SitesBLAST
Comparing WP_009141774.1 NCBI__GCF_000225705.1:WP_009141774.1 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)
1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
56% identity, 95% coverage: 21:509/514 of query aligns to 1:483/489 of 1gldG
- binding adenosine-5'-diphosphate: R14 (= R34), G256 (= G282), T257 (= T283), G300 (= G326), A316 (= A342), G401 (≠ A427), A402 (= A428), N405 (= N431)
- binding glyceraldehyde-3-phosphate: T10 (= T30), R80 (= R100), E81 (= E101), Y132 (= Y152), D235 (= D261), F260 (= F286)
- binding manganese (ii) ion: D7 (= D27), R14 (= R34)
1glcG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
56% identity, 95% coverage: 21:509/514 of query aligns to 1:483/489 of 1glcG
- binding adenosine-5'-diphosphate: G256 (= G282), T257 (= T283), G300 (= G326), A316 (= A342), G401 (≠ A427), A402 (= A428), N405 (= N431)
- binding glyceraldehyde-3-phosphate: T10 (= T30), R80 (= R100), E81 (= E101), W100 (= W120), Y132 (= Y152), D235 (= D261), F260 (= F286)
1glbG Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase (see paper)
56% identity, 95% coverage: 21:509/514 of query aligns to 1:483/489 of 1glbG
- binding adenosine-5'-diphosphate: R14 (= R34), G256 (= G282), T257 (= T283), G300 (= G326), I303 (= I329), A316 (= A342), G401 (≠ A427), A402 (= A428), N405 (= N431)
- binding glycerol: R80 (= R100), E81 (= E101), W100 (= W120), Y132 (= Y152), D235 (= D261), F260 (= F286)
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
56% identity, 95% coverage: 21:509/514 of query aligns to 3:488/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T30), T13 (= T31), G261 (= G282), T262 (= T283), G305 (= G326), I308 (= I329), Q309 (= Q330), A321 (= A342), G406 (≠ A427), N410 (= N431)
- binding glycerol: R82 (= R100), E83 (= E101), Y134 (= Y152), D240 (= D261), Q241 (= Q262), F265 (= F286)
1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
56% identity, 95% coverage: 21:509/514 of query aligns to 3:488/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: T12 (= T30), T13 (= T31), G261 (= G282), T262 (= T283), G305 (= G326), Q309 (= Q330), A321 (= A342), G406 (≠ A427), A407 (= A428)
- binding glycerol: R82 (= R100), E83 (= E101), W102 (= W120), Y134 (= Y152), D240 (= D261), F265 (= F286)
1bwfO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
56% identity, 95% coverage: 21:509/514 of query aligns to 3:488/494 of 1bwfO
- binding phosphodifluoromethylphosphonic acid-adenylate ester: T12 (= T30), T13 (= T31), T262 (= T283), G305 (= G326), I308 (= I329), Q309 (= Q330), A321 (= A342), G406 (≠ A427), N410 (= N431)
- binding glycerol: R82 (= R100), E83 (= E101), W102 (= W120), Y134 (= Y152), D240 (= D261), Q241 (= Q262), F265 (= F286)
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)
56% identity, 95% coverage: 21:509/514 of query aligns to 3:492/499 of 1bu6Y
P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
56% identity, 95% coverage: 21:509/514 of query aligns to 5:494/502 of P0A6F3
- T14 (= T30) binding ADP; binding sn-glycerol 3-phosphate
- R18 (= R34) binding ADP
- S59 (≠ A75) 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 (≠ F82) 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 (= R100) binding glycerol; binding sn-glycerol 3-phosphate
- E85 (= E101) binding glycerol; binding sn-glycerol 3-phosphate
- Y136 (= Y152) binding glycerol; binding sn-glycerol 3-phosphate
- G231 (≠ E247) 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 (≠ M249) modified: N6-malonyllysine
- G235 (≠ H251) binding beta-D-fructose 1,6-bisphosphate
- R237 (≠ P253) 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 (= D261) binding glycerol; binding sn-glycerol 3-phosphate
- Q247 (= Q262) binding glycerol
- T268 (= T283) binding ADP
- G305 (= G320) mutation to S: In glpK22; abolishes glucose control of glycerol utilization.
- G311 (= G326) binding ADP
- G412 (≠ A427) binding ADP
- N416 (= N431) binding ADP
- I475 (≠ G490) 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 (= E494) binding Zn(2+)
- R480 (≠ L495) 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, 95% coverage: 21:509/514 of query aligns to 3:492/498 of 1glfO
- binding adenosine-5'-diphosphate: R16 (= R34), G265 (= G282), T266 (= T283), G309 (= G326), G410 (≠ A427), A411 (= A428)
- binding glycerol: R82 (= R100), E83 (= E101), Y134 (= Y152), D244 (= D261)
- binding phosphate ion: G232 (≠ T250), G233 (≠ H251), R235 (≠ P253)
1bo5O Crystal structure of the complex between escherichia coli glycerol kinase and the allosteric regulator fructose 1,6-bisphosphate. (see paper)
56% identity, 95% coverage: 21:509/514 of query aligns to 3:492/498 of 1bo5O