SitesBLAST
Comparing HSERO_RS17030 FitnessBrowser__HerbieS:HSERO_RS17030 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)
51% identity, 98% coverage: 3:483/493 of query aligns to 2:479/484 of P09099
- D6 (= D7) mutation to A: Loss of activity.
- MH 77:78 (= MH 80:81) binding
- D233 (= D237) mutation to A: Loss of activity.
2itmA Crystal structure of the e. Coli xylulose kinase complexed with xylulose (see paper)
49% identity, 98% coverage: 3:483/493 of query aligns to 2:471/476 of 2itmA
3ll3A The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
25% identity, 99% coverage: 4:491/493 of query aligns to 6:492/492 of 3ll3A
- binding adenosine-5'-triphosphate: G259 (= G258), T260 (≠ S259), G299 (≠ S293), P316 (≠ A310), L320 (≠ V317), G400 (= G399), G401 (= G400), F402 (≠ G401)
- binding 1-deoxy-d-xylulose-5-phosphate: H128 (≠ M127), N296 (≠ H290), E342 (= E341), A349 (= A348)
- binding d-xylulose: Q78 (= Q79), M79 (= M80), H80 (= H81), D238 (= D237), R343 (= R342)
3ll3B The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
25% identity, 99% coverage: 4:491/493 of query aligns to 5:490/490 of 3ll3B
- binding adenosine-5'-diphosphate: G258 (= G258), T259 (≠ S259), G298 (≠ S293), P314 (≠ T309), G399 (= G400), F400 (≠ G401), K402 (≠ R403)
- binding 1-deoxy-d-xylulose-5-phosphate: H127 (≠ M127), N295 (≠ H290), G338 (≠ N339), E340 (= E341), A347 (= A348)
3i8bA The crystal structure of xylulose kinase from bifidobacterium adolescentis
27% identity, 89% coverage: 5:444/493 of query aligns to 8:475/506 of 3i8bA
6k76A Glycerol kinase form thermococcus kodakarensis, complex structure with substrate.
26% identity, 89% coverage: 4:440/493 of query aligns to 2:434/485 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)
26% identity, 89% coverage: 4:440/493 of query aligns to 6:449/499 of 1bu6Y
1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
25% identity, 89% coverage: 4:440/493 of query aligns to 4:440/489 of 1gldG
- binding adenosine-5'-diphosphate: R14 (≠ K14), G256 (= G258), T257 (≠ S259), G300 (≠ A299), A316 (= A320), G401 (= G400), A402 (≠ G401), N405 (≠ S404)
- binding glyceraldehyde-3-phosphate: T10 (= T10), R80 (≠ M80), E81 (≠ H81), Y132 (≠ G129), D235 (= D237), F260 (≠ V262)
- binding manganese (ii) ion: D7 (= D7), R14 (≠ K14)
1glcG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
25% identity, 89% coverage: 4:440/493 of query aligns to 4:440/489 of 1glcG
- binding adenosine-5'-diphosphate: G256 (= G258), T257 (≠ S259), G300 (≠ A299), A316 (= A320), G401 (= G400), A402 (≠ G401), N405 (≠ S404)
- binding glyceraldehyde-3-phosphate: T10 (= T10), R80 (≠ M80), E81 (≠ H81), W100 (= W99), Y132 (≠ G129), D235 (= D237), F260 (≠ V262)
1glbG Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase (see paper)
25% identity, 89% coverage: 4:440/493 of query aligns to 4:440/489 of 1glbG
- binding adenosine-5'-diphosphate: R14 (≠ K14), G256 (= G258), T257 (≠ S259), G300 (≠ A299), I303 (≠ L302), A316 (= A320), G401 (= G400), A402 (≠ G401), N405 (≠ S404)
- binding glycerol: R80 (≠ M80), E81 (≠ H81), W100 (= W99), Y132 (≠ G129), D235 (= D237), F260 (≠ V262)
3kzbA Crystal structure of xylulokinase from chromobacterium violaceum
29% identity, 84% coverage: 6:419/493 of query aligns to 9:429/498 of 3kzbA
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
25% identity, 89% coverage: 4:440/493 of query aligns to 6:445/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T10), T13 (≠ S11), G261 (= G258), T262 (≠ S259), G305 (≠ A299), I308 (≠ L302), Q309 (≠ H303), A321 (= A320), G406 (= G400), N410 (≠ S404)
- binding glycerol: R82 (≠ M80), E83 (≠ H81), Y134 (≠ G129), D240 (= D237), Q241 (≠ N238), F265 (≠ V262)
1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
25% identity, 89% coverage: 4:440/493 of query aligns to 6:445/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: T12 (= T10), T13 (≠ S11), G261 (= G258), T262 (≠ S259), G305 (≠ A299), Q309 (≠ H303), A321 (= A320), G406 (= G400), A407 (≠ G401)
- binding glycerol: R82 (≠ M80), E83 (≠ H81), W102 (= W99), Y134 (≠ G129), D240 (= D237), F265 (≠ V262)
1bwfO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
25% identity, 89% coverage: 4:440/493 of query aligns to 6:445/494 of 1bwfO
- binding phosphodifluoromethylphosphonic acid-adenylate ester: T12 (= T10), T13 (≠ S11), T262 (≠ S259), G305 (≠ A299), I308 (≠ L302), Q309 (≠ H303), A321 (= A320), G406 (= G400), N410 (≠ S404)
- binding glycerol: R82 (≠ M80), E83 (≠ H81), W102 (= W99), Y134 (≠ G129), D240 (= D237), Q241 (≠ N238), F265 (≠ V262)
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)
25% identity, 89% coverage: 4:440/493 of query aligns to 6:449/498 of 1glfO
- binding adenosine-5'-diphosphate: R16 (≠ K14), G265 (= G258), T266 (≠ S259), G309 (≠ A299), G410 (= G400), A411 (≠ G401)
- binding glycerol: R82 (≠ M80), E83 (≠ H81), Y134 (≠ G129), D244 (= D237)
- 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)
25% identity, 89% coverage: 4:440/493 of query aligns to 6:449/498 of 1bo5O
P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
25% identity, 89% coverage: 4:440/493 of query aligns to 8:451/502 of P0A6F3
- T14 (= T10) binding ; binding
- R18 (≠ K14) binding
- S59 (≠ D55) 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 (≠ T62) 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 (≠ M80) binding ; binding
- E85 (≠ H81) binding ; binding
- Y136 (≠ G129) binding ; binding
- G231 (≠ S226) 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 (≠ P228) 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 (= D237) binding ; binding
- Q247 (≠ N238) binding
- T268 (≠ S259) binding
- G305 (≠ S293) mutation to S: In glpK22; abolishes glucose control of glycerol utilization.
- G311 (≠ A299) binding
- G412 (= G400) binding
- N416 (≠ S404) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 475 I→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.
- 479 binding
- 480 R→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.
P18157 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Bacillus subtilis (strain 168) (see paper)
25% identity, 89% coverage: 4:440/493 of query aligns to 6:449/496 of P18157
- H230 (≠ R221) mutation to R: Increased activity.
- F232 (≠ W223) mutation to S: Increased activity.
Q5HGD2 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Staphylococcus aureus (strain COL)
24% identity, 89% coverage: 4:440/493 of query aligns to 6:449/498 of Q5HGD2
- T12 (= T10) binding
- R16 (≠ K14) binding
- R82 (≠ M80) binding
- E83 (≠ H81) binding
- Y134 (≠ G129) binding
- D244 (= D237) binding
- Q245 (≠ N238) binding
- T266 (≠ S259) binding
- G309 (≠ A298) binding
- Q313 (≠ H303) 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, 89% coverage: 4:440/493 of query aligns to 7:450/499 of 3ge1A
Query Sequence
>HSERO_RS17030 FitnessBrowser__HerbieS:HSERO_RS17030
LSYLGIDLGTSEVKLVLTDEDSNVIASTSARLRVDNPHPLWSEQAPQSWWNATLDAIAAL
RTQAPQAFQALRGIGLSGQMHGATLLDRNGNVLRPAILWNDMRAHAECVELEALVPDAVA
ITGNRAMPGFTAPKLLWLSKYEPAVYRAIDKVLLPKDFLGWKLTGEFVSEMSDAAGTLWL
DVARRDWSERMLGATGLDRSHMPRLVEGSAVAGQLRDELRREWGISGPVVVAGGAGDNAA
SAVGIGVIRAGDAFLSLGSSGVLFAATAHHAPNAQQGVHAFCHCLPGQWHQMSVILSAAA
SLHWLSGVTARPVAELVSGAERLSAGQQAQAPLFLPYLNGERTPHNDAAAKGVLFGMTPA
HESAHLAYAVMEGVAFAMADGYAALQAAGTTLESAAFVGGGSRSAFWGVLCATALGIPLR
RHAGAEVGAALGAARLGRLARTGEDAASVCIPPEVLEWYRPDAARQAQLQRRLAQYRRLY
RSLADEFIAFSQS
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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