SitesBLAST
Comparing 7024893 FitnessBrowser__ANA3:7024893 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
4g9bA Crystal structure of beta-phosphoglucomutase homolog from escherichia coli, target efi-501172, with bound mg, open lid
31% identity, 93% coverage: 4:191/202 of query aligns to 3:195/227 of 4g9bA
- active site: D10 (= D11), L11 (≠ M12), D12 (= D13), T18 (≠ S19), K46 (≠ A47), S117 (≠ A113), V118 (≠ Y114), K148 (= K144), E172 (= E168), D173 (= D169)
- binding magnesium ion: D10 (= D11), D12 (= D13), D173 (= D169)
Q8VZ10 Protein SUPPRESSOR OF QUENCHING 1, chloroplastic; EC 3.1.3.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 94% coverage: 2:191/202 of query aligns to 71:264/1055 of Q8VZ10
- D80 (= D11) mutation to N: Complete rescue in complementation test of the nonphotochemical quenching (NPQ) phenotype observed in disrupted plants.
Sites not aligning to the query:
- 431:434 CINC→SINS: No rescue in complementation test of the nonphotochemical quenching (NPQ) phenotype observed in disrupted plants.
- 859 E→K: In soq1-2; high light intensity-dependent and irreversible nonphotochemical quenching (NPQ) due to a decrease in chlorophyll excited-state lifetime.
5olwA 5-fluorotryptophan labeled beta-phosphoglucomutase in an open conformation (see paper)
26% identity, 91% coverage: 5:187/202 of query aligns to 2:188/224 of 5olwA
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (≠ S19), K45 (≠ A47), S114 (≠ T111), A115 (≠ G112), K145 (= K144), E169 (= E168), D170 (= D169)
- binding calcium ion: D8 (= D11), D10 (= D13), P89 (≠ H86), V92 (= V89), E124 (≠ T123), N127 (≠ G126), E169 (= E168), D170 (= D169), S171 (≠ A170)
6qzgA Beta-glucose 1,6-bisphosphonate bound to wild type beta- phosphoglucomutse in an open conformation.
26% identity, 91% coverage: 5:187/202 of query aligns to 2:188/219 of 6qzgA
- binding 3,7-anhydro-1,2,8-trideoxy-1,8-diphosphono-D-glycero-D-gulo-octitol: D8 (= D11), L9 (≠ M12), D10 (= D13), H20 (= H23), G46 (= G48), S114 (≠ T111), A115 (≠ G112), S116 (≠ T115), K117 (≠ E116), K145 (= K144)
- binding magnesium ion: D8 (= D11), D10 (= D13), D170 (= D169)
1z4nA Structure of beta-phosphoglucomutase with inhibitor bound alpha- galactose 1-phosphate cocrystallized with fluoride (see paper)
26% identity, 91% coverage: 5:187/202 of query aligns to 2:188/219 of 1z4nA
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (≠ S19), K45 (≠ A47), S114 (≠ T111), A115 (≠ G112), K145 (= K144), E169 (= E168), D170 (= D169)
- binding 1-O-phosphono-alpha-D-galactopyranose: H20 (= H23), W24 (= W27), V47 (= V49), R49 (≠ T51), S116 (≠ T115), K117 (≠ E116), N118 (≠ E117)
- binding magnesium ion: D8 (= D11), D10 (= D13), E169 (= E168), D170 (= D169)
6h91A Phosphorylated beta-phosphoglucomutase from lactococcus lactis in an open conformer to 2.4 a
26% identity, 91% coverage: 5:187/202 of query aligns to 2:188/218 of 6h91A
4c4rA Structure of beta-phosphoglucomutase in complex with a phosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride (see paper)
26% identity, 91% coverage: 5:187/202 of query aligns to 2:188/218 of 4c4rA
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (≠ S19), K45 (≠ A47), S114 (≠ T111), A115 (≠ G112), K145 (= K144), E169 (= E168), D170 (= D169)
- binding magnesium ion: D8 (= D11), D10 (= D13), D170 (= D169)
- binding trifluoromagnesate: D8 (= D11), L9 (≠ M12), D10 (= D13), S114 (≠ T111), A115 (≠ G112), K145 (= K144)
- binding (1R)-1,5-anhydro-1-(phosphonomethyl)-D-glucitol: D10 (= D13), H20 (= H23), W24 (= W27), L44 (= L46), G46 (= G48), V47 (= V49), R49 (≠ T51), S52 (≠ T54), S116 (≠ T115), K117 (≠ E116)
3zi4A The structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and scandium tetrafluoride
26% identity, 91% coverage: 5:187/202 of query aligns to 2:188/218 of 3zi4A
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (≠ S19), K45 (≠ A47), S114 (≠ T111), A115 (≠ G112), K145 (= K144), E169 (= E168), D170 (= D169)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D13), H20 (= H23), G46 (= G48), V47 (= V49), R49 (≠ T51), S116 (≠ T115), K117 (≠ E116)
- binding magnesium ion: D8 (= D11), D10 (= D13), D170 (= D169)
- binding Scandium Tetrafluoride: D8 (= D11), L9 (≠ M12), D10 (= D13), S114 (≠ T111), A115 (≠ G112), K145 (= K144)
2wf8A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate, glucose-1-phosphate and beryllium trifluoride (see paper)
26% identity, 91% coverage: 5:187/202 of query aligns to 2:188/218 of 2wf8A
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (≠ S19), K45 (≠ A47), S114 (≠ T111), A115 (≠ G112), K145 (= K144), E169 (= E168), D170 (= D169)
- binding beryllium trifluoride ion: D8 (= D11), L9 (≠ M12), D10 (= D13), S114 (≠ T111), A115 (≠ G112), K145 (= K144)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D13), H20 (= H23), G46 (= G48), V47 (= V49), R49 (≠ T51), A115 (≠ G112), S116 (≠ T115), K117 (≠ E116)
- binding 1-O-phosphono-alpha-D-glucopyranose: D10 (= D13), H20 (= H23), W24 (= W27), L44 (= L46), G46 (= G48), V47 (= V49), R49 (≠ T51), S52 (≠ T54), A115 (≠ G112), S116 (≠ T115), K117 (≠ E116)
- binding magnesium ion: D8 (= D11), D10 (= D13), D170 (= D169)
2wf7A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphonate and aluminium tetrafluoride (see paper)
26% identity, 91% coverage: 5:187/202 of query aligns to 2:188/218 of 2wf7A
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (≠ S19), K45 (≠ A47), S114 (≠ T111), A115 (≠ G112), K145 (= K144), E169 (= E168), D170 (= D169)
- binding tetrafluoroaluminate ion: D8 (= D11), L9 (≠ M12), D10 (= D13), S114 (≠ T111), K145 (= K144)
- binding 6,7-dideoxy-7-phosphono-beta-D-gluco-heptopyranose: D10 (= D13), G46 (= G48), V47 (= V49), R49 (≠ T51), S116 (≠ T115), K117 (≠ E116), N118 (≠ E117)
- binding magnesium ion: D8 (= D11), D10 (= D13), D170 (= D169)
2wf6A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and aluminium tetrafluoride (see paper)
26% identity, 91% coverage: 5:187/202 of query aligns to 2:188/218 of 2wf6A
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (≠ S19), K45 (≠ A47), S114 (≠ T111), A115 (≠ G112), K145 (= K144), E169 (= E168), D170 (= D169)
- binding tetrafluoroaluminate ion: D8 (= D11), L9 (≠ M12), D10 (= D13), S114 (≠ T111), K145 (= K144)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D13), G46 (= G48), V47 (= V49), R49 (≠ T51), S116 (≠ T115), K117 (≠ E116)
- binding magnesium ion: D8 (= D11), D10 (= D13), D170 (= D169)
2wf5A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and trifluoromagnesate (see paper)
26% identity, 91% coverage: 5:187/202 of query aligns to 2:188/218 of 2wf5A
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (≠ S19), K45 (≠ A47), S114 (≠ T111), A115 (≠ G112), K145 (= K144), E169 (= E168), D170 (= D169)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D13), H20 (= H23), G46 (= G48), V47 (= V49), R49 (≠ T51), A115 (≠ G112), S116 (≠ T115)
- binding magnesium ion: D8 (= D11), D10 (= D13), D170 (= D169)
- binding trifluoromagnesate: D8 (= D11), L9 (≠ M12), D10 (= D13), S114 (≠ T111), A115 (≠ G112), K145 (= K144)
2wf9A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate, and beryllium trifluoride, crystal form 2 (see paper)
26% identity, 91% coverage: 5:187/202 of query aligns to 2:188/221 of 2wf9A
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (≠ S19), K45 (≠ A47), S114 (≠ T111), A115 (≠ G112), K145 (= K144), E169 (= E168), D170 (= D169)
- binding beryllium trifluoride ion: D8 (= D11), L9 (≠ M12), D10 (= D13), S114 (≠ T111), A115 (≠ G112), K145 (= K144)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D13), H20 (= H23), G46 (= G48), V47 (= V49), R49 (≠ T51), S116 (≠ T115), K117 (≠ E116), N118 (≠ E117)
- binding 6-O-phosphono-alpha-D-glucopyranose: D10 (= D13), H20 (= H23), G46 (= G48), V47 (= V49), R49 (≠ T51), A115 (≠ G112), S116 (≠ T115), K117 (≠ E116), N118 (≠ E117)
- binding magnesium ion: D8 (= D11), D10 (= D13), D170 (= D169)
1o03A Structure of pentavalent phosphorous intermediate of an enzyme catalyzed phosphoryl transfer reaction observed on cocrystallization with glucose 6-phosphate (see paper)
26% identity, 91% coverage: 5:187/202 of query aligns to 2:188/221 of 1o03A
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (≠ S19), K45 (≠ A47), S114 (≠ T111), A115 (≠ G112), K145 (= K144), E169 (= E168), D170 (= D169)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: D8 (= D11), L9 (≠ M12), D10 (= D13), H20 (= H23), G46 (= G48), V47 (= V49), R49 (≠ T51), S114 (≠ T111), A115 (≠ G112), S116 (≠ T115), K117 (≠ E116), K145 (= K144)
- binding magnesium ion: D8 (= D11), D10 (= D13), D170 (= D169)
1lvhA The structure of phosphorylated beta-phosphoglucomutase from lactoccocus lactis to 2.3 angstrom resolution (see paper)
26% identity, 91% coverage: 5:187/202 of query aligns to 2:188/221 of 1lvhA
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (≠ S19), K45 (≠ A47), S114 (≠ T111), A115 (≠ G112), K145 (= K144), E169 (= E168), D170 (= D169)
- binding magnesium ion: D8 (= D11), D10 (= D13), D170 (= D169)
P71447 Beta-phosphoglucomutase; Beta-PGM; EC 5.4.2.6 from Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) (see 3 papers)
26% identity, 91% coverage: 5:187/202 of query aligns to 2:188/221 of P71447
- D8 (= D11) modified: 4-aspartylphosphate; mutation to A: Inactive.; mutation to E: Inactive.
- D10 (= D13) mutation to A: Inactive.; mutation to E: Inactive.; mutation to N: Inactive.; mutation to S: Inactive.
- T16 (≠ S19) mutation to P: 500-fold reduction in the rate constant for Asp-8 phosphorylation by beta-G1,6bisP. 6,700-fold reduction in the apparent rate constant for cycling of the phosphorylated enzyme to convert beta-G1P to G6P. 13-fold increase in the estimated rate constant for phosphoryl transfer from the phospho-Asp8 to water.
- H20 (= H23) mutation to A: Impairs Asp-8 phosphorylation by beta-G1,6bisP and phosphoryl transfer from the phospho-Asp8 to the substrate beta-G1P.; mutation to N: 300-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP.; mutation to Q: 8-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP.
- K45 (≠ A47) mutation to A: 20'000-fold decrease in kcat/KM.
- G46 (= G48) mutation to A: 1'000'000-fold decrease in kcat/KM.; mutation to P: 100'000-fold decrease in kcat/KM.; mutation to V: 10'000-fold decrease in kcat/KM.
- R49 (≠ T51) mutation to K: 1'000'000-fold decrease in kcat/KM.
- S52 (≠ T54) mutation to A: Wild-type activity.
- K76 (≠ M73) mutation to A: 100-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP.
- D170 (= D169) mutation to A: Impaired, but active with an increase in the affinity for G1P.
4c4sA Structure of beta-phosphoglucomutase in complex with an alpha- fluorophosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride (see paper)
27% identity, 91% coverage: 5:187/202 of query aligns to 2:185/215 of 4c4sA
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (≠ S19), K45 (≠ A47), S111 (≠ T111), A112 (≠ G112), K142 (= K144), E166 (= E168), D167 (= D169)
- binding (1R)-1,5-anhydro-1-[(S)-fluoro(phosphono)methyl]-D-glucitol: D10 (= D13), H20 (= H23), W24 (= W27), L44 (= L46), G46 (= G48), V47 (= V49), R49 (≠ T51), S113 (≠ T115)
- binding magnesium ion: D8 (= D11), D10 (= D13), D167 (= D169)
- binding trifluoromagnesate: D8 (= D11), L9 (≠ M12), D10 (= D13), S111 (≠ T111), A112 (≠ G112), K142 (= K144)
5ok0A Structure of the d10n mutant of beta-phosphoglucomutase from lactococcus lactis trapped with native reaction intermediate beta- glucose 1,6-bisphosphate to 2.2a resolution.
25% identity, 91% coverage: 5:187/202 of query aligns to 2:188/218 of 5ok0A
- active site: D8 (= D11), L9 (≠ M12), N10 (≠ D13), T16 (≠ S19), K45 (≠ A47), S114 (≠ T111), A115 (≠ G112), K145 (= K144), E169 (= E168), D170 (= D169)
- binding 1,6-di-O-phosphono-beta-D-glucopyranose: D8 (= D11), L9 (≠ M12), N10 (≠ D13), H20 (= H23), L44 (= L46), V47 (= V49), R49 (≠ T51), S114 (≠ T111), A115 (≠ G112), S116 (≠ T115)
- binding magnesium ion: D8 (= D11), N10 (≠ D13), D170 (= D169)
- binding 1,3-propandiol: I33 (= I36), N34 (≠ P37), G35 (vs. gap), V36 (= V38)
5o6rA Structure of beta-phosphoglucomutase d10n mutant in complex with glucose-1-phosphate and aluminium tetrafluoride
25% identity, 91% coverage: 5:187/202 of query aligns to 2:188/218 of 5o6rA
- active site: D8 (= D11), L9 (≠ M12), N10 (≠ D13), T16 (≠ S19), K45 (≠ A47), S114 (≠ T111), A115 (≠ G112), K145 (= K144), E169 (= E168), D170 (= D169)
- binding tetrafluoroaluminate ion: D8 (= D11), L9 (≠ M12), N10 (≠ D13), G46 (= G48), S114 (≠ T111), K145 (= K144)
- binding magnesium ion: D8 (= D11), N10 (≠ D13), D170 (= D169)
- binding 1-O-phosphono-beta-D-glucopyranose: H20 (= H23), W24 (= W27), L44 (= L46), V47 (= V49), R49 (≠ T51), S52 (≠ T54), S116 (≠ T115), K117 (≠ E116), N118 (≠ E117)
5o6pA Structure of beta-phosphoglucomutase d10n mutant in complex with glucose-1,6-bisphosphate
25% identity, 91% coverage: 5:187/202 of query aligns to 1:187/209 of 5o6pA
- active site: D7 (= D11), L8 (≠ M12), N9 (≠ D13), T15 (≠ S19), K44 (≠ A47), S113 (≠ T111), A114 (≠ G112), K144 (= K144), E168 (= E168), D169 (= D169)
- binding 1,6-di-O-phosphono-beta-D-glucopyranose: D7 (= D11), L8 (≠ M12), N9 (≠ D13), H19 (= H23), L43 (= L46), K44 (≠ A47), G45 (= G48), V46 (= V49), R48 (≠ T51), S113 (≠ T111), A114 (≠ G112), S115 (≠ T115), K116 (≠ E116), K144 (= K144)
- binding magnesium ion: D7 (= D11), N9 (≠ D13), D169 (= D169)
Query Sequence
>7024893 FitnessBrowser__ANA3:7024893
MYTEFDGIIFDMDGTLVDSGQLHEQAWRQTLNHFGIPVEPALMRSLAGVPTIGTLEILIA
HFGVTPTASCEAMNEYKEALVRDTMHLYVKPTALAEFAKQNQGKRPMAVGTGAYTEEAIQ
ILTLCGLLELVDYVVGADQVASPKPAPDTFLRCAELMGIAPERCIVFEDAKAGIQAAEAA
GMFVVDVHAELQIENDYFLGTR
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory