SitesBLAST
Comparing 17625 FitnessBrowser__Keio:17625 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)
100% identity, 100% coverage: 1:484/484 of query aligns to 1:484/484 of P09099
- D6 (= D6) mutation to A: Loss of activity.
- MH 77:78 (= MH 77:78) binding
- D233 (= D233) mutation to A: Loss of activity.
2itmA Crystal structure of the e. Coli xylulose kinase complexed with xylulose (see paper)
98% identity, 100% coverage: 1:484/484 of query aligns to 1:476/476 of 2itmA
3ll3B The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
27% identity, 96% coverage: 3:466/484 of query aligns to 5:469/490 of 3ll3B
- binding adenosine-5'-diphosphate: G258 (= G254), T259 (= T255), G298 (≠ A295), P314 (= P311), G399 (= G395), F400 (≠ G396), K402 (≠ R398)
- binding 1-deoxy-d-xylulose-5-phosphate: H127 (≠ M124), N295 (≠ L292), G338 (≠ S334), E340 (= E336), A347 (≠ P343)
3ll3A The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
27% identity, 96% coverage: 3:466/484 of query aligns to 6:471/492 of 3ll3A
- binding adenosine-5'-triphosphate: G259 (= G254), T260 (= T255), G299 (≠ A295), P316 (= P311), L320 (≠ I314), G400 (= G394), G401 (= G395), F402 (≠ G396)
- binding 1-deoxy-d-xylulose-5-phosphate: H128 (≠ M124), N296 (≠ L292), E342 (= E336), A349 (≠ P343)
- binding d-xylulose: Q78 (= Q76), M79 (= M77), H80 (= H78), D238 (= D233), R343 (= R337)
3i8bA The crystal structure of xylulose kinase from bifidobacterium adolescentis
31% identity, 89% coverage: 1:432/484 of query aligns to 5:468/506 of 3i8bA
6k76A Glycerol kinase form thermococcus kodakarensis, complex structure with substrate.
24% identity, 98% coverage: 3:474/484 of query aligns to 2:476/485 of 6k76A
3kzbA Crystal structure of xylulokinase from chromobacterium violaceum
28% identity, 94% coverage: 1:456/484 of query aligns to 4:471/498 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)
25% identity, 84% coverage: 3:409/484 of query aligns to 6:425/497 of O86033
- R82 (≠ M77) binding
- E83 (≠ H78) binding
- Y134 (≠ G126) binding
- D243 (= D233) binding
- Q244 (≠ N234) binding
1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
24% identity, 96% coverage: 3:466/484 of query aligns to 4:477/489 of 1gldG
- binding adenosine-5'-diphosphate: R14 (≠ K13), G256 (= G254), T257 (= T255), G300 (≠ A295), A316 (≠ P311), G401 (= G395), A402 (≠ G396), N405 (≠ S399)
- binding glyceraldehyde-3-phosphate: T10 (= T9), R80 (≠ M77), E81 (≠ H78), Y132 (≠ G126), D235 (= D233), F260 (≠ Y259)
- 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, 96% coverage: 3:466/484 of query aligns to 4:477/489 of 1glcG
- binding adenosine-5'-diphosphate: G256 (= G254), T257 (= T255), G300 (≠ A295), A316 (≠ P311), G401 (= G395), A402 (≠ G396), N405 (≠ S399)
- binding glyceraldehyde-3-phosphate: T10 (= T9), R80 (≠ M77), E81 (≠ H78), W100 (= W96), Y132 (≠ G126), D235 (= D233), F260 (≠ Y259)
1glbG Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase (see paper)
24% identity, 96% coverage: 3:466/484 of query aligns to 4:477/489 of 1glbG
- binding adenosine-5'-diphosphate: R14 (≠ K13), G256 (= G254), T257 (= T255), G300 (≠ A295), I303 (≠ L298), A316 (≠ P311), G401 (= G395), A402 (≠ G396), N405 (≠ S399)
- binding glycerol: R80 (≠ M77), E81 (≠ H78), W100 (= W96), Y132 (≠ G126), D235 (= D233), F260 (≠ Y259)
P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
24% identity, 96% coverage: 3:466/484 of query aligns to 8:488/502 of P0A6F3
- T14 (= T9) binding ; binding
- R18 (≠ K13) binding
- S59 (≠ A51) 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 (= A58) 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 (≠ M77) binding ; binding
- E85 (≠ H78) binding ; binding
- Y136 (≠ G126) binding ; binding
- G231 (≠ K218) 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 (≠ W220) modified: N6-malonyllysine
- G235 (≠ M222) binding
- R237 (≠ T224) 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 (= D233) binding ; binding
- Q247 (≠ N234) binding
- T268 (= T255) binding
- G305 (≠ S289) mutation to S: In glpK22; abolishes glucose control of glycerol utilization.
- G311 (≠ A295) binding
- G412 (= G395) binding
- N416 (≠ S399) binding
- I475 (≠ A459) 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 (vs. gap) binding
- R480 (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. 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)
25% identity, 96% coverage: 3:466/484 of query aligns to 6:486/498 of 1glfO
- binding adenosine-5'-diphosphate: R16 (≠ K13), G265 (= G254), T266 (= T255), G309 (≠ A295), G410 (= G395), A411 (≠ G396)
- binding glycerol: R82 (≠ M77), E83 (≠ H78), Y134 (≠ G126), D244 (= D233)
- binding phosphate ion: G232 (= G221), G233 (≠ M222), R235 (≠ T224)
1bo5O Crystal structure of the complex between escherichia coli glycerol kinase and the allosteric regulator fructose 1,6-bisphosphate. (see paper)
25% identity, 96% coverage: 3:466/484 of query aligns to 6:486/498 of 1bo5O
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, 96% coverage: 3:466/484 of query aligns to 6:486/499 of 1bu6Y
3ge1A 2.7 angstrom crystal structure of glycerol kinase (glpk) from staphylococcus aureus in complex with adp and glycerol
24% identity, 94% coverage: 3:457/484 of query aligns to 7:472/499 of 3ge1A
Q5HGD2 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Staphylococcus aureus (strain COL)
24% identity, 94% coverage: 3:457/484 of query aligns to 6:471/498 of Q5HGD2
- T12 (= T9) binding
- R16 (≠ K13) binding
- R82 (≠ M77) binding
- E83 (≠ H78) binding
- Y134 (≠ G126) binding
- D244 (= D233) binding
- Q245 (≠ N234) binding
- T266 (= T255) binding
- G309 (≠ A295) binding
- Q313 (≠ D299) binding
- G410 (= G395) binding
- N414 (≠ S399) binding
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
24% identity, 96% coverage: 3:466/484 of query aligns to 6:482/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T9), T13 (≠ S10), G261 (= G254), T262 (= T255), G305 (≠ A295), I308 (≠ L298), Q309 (≠ D299), A321 (≠ P311), G406 (= G395), N410 (≠ S399)
- binding glycerol: R82 (≠ M77), E83 (≠ H78), Y134 (≠ G126), D240 (= D233), Q241 (≠ N234), F265 (≠ Y259)
1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
24% identity, 96% coverage: 3:466/484 of query aligns to 6:482/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: T12 (= T9), T13 (≠ S10), G261 (= G254), T262 (= T255), G305 (≠ A295), Q309 (≠ D299), A321 (≠ P311), G406 (= G395), A407 (≠ G396)
- binding glycerol: R82 (≠ M77), E83 (≠ H78), W102 (= W96), Y134 (≠ G126), D240 (= D233), F265 (≠ Y259)
1bwfO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
24% identity, 96% coverage: 3:466/484 of query aligns to 6:482/494 of 1bwfO
- binding phosphodifluoromethylphosphonic acid-adenylate ester: T12 (= T9), T13 (≠ S10), T262 (= T255), G305 (≠ A295), I308 (≠ L298), Q309 (≠ D299), A321 (≠ P311), G406 (= G395), N410 (≠ S399)
- binding glycerol: R82 (≠ M77), E83 (≠ H78), W102 (= W96), Y134 (≠ G126), D240 (= D233), Q241 (≠ N234), F265 (≠ Y259)
Query Sequence
>17625 FitnessBrowser__Keio:17625
MYIGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALG
DQHSLQDVKALGIAGQMHGATLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRVITG
NLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLRMTGEFASDMSDAAGTMWLDVA
KRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMATVPVVAGGGDNAAGAVG
VGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDW
AAKLTGLSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNE
LARAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGG
DVGPALGAARLAQIAANPEKSLIELLPQLPLEQSHLPDAQRYAAYQPRRETFRRLYQQLL
PLMA
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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