SitesBLAST
Comparing GFF2719 FitnessBrowser__psRCH2:GFF2719 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)
P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
74% identity, 99% coverage: 6:501/502 of query aligns to 4:499/502 of P0A6F3
- T14 (= T16) binding ; binding
- R18 (= R20) binding
- S59 (≠ G61) 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 (= A68) 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 (= R86) binding ; binding
- E85 (= E87) binding ; binding
- Y136 (= Y138) binding ; binding
- G231 (= G233) 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 (≠ G235) modified: N6-malonyllysine
- G235 (≠ S237) binding
- R237 (≠ G239) 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 (= Q249) binding
- T268 (= T270) binding
- G305 (= G307) mutation to S: In glpK22; abolishes glucose control of glycerol utilization.
- G311 (= G313) binding
- G412 (= G414) binding
- N416 (= N418) binding
- I475 (≠ C477) 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 (≠ Q481) binding
- R480 (= R482) 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)
74% identity, 99% coverage: 6:501/502 of query aligns to 2:497/498 of 1glfO
- binding adenosine-5'-diphosphate: R16 (= R20), G265 (= G269), T266 (= T270), G309 (= G313), G410 (= G414), A411 (= A415)
- binding glycerol: R82 (= R86), E83 (= E87), Y134 (= Y138), D244 (= D248)
- binding phosphate ion: G232 (≠ Q236), G233 (≠ S237), R235 (≠ G239)
1bo5O Crystal structure of the complex between escherichia coli glycerol kinase and the allosteric regulator fructose 1,6-bisphosphate. (see paper)
74% identity, 99% coverage: 6:501/502 of query aligns to 2:497/498 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)
73% identity, 99% coverage: 6:501/502 of query aligns to 2:497/499 of 1bu6Y
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
74% identity, 99% coverage: 6:501/502 of query aligns to 2:493/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T16), T13 (= T17), G261 (= G269), T262 (= T270), G305 (= G313), I308 (≠ V316), Q309 (= Q317), A321 (≠ S329), G406 (= G414), N410 (= N418)
- binding glycerol: R82 (= R86), E83 (= E87), Y134 (= Y138), D240 (= D248), Q241 (= Q249), F265 (= F273)
1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
74% identity, 99% coverage: 6:501/502 of query aligns to 2:493/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: T12 (= T16), T13 (= T17), G261 (= G269), T262 (= T270), G305 (= G313), Q309 (= Q317), A321 (≠ S329), G406 (= G414), A407 (= A415)
- binding glycerol: R82 (= R86), E83 (= E87), W102 (= W106), Y134 (= Y138), D240 (= D248), F265 (= F273)
1bwfO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
74% identity, 99% coverage: 6:501/502 of query aligns to 2:493/494 of 1bwfO
- binding phosphodifluoromethylphosphonic acid-adenylate ester: T12 (= T16), T13 (= T17), T262 (= T270), G305 (= G313), I308 (≠ V316), Q309 (= Q317), A321 (≠ S329), G406 (= G414), N410 (= N418)
- binding glycerol: R82 (= R86), E83 (= E87), W102 (= W106), Y134 (= Y138), D240 (= D248), Q241 (= Q249), F265 (= F273)
1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
73% identity, 99% coverage: 7:501/502 of query aligns to 1:488/489 of 1gldG
- binding adenosine-5'-diphosphate: R14 (= R20), G256 (= G269), T257 (= T270), G300 (= G313), A316 (≠ S329), G401 (= G414), A402 (= A415), N405 (= N418)
- binding glyceraldehyde-3-phosphate: T10 (= T16), R80 (= R86), E81 (= E87), Y132 (= Y138), D235 (= D248), F260 (= F273)
- binding manganese (ii) ion: D7 (= D13), R14 (= R20)
1glcG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
73% identity, 99% coverage: 7:501/502 of query aligns to 1:488/489 of 1glcG
- binding adenosine-5'-diphosphate: G256 (= G269), T257 (= T270), G300 (= G313), A316 (≠ S329), G401 (= G414), A402 (= A415), N405 (= N418)
- binding glyceraldehyde-3-phosphate: T10 (= T16), R80 (= R86), E81 (= E87), W100 (= W106), Y132 (= Y138), D235 (= D248), F260 (= F273)
1glbG Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase (see paper)
73% identity, 99% coverage: 7:501/502 of query aligns to 1:488/489 of 1glbG
- binding adenosine-5'-diphosphate: R14 (= R20), G256 (= G269), T257 (= T270), G300 (= G313), I303 (≠ V316), A316 (≠ S329), G401 (= G414), A402 (= A415), N405 (= N418)
- binding glycerol: R80 (= R86), E81 (= E87), W100 (= W106), Y132 (= Y138), D235 (= D248), F260 (= F273)
P18157 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Bacillus subtilis (strain 168) (see paper)
60% identity, 97% coverage: 8:493/502 of query aligns to 4:489/496 of P18157
- H230 (≠ S234) mutation to R: Increased activity.
- F232 (≠ Q236) mutation to S: Increased activity.
Q5HGD2 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Staphylococcus aureus (strain COL)
59% identity, 98% coverage: 6:497/502 of query aligns to 2:493/498 of Q5HGD2
- T12 (= T16) binding
- R16 (= R20) binding
- R82 (= R86) binding
- E83 (= E87) binding
- Y134 (= Y138) binding
- D244 (= D248) binding
- Q245 (= Q249) binding
- T266 (= T270) binding
- G309 (= G313) binding
- Q313 (= Q317) binding
- G410 (= G414) binding
- N414 (= N418) binding
3ge1A 2.7 angstrom crystal structure of glycerol kinase (glpk) from staphylococcus aureus in complex with adp and glycerol
59% identity, 98% coverage: 6:497/502 of query aligns to 3:494/499 of 3ge1A
3h3nX Glycerol kinase h232r with glycerol (see paper)
57% identity, 98% coverage: 6:499/502 of query aligns to 3:496/501 of 3h3nX
O34153 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Enterococcus casseliflavus (Enterococcus flavescens) (see 3 papers)
57% identity, 98% coverage: 6:499/502 of query aligns to 4:497/506 of O34153
- R84 (= R86) binding
- E85 (= E87) binding
- Y136 (= Y138) binding
- H232 (≠ S234) 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 (= Q249) binding
6udeB Crystal structure of glycerol kinase from elizabethkingia anophelis nuhp1 in complex with adp and glycerol
56% identity, 99% coverage: 5:502/502 of query aligns to 1:495/495 of 6udeB
- binding adenosine-5'-diphosphate: R16 (= R20), G262 (= G269), T263 (= T270), G306 (= G313), I309 (≠ V316), S323 (≠ L330), G406 (= G413), G407 (= G414), A408 (= A415)
- binding magnesium ion: G11 (= G15), T12 (= T16), T13 (= T17), S14 (= S18)
O34154 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Enterococcus faecalis (strain ATCC 700802 / V583) (see 2 papers)
57% identity, 98% coverage: 6:499/502 of query aligns to 4:496/501 of O34154
- H231 (≠ S234) modified: Phosphohistidine; by HPr
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6k76A Glycerol kinase form thermococcus kodakarensis, complex structure with substrate.
54% identity, 98% coverage: 9:501/502 of query aligns to 1:482/485 of 6k76A
O86033 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
51% identity, 97% coverage: 8:496/502 of query aligns to 4:493/497 of O86033
- R82 (= R86) binding
- E83 (= E87) binding
- Y134 (= Y138) binding
- D243 (= D248) binding
- Q244 (= Q249) binding
5gn6A Crystal structure of glycerol kinase from trypanosoma brucei gambiense complexed with cumarin derivative-17b (see paper)
45% identity, 99% coverage: 7:501/502 of query aligns to 4:513/513 of 5gn6A
Query Sequence
>GFF2719 FitnessBrowser__psRCH2:GFF2719
MSDQNKQFIVALDQGTTSSRAIVLDRNANVVTIAQREFAQIYPQPSWVEHDPMEIWATQS
GVFVEALAQAGITNEQVAAIGITNQRETAIVWDKITGRPIYNAIVWQSRQSTPICDQLKR
DGMEEHIRKTTGLVIDPYFSGTKIKWILDHVEGSRERARRGELLFGTVDCWLIWKMTQGK
AHVTDYTNASRTLLFDIHKLDWDPVMLEALDIPREMLPEVRSSSEIYGHAYIGSGQSTGI
PIAGIAGDQQAALFGQMCVELGQAKNTYGTGCFLLMNTGTKAVQSEHGLLTTIACGPRGE
VNYALEGAIFNGGSTVQWLRDELKVLNESLDSEYFATKVPDSNGIYLVPAFTGLGAPYWD
PRARGALFGLTRGVKVDHLIRAALESIAYQTRDVLDAMQQDAGERLRALRVDGGAVANNF
LMQFQADLLGTQVERPQMKETTALGAAYLAGLATGFWSDLDELRSKSSIERVFEPACGSE
QREALYRGWQKAVDRTRNWAED
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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