SitesBLAST
Comparing 350225 FitnessBrowser__Btheta:350225 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)
6w04A Crystal structure of had hydrolase, family ia, variant 3 from entamoeba histolytica hm-1:imss
27% identity, 96% coverage: 8:213/215 of query aligns to 3:220/223 of 6w04A
- active site: D7 (= D12), F8 (= F13), N9 (≠ D14), D15 (≠ T20), N44 (≠ G42), T109 (= T105), S110 (= S106), K144 (= K139), E168 (= E163), D169 (= D164)
- binding magnesium ion: D7 (= D12), N9 (≠ D14), D169 (= D164)
4uasA Crystal structure of cbby from rhodobacter sphaeroides in complex with phosphate (see paper)
27% identity, 92% coverage: 8:205/215 of query aligns to 4:217/225 of 4uasA
- active site: D8 (= D12), V9 (≠ F13), D10 (= D14), T16 (= T20), T47 (vs. gap), T115 (= T105), T116 (≠ S106), K151 (= K139), E175 (= E163), D176 (= D164)
- binding magnesium ion: D8 (= D12), D10 (= D14), D176 (= D164)
- binding phosphate ion: D8 (= D12), V9 (≠ F13), D10 (= D14), T115 (= T105), T116 (≠ S106), K151 (= K139)
P95649 Protein CbbY; RuCbby; EC 3.1.3.- from Cereibacter sphaeroides (Rhodobacter sphaeroides) (see paper)
27% identity, 92% coverage: 8:205/215 of query aligns to 4:217/230 of P95649
- D10 (= D14) mutation to N: Loss of catalytic activity.
- E17 (= E21) mutation to A: 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
- H20 (≠ Y24) mutation to A: 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
- Y42 (≠ G32) mutation to A: 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
- R54 (≠ D40) mutation to A: 97% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
- K78 (≠ Q65) mutation to A: 40% to 80% decreased catalytic activity with xylulose-1,5-bisphosphate, but no effect on activity with ribulose-1,5-bisphosphate.
4uauA Crystal structure of cbby (mutant d10n) from rhodobacter sphaeroides in complex with xylulose-(1,5)bisphosphate, crystal form ii (see paper)
27% identity, 92% coverage: 8:205/215 of query aligns to 4:217/226 of 4uauA
- active site: D8 (= D12), V9 (≠ F13), N10 (≠ D14), T16 (= T20), T47 (vs. gap), T115 (= T105), T116 (≠ S106), K151 (= K139), E175 (= E163), D176 (= D164)
- binding magnesium ion: D8 (= D12), N10 (≠ D14), D176 (= D164)
- binding xylulose-1,5-bisphosphate: D8 (= D12), V9 (≠ F13), N10 (≠ D14), E17 (= E21), H20 (≠ Y24), T49 (vs. gap), G50 (vs. gap), G51 (≠ N37), R54 (≠ D40), H75 (≠ P62), K78 (≠ Q65), T115 (= T105), T116 (≠ S106), T117 (≠ S107), S118 (vs. gap)
Q8VZ10 Protein SUPPRESSOR OF QUENCHING 1, chloroplastic; EC 3.1.3.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
27% identity, 98% coverage: 2:211/215 of query aligns to 70:290/1055 of Q8VZ10
- D80 (= D12) 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.
4c4sA Structure of beta-phosphoglucomutase in complex with an alpha- fluorophosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride (see paper)
30% identity, 94% coverage: 8:210/215 of query aligns to 4:209/215 of 4c4sA
- active site: D8 (= D12), L9 (≠ F13), D10 (= D14), T16 (= T20), K45 (= K46), S111 (≠ T105), A112 (≠ S106), K142 (= K139), E166 (= E163), D167 (= D164)
- binding (1R)-1,5-anhydro-1-[(S)-fluoro(phosphono)methyl]-D-glucitol: D10 (= D14), H20 (≠ Y24), W24 (= W28), L44 (≠ I45), G46 (= G47), V47 (vs. gap), R49 (vs. gap), S113 (= S107)
- binding magnesium ion: D8 (= D12), D10 (= D14), D167 (= D164)
- binding trifluoromagnesate: D8 (= D12), L9 (≠ F13), D10 (= D14), S111 (≠ T105), A112 (≠ S106), K142 (= K139)
5olwA 5-fluorotryptophan labeled beta-phosphoglucomutase in an open conformation (see paper)
30% identity, 94% coverage: 8:210/215 of query aligns to 4:212/224 of 5olwA
- active site: D8 (= D12), L9 (≠ F13), D10 (= D14), T16 (= T20), K45 (= K46), S114 (≠ T105), A115 (≠ S106), K145 (= K139), E169 (= E163), D170 (= D164)
- binding calcium ion: D8 (= D12), D10 (= D14), P89 (≠ S80), V92 (≠ Y83), E124 (= E110), N127 (≠ Q113), E169 (= E163), D170 (= D164), S171 (= S165)
6h91A Phosphorylated beta-phosphoglucomutase from lactococcus lactis in an open conformer to 2.4 a
30% identity, 94% coverage: 8:210/215 of query aligns to 4:212/218 of 6h91A
4c4rA Structure of beta-phosphoglucomutase in complex with a phosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride (see paper)
30% identity, 94% coverage: 8:210/215 of query aligns to 4:212/218 of 4c4rA
- active site: D8 (= D12), L9 (≠ F13), D10 (= D14), T16 (= T20), K45 (= K46), S114 (≠ T105), A115 (≠ S106), K145 (= K139), E169 (= E163), D170 (= D164)
- binding magnesium ion: D8 (= D12), D10 (= D14), D170 (= D164)
- binding trifluoromagnesate: D8 (= D12), L9 (≠ F13), D10 (= D14), S114 (≠ T105), A115 (≠ S106), K145 (= K139)
- binding (1R)-1,5-anhydro-1-(phosphonomethyl)-D-glucitol: D10 (= D14), H20 (≠ Y24), W24 (= W28), L44 (≠ I45), G46 (= G47), V47 (vs. gap), R49 (vs. gap), S52 (vs. gap), S116 (= S107), K117 (≠ N108)
3zi4A The structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and scandium tetrafluoride
30% identity, 94% coverage: 8:210/215 of query aligns to 4:212/218 of 3zi4A
- active site: D8 (= D12), L9 (≠ F13), D10 (= D14), T16 (= T20), K45 (= K46), S114 (≠ T105), A115 (≠ S106), K145 (= K139), E169 (= E163), D170 (= D164)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D14), H20 (≠ Y24), G46 (= G47), V47 (vs. gap), R49 (vs. gap), S116 (= S107), K117 (≠ N108)
- binding magnesium ion: D8 (= D12), D10 (= D14), D170 (= D164)
- binding Scandium Tetrafluoride: D8 (= D12), L9 (≠ F13), D10 (= D14), S114 (≠ T105), A115 (≠ S106), K145 (= K139)
2wf8A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate, glucose-1-phosphate and beryllium trifluoride (see paper)
30% identity, 94% coverage: 8:210/215 of query aligns to 4:212/218 of 2wf8A
- active site: D8 (= D12), L9 (≠ F13), D10 (= D14), T16 (= T20), K45 (= K46), S114 (≠ T105), A115 (≠ S106), K145 (= K139), E169 (= E163), D170 (= D164)
- binding beryllium trifluoride ion: D8 (= D12), L9 (≠ F13), D10 (= D14), S114 (≠ T105), A115 (≠ S106), K145 (= K139)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D14), H20 (≠ Y24), G46 (= G47), V47 (vs. gap), R49 (vs. gap), A115 (≠ S106), S116 (= S107), K117 (≠ N108)
- binding 1-O-phosphono-alpha-D-glucopyranose: D10 (= D14), H20 (≠ Y24), W24 (= W28), L44 (≠ I45), G46 (= G47), V47 (vs. gap), R49 (vs. gap), S52 (vs. gap), A115 (≠ S106), S116 (= S107), K117 (≠ N108)
- binding magnesium ion: D8 (= D12), D10 (= D14), D170 (= D164)
2wf7A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphonate and aluminium tetrafluoride (see paper)
30% identity, 94% coverage: 8:210/215 of query aligns to 4:212/218 of 2wf7A
- active site: D8 (= D12), L9 (≠ F13), D10 (= D14), T16 (= T20), K45 (= K46), S114 (≠ T105), A115 (≠ S106), K145 (= K139), E169 (= E163), D170 (= D164)
- binding tetrafluoroaluminate ion: D8 (= D12), L9 (≠ F13), D10 (= D14), S114 (≠ T105), K145 (= K139)
- binding 6,7-dideoxy-7-phosphono-beta-D-gluco-heptopyranose: D10 (= D14), G46 (= G47), V47 (vs. gap), R49 (vs. gap), S116 (= S107), K117 (≠ N108), N118 (≠ E109)
- binding magnesium ion: D8 (= D12), D10 (= D14), D170 (= D164)
2wf6A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and aluminium tetrafluoride (see paper)
30% identity, 94% coverage: 8:210/215 of query aligns to 4:212/218 of 2wf6A
- active site: D8 (= D12), L9 (≠ F13), D10 (= D14), T16 (= T20), K45 (= K46), S114 (≠ T105), A115 (≠ S106), K145 (= K139), E169 (= E163), D170 (= D164)
- binding tetrafluoroaluminate ion: D8 (= D12), L9 (≠ F13), D10 (= D14), S114 (≠ T105), K145 (= K139)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D14), G46 (= G47), V47 (vs. gap), R49 (vs. gap), S116 (= S107), K117 (≠ N108)
- binding magnesium ion: D8 (= D12), D10 (= D14), D170 (= D164)
2wf5A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and trifluoromagnesate (see paper)
30% identity, 94% coverage: 8:210/215 of query aligns to 4:212/218 of 2wf5A
- active site: D8 (= D12), L9 (≠ F13), D10 (= D14), T16 (= T20), K45 (= K46), S114 (≠ T105), A115 (≠ S106), K145 (= K139), E169 (= E163), D170 (= D164)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D14), H20 (≠ Y24), G46 (= G47), V47 (vs. gap), R49 (vs. gap), A115 (≠ S106), S116 (= S107)
- binding magnesium ion: D8 (= D12), D10 (= D14), D170 (= D164)
- binding trifluoromagnesate: D8 (= D12), L9 (≠ F13), D10 (= D14), S114 (≠ T105), A115 (≠ S106), K145 (= K139)
2wf9A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate, and beryllium trifluoride, crystal form 2 (see paper)
30% identity, 94% coverage: 8:210/215 of query aligns to 4:212/221 of 2wf9A
- active site: D8 (= D12), L9 (≠ F13), D10 (= D14), T16 (= T20), K45 (= K46), S114 (≠ T105), A115 (≠ S106), K145 (= K139), E169 (= E163), D170 (= D164)
- binding beryllium trifluoride ion: D8 (= D12), L9 (≠ F13), D10 (= D14), S114 (≠ T105), A115 (≠ S106), K145 (= K139)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D14), H20 (≠ Y24), G46 (= G47), V47 (vs. gap), R49 (vs. gap), S116 (= S107), K117 (≠ N108), N118 (≠ E109)
- binding 6-O-phosphono-alpha-D-glucopyranose: D10 (= D14), H20 (≠ Y24), G46 (= G47), V47 (vs. gap), R49 (vs. gap), A115 (≠ S106), S116 (= S107), K117 (≠ N108), N118 (≠ E109)
- binding magnesium ion: D8 (= D12), D10 (= D14), D170 (= D164)
1o03A Structure of pentavalent phosphorous intermediate of an enzyme catalyzed phosphoryl transfer reaction observed on cocrystallization with glucose 6-phosphate (see paper)
30% identity, 94% coverage: 8:210/215 of query aligns to 4:212/221 of 1o03A
- active site: D8 (= D12), L9 (≠ F13), D10 (= D14), T16 (= T20), K45 (= K46), S114 (≠ T105), A115 (≠ S106), K145 (= K139), E169 (= E163), D170 (= D164)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: D8 (= D12), L9 (≠ F13), D10 (= D14), H20 (≠ Y24), G46 (= G47), V47 (vs. gap), R49 (vs. gap), S114 (≠ T105), A115 (≠ S106), S116 (= S107), K117 (≠ N108), K145 (= K139)
- binding magnesium ion: D8 (= D12), D10 (= D14), D170 (= D164)
1lvhA The structure of phosphorylated beta-phosphoglucomutase from lactoccocus lactis to 2.3 angstrom resolution (see paper)
30% identity, 94% coverage: 8:210/215 of query aligns to 4:212/221 of 1lvhA
- active site: D8 (= D12), L9 (≠ F13), D10 (= D14), T16 (= T20), K45 (= K46), S114 (≠ T105), A115 (≠ S106), K145 (= K139), E169 (= E163), D170 (= D164)
- binding magnesium ion: D8 (= D12), D10 (= D14), D170 (= D164)
P71447 Beta-phosphoglucomutase; Beta-PGM; EC 5.4.2.6 from Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) (see 3 papers)
30% identity, 94% coverage: 8:210/215 of query aligns to 4:212/221 of P71447
- D8 (= D12) modified: 4-aspartylphosphate; mutation to A: Inactive.; mutation to E: Inactive.
- D10 (= D14) mutation to A: Inactive.; mutation to E: Inactive.; mutation to N: Inactive.; mutation to S: Inactive.
- T16 (= T20) 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 (≠ Y24) 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 (= K46) mutation to A: 20'000-fold decrease in kcat/KM.
- G46 (= G47) 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 (vs. gap) mutation to K: 1'000'000-fold decrease in kcat/KM.
- S52 (vs. gap) mutation to A: Wild-type activity.
- K76 (≠ L72) mutation to A: 100-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP.
- D170 (= D164) mutation to A: Impaired, but active with an increase in the affinity for G1P.
6qzgA Beta-glucose 1,6-bisphosphonate bound to wild type beta- phosphoglucomutse in an open conformation.
30% identity, 94% coverage: 8:210/215 of query aligns to 4:212/219 of 6qzgA
- binding 3,7-anhydro-1,2,8-trideoxy-1,8-diphosphono-D-glycero-D-gulo-octitol: D8 (= D12), L9 (≠ F13), D10 (= D14), H20 (≠ Y24), G46 (= G47), S114 (≠ T105), A115 (≠ S106), S116 (= S107), K117 (≠ N108), K145 (= K139)
- binding magnesium ion: D8 (= D12), D10 (= D14), D170 (= D164)
1z4nA Structure of beta-phosphoglucomutase with inhibitor bound alpha- galactose 1-phosphate cocrystallized with fluoride (see paper)
30% identity, 94% coverage: 8:210/215 of query aligns to 4:212/219 of 1z4nA
- active site: D8 (= D12), L9 (≠ F13), D10 (= D14), T16 (= T20), K45 (= K46), S114 (≠ T105), A115 (≠ S106), K145 (= K139), E169 (= E163), D170 (= D164)
- binding 1-O-phosphono-alpha-D-galactopyranose: H20 (≠ Y24), W24 (= W28), V47 (vs. gap), R49 (vs. gap), S116 (= S107), K117 (≠ N108), N118 (≠ E109)
- binding magnesium ion: D8 (= D12), D10 (= D14), E169 (= E163), D170 (= D164)
Query Sequence
>350225 FitnessBrowser__Btheta:350225
MDTTKTIAALFDFDGVIMDTETQYTVFWDEQGRKYLNEEDFGRRIKGQTLTQIYEKYFSD
LPEAQQEITAGLNIYEKSMSYEYIPGVEAFIADLRKHGAKIAVVTSSNEEKMQNVYNAHP
EFKGMVDRILTGEMFARSKPAPDCFLLGMEIFGATPENSYVFEDSFHGLQAGMTSGATVI
GLATTNTREAITGKAHYIIDDFSEMTFEHLLALHR
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