SitesBLAST
Comparing Pf6N2E2_805 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_805 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)
3i8bA The crystal structure of xylulose kinase from bifidobacterium adolescentis
34% identity, 90% coverage: 4:450/495 of query aligns to 3:474/506 of 3i8bA
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)
33% identity, 98% coverage: 6:490/495 of query aligns to 1:474/484 of P09099
- D6 (= D11) mutation to A: Loss of activity.
- MH 77:78 (≠ QH 85:86) binding
- D233 (= D248) mutation to A: Loss of activity.
2itmA Crystal structure of the e. Coli xylulose kinase complexed with xylulose (see paper)
32% identity, 98% coverage: 6:490/495 of query aligns to 1:466/476 of 2itmA
3ll3A The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
24% identity, 89% coverage: 5:444/495 of query aligns to 3:437/492 of 3ll3A
- binding adenosine-5'-triphosphate: G259 (= G269), T260 (≠ S270), G299 (= G298), P316 (≠ I315), L320 (= L319), G400 (= G407), G401 (= G408), F402 (≠ G409)
- binding 1-deoxy-d-xylulose-5-phosphate: H128 (≠ A135), N296 (≠ S295), E342 (= E349), A349 (vs. gap)
- binding d-xylulose: Q78 (= Q84), M79 (≠ Q85), H80 (= H86), D238 (= D248), R343 (= R350)
3ll3B The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
24% identity, 89% coverage: 5:444/495 of query aligns to 2:435/490 of 3ll3B
- binding adenosine-5'-diphosphate: G258 (= G269), T259 (≠ S270), G298 (≠ T309), P314 (≠ I323), G399 (= G408), F400 (≠ G409), K402 (= K411)
- binding 1-deoxy-d-xylulose-5-phosphate: H127 (≠ A135), N295 (≠ M306), G338 (≠ N347), E340 (= E349), A347 (vs. gap)
3kzbA Crystal structure of xylulokinase from chromobacterium violaceum
27% identity, 89% coverage: 10:449/495 of query aligns to 9:456/498 of 3kzbA
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, 100% coverage: 1:493/495 of query aligns to 1:491/501 of O34154
- M1 (= M1) modified: Initiator methionine, Removed
- H231 (≠ A232) modified: Phosphohistidine; by HPr
6k76A Glycerol kinase form thermococcus kodakarensis, complex structure with substrate.
25% identity, 96% coverage: 8:484/495 of query aligns to 2:477/485 of 6k76A
O34153 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Enterococcus casseliflavus (Enterococcus flavescens) (see 3 papers)
23% identity, 100% coverage: 1:493/495 of query aligns to 1:492/506 of O34153
- R84 (≠ Q85) binding
- E85 (≠ H86) binding
- Y136 (≠ G137) binding
- H232 (≠ L234) 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 (= D248) binding
- Q247 (≠ N249) binding
3h3nX Glycerol kinase h232r with glycerol (see paper)
22% identity, 99% coverage: 2:493/495 of query aligns to 1:491/501 of 3h3nX
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
23% identity, 98% coverage: 4:487/495 of query aligns to 2:487/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T14), T13 (≠ Q15), G261 (= G269), T262 (≠ S270), G305 (≠ N310), I308 (vs. gap), Q309 (≠ G313), A321 (= A325), G406 (= G408), N410 (≠ S412)
- binding glycerol: R82 (≠ Q85), E83 (≠ H86), Y134 (≠ G137), D240 (= D248), Q241 (≠ N249), F265 (≠ T273)
1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
23% identity, 98% coverage: 4:487/495 of query aligns to 2:487/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: T12 (= T14), T13 (≠ Q15), G261 (= G269), T262 (≠ S270), G305 (≠ N310), Q309 (≠ G313), A321 (= A325), G406 (= G408), A407 (≠ G409)
- binding glycerol: R82 (≠ Q85), E83 (≠ H86), W102 (= W104), Y134 (≠ G137), D240 (= D248), F265 (≠ T273)
1bwfO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
23% identity, 98% coverage: 4:487/495 of query aligns to 2:487/494 of 1bwfO
- binding phosphodifluoromethylphosphonic acid-adenylate ester: T12 (= T14), T13 (≠ Q15), T262 (≠ S270), G305 (≠ N310), I308 (vs. gap), Q309 (≠ G313), A321 (= A325), G406 (= G408), N410 (≠ S412)
- binding glycerol: R82 (≠ Q85), E83 (≠ H86), W102 (= W104), Y134 (≠ G137), D240 (= D248), Q241 (≠ N249), F265 (≠ T273)
P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
24% identity, 98% coverage: 1:487/495 of query aligns to 1:493/502 of P0A6F3
- M1 (= M1) modified: Initiator methionine, Removed
- T14 (= T14) binding ; binding
- R18 (≠ K18) binding
- S59 (≠ Q60) 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 (= A67) 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 (≠ Q85) binding ; binding
- E85 (≠ H86) binding ; binding
- Y136 (≠ G137) binding ; binding
- G231 (≠ A231) 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 (≠ H233) modified: N6-malonyllysine
- G235 (= G235) binding
- R237 (≠ N237) 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 (= D248) binding ; binding
- Q247 (≠ N249) binding
- T268 (≠ S270) binding
- G305 (≠ C304) mutation to S: In glpK22; abolishes glucose control of glycerol utilization.
- G311 (≠ N310) binding
- G412 (= G408) binding
- N416 (≠ S412) binding
- I475 (≠ S469) 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 (≠ P473) binding
- R480 (≠ I474) 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.
1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
23% identity, 98% coverage: 5:487/495 of query aligns to 1:482/489 of 1gldG
- binding adenosine-5'-diphosphate: R14 (≠ K18), G256 (= G269), T257 (≠ S270), G300 (≠ N310), A316 (= A325), G401 (= G408), A402 (≠ G409), N405 (≠ S412)
- binding glyceraldehyde-3-phosphate: T10 (= T14), R80 (≠ Q85), E81 (≠ H86), Y132 (≠ G137), D235 (= D248), F260 (≠ T273)
- binding manganese (ii) ion: D7 (= D11), R14 (≠ K18)
1glcG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
23% identity, 98% coverage: 5:487/495 of query aligns to 1:482/489 of 1glcG
- binding adenosine-5'-diphosphate: G256 (= G269), T257 (≠ S270), G300 (≠ N310), A316 (= A325), G401 (= G408), A402 (≠ G409), N405 (≠ S412)
- binding glyceraldehyde-3-phosphate: T10 (= T14), R80 (≠ Q85), E81 (≠ H86), W100 (= W104), Y132 (≠ G137), D235 (= D248), F260 (≠ T273)
1glbG Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase (see paper)
23% identity, 98% coverage: 5:487/495 of query aligns to 1:482/489 of 1glbG
- binding adenosine-5'-diphosphate: R14 (≠ K18), G256 (= G269), T257 (≠ S270), G300 (≠ N310), I303 (vs. gap), A316 (= A325), G401 (= G408), A402 (≠ G409), N405 (≠ S412)
- binding glycerol: R80 (≠ Q85), E81 (≠ H86), W100 (= W104), Y132 (≠ G137), D235 (= D248), F260 (≠ T273)
5ya2A Crystal structure of lsrk-hpr complex with adp (see paper)
23% identity, 95% coverage: 3:473/495 of query aligns to 1:466/478 of 5ya2A
5ya1A Crystal structure of lsrk-hpr complex with atp (see paper)
23% identity, 95% coverage: 3:473/495 of query aligns to 1:466/478 of 5ya1A
3ge1A 2.7 angstrom crystal structure of glycerol kinase (glpk) from staphylococcus aureus in complex with adp and glycerol
23% identity, 94% coverage: 2:468/495 of query aligns to 1:473/499 of 3ge1A
Query Sequence
>Pf6N2E2_805 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_805
MANQQLFLGIDCGTQGTKALILDATSGQVLGLGAAAHSMISGANGRREQDTQQWLDAFTQ
ATHQALAAAGVDGQAILGIGVSGQQHGLVLLDDQGQVLRPAKLWCDTETTPENDRLLAHL
GGEDGSLERLGVVIAPGYTVSKLLWTREQHPQVFERIASVLLPHDFLNYWLTGRHCSEYG
DASGTGYFNVRTRQWDVQLLQHIDPSARLQAALPELIEAHQPVGRILPAIAAHLGINPEA
VVASGGGDNMMGAIGTGNIQPGVITMSLGSSGTVYAYAAEPAVSPQPSVATFCSSSGGWL
PLICTMNLTNATGAIRELLDLDIDAFNALVAKAPIGAEGVCMLPFLNGERVPALPHATGS
LLGLTTTNLTRANLCRAVVEGTTFGLRYGLDLLRANGLQAQSIRLIGGGSKSAQWRQIVA
DTMDTTVICTEQSEAAALGAAIQAAWCHSGSQTGLAELCERCVKLDPSSETRPIAAHVAA
SQQAYERYRQHVATL
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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