SitesBLAST
Comparing WP_038210079.1 NCBI__GCF_000745855.1:WP_038210079.1 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)
6udeB Crystal structure of glycerol kinase from elizabethkingia anophelis nuhp1 in complex with adp and glycerol
56% identity, 99% coverage: 4:496/497 of query aligns to 5:491/495 of 6udeB
- binding adenosine-5'-diphosphate: R16 (= R15), G262 (= G263), T263 (= T264), G306 (= G307), I309 (≠ V310), S323 (≠ G324), G406 (= G411), G407 (= G412), A408 (= A413)
- binding magnesium ion: G11 (= G10), T12 (= T11), T13 (≠ S12), S14 (= S13)
P18157 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Bacillus subtilis (strain 168) (see paper)
54% identity, 100% coverage: 2:496/497 of query aligns to 3:494/496 of P18157
- H230 (≠ A228) mutation to R: Increased activity.
- F232 (≠ L230) mutation to S: Increased activity.
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
56% identity, 99% coverage: 3:496/497 of query aligns to 4:490/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T11), T13 (≠ S12), G261 (= G263), T262 (= T264), G305 (= G307), I308 (≠ V310), Q309 (= Q311), A321 (≠ S323), G406 (= G412), N410 (= N416)
- 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)
56% identity, 99% coverage: 3:496/497 of query aligns to 4:490/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: T12 (= T11), T13 (≠ S12), G261 (= G263), T262 (= T264), G305 (= G307), Q309 (= Q311), A321 (≠ S323), G406 (= G412), A407 (= A413)
- 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)
56% identity, 99% coverage: 3:496/497 of query aligns to 4:490/494 of 1bwfO
- binding phosphodifluoromethylphosphonic acid-adenylate ester: T12 (= T11), T13 (≠ S12), T262 (= T264), G305 (= G307), I308 (≠ V310), Q309 (= Q311), A321 (≠ S323), G406 (= G412), N410 (= N416)
- 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)
56% identity, 99% coverage: 3:496/497 of query aligns to 6:496/502 of P0A6F3
- T14 (= T11) binding ADP; binding sn-glycerol 3-phosphate
- R18 (= R15) binding ADP
- S59 (≠ A56) 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 (= A63) 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 (≠ A228) 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 (≠ L230) modified: N6-malonyllysine
- G235 (≠ A232) binding beta-D-fructose 1,6-bisphosphate
- R237 (vs. gap) 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 (= G412) binding ADP
- N416 (= N416) binding ADP
- I475 (≠ M475) 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 (≠ Q479) binding Zn(2+)
- R480 (≠ A480) 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.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1glfO Crystal structures of escherichia coli glycerol kinase and the mutant a65t in an inactive tetramer: conformational changes and implications for allosteric regulation (see paper)
56% identity, 99% coverage: 3:496/497 of query aligns to 4:494/498 of 1glfO
- binding adenosine-5'-diphosphate: R16 (= R15), G265 (= G263), T266 (= T264), G309 (= G307), G410 (= G412), A411 (= A413)
- binding glycerol: R82 (= R81), E83 (= E82), Y134 (= Y133), D244 (= D242)
- binding phosphate ion: G232 (= G231), G233 (≠ A232), R235 (vs. gap)
1bo5O Crystal structure of the complex between escherichia coli glycerol kinase and the allosteric regulator fructose 1,6-bisphosphate. (see paper)
56% identity, 99% coverage: 3:496/497 of query aligns to 4:494/498 of 1bo5O
1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
56% identity, 99% coverage: 3:496/497 of query aligns to 2:485/489 of 1gldG
- binding adenosine-5'-diphosphate: R14 (= R15), G256 (= G263), T257 (= T264), G300 (= G307), A316 (≠ S323), G401 (= G412), A402 (= A413), N405 (= N416)
- binding glyceraldehyde-3-phosphate: T10 (= T11), R80 (= R81), E81 (= E82), Y132 (= Y133), D235 (= D242), F260 (= F267)
- binding manganese (ii) ion: D7 (= D8), R14 (= R15)
1glcG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
56% identity, 99% coverage: 3:496/497 of query aligns to 2:485/489 of 1glcG