SitesBLAST
Comparing BWI76_RS07870 FitnessBrowser__Koxy:BWI76_RS07870 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)
31% identity, 97% coverage: 3:481/495 of query aligns to 1:482/484 of P09099
- D6 (= D8) mutation to A: Loss of activity.
- MH 77:78 (≠ GE 81:82) binding
- D233 (= D242) mutation to A: Loss of activity.
2itmA Crystal structure of the e. Coli xylulose kinase complexed with xylulose (see paper)
30% identity, 97% coverage: 3:481/495 of query aligns to 1:474/476 of 2itmA
3ll3A The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
24% identity, 97% coverage: 1:478/495 of query aligns to 2:484/492 of 3ll3A
- binding adenosine-5'-triphosphate: G259 (= G263), T260 (= T264), G299 (≠ T303), P316 (≠ R320), L320 (≠ Q324), G400 (= G399), G401 (= G400), F402 (≠ G401)
- binding 1-deoxy-d-xylulose-5-phosphate: H128 (≠ Q131), N296 (≠ Q300), E342 (= E345), A349 (≠ P352)
- binding d-xylulose: Q78 (= Q80), M79 (≠ G81), H80 (≠ E82), D238 (= D242), R343 (= R346)
3ll3B The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
23% identity, 97% coverage: 1:478/495 of query aligns to 1:482/490 of 3ll3B
- binding adenosine-5'-diphosphate: G258 (= G263), T259 (= T264), G298 (≠ T303), P314 (≠ L319), G399 (= G400), F400 (≠ G401), K402 (≠ A403)
- binding 1-deoxy-d-xylulose-5-phosphate: H127 (≠ Q131), N295 (≠ Q300), G338 (≠ N343), E340 (= E345), A347 (≠ P352)
3kzbA Crystal structure of xylulokinase from chromobacterium violaceum
30% identity, 89% coverage: 1:441/495 of query aligns to 2:452/498 of 3kzbA
Q5HGD2 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Staphylococcus aureus (strain COL)
24% identity, 100% coverage: 3:495/495 of query aligns to 4:498/498 of Q5HGD2
- T12 (= T11) binding
- R16 (≠ K15) binding
- R82 (≠ G81) binding
- E83 (= E82) binding
- Y134 (≠ C133) binding
- D244 (= D242) binding
- Q245 (≠ V243) binding
- T266 (= T264) binding
- G309 (vs. gap) binding
- Q313 (≠ D307) binding
- G410 (= G400) binding
- N414 (≠ S404) binding
3ge1A 2.7 angstrom crystal structure of glycerol kinase (glpk) from staphylococcus aureus in complex with adp and glycerol
24% identity, 100% coverage: 3:495/495 of query aligns to 5:499/499 of 3ge1A
O86033 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
25% identity, 94% coverage: 3:467/495 of query aligns to 4:483/497 of O86033
- R82 (≠ G81) binding
- E83 (= E82) binding
- Y134 (≠ C133) binding
- D243 (= D242) binding
- Q244 (≠ V243) binding
P18157 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Bacillus subtilis (strain 168) (see paper)
24% identity, 88% coverage: 3:440/495 of query aligns to 4:450/496 of P18157
- H230 (≠ T228) mutation to R: Increased activity.
- F232 (≠ L230) mutation to S: Increased activity.
6k76A Glycerol kinase form thermococcus kodakarensis, complex structure with substrate.
25% identity, 88% coverage: 5:441/495 of query aligns to 2:436/485 of 6k76A
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
24% identity, 93% coverage: 3:463/495 of query aligns to 4:474/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T11), T13 (≠ S12), G261 (= G263), T262 (= T264), G305 (vs. gap), I308 (= I306), Q309 (≠ D307), A321 (≠ L319), G406 (= G400), N410 (≠ S404)
- binding glycerol: R82 (≠ G81), E83 (= E82), Y134 (≠ C133), D240 (= D242), Q241 (≠ V243), F265 (≠ C267)
1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
24% identity, 93% coverage: 3:463/495 of query aligns to 4:474/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: T12 (= T11), T13 (≠ S12), G261 (= G263), T262 (= T264), G305 (vs. gap), Q309 (≠ D307), A321 (≠ L319), G406 (= G400), A407 (≠ G401)
- binding glycerol: R82 (≠ G81), E83 (= E82), W102 (= W100), Y134 (≠ C133), D240 (= D242), F265 (≠ C267)
1bwfO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
24% identity, 93% coverage: 3:463/495 of query aligns to 4:474/494 of 1bwfO
- binding phosphodifluoromethylphosphonic acid-adenylate ester: T12 (= T11), T13 (≠ S12), T262 (= T264), G305 (vs. gap), I308 (= I306), Q309 (≠ D307), A321 (≠ L319), G406 (= G400), N410 (≠ S404)
- binding glycerol: R82 (≠ G81), E83 (= E82), W102 (= W100), Y134 (≠ C133), D240 (= D242), Q241 (≠ V243), F265 (≠ C267)
6udeB Crystal structure of glycerol kinase from elizabethkingia anophelis nuhp1 in complex with adp and glycerol
24% identity, 88% coverage: 5:440/495 of query aligns to 6:447/495 of 6udeB
- binding adenosine-5'-diphosphate: R16 (≠ K15), G262 (= G263), T263 (= T264), G306 (≠ T303), I309 (= I306), S323 (≠ R320), G406 (= G399), G407 (= G400), A408 (≠ G401)
- binding magnesium ion: G11 (= G10), T12 (= T11), T13 (≠ S12), S14 (≠ R13)
1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
24% identity, 93% coverage: 3:463/495 of query aligns to 2:469/489 of 1gldG
- binding adenosine-5'-diphosphate: R14 (≠ K15), G256 (= G263), T257 (= T264), G300 (vs. gap), A316 (≠ L319), G401 (= G400), A402 (≠ G401), N405 (≠ S404)
- binding glyceraldehyde-3-phosphate: T10 (= T11), R80 (≠ G81), E81 (= E82), Y132 (≠ C133), D235 (= D242), F260 (≠ C267)
- binding manganese (ii) ion: D7 (= D8), R14 (≠ K15)
1glcG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
24% identity, 93% coverage: 3:463/495 of query aligns to 2:469/489 of 1glcG
- binding adenosine-5'-diphosphate: G256 (= G263), T257 (= T264), G300 (vs. gap), A316 (≠ L319), G401 (= G400), A402 (≠ G401), N405 (≠ S404)
- binding glyceraldehyde-3-phosphate: T10 (= T11), R80 (≠ G81), E81 (= E82), W100 (= W100), Y132 (≠ C133), D235 (= D242), F260 (≠ C267)
1glbG Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase (see paper)
24% identity, 93% coverage: 3:463/495 of query aligns to 2:469/489 of 1glbG
- binding adenosine-5'-diphosphate: R14 (≠ K15), G256 (= G263), T257 (= T264), G300 (vs. gap), I303 (= I306), A316 (≠ L319), G401 (= G400), A402 (≠ G401), N405 (≠ S404)
- binding glycerol: R80 (≠ G81), E81 (= E82), W100 (= W100), Y132 (≠ C133), D235 (= D242), F260 (≠ C267)
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)
23% identity, 93% coverage: 3:463/495 of query aligns to 4:478/499 of 1bu6Y
P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
23% identity, 93% coverage: 3:463/495 of query aligns to 6:480/502 of P0A6F3
- T14 (= T11) binding ; binding
- R18 (≠ K15) binding
- S59 (≠ A56) 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 (≠ R63) 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 (≠ G81) binding ; binding
- E85 (= E82) binding ; binding
- Y136 (≠ C133) binding ; binding
- G231 (≠ P231) 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 (≠ D233) 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.
- D246 (= D242) binding ; binding
- Q247 (≠ V243) binding
- T268 (= T264) binding
- G305 (≠ A301) mutation to S: In glpK22; abolishes glucose control of glycerol utilization.
- G311 (vs. gap) binding
- G412 (= G400) binding
- N416 (≠ S404) binding
- I475 (≠ P458) 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 (≠ S462) binding
- R480 (= R463) 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)
23% identity, 93% coverage: 3:463/495 of query aligns to 4:478/498 of 1glfO
- binding adenosine-5'-diphosphate: R16 (≠ K15), G265 (= G263), T266 (= T264), G309 (vs. gap), G410 (= G400), A411 (≠ G401)
- binding glycerol: R82 (≠ G81), E83 (= E82), Y134 (≠ C133), D244 (= D242)
- binding phosphate ion: G232 (vs. gap), G233 (vs. gap), R235 (vs. gap)
Query Sequence
>BWI76_RS07870 FitnessBrowser__Koxy:BWI76_RS07870
MDFYLGIDIGTSRVKAVLFDQRFQACASAAQNTGPRLSANGDAEQDMAQLWQSVVAILRD
IARHPALQNGRLRAIGLAGQGEGVWLSDAEGEPVGPGILWSDTRSRELMSELLSRPGFDR
RFFDDTGTHLQPCNTSMQLCWLKHHQPERLAAARYLFFAKDWIRFRLTGVAALDLTDAST
SLLNQQSGKLSTVVLNEMGLADLQHLFPPLLAPDAQAGALREEVAALTGLPADTPVAAGA
LDVCSAALGCGAVNDGDIYTILGTTCCTGIVCHGRQSVNEGTRYVTHTEAGSFINLFPMQ
AGTPNIDWLQQQISLEPDLRQLEQNIASVEPGSGGVFWQPYLNGERAPFFSPEARAGYFG
ISQHTTRAELQRAVFEGLAYAIVDSLQGYPQGGELYLTGGGAASATWLQMIADCTGRTVV
SSPFNELSARGAAILAARSVDALSRYPALEQTRYRPNPQAHSRYAALYPVYRLLREQMLP
VWQARREALQRISQE
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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