SitesBLAST
Comparing 3608604 FitnessBrowser__Dino:3608604 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)
49% identity, 99% coverage: 1:475/480 of query aligns to 1:479/484 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)
47% identity, 99% coverage: 1:475/480 of query aligns to 1:471/476 of 2itmA
3kzbA Crystal structure of xylulokinase from chromobacterium violaceum
32% identity, 84% coverage: 5:405/480 of query aligns to 9:422/498 of 3kzbA
3ll3A The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
27% identity, 85% coverage: 3:412/480 of query aligns to 6:420/492 of 3ll3A
- binding adenosine-5'-triphosphate: G259 (= G254), T260 (= T255), G299 (≠ T295), P316 (≠ L312), L320 (= L316), G400 (= G392), G401 (= G393), F402 (≠ G394)
- binding 1-deoxy-d-xylulose-5-phosphate: H128 (≠ F123), N296 (≠ L292), E342 (= E334), A349 (= A341)
- binding d-xylulose: Q78 (= Q76), M79 (= M77), H80 (= H78), D238 (= D233), R343 (= R335)
3ll3B The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
28% identity, 85% coverage: 3:412/480 of query aligns to 5:418/490 of 3ll3B
- binding adenosine-5'-diphosphate: G258 (= G254), T259 (= T255), G298 (≠ T295), P314 (≠ L312), G399 (= G393), F400 (≠ G394), K402 (= K396)
- binding 1-deoxy-d-xylulose-5-phosphate: H127 (≠ F123), N295 (≠ L292), G338 (= G332), E340 (= E334), A347 (= A341)
3i8bA The crystal structure of xylulose kinase from bifidobacterium adolescentis
27% identity, 96% coverage: 4:465/480 of query aligns to 8:505/506 of 3i8bA
1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
24% identity, 94% coverage: 3:453/480 of query aligns to 4:462/489 of 1gldG
- binding adenosine-5'-diphosphate: R14 (≠ K13), G256 (= G254), T257 (= T255), G300 (≠ T295), A316 (= A309), G401 (= G393), A402 (≠ G394), N405 (≠ S397)
- binding glyceraldehyde-3-phosphate: T10 (= T9), R80 (≠ M77), E81 (≠ H78), Y132 (≠ G125), D235 (= D233), F260 (≠ V258)
- 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, 94% coverage: 3:453/480 of query aligns to 4:462/489 of 1glcG
- binding adenosine-5'-diphosphate: G256 (= G254), T257 (= T255), G300 (≠ T295), A316 (= A309), G401 (= G393), A402 (≠ G394), N405 (≠ S397)
- binding glyceraldehyde-3-phosphate: T10 (= T9), R80 (≠ M77), E81 (≠ H78), W100 (= W96), Y132 (≠ G125), D235 (= D233), F260 (≠ V258)
1glbG Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase (see paper)
24% identity, 94% coverage: 3:453/480 of query aligns to 4:462/489 of 1glbG
- binding adenosine-5'-diphosphate: R14 (≠ K13), G256 (= G254), T257 (= T255), G300 (≠ T295), I303 (≠ L298), A316 (= A309), G401 (= G393), A402 (≠ G394), N405 (≠ S397)
- binding glycerol: R80 (≠ M77), E81 (≠ H78), W100 (= W96), Y132 (≠ G125), D235 (= D233), F260 (≠ V258)
6k76A Glycerol kinase form thermococcus kodakarensis, complex structure with substrate.
25% identity, 90% coverage: 3:434/480 of query aligns to 2:435/485 of 6k76A
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, 94% coverage: 3:453/480 of query aligns to 6:471/498 of 1glfO
- binding adenosine-5'-diphosphate: R16 (≠ K13), G265 (= G254), T266 (= T255), G309 (≠ T295), G410 (= G393), A411 (≠ G394)
- binding glycerol: R82 (≠ M77), E83 (≠ H78), Y134 (≠ G125), D244 (= D233)
- binding phosphate ion: G232 (≠ W219), G233 (= G220), R235 (≠ P222)
1bo5O Crystal structure of the complex between escherichia coli glycerol kinase and the allosteric regulator fructose 1,6-bisphosphate. (see paper)
24% identity, 94% coverage: 3:453/480 of query aligns to 6:471/498 of 1bo5O
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
24% identity, 94% coverage: 3:453/480 of query aligns to 6:467/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T9), T13 (≠ S10), G261 (= G254), T262 (= T255), G305 (≠ T295), I308 (≠ L298), Q309 (≠ N299), A321 (= A309), G406 (= G393), N410 (≠ S397)
- binding glycerol: R82 (≠ M77), E83 (≠ H78), Y134 (≠ G125), D240 (= D233), Q241 (≠ N234), F265 (≠ V258)
1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
24% identity, 94% coverage: 3:453/480 of query aligns to 6:467/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: T12 (= T9), T13 (≠ S10), G261 (= G254), T262 (= T255), G305 (≠ T295), Q309 (≠ N299), A321 (= A309), G406 (= G393), A407 (≠ G394)
- binding glycerol: R82 (≠ M77), E83 (≠ H78), W102 (= W96), Y134 (≠ G125), D240 (= D233), F265 (≠ V258)
1bwfO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
24% identity, 94% coverage: 3:453/480 of query aligns to 6:467/494 of 1bwfO
- binding phosphodifluoromethylphosphonic acid-adenylate ester: T12 (= T9), T13 (≠ S10), T262 (= T255), G305 (≠ T295), I308 (≠ L298), Q309 (≠ N299), A321 (= A309), G406 (= G393), N410 (≠ S397)
- binding glycerol: R82 (≠ M77), E83 (≠ H78), W102 (= W96), Y134 (≠ G125), D240 (= D233), Q241 (≠ N234), F265 (≠ V258)
P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
24% identity, 94% coverage: 3:453/480 of query aligns to 8:473/502 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 (= A61) 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 (≠ G125) binding ; binding
- G231 (≠ A216) 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 (≠ A218) modified: N6-malonyllysine
- G235 (= G220) binding
- R237 (≠ P222) 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 (= G289) mutation to S: In glpK22; abolishes glucose control of glycerol utilization.
- G311 (≠ T295) binding
- G412 (= G393) binding
- N416 (≠ S397) 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)
24% identity, 94% coverage: 3:453/480 of query aligns to 6:471/499 of 1bu6Y
5ya2A Crystal structure of lsrk-hpr complex with adp (see paper)
25% identity, 91% coverage: 3:437/480 of query aligns to 6:453/478 of 5ya2A
5ya1A Crystal structure of lsrk-hpr complex with atp (see paper)
25% identity, 91% coverage: 3:437/480 of query aligns to 6:453/478 of 5ya1A
6udeB Crystal structure of glycerol kinase from elizabethkingia anophelis nuhp1 in complex with adp and glycerol
24% identity, 90% coverage: 1:434/480 of query aligns to 4:447/495 of 6udeB
- binding adenosine-5'-diphosphate: R16 (≠ K13), G262 (= G254), T263 (= T255), G306 (vs. gap), I309 (≠ L298), S323 (≠ A310), G406 (= G392), G407 (= G393), A408 (≠ G394)
- binding magnesium ion: G11 (= G8), T12 (= T9), T13 (≠ S10), S14 (≠ G11)
Query Sequence
>3608604 FitnessBrowser__Dino:3608604
MYLGLDLGTSGLKAVLIDENQALVAEATAPLEVARPHPGWSEQMPCDWLAATEAAMAALG
ARADLSGVRAIGLSGQMHGATLLDASHEVLRPCILWNDTRAAAEAAALDADPAFRSVTGN
IVFPGFTAPKLAWVRAHEPDVFDRTALVLLPKDYLRLWLTGEAVAEMSDAAGTSWLDTGA
RDWSAPLLAATGLSRDHMPRLVEGSEVSGTLRDSLADAWGLPRGVPVAGGGGDNAASGIG
MGVVRAGDGFVSLGTSGVLFAACDAYAPDPATAVHTFCHALPETWHQMGVILAATDALNW
FARTCGTDAATLTGGLGPLQAPGRPVFLPYLGGERTPHNDAAIRGAFARIDHAADRDALA
RAVLEGVAFAFRDSFDALAATGTRLERLVAVGGGAKSDTWVRMIATLIGLPIDLPQAGDY
GGAFGAARLGMMAATGQGAALATRPPIARSLDPVPALADAFGEAHATYRATYTALKGLDR
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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