SitesBLAST
Comparing WP_064574984.1 NCBI__GCF_001655005.1:WP_064574984.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
Q8VZ10 Protein SUPPRESSOR OF QUENCHING 1, chloroplastic; EC 3.1.3.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
32% identity, 98% coverage: 2:186/188 of query aligns to 71:261/1055 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.
4g9bA Crystal structure of beta-phosphoglucomutase homolog from escherichia coli, target efi-501172, with bound mg, open lid
28% identity, 97% coverage: 4:185/188 of query aligns to 3:191/227 of 4g9bA
- active site: D10 (= D11), L11 (≠ M12), D12 (= D13), T18 (= T19), K46 (≠ N47), S117 (= S111), V118 (≠ E112), K148 (= K142), E172 (= E166), D173 (= D167)
- binding magnesium ion: D10 (= D11), D12 (= D13), D173 (= D167)
6w04A Crystal structure of had hydrolase, family ia, variant 3 from entamoeba histolytica hm-1:imss
27% identity, 92% coverage: 6:178/188 of query aligns to 2:180/223 of 6w04A
- active site: D7 (= D11), F8 (≠ M12), N9 (≠ D13), D15 (≠ T19), N44 (= N47), T109 (= T109), S110 (≠ G110), K144 (= K142), E168 (= E166), D169 (= D167)
- binding magnesium ion: D7 (= D11), N9 (≠ D13), D169 (= D167)
4c4sA Structure of beta-phosphoglucomutase in complex with an alpha- fluorophosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride (see paper)
29% identity, 90% coverage: 5:174/188 of query aligns to 2:174/215 of 4c4sA
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (= T19), K45 (≠ N47), S111 (= S111), A112 (≠ E112), K142 (= K142), E166 (= E166), D167 (= D167)
- binding (1R)-1,5-anhydro-1-[(S)-fluoro(phosphono)methyl]-D-glucitol: D10 (= D13), H20 (= H23), W24 (= W27), L44 (= L46), G46 (= G48), V47 (≠ S49), R49 (≠ T51), S113 (≠ H113)
- binding magnesium ion: D8 (= D11), D10 (= D13), D167 (= D167)
- binding trifluoromagnesate: D8 (= D11), L9 (≠ M12), D10 (= D13), S111 (= S111), A112 (≠ E112), K142 (= K142)
7ocrB NADPH and fructose-6-phosphate bound to the dehydrogenase domain of the bifunctional mannitol-1-phosphate dehydrogenase/phosphatase mtld from acinetobacter baumannii (see paper)
27% identity, 91% coverage: 7:178/188 of query aligns to 11:180/675 of 7ocrB
Sites not aligning to the query:
- binding fructose -6-phosphate: 362, 403, 508, 513, 516, 587, 590, 594, 595, 601
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: 244, 246, 247, 248, 273, 274, 329, 330, 333, 361, 362, 406, 587, 590
7ocqB Nadh bound to the dehydrogenase domain of the bifunctional mannitol-1- phosphate dehydrogenase/phosphatase mtld from acinetobacter baumannii (see paper)
27% identity, 91% coverage: 7:178/188 of query aligns to 11:181/679 of 7ocqB
Sites not aligning to the query:
- binding 1,4-dihydronicotinamide adenine dinucleotide: 245, 246, 247, 248, 249, 274, 275, 329, 330, 334, 363, 403, 405, 407, 591, 594
2wf9A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate, and beryllium trifluoride, crystal form 2 (see paper)
28% identity, 90% coverage: 5:174/188 of query aligns to 2:177/221 of 2wf9A
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (= T19), K45 (≠ N47), S114 (= S111), A115 (≠ E112), K145 (= K142), E169 (= E166), D170 (= D167)
- binding beryllium trifluoride ion: D8 (= D11), L9 (≠ M12), D10 (= D13), S114 (= S111), A115 (≠ E112), K145 (= K142)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D13), H20 (= H23), G46 (= G48), V47 (≠ S49), R49 (≠ T51), S116 (≠ H113), K117 (≠ R114), N118 (≠ M115)
- binding 6-O-phosphono-alpha-D-glucopyranose: D10 (= D13), H20 (= H23), G46 (= G48), V47 (≠ S49), R49 (≠ T51), A115 (≠ E112), S116 (≠ H113), K117 (≠ R114), N118 (≠ M115)
- binding magnesium ion: D8 (= D11), D10 (= D13), D170 (= D167)
1o03A Structure of pentavalent phosphorous intermediate of an enzyme catalyzed phosphoryl transfer reaction observed on cocrystallization with glucose 6-phosphate (see paper)
28% identity, 90% coverage: 5:174/188 of query aligns to 2:177/221 of 1o03A
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (= T19), K45 (≠ N47), S114 (= S111), A115 (≠ E112), K145 (= K142), E169 (= E166), D170 (= D167)
- binding 1,6-di-O-phosphono-alpha-D-glucopyranose: D8 (= D11), L9 (≠ M12), D10 (= D13), H20 (= H23), G46 (= G48), V47 (≠ S49), R49 (≠ T51), S114 (= S111), A115 (≠ E112), S116 (≠ H113), K117 (≠ R114), K145 (= K142)
- binding magnesium ion: D8 (= D11), D10 (= D13), D170 (= D167)
1lvhA The structure of phosphorylated beta-phosphoglucomutase from lactoccocus lactis to 2.3 angstrom resolution (see paper)
28% identity, 90% coverage: 5:174/188 of query aligns to 2:177/221 of 1lvhA
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (= T19), K45 (≠ N47), S114 (= S111), A115 (≠ E112), K145 (= K142), E169 (= E166), D170 (= D167)
- binding magnesium ion: D8 (= D11), D10 (= D13), D170 (= D167)
6qzgA Beta-glucose 1,6-bisphosphonate bound to wild type beta- phosphoglucomutse in an open conformation.
28% identity, 90% coverage: 5:174/188 of query aligns to 2:177/219 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 (= S111), A115 (≠ E112), S116 (≠ H113), K117 (≠ R114), K145 (= K142)
- binding magnesium ion: D8 (= D11), D10 (= D13), D170 (= D167)
1z4nA Structure of beta-phosphoglucomutase with inhibitor bound alpha- galactose 1-phosphate cocrystallized with fluoride (see paper)
28% identity, 90% coverage: 5:174/188 of query aligns to 2:177/219 of 1z4nA
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (= T19), K45 (≠ N47), S114 (= S111), A115 (≠ E112), K145 (= K142), E169 (= E166), D170 (= D167)
- binding 1-O-phosphono-alpha-D-galactopyranose: H20 (= H23), W24 (= W27), V47 (≠ S49), R49 (≠ T51), S116 (≠ H113), K117 (≠ R114), N118 (≠ M115)
- binding magnesium ion: D8 (= D11), D10 (= D13), E169 (= E166), D170 (= D167)
5olwA 5-fluorotryptophan labeled beta-phosphoglucomutase in an open conformation (see paper)
28% identity, 90% coverage: 5:174/188 of query aligns to 2:177/224 of 5olwA
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (= T19), K45 (≠ N47), S114 (= S111), A115 (≠ E112), K145 (= K142), E169 (= E166), D170 (= D167)
- binding calcium ion: D8 (= D11), D10 (= D13), P89 (= P89), V92 (vs. gap), E124 (≠ R121), N127 (≠ G124), E169 (= E166), D170 (= D167), S171 (≠ A168)
6h91A Phosphorylated beta-phosphoglucomutase from lactococcus lactis in an open conformer to 2.4 a
28% identity, 90% coverage: 5:174/188 of query aligns to 2:177/218 of 6h91A
4c4rA Structure of beta-phosphoglucomutase in complex with a phosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride (see paper)
28% identity, 90% coverage: 5:174/188 of query aligns to 2:177/218 of 4c4rA
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (= T19), K45 (≠ N47), S114 (= S111), A115 (≠ E112), K145 (= K142), E169 (= E166), D170 (= D167)
- binding magnesium ion: D8 (= D11), D10 (= D13), D170 (= D167)
- binding trifluoromagnesate: D8 (= D11), L9 (≠ M12), D10 (= D13), S114 (= S111), A115 (≠ E112), K145 (= K142)
- binding (1R)-1,5-anhydro-1-(phosphonomethyl)-D-glucitol: D10 (= D13), H20 (= H23), W24 (= W27), L44 (= L46), G46 (= G48), V47 (≠ S49), R49 (≠ T51), S52 (≠ I54), S116 (≠ H113), K117 (≠ R114)
3zi4A The structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and scandium tetrafluoride
28% identity, 90% coverage: 5:174/188 of query aligns to 2:177/218 of 3zi4A
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (= T19), K45 (≠ N47), S114 (= S111), A115 (≠ E112), K145 (= K142), E169 (= E166), D170 (= D167)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D13), H20 (= H23), G46 (= G48), V47 (≠ S49), R49 (≠ T51), S116 (≠ H113), K117 (≠ R114)
- binding magnesium ion: D8 (= D11), D10 (= D13), D170 (= D167)
- binding Scandium Tetrafluoride: D8 (= D11), L9 (≠ M12), D10 (= D13), S114 (= S111), A115 (≠ E112), K145 (= K142)
2wf8A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate, glucose-1-phosphate and beryllium trifluoride (see paper)
28% identity, 90% coverage: 5:174/188 of query aligns to 2:177/218 of 2wf8A
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (= T19), K45 (≠ N47), S114 (= S111), A115 (≠ E112), K145 (= K142), E169 (= E166), D170 (= D167)
- binding beryllium trifluoride ion: D8 (= D11), L9 (≠ M12), D10 (= D13), S114 (= S111), A115 (≠ E112), K145 (= K142)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D13), H20 (= H23), G46 (= G48), V47 (≠ S49), R49 (≠ T51), A115 (≠ E112), S116 (≠ H113), K117 (≠ R114)
- binding 1-O-phosphono-alpha-D-glucopyranose: D10 (= D13), H20 (= H23), W24 (= W27), L44 (= L46), G46 (= G48), V47 (≠ S49), R49 (≠ T51), S52 (≠ I54), A115 (≠ E112), S116 (≠ H113), K117 (≠ R114)
- binding magnesium ion: D8 (= D11), D10 (= D13), D170 (= D167)
2wf7A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphonate and aluminium tetrafluoride (see paper)
28% identity, 90% coverage: 5:174/188 of query aligns to 2:177/218 of 2wf7A
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (= T19), K45 (≠ N47), S114 (= S111), A115 (≠ E112), K145 (= K142), E169 (= E166), D170 (= D167)
- binding tetrafluoroaluminate ion: D8 (= D11), L9 (≠ M12), D10 (= D13), S114 (= S111), K145 (= K142)
- binding 6,7-dideoxy-7-phosphono-beta-D-gluco-heptopyranose: D10 (= D13), G46 (= G48), V47 (≠ S49), R49 (≠ T51), S116 (≠ H113), K117 (≠ R114), N118 (≠ M115)
- binding magnesium ion: D8 (= D11), D10 (= D13), D170 (= D167)
2wf6A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and aluminium tetrafluoride (see paper)
28% identity, 90% coverage: 5:174/188 of query aligns to 2:177/218 of 2wf6A
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (= T19), K45 (≠ N47), S114 (= S111), A115 (≠ E112), K145 (= K142), E169 (= E166), D170 (= D167)
- binding tetrafluoroaluminate ion: D8 (= D11), L9 (≠ M12), D10 (= D13), S114 (= S111), K145 (= K142)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D13), G46 (= G48), V47 (≠ S49), R49 (≠ T51), S116 (≠ H113), K117 (≠ R114)
- binding magnesium ion: D8 (= D11), D10 (= D13), D170 (= D167)
2wf5A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and trifluoromagnesate (see paper)
28% identity, 90% coverage: 5:174/188 of query aligns to 2:177/218 of 2wf5A
- active site: D8 (= D11), L9 (≠ M12), D10 (= D13), T16 (= T19), K45 (≠ N47), S114 (= S111), A115 (≠ E112), K145 (= K142), E169 (= E166), D170 (= D167)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D13), H20 (= H23), G46 (= G48), V47 (≠ S49), R49 (≠ T51), A115 (≠ E112), S116 (≠ H113)
- binding magnesium ion: D8 (= D11), D10 (= D13), D170 (= D167)
- binding trifluoromagnesate: D8 (= D11), L9 (≠ M12), D10 (= D13), S114 (= S111), A115 (≠ E112), K145 (= K142)
P71447 Beta-phosphoglucomutase; Beta-PGM; EC 5.4.2.6 from Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) (see 7 papers)
28% identity, 90% coverage: 5:174/188 of query aligns to 2:177/221 of P71447
- D8 (= D11) binding Mg(2+); modified: 4-aspartylphosphate; mutation D->A,E: Inactive.
- D10 (= D13) binding beta-D-glucose 6-phosphate; binding Mg(2+); mutation D->A,E,N,S: Inactive.
- T16 (= T19) 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 (≠ N47) mutation to A: 20'000-fold decrease in catalytic efficiency.
- G46 (= G48) binding beta-D-glucose 6-phosphate; mutation to A: 1'000'000-fold decrease in catalytic efficiency.; mutation to P: 100'000-fold decrease in catalytic efficiency.; mutation to V: 10'000-fold decrease in catalytic efficiency.
- V47 (≠ S49) binding beta-D-glucose 6-phosphate
- R49 (≠ T51) binding beta-D-glucose 6-phosphate; mutation to K: 1'000'000-fold decrease in catalytic efficiency.
- S52 (≠ I54) mutation to A: Wild-type activity.
- K76 (= K75) mutation to A: 100-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP.
- S116 (≠ H113) binding beta-D-glucose 6-phosphate
- K117 (≠ R114) binding beta-D-glucose 6-phosphate
- N118 (≠ M115) binding beta-D-glucose 6-phosphate
- D170 (= D167) binding Mg(2+); mutation to A: Impaired, but active with an increase in the affinity for G1P.
Query Sequence
>WP_064574984.1 NCBI__GCF_001655005.1:WP_064574984.1
MYDRFQGLIFDMDGTLLDTEPTHRRAWRQVLGQYGMTYDENAMVALNGSPTWRIAQIIIE
NNQADMDPHHLAALKTAAVESMLLDSVKPLPLIDVVLAYKGKKPMAVGTGSEHRMADALL
RHLGLHNCFQAIVGADDVTRHKPEPDTFLRCAELIGVSPKDCVVFEDADFGIQAAQRANM
AWVDVRKL
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