SitesBLAST
Comparing SMc01502 FitnessBrowser__Smeli:SMc01502 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)
2fdrA Crystal structure of conserved haloacid dehalogenase-like protein of unknown function atu0790 from agrobacterium tumefaciens str. C58
39% identity, 82% coverage: 10:193/224 of query aligns to 4:189/222 of 2fdrA
4eenA Crystal structure of had family hydrolase dr_1622 from deinococcus radiodurans r1 (target efi-501256) with bound magnesium
35% identity, 72% coverage: 11:171/224 of query aligns to 7:170/229 of 4eenA
- active site: D10 (= D14), D12 (= D16), V16 (= V20), S18 (= S22), M44 (≠ E48), Y45 (≠ R49), T47 (≠ L51), S109 (= S111), N110 (≠ S112), K144 (= K145), E168 (= E169), D169 (= D170)
- binding magnesium ion: D10 (= D14), D12 (= D16), D169 (= D170)
Q8VZ10 Protein SUPPRESSOR OF QUENCHING 1, chloroplastic; EC 3.1.3.- from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 93% coverage: 11:218/224 of query aligns to 77:284/1055 of Q8VZ10
- D80 (= D14) 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.
1te2A Putative phosphatase ynic from escherichia coli k12
31% identity, 83% coverage: 12:197/224 of query aligns to 7:195/218 of 1te2A
- active site: D9 (= D14), D11 (= D16), S17 (= S22), D44 (≠ R49), S111 (= S111), A112 (≠ S112), K144 (= K145), E168 (= E169), D169 (= D170)
- binding calcium ion: D9 (= D14), D11 (= D16), D169 (= D170)
- binding 2-phosphoglycolic acid: D9 (= D14), M10 (≠ C15), D11 (= D16), G47 (= G52), S111 (= S111), A112 (≠ S112), K144 (= K145)
P77247 Hexitol phosphatase B; 2-deoxyglucose-6-phosphate phosphatase; Mannitol-1-phosphatase; Sorbitol-6-phosphatase; Sugar-phosphatase; EC 3.1.3.68; EC 3.1.3.22; EC 3.1.3.50; EC 3.1.3.23 from Escherichia coli (strain K12) (see paper)
31% identity, 83% coverage: 12:197/224 of query aligns to 11:199/222 of P77247
- D13 (= D14) binding ; mutation to A: Loss of phosphatase activity.
- D15 (= D16) binding
- D173 (= D170) binding
4ygrA Crystal structure of had phosphatase from thermococcus onnurineus (see paper)
28% identity, 88% coverage: 11:206/224 of query aligns to 4:206/215 of 4ygrA
- active site: D7 (= D14), D9 (= D16), E15 (≠ S22), K38 (≠ A43), T109 (≠ S112), S110 (= S113), G111 (≠ Q114), K141 (= K145), G165 (≠ E169), D166 (= D170), L168 (vs. gap), Q170 (≠ A173), D171 (≠ G174)
- binding magnesium ion: D7 (= D14), D9 (= D16), D166 (= D170)
- binding 2-[n-cyclohexylamino]ethane sulfonic acid: D9 (= D16), L50 (= L55), R53 (≠ M58), W58 (≠ H63), W58 (≠ H63), W61 (≠ H66)
3dv9A Putative beta-phosphoglucomutase from bacteroides vulgatus.
25% identity, 92% coverage: 9:215/224 of query aligns to 24:227/243 of 3dv9A
- active site: D29 (= D14), M30 (≠ C15), D31 (= D16), S37 (= S22), E65 (≠ F50), T131 (= T123), G132 (≠ V124), K162 (= K145), E186 (= E169), N187 (≠ D170)
- binding magnesium ion: D29 (= D14), D31 (= D16), E65 (≠ F50), N187 (≠ D170)
3s6jE The crystal structure of a hydrolase from pseudomonas syringae
30% identity, 75% coverage: 12:179/224 of query aligns to 6:177/220 of 3s6jE
- active site: D8 (= D14), D10 (= D16), S16 (= S22), I44 (≠ L51), T110 (≠ S111), S111 (= S112), K143 (= K145), G167 (≠ E169), D168 (= D170)
- binding calcium ion: D8 (= D14), D10 (= D16), D168 (= D170)
4g9bA Crystal structure of beta-phosphoglucomutase homolog from escherichia coli, target efi-501172, with bound mg, open lid
29% identity, 81% coverage: 11:191/224 of query aligns to 7:194/227 of 4g9bA
- active site: D10 (= D14), L11 (≠ C15), D12 (= D16), T18 (≠ S22), K46 (≠ R49), S117 (vs. gap), V118 (vs. gap), K148 (= K145), E172 (= E169), D173 (= D170)
- binding magnesium ion: D10 (= D14), D12 (= D16), D173 (= D170)
6w04A Crystal structure of had hydrolase, family ia, variant 3 from entamoeba histolytica hm-1:imss
35% identity, 38% coverage: 98:182/224 of query aligns to 96:181/223 of 6w04A
Sites not aligning to the query:
5olwA 5-fluorotryptophan labeled beta-phosphoglucomutase in an open conformation (see paper)
27% identity, 78% coverage: 9:182/224 of query aligns to 3:182/224 of 5olwA
- active site: D8 (= D14), L9 (≠ C15), D10 (= D16), T16 (≠ S22), K45 (≠ L51), S114 (= S111), A115 (≠ S112), K145 (= K145), E169 (= E169), D170 (= D170)
- binding calcium ion: D8 (= D14), D10 (= D16), P89 (= P92), V92 (vs. gap), E124 (≠ S121), N127 (≠ T123), E169 (= E169), D170 (= D170), S171 (= S171)
P71447 Beta-phosphoglucomutase; Beta-PGM; EC 5.4.2.6 from Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis) (see 3 papers)
27% identity, 78% coverage: 9:182/224 of query aligns to 3:182/221 of P71447
- D8 (= D14) modified: 4-aspartylphosphate; mutation to A: Inactive.; mutation to E: Inactive.
- D10 (= D16) mutation to A: Inactive.; mutation to E: Inactive.; mutation to N: Inactive.; mutation to S: Inactive.
- T16 (≠ S22) 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 (≠ S26) 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 (≠ L51) mutation to A: 20'000-fold decrease in kcat/KM.
- G46 (= G52) 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 (≠ L55) mutation to K: 1'000'000-fold decrease in kcat/KM.
- S52 (≠ T57) mutation to A: Wild-type activity.
- K76 (≠ R79) mutation to A: 100-fold reduction in the conversion of beta-G1P to G6P in the presence of beta-G1,6bisP.
- D170 (= D170) mutation to A: Impaired, but active with an increase in the affinity for G1P.
6h91A Phosphorylated beta-phosphoglucomutase from lactococcus lactis in an open conformer to 2.4 a
27% identity, 78% coverage: 9:182/224 of query aligns to 3:182/218 of 6h91A
4c4rA Structure of beta-phosphoglucomutase in complex with a phosphonate analogue of beta-glucose-1-phosphate and magnesium trifluoride (see paper)
27% identity, 78% coverage: 9:182/224 of query aligns to 3:182/218 of 4c4rA
- active site: D8 (= D14), L9 (≠ C15), D10 (= D16), T16 (≠ S22), K45 (≠ L51), S114 (= S111), A115 (≠ S112), K145 (= K145), E169 (= E169), D170 (= D170)
- binding magnesium ion: D8 (= D14), D10 (= D16), D170 (= D170)
- binding trifluoromagnesate: D8 (= D14), L9 (≠ C15), D10 (= D16), S114 (= S111), A115 (≠ S112), K145 (= K145)
- binding (1R)-1,5-anhydro-1-(phosphonomethyl)-D-glucitol: D10 (= D16), H20 (≠ S26), W24 (≠ L30), L44 (≠ F50), G46 (= G52), V47 (≠ R53), R49 (≠ L55), S52 (≠ T57), S116 (= S113), K117 (≠ Q114)
3zi4A The structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and scandium tetrafluoride
27% identity, 78% coverage: 9:182/224 of query aligns to 3:182/218 of 3zi4A
- active site: D8 (= D14), L9 (≠ C15), D10 (= D16), T16 (≠ S22), K45 (≠ L51), S114 (= S111), A115 (≠ S112), K145 (= K145), E169 (= E169), D170 (= D170)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D16), H20 (≠ S26), G46 (= G52), V47 (≠ R53), R49 (≠ L55), S116 (= S113), K117 (≠ Q114)
- binding magnesium ion: D8 (= D14), D10 (= D16), D170 (= D170)
- binding Scandium Tetrafluoride: D8 (= D14), L9 (≠ C15), D10 (= D16), S114 (= S111), A115 (≠ S112), K145 (= K145)
2wf8A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate, glucose-1-phosphate and beryllium trifluoride (see paper)
27% identity, 78% coverage: 9:182/224 of query aligns to 3:182/218 of 2wf8A
- active site: D8 (= D14), L9 (≠ C15), D10 (= D16), T16 (≠ S22), K45 (≠ L51), S114 (= S111), A115 (≠ S112), K145 (= K145), E169 (= E169), D170 (= D170)
- binding beryllium trifluoride ion: D8 (= D14), L9 (≠ C15), D10 (= D16), S114 (= S111), A115 (≠ S112), K145 (= K145)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D16), H20 (≠ S26), G46 (= G52), V47 (≠ R53), R49 (≠ L55), A115 (≠ S112), S116 (= S113), K117 (≠ Q114)
- binding 1-O-phosphono-alpha-D-glucopyranose: D10 (= D16), H20 (≠ S26), W24 (≠ L30), L44 (≠ F50), G46 (= G52), V47 (≠ R53), R49 (≠ L55), S52 (≠ T57), A115 (≠ S112), S116 (= S113), K117 (≠ Q114)
- binding magnesium ion: D8 (= D14), D10 (= D16), D170 (= D170)
2wf7A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphonate and aluminium tetrafluoride (see paper)
27% identity, 78% coverage: 9:182/224 of query aligns to 3:182/218 of 2wf7A
- active site: D8 (= D14), L9 (≠ C15), D10 (= D16), T16 (≠ S22), K45 (≠ L51), S114 (= S111), A115 (≠ S112), K145 (= K145), E169 (= E169), D170 (= D170)
- binding tetrafluoroaluminate ion: D8 (= D14), L9 (≠ C15), D10 (= D16), S114 (= S111), K145 (= K145)
- binding 6,7-dideoxy-7-phosphono-beta-D-gluco-heptopyranose: D10 (= D16), G46 (= G52), V47 (≠ R53), R49 (≠ L55), S116 (= S113), K117 (≠ Q114), N118 (≠ P115)
- binding magnesium ion: D8 (= D14), D10 (= D16), D170 (= D170)
2wf6A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and aluminium tetrafluoride (see paper)
27% identity, 78% coverage: 9:182/224 of query aligns to 3:182/218 of 2wf6A
- active site: D8 (= D14), L9 (≠ C15), D10 (= D16), T16 (≠ S22), K45 (≠ L51), S114 (= S111), A115 (≠ S112), K145 (= K145), E169 (= E169), D170 (= D170)
- binding tetrafluoroaluminate ion: D8 (= D14), L9 (≠ C15), D10 (= D16), S114 (= S111), K145 (= K145)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D16), G46 (= G52), V47 (≠ R53), R49 (≠ L55), S116 (= S113), K117 (≠ Q114)
- binding magnesium ion: D8 (= D14), D10 (= D16), D170 (= D170)
2wf5A Structure of beta-phosphoglucomutase inhibited with glucose-6- phosphate and trifluoromagnesate (see paper)
27% identity, 78% coverage: 9:182/224 of query aligns to 3:182/218 of 2wf5A
- active site: D8 (= D14), L9 (≠ C15), D10 (= D16), T16 (≠ S22), K45 (≠ L51), S114 (= S111), A115 (≠ S112), K145 (= K145), E169 (= E169), D170 (= D170)
- binding 6-O-phosphono-beta-D-glucopyranose: D10 (= D16), H20 (≠ S26), G46 (= G52), V47 (≠ R53), R49 (≠ L55), A115 (≠ S112), S116 (= S113)
- binding magnesium ion: D8 (= D14), D10 (= D16), D170 (= D170)
- binding trifluoromagnesate: D8 (= D14), L9 (≠ C15), D10 (= D16), S114 (= S111), A115 (≠ S112), K145 (= K145)
6qzgA Beta-glucose 1,6-bisphosphonate bound to wild type beta- phosphoglucomutse in an open conformation.
27% identity, 78% coverage: 9:182/224 of query aligns to 3:182/219 of 6qzgA
- binding 3,7-anhydro-1,2,8-trideoxy-1,8-diphosphono-D-glycero-D-gulo-octitol: D8 (= D14), L9 (≠ C15), D10 (= D16), H20 (≠ S26), G46 (= G52), S114 (= S111), A115 (≠ S112), S116 (= S113), K117 (≠ Q114), K145 (= K145)
- binding magnesium ion: D8 (= D14), D10 (= D16), D170 (= D170)
Query Sequence
>SMc01502 FitnessBrowser__Smeli:SMc01502
MTMVGHASRLVIFDCDGVLVDSEPISLGVLVDALAAAGVSMTAEEASERFLGRSLKTMST
ILHEEHGLATDEVFLEGMRTRLYARFREELRPIARIREAVEGLGTAHCVASSSQPERIRL
SLTVTGLIDLFEPNIFSASMVARGKPAPDLFLHASAEMGYHPSDCIVIEDSPAGIEAAKS
AGMRVFAFAGGSHARNDRHRRTLASLEPDVLFDDMGELIQFVRQ
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