SitesBLAST
Comparing WP_017557777.1 NCBI__GCF_000341205.1:WP_017557777.1 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)
P18157 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Bacillus subtilis (strain 168) (see paper)
47% identity, 98% coverage: 3:483/492 of query aligns to 5:490/496 of P18157
- H230 (≠ E225) mutation to R: Increased activity.
- F232 (≠ L227) mutation to S: Increased activity.
3ge1A 2.7 angstrom crystal structure of glycerol kinase (glpk) from staphylococcus aureus in complex with adp and glycerol
48% identity, 98% coverage: 3:486/492 of query aligns to 6:494/499 of 3ge1A
Q5HGD2 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Staphylococcus aureus (strain COL)
48% identity, 98% coverage: 3:486/492 of query aligns to 5:493/498 of Q5HGD2
- T12 (= T10) binding ADP
- R16 (≠ T14) binding ADP
- R82 (= R77) binding glycerol
- E83 (= E78) binding glycerol
- Y134 (= Y129) binding glycerol
- D244 (= D239) binding glycerol
- Q245 (= Q240) binding glycerol
- T266 (= T261) binding ADP
- G309 (= G305) binding ADP
- Q313 (= Q309) binding ADP
- G410 (= G406) binding ADP
- N414 (= N410) binding ADP
6udeB Crystal structure of glycerol kinase from elizabethkingia anophelis nuhp1 in complex with adp and glycerol
48% identity, 99% coverage: 3:490/492 of query aligns to 5:494/495 of 6udeB
- binding adenosine-5'-diphosphate: R16 (≠ T14), G262 (= G260), T263 (= T261), G306 (= G305), I309 (≠ V308), S323 (≠ A322), G406 (= G405), G407 (= G406), A408 (= A407)
- binding magnesium ion: G11 (= G9), T12 (= T10), T13 (= T11), S14 (≠ G12)
6k76A Glycerol kinase form thermococcus kodakarensis, complex structure with substrate.
51% identity, 99% coverage: 3:491/492 of query aligns to 1:483/485 of 6k76A
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)
47% identity, 99% coverage: 3:490/492 of query aligns to 5:497/499 of 1bu6Y
P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
47% identity, 99% coverage: 3:490/492 of query aligns to 7:499/502 of P0A6F3
- T14 (= T10) binding ADP; binding sn-glycerol 3-phosphate
- R18 (≠ T14) binding ADP
- S59 (≠ A52) 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 (≠ S59) 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 (= R77) binding glycerol; binding sn-glycerol 3-phosphate
- E85 (= E78) binding glycerol; binding sn-glycerol 3-phosphate
- Y136 (= Y129) binding glycerol; binding sn-glycerol 3-phosphate
- G231 (≠ E224) 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 (≠ F226) modified: N6-malonyllysine
- G235 (= G228) binding beta-D-fructose 1,6-bisphosphate
- R237 (= R230) 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 (= D239) binding glycerol; binding sn-glycerol 3-phosphate
- Q247 (= Q240) binding glycerol
- T268 (= T261) binding ADP
- G305 (= G299) mutation to S: In glpK22; abolishes glucose control of glycerol utilization.
- G311 (= G305) binding ADP
- G412 (= G406) binding ADP
- N416 (= N410) binding ADP
- I475 (vs. gap) 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 (≠ D472) binding Zn(2+)
- R480 (≠ A473) 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
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
47% identity, 99% coverage: 3:490/492 of query aligns to 5:493/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T10), T13 (= T11), G261 (= G260), T262 (= T261), G305 (= G305), I308 (≠ V308), Q309 (= Q309), A321 (= A321), G406 (= G406), N410 (= N410)
- binding glycerol: R82 (= R77), E83 (= E78), Y134 (= Y129), D240 (= D239), Q241 (= Q240), F265 (= F264)
1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
47% identity, 99% coverage: 3:490/492 of query aligns to 5:493/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: T12 (= T10), T13 (= T11), G261 (= G260), T262 (= T261), G305 (= G305), Q309 (= Q309), A321 (= A321), G406 (= G406), A407 (= A407)
- binding glycerol: R82 (= R77), E83 (= E78), W102 (= W97), Y134 (= Y129), D240 (= D239), F265 (= F264)
1bwfO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
47% identity, 99% coverage: 3:490/492 of query aligns to 5:493/494 of 1bwfO