SitesBLAST
Comparing HSERO_RS02220 FitnessBrowser__HerbieS:HSERO_RS02220 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)
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)
53% identity, 99% coverage: 1:485/490 of query aligns to 1:482/484 of P09099
- D6 (= D6) mutation to A: Loss of activity.
- MH 77:78 (= MH 80:81) binding
- D233 (= D237) mutation to A: Loss of activity.
2itmA Crystal structure of the e. Coli xylulose kinase complexed with xylulose (see paper)
51% identity, 99% coverage: 1:485/490 of query aligns to 1:474/476 of 2itmA
3ll3B The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
27% identity, 99% coverage: 3:488/490 of query aligns to 5:488/490 of 3ll3B
- binding adenosine-5'-diphosphate: G258 (= G258), T259 (= T259), G298 (≠ A299), P314 (≠ S315), G399 (= G400), F400 (≠ G401), K402 (≠ R403)
- binding 1-deoxy-d-xylulose-5-phosphate: H127 (≠ M127), N295 (≠ L296), G338 (≠ S339), E340 (= E341), A347 (≠ P348)
3ll3A The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
27% identity, 99% coverage: 3:488/490 of query aligns to 6:490/492 of 3ll3A
- binding adenosine-5'-triphosphate: G259 (= G258), T260 (= T259), G299 (≠ S300), P316 (≠ S315), L320 (≠ A318), G400 (= G399), G401 (= G400), F402 (≠ G401)
- binding 1-deoxy-d-xylulose-5-phosphate: H128 (≠ M127), N296 (≠ S297), E342 (= E341), A349 (≠ P348)
- binding d-xylulose: Q78 (= Q79), M79 (= M80), H80 (= H81), D238 (= D237), R343 (= R342)
3kzbA Crystal structure of xylulokinase from chromobacterium violaceum
31% identity, 89% coverage: 5:438/490 of query aligns to 9:453/498 of 3kzbA
3i8bA The crystal structure of xylulose kinase from bifidobacterium adolescentis
28% identity, 91% coverage: 1:445/490 of query aligns to 5:477/506 of 3i8bA
6k76A Glycerol kinase form thermococcus kodakarensis, complex structure with substrate.
25% identity, 93% coverage: 3:460/490 of query aligns to 2:456/485 of 6k76A
6udeB Crystal structure of glycerol kinase from elizabethkingia anophelis nuhp1 in complex with adp and glycerol
26% identity, 90% coverage: 1:442/490 of query aligns to 4:448/495 of 6udeB
- binding adenosine-5'-diphosphate: R16 (≠ K13), G262 (= G258), T263 (= T259), G306 (vs. gap), I309 (≠ L302), S323 (≠ A318), G406 (= G399), G407 (= G400), A408 (≠ G401)
- binding magnesium ion: G11 (= G8), T12 (= T9), T13 (≠ S10), S14 (≠ E11)
P18157 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Bacillus subtilis (strain 168) (see paper)
25% identity, 94% coverage: 3:461/490 of query aligns to 6:472/496 of P18157
- H230 (≠ W223) mutation to R: Increased activity.
- F232 (≠ L225) mutation to S: Increased activity.
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)
26% identity, 90% coverage: 3:442/490 of query aligns to 6:451/499 of 1bu6Y
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)
26% identity, 90% coverage: 3:442/490 of query aligns to 6:451/498 of 1glfO
- binding adenosine-5'-diphosphate: R16 (≠ K13), G265 (= G258), T266 (= T259), G309 (≠ A299), G410 (= G400), A411 (≠ G401)
- binding glycerol: R82 (≠ M80), E83 (≠ H81), Y134 (≠ G129), D244 (= D237)
- binding phosphate ion: G232 (≠ W223), G233 (= G224), R235 (= R226)
1bo5O Crystal structure of the complex between escherichia coli glycerol kinase and the allosteric regulator fructose 1,6-bisphosphate. (see paper)
26% identity, 90% coverage: 3:442/490 of query aligns to 6:451/498 of 1bo5O
P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
26% identity, 90% coverage: 3:442/490 of query aligns to 8:453/502 of P0A6F3
- T14 (= T9) binding ; binding
- R18 (≠ K13) binding
- S59 (≠ D54) 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 (vs. gap) 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 (≠ M80) binding ; binding
- E85 (≠ H81) binding ; binding
- Y136 (≠ G129) binding ; binding
- G231 (≠ A220) 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 (≠ A222) modified: N6-malonyllysine
- G235 (= G224) binding
- R237 (= R226) 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 (= D237) binding ; binding
- Q247 (≠ G238) binding
- T268 (= T259) binding
- G305 (vs. gap) mutation to S: In glpK22; abolishes glucose control of glycerol utilization.
- G311 (≠ A299) binding
- G412 (= G400) binding
- N416 (≠ S404) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 475 I→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.
- 479 binding
- 480 R→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)
25% identity, 90% coverage: 3:442/490 of query aligns to 4:442/489 of 1gldG
- binding adenosine-5'-diphosphate: R14 (≠ K13), G256 (= G258), T257 (= T259), G300 (≠ A299), A316 (≠ I320), G401 (= G400), A402 (≠ G401), N405 (≠ S404)
- binding glyceraldehyde-3-phosphate: T10 (= T9), R80 (≠ M80), E81 (≠ H81), Y132 (≠ G129), D235 (= D237), F260 (≠ L263)
- binding manganese (ii) ion: D7 (= D6), R14 (≠ K13)
1glcG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
25% identity, 90% coverage: 3:442/490 of query aligns to 4:442/489 of 1glcG
- binding adenosine-5'-diphosphate: G256 (= G258), T257 (= T259), G300 (≠ A299), A316 (≠ I320), G401 (= G400), A402 (≠ G401), N405 (≠ S404)
- binding glyceraldehyde-3-phosphate: T10 (= T9), R80 (≠ M80), E81 (≠ H81), W100 (= W99), Y132 (≠ G129), D235 (= D237), F260 (≠ L263)
1glbG Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase (see paper)
25% identity, 90% coverage: 3:442/490 of query aligns to 4:442/489 of 1glbG
- binding adenosine-5'-diphosphate: R14 (≠ K13), G256 (= G258), T257 (= T259), G300 (≠ A299), I303 (≠ L302), A316 (≠ I320), G401 (= G400), A402 (≠ G401), N405 (≠ S404)
- binding glycerol: R80 (≠ M80), E81 (≠ H81), W100 (= W99), Y132 (≠ G129), D235 (= D237), F260 (≠ L263)
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, 93% coverage: 3:460/490 of query aligns to 8:472/501 of O34154
- H231 (≠ Q221) modified: Phosphohistidine; by HPr
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5ya2A Crystal structure of lsrk-hpr complex with adp (see paper)
25% identity, 95% coverage: 3:469/490 of query aligns to 6:473/478 of 5ya2A
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
25% identity, 90% coverage: 3:442/490 of query aligns to 6:447/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T9), T13 (≠ S10), G261 (= G258), T262 (= T259), G305 (≠ A299), I308 (≠ L302), Q309 (≠ R303), A321 (≠ I320), G406 (= G400), N410 (≠ S404)
- binding glycerol: R82 (≠ M80), E83 (≠ H81), Y134 (≠ G129), D240 (= D237), Q241 (≠ G238), F265 (≠ L263)
1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
25% identity, 90% coverage: 3:442/490 of query aligns to 6:447/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: T12 (= T9), T13 (≠ S10), G261 (= G258), T262 (= T259), G305 (≠ A299), Q309 (≠ R303), A321 (≠ I320), G406 (= G400), A407 (≠ G401)
- binding glycerol: R82 (≠ M80), E83 (≠ H81), W102 (= W99), Y134 (≠ G129), D240 (= D237), F265 (≠ L263)
Query Sequence
>HSERO_RS02220 FitnessBrowser__HerbieS:HSERO_RS02220
MYLGIDLGTSEVKAVVIDAQGSLVALAGSTLNVARPHPRWSEQAPADWWQATCDTVAKLR
TQLGSERFGSIRAIGLSGQMHGAVLLDERDEVLRPAILWSDSRSAPECAELESRAPRLHG
IAGNLAMPGFTAPKLLWVARHEPQLFARIATVLLPKDWLRLKMTGRKVSDPSDAAGTLWL
DVEGRNWSDELLAASGMRRDQMPALVDGSAVSGSLLPEVAQAWGLRSDVIVAGGAGDGAA
SAVGIGAVKPGDGFLSLGTSGVLFVVNDRFRPNPGRAIHAFCHTLPQRWHQMSVMLSAAS
CLRWFCRLCSVDEKSLLAEIEQLDEQACNNAPLFLPYLSGERTPHNDPYATGVFHGLTPE
HQRAALGYAVLEGVAFGMVDGLDALRAAGTDVAELSLVGGGARSAYWAQLLADALQVRIV
THVGSEAGGALGAARLAWLADGGDEAEVCRKPAQQALYQPDPARHAALQARLQRYRAIYA
PFAPLHGEGH
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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