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Comparing WP_022949983.1 NCBI__GCF_000421465.1:WP_022949983.1 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)
6udeB Crystal structure of glycerol kinase from elizabethkingia anophelis nuhp1 in complex with adp and glycerol
59% identity, 100% coverage: 2:495/496 of query aligns to 3:494/495 of 6udeB
- binding adenosine-5'-diphosphate: R16 (= R15), G262 (= G263), T263 (= T264), G306 (= G307), I309 (≠ V310), S323 (≠ E324), G406 (= G407), G407 (= G408), A408 (= A409)
- binding magnesium ion: G11 (= G10), T12 (= T11), T13 (= T12), S14 (= S13)
1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
57% identity, 100% coverage: 2:495/496 of query aligns to 1:488/489 of 1gldG
- binding adenosine-5'-diphosphate: R14 (= R15), G256 (= G263), T257 (= T264), G300 (= G307), A316 (≠ S323), G401 (= G408), A402 (= A409), N405 (= N412)
- binding glyceraldehyde-3-phosphate: T10 (= T11), R80 (= R81), E81 (= E82), Y132 (= Y133), D235 (= D242), F260 (= F267)
- binding manganese (ii) ion: D7 (= D8), R14 (= R15)
1glcG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
57% identity, 100% coverage: 2:495/496 of query aligns to 1:488/489 of 1glcG
- binding adenosine-5'-diphosphate: G256 (= G263), T257 (= T264), G300 (= G307), A316 (≠ S323), G401 (= G408), A402 (= A409), N405 (= N412)
- binding glyceraldehyde-3-phosphate: T10 (= T11), R80 (= R81), E81 (= E82), W100 (= W101), Y132 (= Y133), D235 (= D242), F260 (= F267)
1glbG Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase (see paper)
57% identity, 100% coverage: 2:495/496 of query aligns to 1:488/489 of 1glbG
- binding adenosine-5'-diphosphate: R14 (= R15), G256 (= G263), T257 (= T264), G300 (= G307), I303 (≠ V310), A316 (≠ S323), G401 (= G408), A402 (= A409), N405 (= N412)
- binding glycerol: R80 (= R81), E81 (= E82), W100 (= W101), Y132 (= Y133), D235 (= D242), F260 (= F267)
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
57% identity, 100% coverage: 2:495/496 of query aligns to 3:493/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T11), T13 (= T12), G261 (= G263), T262 (= T264), G305 (= G307), I308 (≠ V310), Q309 (≠ H311), A321 (≠ S323), G406 (= G408), N410 (= N412)
- binding glycerol: R82 (= R81), E83 (= E82), Y134 (= Y133), D240 (= D242), Q241 (= Q243), F265 (= F267)
1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
57% identity, 100% coverage: 2:495/496 of query aligns to 3:493/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: T12 (= T11), T13 (= T12), G261 (= G263), T262 (= T264), G305 (= G307), Q309 (≠ H311), A321 (≠ S323), G406 (= G408), A407 (= A409)
- binding glycerol: R82 (= R81), E83 (= E82), W102 (= W101), Y134 (= Y133), D240 (= D242), F265 (= F267)
1bwfO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
57% identity, 100% coverage: 2:495/496 of query aligns to 3:493/494 of 1bwfO
- binding phosphodifluoromethylphosphonic acid-adenylate ester: T12 (= T11), T13 (= T12), T262 (= T264), G305 (= G307), I308 (≠ V310), Q309 (≠ H311), A321 (≠ S323), G406 (= G408), N410 (= N412)
- binding glycerol: R82 (= R81), E83 (= E82), W102 (= W101), Y134 (= Y133), D240 (= D242), Q241 (= Q243), F265 (= F267)
P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
57% identity, 100% coverage: 2:495/496 of query aligns to 5:499/502 of P0A6F3
- T14 (= T11) binding ADP; binding sn-glycerol 3-phosphate
- R18 (= R15) binding ADP
- S59 (≠ Q56) 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 (= A63) 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 (= R81) binding glycerol; binding sn-glycerol 3-phosphate
- E85 (= E82) binding glycerol; binding sn-glycerol 3-phosphate
- Y136 (= Y133) binding glycerol; binding sn-glycerol 3-phosphate
- G231 (≠ F230) 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 (≠ R232) modified: N6-malonyllysine
- G235 (vs. gap) binding beta-D-fructose 1,6-bisphosphate
- R237 (vs. gap) binding beta-D-fructose 1,6-bisphosphate; 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 (= D242) binding glycerol; binding sn-glycerol 3-phosphate
- Q247 (= Q243) binding glycerol
- T268 (= T264) binding ADP
- G305 (= G301) mutation to S: In glpK22; abolishes glucose control of glycerol utilization.
- G311 (= G307) binding ADP
- G412 (= G408) binding ADP
- N416 (= N412) binding ADP
- I475 (≠ L471) 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 (≠ R475) binding Zn(2+)
- R480 (≠ V476) 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)
57% identity, 100% coverage: 2:495/496 of query aligns to 3:497/498 of 1glfO
- binding adenosine-5'-diphosphate: R16 (= R15), G265 (= G263), T266 (= T264), G309 (= G307), G410 (= G408), A411 (= A409)
- binding glycerol: R82 (= R81), E83 (= E82), Y134 (= Y133), D244 (= D242)
- binding phosphate ion: G232 (≠ S233), G233 (vs. gap), R235 (vs. gap)
1bo5O Crystal structure of the complex between escherichia coli glycerol kinase and the allosteric regulator fructose 1,6-bisphosphate. (see paper)
57% identity, 100% coverage: 2:495/496 of query aligns to 3:497/498 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)
56% identity, 100% coverage: 2:495/496 of query aligns to 3:497/499 of 1bu6Y
P18157 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Bacillus subtilis (strain 168) (see paper)
55% identity, 99% coverage: 3:493/496 of query aligns to 4:495/496 of P18157
- H230 (≠ E228) mutation to R: Increased activity.
- F232 (= F230) mutation to S: Increased activity.
3ge1A 2.7 angstrom crystal structure of glycerol kinase (glpk) from staphylococcus aureus in complex with adp and glycerol
54% identity, 99% coverage: 2:493/496 of query aligns to 4:496/499 of 3ge1A
Q5HGD2 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Staphylococcus aureus (strain COL)
54% identity, 99% coverage: 2:493/496 of query aligns to 3:495/498 of Q5HGD2
- T12 (= T11) binding ADP
- R16 (= R15) binding ADP
- R82 (= R81) binding glycerol
- E83 (= E82) binding glycerol
- Y134 (= Y133) binding glycerol
- D244 (= D242) binding glycerol
- Q245 (= Q243) binding glycerol
- T266 (= T264) binding ADP
- G309 (= G307) binding ADP
- Q313 (≠ H311) binding ADP
- G410 (= G408) binding ADP
- N414 (= N412) binding ADP
O34153 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Enterococcus casseliflavus (Enterococcus flavescens) (see 3 papers)
53% identity, 98% coverage: 2:487/496 of query aligns to 5:491/506 of O34153
- R84 (= R81) binding glycerol
- E85 (= E82) binding glycerol
- Y136 (= Y133) binding glycerol
- H232 (≠ E228) 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 (= D242) binding glycerol
- Q247 (= Q243) binding glycerol
3h3nX Glycerol kinase h232r with glycerol (see paper)
53% identity, 98% coverage: 2:487/496 of query aligns to 4:490/501 of 3h3nX
O34154 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Enterococcus faecalis (strain ATCC 700802 / V583) (see 2 papers)
53% identity, 98% coverage: 2:487/496 of query aligns to 5:490/501 of O34154
- H231 (≠ E228) modified: Phosphohistidine; by HPr
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
O86033 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
55% identity, 98% coverage: 3:489/496 of query aligns to 4:492/497 of O86033
- R82 (= R81) binding glycerol
- E83 (= E82) binding glycerol
- Y134 (= Y133) binding glycerol
- D243 (= D242) binding glycerol
- Q244 (= Q243) binding glycerol
6k76A Glycerol kinase form thermococcus kodakarensis, complex structure with substrate.
53% identity, 99% coverage: 4:493/496 of query aligns to 1:480/485 of 6k76A
Q9NJP9 Glycerol kinase, glycosomal; GK; Glycerokinase; ATP:glycerol 3-phosphotransferase; EC 2.7.1.30 from Trypanosoma brucei brucei (see 2 papers)
45% identity, 99% coverage: 1:491/496 of query aligns to 1:508/512 of Q9NJP9
- Y3 (= Y3) natural variant: Y -> I
- A141 (= A135) mutation to S: Increased affinity for glycerol and glycerol 3-phosphate.
Query Sequence
>WP_022949983.1 NCBI__GCF_000421465.1:WP_022949983.1
MRYILALDQGTTSSRAIVCDRGGGIRALAQKEFPQYFPRSGWVEHDPEEIWSSQRQVARE
ALAKAGLRAEDIAAVGIANQRETTLIWDRATGEPIHNAIVWQDRRTAGLCDRLRKDGVEP
VFQRKTGLILDPYFAGSKIRWLLDHVPGARRRAEAGELAFGTVDSWLVWKFTQGRSHCTD
VTNASRTLLYNIHTGDWDEELLRLLEVPRELLPEVRASSEVYAETSREIFSRSLPIAGIA
GDQQAALFGQICTEPGLAKNTYGTGCFVLLHTGDRPVVSKQNLLTTVAWKIGDRTDYALE
GSVFIAGAVVHWLRDQLGFIRRSEDVESLADRVADSGGVYLVPAFAGLGAPHWDPYARGA
LVGISRGTGAAHIARAALESIAHQSVDVIRAMEADAGLGLSELRVDGGAARNDLLMQLQA
DLLGVPVVRPRLLETTALGAAYLAGLAVNYWKDTREIAAHWEQERVFMPRLDSERVAELR
AGWNKALQRAKAWTDT
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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