SitesBLAST
Comparing N515DRAFT_3230 N515DRAFT_3230 xylulokinase 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)
59% identity, 100% coverage: 1:490/490 of query aligns to 1:481/484 of P09099
- D6 (= D6) mutation to A: Loss of activity.
- MH 77:78 (= MH 82:83) binding
- D233 (= D237) mutation to A: Loss of activity.
2itmA Crystal structure of the e. Coli xylulose kinase complexed with xylulose (see paper)
58% identity, 100% coverage: 1:490/490 of query aligns to 1:473/476 of 2itmA
3ll3B The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
27% identity, 96% coverage: 2:471/490 of query aligns to 4:470/490 of 3ll3B
- binding adenosine-5'-diphosphate: G258 (= G258), T259 (= T259), G298 (≠ S300), P314 (≠ A316), G399 (= G399), F400 (≠ G400), K402 (≠ R402)
- binding 1-deoxy-d-xylulose-5-phosphate: H127 (≠ M128), N295 (= N297), G338 (≠ T338), E340 (= E340), A347 (≠ V347)
3ll3A The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
26% identity, 96% coverage: 2:471/490 of query aligns to 5:472/492 of 3ll3A
- binding adenosine-5'-triphosphate: G259 (= G258), T260 (= T259), G299 (≠ S300), P316 (≠ V314), L320 (= L318), G400 (= G398), G401 (= G399), F402 (≠ G400)
- binding 1-deoxy-d-xylulose-5-phosphate: H128 (≠ M128), N296 (= N297), E342 (= E340), A349 (≠ V347)
- binding d-xylulose: Q78 (= Q81), M79 (= M82), H80 (= H83), D238 (= D237), R343 (= R341)
6k76A Glycerol kinase form thermococcus kodakarensis, complex structure with substrate.
26% identity, 92% coverage: 3:452/490 of query aligns to 2:447/485 of 6k76A
6udeB Crystal structure of glycerol kinase from elizabethkingia anophelis nuhp1 in complex with adp and glycerol
27% identity, 94% coverage: 1:461/490 of query aligns to 4:468/495 of 6udeB
- binding adenosine-5'-diphosphate: R16 (≠ K13), G262 (= G258), T263 (= T259), G306 (≠ A298), I309 (≠ C301), S323 (≠ D313), G406 (= G398), G407 (= G399), A408 (≠ G400)
- binding magnesium ion: G11 (= G8), T12 (= T9), T13 (≠ S10), S14 (≠ A11)
3kzbA Crystal structure of xylulokinase from chromobacterium violaceum
31% identity, 89% coverage: 5:441/490 of query aligns to 9:452/498 of 3kzbA
3i8bA The crystal structure of xylulose kinase from bifidobacterium adolescentis
28% identity, 89% coverage: 1:436/490 of query aligns to 5:468/506 of 3i8bA
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)
26% identity, 94% coverage: 2:461/490 of query aligns to 5:471/498 of 1glfO
- binding adenosine-5'-diphosphate: R16 (≠ K13), G265 (= G258), T266 (= T259), G309 (≠ A298), G410 (= G399), A411 (≠ G400)
- binding glycerol: R82 (≠ M82), E83 (≠ H83), Y134 (≠ G130), D244 (= D237)
- binding phosphate ion: G232 (= G225), G233 (≠ M226), R235 (= R228)
1bo5O Crystal structure of the complex between escherichia coli glycerol kinase and the allosteric regulator fructose 1,6-bisphosphate. (see paper)
26% identity, 94% coverage: 2:461/490 of query aligns to 5:471/498 of 1bo5O
P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
26% identity, 94% coverage: 2:461/490 of query aligns to 7:473/502 of P0A6F3
- T14 (= T9) binding ; binding
- R18 (≠ K13) binding
- S59 (≠ A54) 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 (= A64) 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 (≠ M82) binding ; binding
- E85 (≠ H83) binding ; binding
- Y136 (≠ G130) binding ; binding
- G231 (≠ E219) 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 (≠ A221) modified: N6-malonyllysine
- G235 (≠ M226) binding
- R237 (= R228) 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 (= T259) binding
- G305 (= G287) mutation to S: In glpK22; abolishes glucose control of glycerol utilization.
- G311 (≠ A298) binding
- G412 (= G399) binding
- N416 (≠ S403) 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.
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, 94% coverage: 2:461/490 of query aligns to 5:471/499 of 1bu6Y
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
25% identity, 94% coverage: 2:461/490 of query aligns to 5:467/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T9), T13 (≠ S10), G261 (= G258), T262 (= T259), G305 (≠ A298), I308 (≠ C301), Q309 (vs. gap), A321 (= A312), G406 (= G399), N410 (≠ S403)
- binding glycerol: R82 (≠ M82), E83 (≠ H83), Y134 (≠ G130), D240 (= D237), Q241 (≠ N238), F265 (≠ Y263)
1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
25% identity, 94% coverage: 2:461/490 of query aligns to 5:467/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: T12 (= T9), T13 (≠ S10), G261 (= G258), T262 (= T259), G305 (≠ A298), Q309 (vs. gap), A321 (= A312), G406 (= G399), A407 (≠ G400)
- binding glycerol: R82 (≠ M82), E83 (≠ H83), W102 (= W101), Y134 (≠ G130), D240 (= D237), F265 (≠ Y263)
1bwfO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
25% identity, 94% coverage: 2:461/490 of query aligns to 5:467/494 of 1bwfO
- binding phosphodifluoromethylphosphonic acid-adenylate ester: T12 (= T9), T13 (≠ S10), T262 (= T259), G305 (≠ A298), I308 (≠ C301), Q309 (vs. gap), A321 (= A312), G406 (= G399), N410 (≠ S403)
- binding glycerol: R82 (≠ M82), E83 (≠ H83), W102 (= W101), Y134 (≠ G130), D240 (= D237), Q241 (≠ N238), F265 (≠ Y263)
1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
25% identity, 94% coverage: 2:461/490 of query aligns to 3:462/489 of 1gldG
- binding adenosine-5'-diphosphate: R14 (≠ K13), G256 (= G258), T257 (= T259), G300 (≠ A298), A316 (= A312), G401 (= G399), A402 (≠ G400), N405 (≠ S403)
- binding glyceraldehyde-3-phosphate: T10 (= T9), R80 (≠ M82), E81 (≠ H83), Y132 (≠ G130), D235 (= D237), F260 (≠ Y263)
- 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)
25% identity, 94% coverage: 2:461/490 of query aligns to 3:462/489 of 1glcG
- binding adenosine-5'-diphosphate: G256 (= G258), T257 (= T259), G300 (≠ A298), A316 (= A312), G401 (= G399), A402 (≠ G400), N405 (≠ S403)
- binding glyceraldehyde-3-phosphate: T10 (= T9), R80 (≠ M82), E81 (≠ H83), W100 (= W101), Y132 (≠ G130), D235 (= D237), F260 (≠ Y263)
1glbG Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase (see paper)
25% identity, 94% coverage: 2:461/490 of query aligns to 3:462/489 of 1glbG
- binding adenosine-5'-diphosphate: R14 (≠ K13), G256 (= G258), T257 (= T259), G300 (≠ A298), I303 (≠ C301), A316 (= A312), G401 (= G399), A402 (≠ G400), N405 (≠ S403)
- binding glycerol: R80 (≠ M82), E81 (≠ H83), W100 (= W101), Y132 (≠ G130), D235 (= D237), F260 (≠ Y263)
Q5HGD2 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Staphylococcus aureus (strain COL)
25% identity, 96% coverage: 2:470/490 of query aligns to 5:483/498 of Q5HGD2
- T12 (= T9) binding
- R16 (≠ K13) binding
- R82 (≠ M82) binding
- E83 (≠ H83) binding
- Y134 (≠ G130) binding
- D244 (= D237) binding
- Q245 (≠ N238) binding
- T266 (= T259) binding
- G309 (= G310) binding
- Q313 (vs. gap) binding
- G410 (= G399) binding
- N414 (≠ S403) binding
3ge1A 2.7 angstrom crystal structure of glycerol kinase (glpk) from staphylococcus aureus in complex with adp and glycerol
25% identity, 96% coverage: 2:470/490 of query aligns to 6:484/499 of 3ge1A
Query Sequence
>N515DRAFT_3230 N515DRAFT_3230 xylulokinase
MFLGLDLGTSAVKAVLVDAAGAVRAVASQPLTVSHPRPRWSEQDPVDWWRAAVAAIDELL
QAAARDGIPASRVAAIGLSGQMHGATLLDRSDRVLRPAILWNDGRSDAQCRWMETLPDFH
AITGNLAMPGFTAPKLAWVREHEPSVFDAVAKVLLPKDYLRLCLTGDYASDVSDAAGTLW
LDVGKRQWSDPMLAACGLSREQMPGVHEGSESAGRLRAELAERWGMARVPVAAGGGDNAA
GAVGAGIVRHGQAMLSLGTSGVYFAVSDGFLSRPEQAVHSFCHALPGTWHLMSVMLNAAS
CLDYTARLTGHADVGAMLAEAQAAPRRDDGPLFLPYLTGERTPHNDVHATGSFTGLQADT
TRADLANATLEGVGLGLLDGIEAVDAAGLRADRVAVIGGGTRSAYWLQMLADIAGRPLEL
RAGGDVGAALGAARLAHLAAEPGARIDEVCAMPPLVSEYLPDAARHAYYREHRQPRFRDT
YRRLRTATTP
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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