SitesBLAST
Comparing SMc02341 FitnessBrowser__Smeli:SMc02341 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)
32% identity, 99% coverage: 1:474/477 of query aligns to 1:475/484 of P09099
- D6 (= D6) mutation to A: Loss of activity.
- MH 77:78 (≠ AH 76:77) binding
- D233 (= D233) mutation to A: Loss of activity.
2itmA Crystal structure of the e. Coli xylulose kinase complexed with xylulose (see paper)
32% identity, 99% coverage: 1:474/477 of query aligns to 1:467/476 of 2itmA
3ll3B The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
25% identity, 98% coverage: 3:468/477 of query aligns to 5:479/490 of 3ll3B
- binding adenosine-5'-diphosphate: G258 (= G254), T259 (≠ S255), G298 (= G294), P314 (vs. gap), G399 (= G393), F400 (≠ G394), K402 (≠ T396)
- binding 1-deoxy-d-xylulose-5-phosphate: H127 (≠ V123), N295 (≠ Q291), G338 (≠ T332), E340 (= E334), A347 (≠ P341)
3ll3A The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
24% identity, 98% coverage: 3:468/477 of query aligns to 6:481/492 of 3ll3A
- binding adenosine-5'-triphosphate: G259 (= G254), T260 (≠ S255), G299 (= G294), P316 (≠ W308), L320 (≠ Y312), G400 (= G392), G401 (= G393), F402 (≠ G394)
- binding 1-deoxy-d-xylulose-5-phosphate: H128 (≠ V123), N296 (≠ Q291), E342 (= E334), A349 (≠ P341)
- binding d-xylulose: Q78 (= Q75), M79 (≠ A76), H80 (= H77), D238 (= D233), R343 (= R335)
3kzbA Crystal structure of xylulokinase from chromobacterium violaceum
28% identity, 87% coverage: 5:417/477 of query aligns to 9:434/498 of 3kzbA
6udeB Crystal structure of glycerol kinase from elizabethkingia anophelis nuhp1 in complex with adp and glycerol
25% identity, 96% coverage: 1:456/477 of query aligns to 4:470/495 of 6udeB
- binding adenosine-5'-diphosphate: R16 (≠ K13), G262 (= G254), T263 (≠ S255), G306 (= G294), I309 (≠ F297), S323 (≠ M311), G406 (= G392), G407 (= G393), A408 (≠ G394)
- binding magnesium ion: G11 (= G8), T12 (= T9), T13 (≠ G10), S14 (= S11)
O34154 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Enterococcus faecalis (strain ATCC 700802 / V583) (see 2 papers)
25% identity, 95% coverage: 3:454/477 of query aligns to 8:472/501 of O34154
- H231 (≠ A216) modified: Phosphohistidine; by HPr
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3i8bA The crystal structure of xylulose kinase from bifidobacterium adolescentis
27% identity, 87% coverage: 1:417/477 of query aligns to 5:457/506 of 3i8bA
6k76A Glycerol kinase form thermococcus kodakarensis, complex structure with substrate.
25% identity, 100% coverage: 3:477/477 of query aligns to 2:473/485 of 6k76A
P18157 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Bacillus subtilis (strain 168) (see paper)
25% identity, 95% coverage: 3:455/477 of query aligns to 6:472/496 of P18157
- H230 (≠ L219) mutation to R: Increased activity.
- F232 (≠ L221) mutation to S: Increased activity.
3h3nX Glycerol kinase h232r with glycerol (see paper)
25% identity, 100% coverage: 3:477/477 of query aligns to 7:489/501 of 3h3nX
O34153 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Enterococcus casseliflavus (Enterococcus flavescens) (see 3 papers)
25% identity, 100% coverage: 3:477/477 of query aligns to 8:490/506 of O34153
- R84 (≠ A76) binding
- E85 (≠ H77) binding
- Y136 (≠ G125) binding
- H232 (≠ L219) modified: Phosphohistidine; by HPr; mutation to A: Loss of phosphorylation, no effect on activity.; mutation to E: Loss of phosphorylation, 2.5-fold reduced activity.; mutation to R: Loss of phosphorylation, 3.4-fold increased activity.
- D246 (= D233) binding
- Q247 (≠ T234) binding
P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
24% identity, 100% coverage: 3:477/477 of query aligns to 8:490/502 of P0A6F3
- T14 (= T9) binding ; binding
- R18 (≠ K13) binding
- S59 (≠ Q51) 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 (≠ A76) binding ; binding
- E85 (≠ H77) binding ; binding
- Y136 (≠ G125) binding ; binding
- G231 (= G220) 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 (≠ A222) modified: N6-malonyllysine
- G235 (= G224) 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 (= D233) binding ; binding
- Q247 (≠ T234) binding
- T268 (≠ S255) binding
- G305 (vs. gap) mutation to S: In glpK22; abolishes glucose control of glycerol utilization.
- G311 (= G294) binding
- G412 (= G393) binding
- N416 (≠ D397) binding
- I475 (≠ L460) 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 (≠ L464) binding
- R480 (≠ P465) 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)
24% identity, 100% coverage: 3:477/477 of query aligns to 6:488/498 of 1glfO
- binding adenosine-5'-diphosphate: R16 (≠ K13), G265 (= G254), T266 (≠ S255), G309 (= G294), G410 (= G393), A411 (≠ G394)
- binding glycerol: R82 (≠ A76), E83 (≠ H77), Y134 (≠ G125), D244 (= D233)
- binding phosphate ion: G232 (≠ A223), G233 (= G224), R235 (vs. gap)
1bo5O Crystal structure of the complex between escherichia coli glycerol kinase and the allosteric regulator fructose 1,6-bisphosphate. (see paper)
24% identity, 100% coverage: 3:477/477 of query aligns to 6:488/498 of 1bo5O
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
24% identity, 100% coverage: 3:477/477 of query aligns to 6:484/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T9), T13 (≠ G10), G261 (= G254), T262 (≠ S255), G305 (= G294), I308 (≠ F297), Q309 (≠ E298), A321 (≠ S307), G406 (= G393), N410 (≠ D397)
- binding glycerol: R82 (≠ A76), E83 (≠ H77), Y134 (≠ G125), D240 (= D233), Q241 (≠ T234), F265 (≠ I257)
1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
24% identity, 100% coverage: 3:477/477 of query aligns to 6:484/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: T12 (= T9), T13 (≠ G10), G261 (= G254), T262 (≠ S255), G305 (= G294), Q309 (≠ E298), A321 (≠ S307), G406 (= G393), A407 (≠ G394)
- binding glycerol: R82 (≠ A76), E83 (≠ H77), W102 (= W95), Y134 (≠ G125), D240 (= D233), F265 (≠ I257)
1bwfO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
24% identity, 100% coverage: 3:477/477 of query aligns to 6:484/494 of 1bwfO
- binding phosphodifluoromethylphosphonic acid-adenylate ester: T12 (= T9), T13 (≠ G10), T262 (≠ S255), G305 (= G294), I308 (≠ F297), Q309 (≠ E298), A321 (≠ S307), G406 (= G393), N410 (≠ D397)
- binding glycerol: R82 (≠ A76), E83 (≠ H77), W102 (= W95), Y134 (≠ G125), D240 (= D233), Q241 (≠ T234), F265 (≠ I257)
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, 100% coverage: 3:477/477 of query aligns to 6:488/499 of 1bu6Y
1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
24% identity, 100% coverage: 3:477/477 of query aligns to 4:479/489 of 1gldG
- binding adenosine-5'-diphosphate: R14 (≠ K13), G256 (= G254), T257 (≠ S255), G300 (= G294), A316 (≠ S307), G401 (= G393), A402 (≠ G394), N405 (≠ D397)
- binding glyceraldehyde-3-phosphate: T10 (= T9), R80 (≠ A76), E81 (≠ H77), Y132 (≠ G125), D235 (= D233), F260 (≠ I257)
- binding manganese (ii) ion: D7 (= D6), R14 (≠ K13)
Query Sequence
>SMc02341 FitnessBrowser__Smeli:SMc02341
MYLGIDLGTGSVKALLIDGDGKAVAEAARAYPVSSPMPGYAETSPADWWAQTVAAVRACC
DGHGGDVRGIGLSGQAHGLVAVGADAKPLRPAILWADQRATAEMEAVLALPEAVRRPLAN
PVVSGMAGLSLLWLRRNEPATYAAIRRILAPKDWLRLVMTGEAATEPSDASMTLLYDVGA
GRWATDVLSSLSIDPAILAPIVESHSIAGRLSAAAAAELGLAAGTPVAAGLSDTASCLFG
MGQTKPGSTILQVGSGIQIMSVVESIEPRVQPFYNSYRGIGGNLYSMAALQNGGTVFEWA
RTVLGASWAEMYRSGFEENEGNGGVIFLPYVTGERAPLLDPNASAAWANMRLGCTRGQLI
RSVFEGVALAVRDSWDALRGVGVSADRILLTGGGSTDPRWQQMLADILEVPLVPAHDLGN
ATIGAAYLGGMAAGHWRCIEAIPFPDDLGRPIEPRPFQGLDALLPRFRATYRGLKHA
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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