SitesBLAST
Comparing 208653 MicrobesOnline__882:208653 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
P18157 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Bacillus subtilis (strain 168) (see paper)
62% identity, 99% coverage: 1:494/497 of query aligns to 1:495/496 of P18157
- H230 (≠ E229) mutation to R: Increased activity.
- F232 (≠ L231) mutation to S: Increased activity.
6udeB Crystal structure of glycerol kinase from elizabethkingia anophelis nuhp1 in complex with adp and glycerol
61% identity, 99% coverage: 5:496/497 of query aligns to 5:494/495 of 6udeB
- binding adenosine-5'-diphosphate: R16 (= R16), G262 (= G264), T263 (= T265), G306 (= G308), I309 (≠ V311), S323 (≠ P325), G406 (= G408), G407 (= G409), A408 (= A410)
- binding magnesium ion: G11 (= G11), T12 (= T12), T13 (= T13), S14 (= S14)
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
58% identity, 100% coverage: 2:496/497 of query aligns to 2:493/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T12), T13 (= T13), G261 (= G264), T262 (= T265), G305 (= G308), I308 (≠ V311), Q309 (= Q312), A321 (= A324), G406 (= G409), N410 (= N413)
- binding glycerol: R82 (= R82), E83 (= E83), Y134 (= Y134), D240 (= D243), Q241 (= Q244), F265 (= F268)
1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
58% identity, 100% coverage: 2:496/497 of query aligns to 2:493/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: T12 (= T12), T13 (= T13), G261 (= G264), T262 (= T265), G305 (= G308), Q309 (= Q312), A321 (= A324), G406 (= G409), A407 (= A410)
- binding glycerol: R82 (= R82), E83 (= E83), W102 (= W102), Y134 (= Y134), D240 (= D243), F265 (= F268)
1bwfO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
58% identity, 100% coverage: 2:496/497 of query aligns to 2:493/494 of 1bwfO
- binding phosphodifluoromethylphosphonic acid-adenylate ester: T12 (= T12), T13 (= T13), T262 (= T265), G305 (= G308), I308 (≠ V311), Q309 (= Q312), A321 (= A324), G406 (= G409), N410 (= N413)
- binding glycerol: R82 (= R82), E83 (= E83), W102 (= W102), Y134 (= Y134), D240 (= D243), Q241 (= Q244), F265 (= F268)
Q5HGD2 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Staphylococcus aureus (strain COL)
58% identity, 98% coverage: 1:489/497 of query aligns to 1:490/498 of Q5HGD2
- T12 (= T12) binding
- R16 (= R16) binding
- R82 (= R82) binding
- E83 (= E83) binding
- Y134 (= Y134) binding
- D244 (= D243) binding
- Q245 (= Q244) binding
- T266 (= T265) binding
- G309 (= G308) binding
- Q313 (= Q312) binding
- G410 (= G409) binding
- N414 (= N413) binding
3ge1A 2.7 angstrom crystal structure of glycerol kinase (glpk) from staphylococcus aureus in complex with adp and glycerol
58% identity, 98% coverage: 1:489/497 of query aligns to 2:491/499 of 3ge1A
1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
58% identity, 99% coverage: 4:496/497 of query aligns to 2:488/489 of 1gldG
- binding adenosine-5'-diphosphate: R14 (= R16), G256 (= G264), T257 (= T265), G300 (= G308), A316 (= A324), G401 (= G409), A402 (= A410), N405 (= N413)
- binding glyceraldehyde-3-phosphate: T10 (= T12), R80 (= R82), E81 (= E83), Y132 (= Y134), D235 (= D243), F260 (= F268)
- binding manganese (ii) ion: D7 (= D9), R14 (= R16)
1glcG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
58% identity, 99% coverage: 4:496/497 of query aligns to 2:488/489 of 1glcG
- binding adenosine-5'-diphosphate: G256 (= G264), T257 (= T265), G300 (= G308), A316 (= A324), G401 (= G409), A402 (= A410), N405 (= N413)
- binding glyceraldehyde-3-phosphate: T10 (= T12), R80 (= R82), E81 (= E83), W100 (= W102), Y132 (= Y134), D235 (= D243), F260 (= F268)
1glbG Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase (see paper)
58% identity, 99% coverage: 4:496/497 of query aligns to 2:488/489 of 1glbG
- binding adenosine-5'-diphosphate: R14 (= R16), G256 (= G264), T257 (= T265), G300 (= G308), I303 (≠ V311), A316 (= A324), G401 (= G409), A402 (= A410), N405 (= N413)
- binding glycerol: R80 (= R82), E81 (= E83), W100 (= W102), Y132 (= Y134), D235 (= D243), F260 (= F268)
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)
58% identity, 99% coverage: 3:496/497 of query aligns to 3:497/498 of 1glfO
- binding adenosine-5'-diphosphate: R16 (= R16), G265 (= G264), T266 (= T265), G309 (= G308), G410 (= G409), A411 (= A410)
- binding glycerol: R82 (= R82), E83 (= E83), Y134 (= Y134), D244 (= D243)
- binding phosphate ion: G232 (= G232), G233 (≠ K233), R235 (vs. gap)
1bo5O Crystal structure of the complex between escherichia coli glycerol kinase and the allosteric regulator fructose 1,6-bisphosphate. (see paper)
58% identity, 99% coverage: 3:496/497 of query aligns to 3:497/498 of 1bo5O
P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
58% identity, 99% coverage: 3:496/497 of query aligns to 5:499/502 of P0A6F3
- T14 (= T12) binding ; binding
- R18 (= R16) binding
- S59 (≠ W57) 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 (≠ Q64) 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 (= R82) binding ; binding
- E85 (= E83) binding ; binding
- Y136 (= Y134) binding ; binding
- G231 (≠ E229) 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 (≠ L231) modified: N6-malonyllysine
- G235 (≠ K233) 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 (= D243) binding ; binding
- Q247 (= Q244) binding
- T268 (= T265) binding
- G305 (= G302) mutation to S: In glpK22; abolishes glucose control of glycerol utilization.
- G311 (= G308) binding
- G412 (= G409) binding
- N416 (= N413) binding
- I475 (≠ M472) 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 (≠ K476) binding
- R480 (= R477) 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
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)
58% identity, 99% coverage: 4:496/497 of query aligns to 4:497/499 of 1bu6Y
O34154 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Enterococcus faecalis (strain ATCC 700802 / V583) (see 2 papers)
55% identity, 98% coverage: 4:488/497 of query aligns to 6:490/501 of O34154
- H231 (≠ E229) modified: Phosphohistidine; by HPr
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
O34153 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Enterococcus casseliflavus (Enterococcus flavescens) (see 3 papers)
55% identity, 98% coverage: 3:488/497 of query aligns to 5:491/506 of O34153
- R84 (= R82) binding
- E85 (= E83) binding
- Y136 (= Y134) binding
- H232 (≠ E229) 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 (= D243) binding
- Q247 (= Q244) binding
3h3nX Glycerol kinase h232r with glycerol (see paper)
55% identity, 98% coverage: 3:488/497 of query aligns to 4:490/501 of 3h3nX
O86033 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
54% identity, 99% coverage: 1:490/497 of query aligns to 1:492/497 of O86033
- R82 (= R82) binding
- E83 (= E83) binding
- Y134 (= Y134) binding
- D243 (= D243) binding
- Q244 (= Q244) binding
6k76A Glycerol kinase form thermococcus kodakarensis, complex structure with substrate.
56% identity, 99% coverage: 5:494/497 of query aligns to 1:480/485 of 6k76A
5gn6A Crystal structure of glycerol kinase from trypanosoma brucei gambiense complexed with cumarin derivative-17b (see paper)
44% identity, 99% coverage: 3:492/497 of query aligns to 4:510/513 of 5gn6A
Query Sequence
>208653 MicrobesOnline__882:208653
MSNYVLALDQGTTSSRAILFTREGDIKQISQKEFTQIYPQPGWVEHNANEIFDTQSWVMR
ECLQEAGIGAADVVAAGITNQRETTVVWDKATGAPVYNAIVWQDRRTAGFCDELKARGLA
DVFRKKTGLVLDAYFSGTKVRWILDNVPGARAKAEKGELLFGTIDTWLIWNLTKGKAHVT
DSSNASRTLMFNINTGAWDDELLGILDVPRSMLPRVTGSSEVVGDIHPEFLGKAIPIAGN
AGDQQAATYGNACLKPGMAKNTYGTGCFMLMNTGTEVRSSQNNLLSTVAWTTPSGRFYAL
EGSVFIAGAVVQWLRDGLGIIKAAPEVEQLALSVPDNGGVYLVPAFAGLGAPHWDQYARG
TMVGITRGATKAHIARAALESIALQTLDIMDCMQKDSGIKLAALRADGGATRNNLLMQFQ
ADVLGVPVERPKVTETTALGAAYLAGLATGFWKSEDEIATMWQLDRRFEPNMSDDKRQHL
VYEWQRAVERAKAWVEA
Or try a new SitesBLAST search
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