SitesBLAST
Comparing Ga0059261_0833 FitnessBrowser__Korea:Ga0059261_0833 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)
O86033 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
48% identity, 100% coverage: 1:490/491 of query aligns to 1:494/497 of O86033
- R82 (= R81) binding glycerol
- E83 (= E82) binding glycerol
- Y134 (= Y133) binding glycerol
- D243 (= D242) binding glycerol
- Q244 (= Q243) binding glycerol
P18157 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Bacillus subtilis (strain 168) (see paper)
44% identity, 100% coverage: 1:491/491 of query aligns to 1:494/496 of P18157
- H230 (vs. gap) mutation to R: Increased activity.
- F232 (= F230) mutation to S: Increased activity.
3ge1A 2.7 angstrom crystal structure of glycerol kinase (glpk) from staphylococcus aureus in complex with adp and glycerol
46% identity, 99% coverage: 1:487/491 of query aligns to 2:491/499 of 3ge1A
Q5HGD2 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Staphylococcus aureus (strain COL)
46% identity, 99% coverage: 1:487/491 of query aligns to 1:490/498 of Q5HGD2
- T12 (= T12) binding ADP
- R16 (= R16) binding ADP
- R82 (= R81) binding glycerol
- E83 (= E82) binding glycerol
- Y134 (= Y133) binding glycerol
- D244 (= D242) binding glycerol
- Q245 (= Q243) binding glycerol
- T266 (= T264) binding ADP
- G309 (= G307) binding ADP
- Q313 (≠ K311) binding ADP
- G410 (= G407) binding ADP
- N414 (= N411) binding ADP
6udeB Crystal structure of glycerol kinase from elizabethkingia anophelis nuhp1 in complex with adp and glycerol
46% identity, 99% coverage: 2:487/491 of query aligns to 1:487/495 of 6udeB
- binding adenosine-5'-diphosphate: R16 (= R16), G262 (= G263), T263 (= T264), G306 (= G307), I309 (≠ V310), S323 (≠ G324), G406 (= G406), G407 (= G407), A408 (≠ M408)
- binding magnesium ion: G11 (= G11), T12 (= T12), T13 (= T13), S14 (= S14)
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
45% identity, 99% coverage: 5:491/491 of query aligns to 5:490/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T12), T13 (= T13), G261 (= G263), T262 (= T264), G305 (= G307), I308 (≠ V310), Q309 (≠ K311), A321 (= A323), G406 (= G407), N410 (= N411)
- binding glycerol: R82 (= R81), E83 (= E82), Y134 (= Y133), D240 (= D242), Q241 (= Q243), F265 (= F267)
1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
45% identity, 99% coverage: 5:491/491 of query aligns to 5:490/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: T12 (= T12), T13 (= T13), G261 (= G263), T262 (= T264), G305 (= G307), Q309 (≠ K311), A321 (= A323), G406 (= G407), A407 (≠ M408)
- binding glycerol: R82 (= R81), E83 (= E82), W102 (= W101), Y134 (= Y133), D240 (= D242), F265 (= F267)
1bwfO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
45% identity, 99% coverage: 5:491/491 of query aligns to 5:490/494 of 1bwfO
- binding phosphodifluoromethylphosphonic acid-adenylate ester: T12 (= T12), T13 (= T13), T262 (= T264), G305 (= G307), I308 (≠ V310), Q309 (≠ K311), A321 (= A323), G406 (= G407), N410 (= N411)
- binding glycerol: R82 (= R81), E83 (= E82), W102 (= W101), Y134 (= Y133), D240 (= D242), Q241 (= Q243), F265 (= F267)
P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
45% identity, 100% coverage: 1:491/491 of query aligns to 1:496/502 of P0A6F3
- M1 (= M1) modified: Initiator methionine, Removed
- T14 (= T12) binding ADP; binding sn-glycerol 3-phosphate
- R18 (= R16) binding ADP
- S59 (≠ G57) mutation to W: Abolishes inhibition of GK by FBP via disruption of the dimer-tetramer assembly reaction. Inhibition by EIIA-Glc is unchanged compared to wild type. The activity of this mutant is significantly higher than wild-type, and the Michaelis constants are increased slightly compared to wild-type.
- A66 (≠ E64) mutation to T: Although it completely abolishes FBP regulation and disrupts dimer-tetramer equilibrium, the crystal structure is essentially identical to the symmetric tetramer found in the FBP-bound form of the enzyme.
- R84 (= R81) binding glycerol; binding sn-glycerol 3-phosphate
- E85 (= E82) binding glycerol; binding sn-glycerol 3-phosphate
- Y136 (= Y133) binding glycerol; binding sn-glycerol 3-phosphate
- G231 (≠ F230) mutation to D: Displays an increased enzymatic activity and a decreased allosteric regulation by FBP compared to wild-type. It displays a dimer form and is resistant to tetramer formation in the presence of FBP, whereas wild-type dimers are converted into inactive tetramers in the presence of FBP.
- K233 (≠ G232) modified: N6-malonyllysine
- G235 (vs. gap) binding beta-D-fructose 1,6-bisphosphate
- R237 (≠ P233) binding beta-D-fructose 1,6-bisphosphate; mutation to A: Drastically reduces inhibition of GK by FBP and lowers, but did not eliminate, the ability of FBP to promote tetramer association.
- D246 (= D242) binding glycerol; binding sn-glycerol 3-phosphate
- Q247 (= Q243) binding glycerol
- T268 (= T264) binding ADP
- G305 (= G301) mutation to S: In glpK22; abolishes glucose control of glycerol utilization.
- G311 (= G307) binding ADP
- G412 (= G407) binding ADP
- N416 (= N411) binding ADP
- I475 (≠ M470) mutation to D: It decreases Vmax to about 10% of the wild-type value and the affinity for substrate is increased about two- to fourfold. This mutation decreases the catalytic activity in a manner that is analogous to that obtained upon EIIA-Glc binding. It increases the affinity for FBP about fivefold.
- E479 (≠ A474) binding Zn(2+)
- R480 (= R475) mutation to D: It decreases Vmax to about 10% of the wild-type value and the affinity for substrate is increased about two- to fourfold. This mutation decreases the catalytic activity in a manner that is analogous to that obtained upon EIIA-Glc binding. Regulation by FBP is not affected by this substitution. No inhibition by EIIA-Glc is observed, which is consistent with a decrease in affinity for EIIA-Glc of about 250-fold.
1bu6Y Crystal structures of escherichia coli glycerol kinase and the mutant a65t in an inactive tetramer: conformational changes and implications for allosteric regulation (see paper)
45% identity, 99% coverage: 5:491/491 of query aligns to 5:494/499 of 1bu6Y