SitesBLAST
Comparing 3607827 Dshi_1235 xylulokinase (RefSeq) 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)
P09099 Xylulose kinase; XK; Xylulokinase; 1-deoxy-D-xylulokinase; EC 2.7.1.17; EC 2.7.1.- from Escherichia coli (strain K12) (see paper)
42% identity, 99% coverage: 1:473/480 of query aligns to 1:479/484 of P09099
- D6 (= D6) mutation to A: Loss of activity.
- MH 77:78 (= MH 76:77) binding
- D233 (= D232) mutation to A: Loss of activity.
2itmA Crystal structure of the e. Coli xylulose kinase complexed with xylulose (see paper)
41% identity, 99% coverage: 1:473/480 of query aligns to 1:471/476 of 2itmA
3ll3B The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
29% identity, 99% coverage: 3:478/480 of query aligns to 5:483/490 of 3ll3B
- binding adenosine-5'-diphosphate: G258 (= G253), T259 (= T254), G298 (≠ A294), P314 (≠ V308), G399 (= G392), F400 (≠ G393), K402 (≠ R395)
- binding 1-deoxy-d-xylulose-5-phosphate: H127 (≠ M122), N295 (≠ L291), G338 (≠ T331), E340 (= E333), A347 (≠ P340)
3ll3A The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
28% identity, 99% coverage: 3:478/480 of query aligns to 6:485/492 of 3ll3A
- binding adenosine-5'-triphosphate: G259 (= G253), T260 (= T254), G299 (≠ A294), P316 (≠ V308), L320 (= L312), G400 (= G391), G401 (= G392), F402 (≠ G393)
- binding 1-deoxy-d-xylulose-5-phosphate: H128 (≠ M122), N296 (≠ L291), E342 (= E333), A349 (≠ P340)
- binding d-xylulose: Q78 (= Q75), M79 (= M76), H80 (= H77), D238 (= D232), R343 (= R334)
3i8bA The crystal structure of xylulose kinase from bifidobacterium adolescentis
29% identity, 90% coverage: 1:430/480 of query aligns to 5:469/506 of 3i8bA
3kzbA Crystal structure of xylulokinase from chromobacterium violaceum
31% identity, 94% coverage: 5:456/480 of query aligns to 9:477/498 of 3kzbA
O86033 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
26% identity, 91% coverage: 2:437/480 of query aligns to 5:455/497 of O86033
- R82 (≠ M76) binding
- E83 (≠ H77) binding
- Y134 (≠ G124) binding
- D243 (= D232) binding
- Q244 (≠ A233) binding
6k76A Glycerol kinase form thermococcus kodakarensis, complex structure with substrate.
25% identity, 96% coverage: 3:465/480 of query aligns to 2:468/485 of 6k76A
6udeB Crystal structure of glycerol kinase from elizabethkingia anophelis nuhp1 in complex with adp and glycerol
25% identity, 90% coverage: 1:434/480 of query aligns to 4:448/495 of 6udeB
- binding adenosine-5'-diphosphate: R16 (≠ K13), G262 (= G253), T263 (= T254), G306 (≠ A294), I309 (≠ M297), S323 (≠ P309), G406 (= G391), G407 (= G392), A408 (≠ G393)
- binding magnesium ion: G11 (= G8), T12 (= T9), T13 (≠ S10), S14 (≠ A11)
Q5HGD2 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Staphylococcus aureus (strain COL)
24% identity, 97% coverage: 3:467/480 of query aligns to 6:483/498 of Q5HGD2
- T12 (= T9) binding
- R16 (≠ K13) binding
- R82 (≠ M76) binding
- E83 (≠ H77) binding
- Y134 (≠ G124) binding
- D244 (= D232) binding
- Q245 (≠ A233) binding
- T266 (= T254) binding
- G309 (≠ A294) binding
- Q313 (≠ A298) binding
- G410 (= G392) binding
- N414 (≠ S396) binding
3ge1A 2.7 angstrom crystal structure of glycerol kinase (glpk) from staphylococcus aureus in complex with adp and glycerol
24% identity, 97% coverage: 3:467/480 of query aligns to 7:484/499 of 3ge1A
P18157 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Bacillus subtilis (strain 168) (see paper)
23% identity, 96% coverage: 3:465/480 of query aligns to 6:483/496 of P18157
- H230 (≠ K221) mutation to R: Increased activity.
- F232 (vs. gap) mutation to S: Increased activity.
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)
24% identity, 97% coverage: 2:466/480 of query aligns to 5:482/498 of 1glfO
- binding adenosine-5'-diphosphate: R16 (≠ K13), G265 (= G253), T266 (= T254), G309 (≠ A294), G410 (= G392), A411 (≠ G393)
- binding glycerol: R82 (≠ M76), E83 (≠ H77), Y134 (≠ G124), D244 (= D232)
- binding phosphate ion: G232 (≠ P222), G233 (= G223), R235 (vs. gap)
1bo5O Crystal structure of the complex between escherichia coli glycerol kinase and the allosteric regulator fructose 1,6-bisphosphate. (see paper)
24% identity, 97% coverage: 2:466/480 of query aligns to 5:482/498 of 1bo5O
P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
24% identity, 97% coverage: 2:466/480 of query aligns to 7:484/502 of P0A6F3
- T14 (= T9) binding ; binding
- R18 (≠ K13) binding
- S59 (≠ A53) 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 (= A60) 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 (≠ M76) binding ; binding
- E85 (≠ H77) binding ; binding
- Y136 (≠ G124) binding ; binding
- G231 (= G219) 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 (= K221) modified: N6-malonyllysine
- G235 (= G223) 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.
- D246 (= D232) binding ; binding
- Q247 (≠ A233) binding
- T268 (= T254) binding
- G305 (vs. gap) mutation to S: In glpK22; abolishes glucose control of glycerol utilization.
- G311 (≠ A294) binding
- G412 (= G392) binding
- N416 (≠ S396) binding
- I475 (≠ A457) 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 (≠ A461) binding
- R480 (= R462) 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
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)
24% identity, 97% coverage: 2:466/480 of query aligns to 5:482/499 of 1bu6Y
1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
24% identity, 97% coverage: 2:466/480 of query aligns to 3:473/489 of 1gldG
- binding adenosine-5'-diphosphate: R14 (≠ K13), G256 (= G253), T257 (= T254), G300 (≠ A294), A316 (≠ V308), G401 (= G392), A402 (≠ G393), N405 (≠ S396)
- binding glyceraldehyde-3-phosphate: T10 (= T9), R80 (≠ M76), E81 (≠ H77), Y132 (≠ G124), D235 (= D232), F260 (≠ Y258)
- binding manganese (ii) ion: D7 (= D6), R14 (≠ K13)
1glcG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
24% identity, 97% coverage: 2:466/480 of query aligns to 3:473/489 of 1glcG
- binding adenosine-5'-diphosphate: G256 (= G253), T257 (= T254), G300 (≠ A294), A316 (≠ V308), G401 (= G392), A402 (≠ G393), N405 (≠ S396)
- binding glyceraldehyde-3-phosphate: T10 (= T9), R80 (≠ M76), E81 (≠ H77), W100 (= W95), Y132 (≠ G124), D235 (= D232), F260 (≠ Y258)
1glbG Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase (see paper)
24% identity, 97% coverage: 2:466/480 of query aligns to 3:473/489 of 1glbG
- binding adenosine-5'-diphosphate: R14 (≠ K13), G256 (= G253), T257 (= T254), G300 (≠ A294), I303 (≠ M297), A316 (≠ V308), G401 (= G392), A402 (≠ G393), N405 (≠ S396)
- binding glycerol: R80 (≠ M76), E81 (≠ H77), W100 (= W95), Y132 (≠ G124), D235 (= D232), F260 (≠ Y258)
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
24% identity, 97% coverage: 2:466/480 of query aligns to 5:478/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T9), T13 (≠ S10), G261 (= G253), T262 (= T254), G305 (≠ A294), I308 (≠ M297), Q309 (≠ A298), A321 (≠ V308), G406 (= G392), N410 (≠ S396)
- binding glycerol: R82 (≠ M76), E83 (≠ H77), Y134 (≠ G124), D240 (= D232), Q241 (≠ A233), F265 (≠ Q257)
Query Sequence
>3607827 Dshi_1235 xylulokinase (RefSeq)
MFLGLDIGTSAVKGLVWDGARVLGAASAPLKVQVPVPGASEQDPEAWWRGILAVCAELSA
QPGWAEVSAIGLSGQMHGAVCLGPDGAVLRPAILWNDNRAVREAAEMAALPGLAARVGVP
PMPGFPAPKLAWLARTEPELHAATTMVMQAKDWVGMRLHGRAVTEYSEAAGTLWLDQAAR
DWDREALAFSGLERAQMPALGAGTDLAGPLSAAAAAALGLKPGVPVIRGGGDAMVGAAGI
GVVAPGQAMISLGTSGQYLVASEAHRPNPAGLVHSFAHCVPGAYIQMAAMLNGAAPMAWL
AGVLGRSVPDLLAAAETADPAHVPLFLPYLTGERTPHGDPEARAGFEGLSHGSGPGEMMR
AVVDAIAYSFADAQAVLGEAGVRAASPLAIGGGARSDLVLQTLADVLEVPVQRPASADLG
PALGAAKLAAVGSGAMPAARLADPPEIGAVFHPRPSARHGARLARYRALYSELRGVCARP
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory