis 691499754 KGF76471.1 (Genbank) MB URP
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Uniprot

Protein NameAccessionEC Number IdentifierModel
Beta-phosphoglucomutase P71447 5.4.2.6 PGMB_LACLA (Swiss-Prot) MB
n/a A0A0A7T4I1 A0A0A7T4I1_LACLL (TrEMBL) MB
n/a D2BNW1 D2BNW1_LACLK (TrEMBL) MB
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Sequence

Length of Enzyme (full-length): 221 | Length of Functional Domain: 218

1       10        20        30        40        50        60

MFKAVLFDLDGVITDTAEYHFRAWKALAEEIGINGVDRQFNEQLKGVSREDSLQKILDLA
DKKVSAEEFKELAKRKNDNYVKMIQDVSPADVYPGILQLLKDLRSNKIKIALASASKNGP
FLLERMNLTGYFDAIADPAEVAASKPAPDIFIAAAHAVGVAPSESIGLEDSQAGIQAIKD
SGALPIGVGRPEDLGDDIVIVPDTSHYTLEFLKEVWLQ
KQK

FASTA | BLAST | HMM

This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues

This EFD conserves 8/8 Family-specific CRs and 4/5 Subgroup-specific CRs.
Position Amino Acid Location Family/Subgroup CAR Function Role Evidence Code Reference
8 Asp (D) side chain subgroup Mg2+ ligand, nucleophile: attacks phosphate moiety of intermediate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding
ICS
8 Asp (D) side chain family Mg2+ ligand, nucleophile: attacks phosphate moiety of intermediate to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding
ICS
10 Asp (D) side chain family Mg2+ ligand, nucleophile: attacks phosphate moiety of cofactor to form covalent intermediate covalent catalysis -- reactant,
metal ligand -- binding
ICS
16 Thr (T) side chain family interacts with phosphate moiety of intermediate substrate binding -- binding ICS
45 Lys (K) side chain family interacts with phosphate moiety of intermediate substrate binding -- binding ICS
114 Ser (S) side chain family interacts with phosphate moiety of intermediate substrate binding -- binding ICS
145 Lys (K) side chain subgroup None -- ICS
145 Lys (K) side chain family interacts with phosphate moiety of intermediate substrate binding -- binding ICS
169 Glu (E) side chain family Mg2+ ligand metal ligand -- binding ICS
169 Glu (E) side chain subgroup Mg2+ ligand
Notes: Sequences in this subgroup may have one or more of the final three D/E listed as Mg2+ ligands
metal ligand -- binding ICS
170 Asp (D) side chain family Mg2+ ligand metal ligand -- binding ICS
170 Asp (D) side chain subgroup Mg2+ ligand
Notes: Sequences in this subgroup may have one or more of the final three D/E listed as Mg2+ ligands
metal ligand -- binding ICS
174 Gly (G) side chain subgroup MISMATCH: This residue does not match the specified amino acid type of D,E, and thus may not function in the same manner as other sequences in the subgroup

Catalyzed Reaction

beta-phosphoglucomutase

beta-D-glucose 1-phosphate(2-)
57684
beta-D-glucose 6-phosphate(2-)
58247

EC: | IntEnz: | Kegg: | BioCyc: | BRENDA: |

Structures

PDB ID Title Molecule Name Number of
EFDs
Resolution (Å) Mutant? Het group Chimera Session Links
2WHE Structure Of Native Beta-Phosphoglucomutase In An Open Conformation Without Bound Ligands. Beta-Phosphoglucomutase 5 1.55 Magnesium Ion CSA • PDB • PDBSum
1Z4O Structure Of Beta-Phosphoglucomutase With Inhibitor Bound Alpha-Galactose 1-Phosphate Beta-Phosphoglucomutase 5 1.9 Magnesium Ion • 1-O-Phosphono-Alpha-D-Galactopyranose CSA • PDB • PDBSum
1Z4N Structure Of Beta-Phosphoglucomutase With Inhibitor Bound Alpha-Galactose 1-Phosphate Cocrystallized With Fluoride Beta-Phosphoglucomutase 5 1.97 Magnesium Ion • 1-O-Phosphono-Alpha-D-Galactopyranose CSA • PDB • PDBSum
2WFA Structure Of Beta-Phosphoglucomutase Inhibited With Beryllium Trifluoride, In An Open Conformation. Beta-Phosphoglucomutase 5 1.65 Beryllium Trifluoride Ion • Magnesium Ion CSA • PDB • PDBSum
1O08 Structure Of Pentavalent Phosphorous Intermediate Of An Enzyme Catalyzed Phosphoryl Transfer Reaction Observed On Cocrystallization With Glucose 1-Phosphate Beta-Phosphoglucomutase 5 1.2 Alpha-D-Glucose 1,6-Bisphosphate • Magnesium Ion CSA • PDB • PDBSum
2WF9 Structure Of Beta-Phosphoglucomutase Inhibited With Glucose-6-Phosphate, And Beryllium Trifluoride, Crystal Form 2 Beta-Phosphoglucomutase 5 1.4 Magnesium Ion
(4 more ⇓)
CSA • PDB • PDBSum
2WF8 Structure Of Beta-Phosphoglucomutase Inhibited With Glucose-6-Phosphate, Glucose-1-Phosphate And Beryllium Trifluoride Beta-Phosphoglucomutase 5 1.2 Beta-D-Glucose-6-Phosphate
(5 more ⇓)
CSA • PDB • PDBSum
1ZOL Native Beta-Pgm Beta-Phosphoglucomutase 5 1.9 Magnesium Ion CSA • PDB • PDBSum
1O03 Structure Of Pentavalent Phosphorous Intermediate Of An Enzyme Catalyzed Phosphoryl Transfer Reaction Observed On Cocrystallization With Glucose 6-Phosphate Beta-Phosphoglucomutase 5 1.4 Alpha-D-Glucose 1,6-Bisphosphate • Magnesium Ion CSA • PDB • PDBSum
2WF7 Structure Of Beta-Phosphoglucomutase Inhibited With Glucose-6-Phosphonate And Aluminium Tetrafluoride Beta-Phosphoglucomutase 5 1.05 6,7-Dideoxy-7-Phosphono-Beta-D-Gluco-Heptopyranose
(2 more ⇓)
CSA • PDB • PDBSum
2WF6 Structure Of Beta-Phosphoglucomutase Inhibited With Glucose-6-Phospahte And Aluminium Tetrafluoride Beta-Phosphoglucomutase 5 1.4 Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
2WF5 Structure Of Beta-Phosphoglucomutase Inhibited With Glucose-6-Phospahte And Trifluoromagnesate Beta-Phosphoglucomutase 5 1.3 Beta-D-Glucose-6-Phosphate
(2 more ⇓)
CSA • PDB • PDBSum
3ZI4 The Structure Of Beta-Phosphoglucomutase Inhibited With Glucose-6-Phospahte And Scandium Tetrafluoride Beta-Phosphoglucomutase 5 1.33 Scandium Tetraflouride
(2 more ⇓)
CSA • PDB • PDBSum
4C4T Structure Of Beta-Phosphoglucomutase In Complex With A Phosphonate Analogue Of Beta-Glucose-1-Phosphate And Aluminium Tetrafluoride Beta-Phosphoglucomutase 5 1.5 (S)-1-Beta-Phosphonofluoromethylene-1-Deoxy-D-Glucopyranose
(2 more ⇓)
CSA • PDB • PDBSum
4C4S Structure Of Beta-Phosphoglucomutase In Complex With An Alpha-Fluorophosphonate Analogue Of Beta-Glucose-1-Phosphate And Magnesium Trifluoride Beta-Phosphoglucomutase 5 1.5 (S)-1-Beta-Phosphonofluoromethylene-1-Deoxy-D-Glucopyranose
(2 more ⇓)
CSA • PDB • PDBSum
4C4R Structure Of Beta-Phosphoglucomutase In Complex With A Phosphonate Analogue Of Beta-Glucose-1-Phosphate And Magnesium Trifluoride Beta-Phosphoglucomutase 5 1.1 Beta-1 Phosphonomethylene-D-Glucopyranose
(2 more ⇓)
CSA • PDB • PDBSum
1LVH The Structure Of Phosphorylated Beta-Phosphoglucomutase From Lactoccocus Lactis To 2.3 Angstrom Resolution Beta-Phosphoglucomutase 5 2.3 Aspartyl Phosphate • Magnesium Ion CSA • PDB • PDBSum
3FM9 Analysis Of The Structural Determinants Underlying Discrimination Between Substrate And Solvent In Beta-Phosphoglucomutase Catalysis Beta-Phosphoglucomutase 5 2.7 Yes Magnesium Ion CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History

Time Change Annotation Old Value New Value
Nov. 3, 2014, 9:26 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.