SitesBLAST
Comparing WP_068330536.1 NCBI__GCF_001650345.1:WP_068330536.1 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)
P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
79% identity, 98% coverage: 3:498/506 of query aligns to 2:497/502 of P0A6F3
- T14 (= T15) binding ADP; binding sn-glycerol 3-phosphate
- R18 (= R19) binding ADP
- S59 (= S60) 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 (= A67) 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 (= R85) binding glycerol; binding sn-glycerol 3-phosphate
- E85 (= E86) binding glycerol; binding sn-glycerol 3-phosphate
- Y136 (= Y137) binding glycerol; binding sn-glycerol 3-phosphate
- G231 (= G232) 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 (= K234) modified: N6-malonyllysine
- G235 (= G236) binding beta-D-fructose 1,6-bisphosphate
- R237 (= R238) 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 (= D247) binding glycerol; binding sn-glycerol 3-phosphate
- Q247 (= Q248) binding glycerol
- T268 (= T269) binding ADP
- G305 (= G306) mutation to S: In glpK22; abolishes glucose control of glycerol utilization.
- G311 (= G312) binding ADP
- G412 (= G413) binding ADP
- N416 (= N417) binding ADP
- I475 (≠ A476) 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 (≠ K480) binding Zn(2+)
- R480 (= R481) 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)
79% identity, 98% coverage: 4:498/506 of query aligns to 1:495/498 of 1glfO
- binding adenosine-5'-diphosphate: R16 (= R19), G265 (= G268), T266 (= T269), G309 (= G312), G410 (= G413), A411 (= A414)
- binding glycerol: R82 (= R85), E83 (= E86), Y134 (= Y137), D244 (= D247)
- binding phosphate ion: G232 (= G235), G233 (= G236), R235 (= R238)
1bo5O Crystal structure of the complex between escherichia coli glycerol kinase and the allosteric regulator fructose 1,6-bisphosphate. (see paper)
79% identity, 98% coverage: 4:498/506 of query aligns to 1:495/498 of 1bo5O
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)
79% identity, 98% coverage: 4:498/506 of query aligns to 1:495/499 of 1bu6Y
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
78% identity, 98% coverage: 4:498/506 of query aligns to 1:491/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T15), T13 (= T16), G261 (= G268), T262 (= T269), G305 (= G312), I308 (= I315), Q309 (= Q316), A321 (= A328), G406 (= G413), N410 (= N417)
- binding glycerol: R82 (= R85), E83 (= E86), Y134 (= Y137), D240 (= D247), Q241 (= Q248), F265 (= F272)
1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
78% identity, 98% coverage: 4:498/506 of query aligns to 1:491/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: T12 (= T15), T13 (= T16), G261 (= G268), T262 (= T269), G305 (= G312), Q309 (= Q316), A321 (= A328), G406 (= G413), A407 (= A414)
- binding glycerol: R82 (= R85), E83 (= E86), W102 (= W105), Y134 (= Y137), D240 (= D247), F265 (= F272)
1bwfO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
78% identity, 98% coverage: 4:498/506 of query aligns to 1:491/494 of 1bwfO
- binding phosphodifluoromethylphosphonic acid-adenylate ester: T12 (= T15), T13 (= T16), T262 (= T269), G305 (= G312), I308 (= I315), Q309 (= Q316), A321 (= A328), G406 (= G413), N410 (= N417)
- binding glycerol: R82 (= R85), E83 (= E86), W102 (= W105), Y134 (= Y137), D240 (= D247), Q241 (= Q248), F265 (= F272)
1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
77% identity, 97% coverage: 6:498/506 of query aligns to 1:486/489 of 1gldG
- binding adenosine-5'-diphosphate: R14 (= R19), G256 (= G268), T257 (= T269), G300 (= G312), A316 (= A328), G401 (= G413), A402 (= A414), N405 (= N417)
- binding glyceraldehyde-3-phosphate: T10 (= T15), R80 (= R85), E81 (= E86), Y132 (= Y137), D235 (= D247), F260 (= F272)
- binding manganese (ii) ion: D7 (= D12), R14 (= R19)
1glcG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
77% identity, 97% coverage: 6:498/506 of query aligns to 1:486/489 of 1glcG
- binding adenosine-5'-diphosphate: G256 (= G268), T257 (= T269), G300 (= G312), A316 (= A328), G401 (= G413), A402 (= A414), N405 (= N417)
- binding glyceraldehyde-3-phosphate: T10 (= T15), R80 (= R85), E81 (= E86), W100 (= W105), Y132 (= Y137), D235 (= D247), F260 (= F272)
1glbG Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase (see paper)
77% identity, 97% coverage: 6:498/506 of query aligns to 1:486/489 of 1glbG