SitesBLAST
Comparing PP_1075 FitnessBrowser__Putida:PP_1075 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 8 papers)
74% identity, 99% coverage: 6:498/499 of query aligns to 3:501/502 of P0A6F3
- T14 (= T17) binding
- S59 (≠ A62) 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 (= A69) 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.
- Y136 (= Y139) binding
- G231 (= G234) 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 (vs. gap) modified: N6-malonyllysine
- G235 (vs. gap) binding
- R237 (vs. gap) binding ; mutation to A: Drastically reduces inhibition of GK by FBP and lowers, but did not eliminate, the ability of FBP to promote tetramer association.
- G305 (= G302) mutation to S: In glpK22; abolishes glucose control of glycerol utilization.
- I475 (≠ L472) 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.
- R480 (≠ K477) 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)
74% identity, 99% coverage: 6:497/499 of query aligns to 1:498/498 of 1glfO
- binding adenosine-5'-diphosphate: T12 (= T17), R16 (= R21), G265 (= G264), T266 (= T265), G309 (= G308), I312 (≠ V311), Q313 (= Q312), A325 (= A324), Y326 (≠ L325), G409 (= G408), G410 (= G409), A411 (= A410), N414 (= N413)
- binding glycerol: T12 (= T17), Q81 (= Q86), R82 (= R87), E83 (= E88), W102 (= W107), Y134 (= Y139), D244 (= D243), Q245 (= Q244), F269 (= F268)
- binding phosphate ion: G232 (vs. gap), G233 (vs. gap), R235 (vs. gap)
1bo5O Crystal structure of the complex between escherichia coli glycerol kinase and the allosteric regulator fructose 1,6-bisphosphate. (see paper)
74% identity, 99% coverage: 6:497/499 of query aligns to 1:498/498 of 1bo5O
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: G232 (vs. gap), G233 (vs. gap), R235 (vs. gap)
- binding glycerol: Q81 (= Q86), R82 (= R87), E83 (= E88), W102 (= W107), Y134 (= Y139), D244 (= D243), Q245 (= Q244), F269 (= F268)
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
74% identity, 99% coverage: 6:497/499 of query aligns to 1:494/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: G11 (= G16), T12 (= T17), T13 (= T18), G261 (= G264), T262 (= T265), G305 (= G308), I308 (≠ V311), Q309 (= Q312), A321 (= A324), Y322 (≠ L325), S324 (≠ T327), G406 (= G409), A407 (= A410), N410 (= N413)
- binding glycerol: Q81 (= Q86), R82 (= R87), E83 (= E88), W102 (= W107), Y134 (= Y139), D240 (= D243), Q241 (= Q244), F265 (= F268)
1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
74% identity, 99% coverage: 6:497/499 of query aligns to 1:494/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: G11 (= G16), T12 (= T17), T13 (= T18), G261 (= G264), T262 (= T265), G305 (= G308), A306 (≠ S309), I308 (≠ V311), Q309 (= Q312), A321 (= A324), Y322 (≠ L325), S324 (≠ T327), G406 (= G409), A407 (= A410), N410 (= N413)
- binding glycerol: Q81 (= Q86), R82 (= R87), E83 (= E88), W102 (= W107), Y134 (= Y139), D240 (= D243), Q241 (= Q244), F265 (= F268)
1bwfO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
74% identity, 99% coverage: 6:497/499 of query aligns to 1:494/494 of 1bwfO
- binding phosphodifluoromethylphosphonic acid-adenylate ester: G11 (= G16), T12 (= T17), T13 (= T18), G261 (= G264), T262 (= T265), G305 (= G308), I308 (≠ V311), Q309 (= Q312), A321 (= A324), Y322 (≠ L325), S324 (≠ T327), G405 (= G408), G406 (= G409), A407 (= A410), N410 (= N413)
- binding glycerol: Q81 (= Q86), R82 (= R87), E83 (= E88), W102 (= W107), Y134 (= Y139), D240 (= D243), Q241 (= Q244), F265 (= F268)
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)
74% identity, 99% coverage: 6:498/499 of query aligns to 1:499/499 of 1bu6Y
1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
75% identity, 98% coverage: 9:497/499 of query aligns to 2:489/489 of 1gldG
- binding adenosine-5'-diphosphate: G9 (= G16), T11 (= T18), R14 (= R21), Y255 (= Y263), G256 (= G264), T257 (= T265), G300 (= G308), I303 (≠ V311), Q304 (= Q312), A316 (= A324), Y317 (≠ L325), S319 (≠ T327), G400 (= G408), G401 (= G409), A402 (= A410), N405 (= N413)
- binding glyceraldehyde-3-phosphate: G9 (= G16), T10 (= T17), Q79 (= Q86), R80 (= R87), E81 (= E88), W100 (= W107), Y132 (= Y139), D235 (= D243), Q236 (= Q244), T257 (= T265), F260 (= F268)
- binding manganese (ii) ion: D7 (= D14), R14 (= R21), D235 (= D243)
1glcG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
75% identity, 98% coverage: 9:497/499 of query aligns to 2:489/489 of 1glcG