SitesBLAST
Comparing AZOBR_RS25905 FitnessBrowser__azobra:AZOBR_RS25905 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)
O86033 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
61% identity, 98% coverage: 5:496/501 of query aligns to 3:492/497 of O86033
- R82 (= R84) binding
- E83 (= E85) binding
- Y134 (= Y136) binding
- D243 (= D245) binding
- Q244 (= Q246) binding
P18157 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Bacillus subtilis (strain 168) (see paper)
52% identity, 98% coverage: 6:495/501 of query aligns to 4:490/496 of P18157
- H230 (≠ D231) mutation to R: Increased activity.
- F232 (≠ L233) mutation to S: Increased activity.
Q5HGD2 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Staphylococcus aureus (strain COL)
54% identity, 98% coverage: 6:495/501 of query aligns to 4:490/498 of Q5HGD2
- T12 (= T14) binding
- R16 (= R18) binding
- R82 (= R84) binding
- E83 (= E85) binding
- Y134 (= Y136) binding
- D244 (= D245) binding
- Q245 (= Q246) binding
- T266 (= T267) binding
- G309 (= G310) binding
- Q313 (≠ K314) binding
- G410 (= G415) binding
- N414 (= N419) binding
3ge1A 2.7 angstrom crystal structure of glycerol kinase (glpk) from staphylococcus aureus in complex with adp and glycerol
54% identity, 98% coverage: 6:495/501 of query aligns to 5:491/499 of 3ge1A
6udeB Crystal structure of glycerol kinase from elizabethkingia anophelis nuhp1 in complex with adp and glycerol
53% identity, 98% coverage: 7:496/501 of query aligns to 5:488/495 of 6udeB
- binding adenosine-5'-diphosphate: R16 (= R18), G262 (= G266), T263 (= T267), G306 (= G310), I309 (= I313), S323 (= S327), G406 (= G414), G407 (= G415), A408 (≠ M416)
- binding magnesium ion: G11 (= G13), T12 (= T14), T13 (= T15), S14 (= S16)
O34154 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Enterococcus faecalis (strain ATCC 700802 / V583) (see 2 papers)
52% identity, 99% coverage: 1:494/501 of query aligns to 1:490/501 of O34154
- M1 (= M1) modified: Initiator methionine, Removed
- H231 (≠ D231) modified: Phosphohistidine; by HPr
6k76A Glycerol kinase form thermococcus kodakarensis, complex structure with substrate.
54% identity, 98% coverage: 7:496/501 of query aligns to 1:476/485 of 6k76A
O34153 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Enterococcus casseliflavus (Enterococcus flavescens) (see 3 papers)
51% identity, 99% coverage: 1:494/501 of query aligns to 1:491/506 of O34153
- R84 (= R84) binding
- E85 (= E85) binding
- Y136 (= Y136) binding
- H232 (≠ D231) 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 (= D245) binding
- Q247 (= Q246) binding
P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
52% identity, 99% coverage: 1:496/501 of query aligns to 1:493/502 of P0A6F3
- M1 (= M1) modified: Initiator methionine, Removed
- T14 (= T14) binding ; binding
- R18 (= R18) binding
- S59 (≠ A59) 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 (≠ D66) 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 (= R84) binding ; binding
- E85 (= E85) binding ; binding
- Y136 (= Y136) binding ; binding
- G231 (≠ L233) 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 (≠ R235) modified: N6-malonyllysine
- G235 (vs. gap) 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 (= D245) binding ; binding
- Q247 (= Q246) binding
- T268 (= T267) binding
- G305 (= G304) mutation to S: In glpK22; abolishes glucose control of glycerol utilization.
- G311 (= G310) binding
- G412 (= G415) binding
- N416 (= N419) binding
- I475 (≠ M478) 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 (≠ K482) binding
- R480 (= R483) 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.
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
52% identity, 99% coverage: 3:496/501 of query aligns to 1:487/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T14), T13 (= T15), G261 (= G266), T262 (= T267), G305 (= G310), I308 (= I313), Q309 (≠ K314), A321 (= A326), G406 (= G415), N410 (= N419)
- binding glycerol: R82 (= R84), E83 (= E85), Y134 (= Y136), D240 (= D245), Q241 (= Q246), F265 (= F270)
1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
52% identity, 99% coverage: 3:496/501 of query aligns to 1:487/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: T12 (= T14), T13 (= T15), G261 (= G266), T262 (= T267), G305 (= G310), Q309 (≠ K314), A321 (= A326), G406 (= G415), A407 (≠ M416)
- binding glycerol: R82 (= R84), E83 (= E85), W102 (= W104), Y134 (= Y136), D240 (= D245), F265 (= F270)
1bwfO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
52% identity, 99% coverage: 3:496/501 of query aligns to 1:487/494 of 1bwfO
- binding phosphodifluoromethylphosphonic acid-adenylate ester: T12 (= T14), T13 (= T15), T262 (= T267), G305 (= G310), I308 (= I313), Q309 (≠ K314), A321 (= A326), G406 (= G415), N410 (= N419)
- binding glycerol: R82 (= R84), E83 (= E85), W102 (= W104), Y134 (= Y136), D240 (= D245), Q241 (= Q246), F265 (= F270)
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)
52% identity, 99% coverage: 3:496/501 of query aligns to 1:491/499 of 1bu6Y
3h3nX Glycerol kinase h232r with glycerol (see paper)
51% identity, 98% coverage: 2:494/501 of query aligns to 1:490/501 of 3h3nX
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)
52% identity, 99% coverage: 3:496/501 of query aligns to 1:491/498 of 1glfO
- binding adenosine-5'-diphosphate: R16 (= R18), G265 (= G266), T266 (= T267), G309 (= G310), G410 (= G415), A411 (≠ M416)
- binding glycerol: R82 (= R84), E83 (= E85), Y134 (= Y136), D244 (= D245)
- binding phosphate ion: G232 (≠ A236), 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)
52% identity, 99% coverage: 3:496/501 of query aligns to 1:491/498 of 1bo5O
1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
52% identity, 98% coverage: 6:496/501 of query aligns to 2:482/489 of 1gldG
- binding adenosine-5'-diphosphate: R14 (= R18), G256 (= G266), T257 (= T267), G300 (= G310), A316 (= A326), G401 (= G415), A402 (≠ M416), N405 (= N419)
- binding glyceraldehyde-3-phosphate: T10 (= T14), R80 (= R84), E81 (= E85), Y132 (= Y136), D235 (= D245), F260 (= F270)
- binding manganese (ii) ion: D7 (= D11), R14 (= R18)
1glcG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
52% identity, 98% coverage: 6:496/501 of query aligns to 2:482/489 of 1glcG
- binding adenosine-5'-diphosphate: G256 (= G266), T257 (= T267), G300 (= G310), A316 (= A326), G401 (= G415), A402 (≠ M416), N405 (= N419)
- binding glyceraldehyde-3-phosphate: T10 (= T14), R80 (= R84), E81 (= E85), W100 (= W104), Y132 (= Y136), D235 (= D245), F260 (= F270)
1glbG Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase (see paper)
52% identity, 98% coverage: 6:496/501 of query aligns to 2:482/489 of 1glbG
- binding adenosine-5'-diphosphate: R14 (= R18), G256 (= G266), T257 (= T267), G300 (= G310), I303 (= I313), A316 (= A326), G401 (= G415), A402 (≠ M416), N405 (= N419)
- binding glycerol: R80 (= R84), E81 (= E85), W100 (= W104), Y132 (= Y136), D235 (= D245), F260 (= F270)
5gn6A Crystal structure of glycerol kinase from trypanosoma brucei gambiense complexed with cumarin derivative-17b (see paper)
42% identity, 98% coverage: 6:498/501 of query aligns to 5:510/513 of 5gn6A
Query Sequence
>AZOBR_RS25905 FitnessBrowser__azobra:AZOBR_RS25905
MSEAGHVLAIDQGTTSTRAIVFDRRGVPAGVARREFAQHYPADGWVEHDPEDIWRDTVAV
MRGAVDEAGLSAADIAAIGITNQRETTVVWDRRTGEPVHRAIVWQDRRTSDLCRKLVEEG
CGPLVRRKTGLLIDSYFSATKIAWILDHVPGARERAERGELCFGTIDSFLLHRLTGGRVH
ATDATNASRSMVFDIHRQDWDDELLALFRIPRAMMPEVLDSSAEFGATEPDLLGRAIPIT
GIAGDQQAATFGQACFQPGMVKSTYGTGCFALLNTGDEPVESRSNMLTTVAYRLDGRTTY
ALEGSIFIAGAAIKWLRDGLGIITHASQTDDMATRVPDSHGVYLVPAFVGLGAPHWDPQA
RAAIFGLTLDAGPAHIARAALEAVAFQTRDLRDAMVSDWSAAHTATSDALRVDGGMAAND
WLCQFLADVLDLPVERPAVIETTALGAAGLAGLKVGVYRDQAALAGAWRCDRRFEPRMDA
AKRVRLYDGWLDAVRRVRRER
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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