SitesBLAST
Comparing BPHYT_RS16080 FitnessBrowser__BFirm:BPHYT_RS16080 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)
54% identity, 98% coverage: 1:485/493 of query aligns to 1:483/484 of P09099
- D6 (= D6) mutation to A: Loss of activity.
- MH 77:78 (= MH 79:80) binding
- D233 (= D236) mutation to A: Loss of activity.
2itmA Crystal structure of the e. Coli xylulose kinase complexed with xylulose (see paper)
53% identity, 98% coverage: 1:485/493 of query aligns to 1:475/476 of 2itmA
3ll3B The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
26% identity, 100% coverage: 3:493/493 of query aligns to 5:483/490 of 3ll3B
- binding adenosine-5'-diphosphate: G258 (= G257), T259 (= T258), G298 (≠ A298), P314 (vs. gap), G399 (= G399), F400 (≠ G400), K402 (≠ R402)
- binding 1-deoxy-d-xylulose-5-phosphate: H127 (≠ M126), N295 (≠ L295), G338 (≠ S338), E340 (= E340), A347 (≠ P347)
3ll3A The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
26% identity, 100% coverage: 3:493/493 of query aligns to 6:485/492 of 3ll3A
- binding adenosine-5'-triphosphate: G259 (= G257), T260 (= T258), G299 (≠ A298), P316 (vs. gap), L320 (= L316), G400 (= G398), G401 (= G399), F402 (≠ G400)
- binding 1-deoxy-d-xylulose-5-phosphate: H128 (≠ M126), N296 (≠ L295), E342 (= E340), A349 (≠ P347)
- binding d-xylulose: Q78 (= Q78), M79 (= M79), H80 (= H80), D238 (= D236), R343 (= R341)
3kzbA Crystal structure of xylulokinase from chromobacterium violaceum
31% identity, 84% coverage: 5:417/493 of query aligns to 9:428/498 of 3kzbA
3i8bA The crystal structure of xylulose kinase from bifidobacterium adolescentis
28% identity, 92% coverage: 1:452/493 of query aligns to 5:479/506 of 3i8bA
P18157 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Bacillus subtilis (strain 168) (see paper)
24% identity, 97% coverage: 3:482/493 of query aligns to 6:490/496 of P18157
- H230 (≠ F222) mutation to R: Increased activity.
- F232 (≠ L224) mutation to S: Increased activity.
6udeB Crystal structure of glycerol kinase from elizabethkingia anophelis nuhp1 in complex with adp and glycerol
26% identity, 94% coverage: 1:463/493 of query aligns to 4:472/495 of 6udeB
- binding adenosine-5'-diphosphate: R16 (≠ K13), G262 (= G257), T263 (= T258), G306 (≠ A298), I309 (≠ L301), S323 (≠ T310), G406 (= G398), G407 (= G399), A408 (≠ G400)
- binding magnesium ion: G11 (= G8), T12 (= T9), T13 (≠ S10), S14 (≠ E11)
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, 89% coverage: 3:441/493 of query aligns to 8:452/501 of O34154
- H231 (≠ R220) 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.
25% identity, 89% coverage: 3:440/493 of query aligns to 2:435/485 of 6k76A
3ge1A 2.7 angstrom crystal structure of glycerol kinase (glpk) from staphylococcus aureus in complex with adp and glycerol
24% identity, 89% coverage: 3:441/493 of query aligns to 7:452/499 of 3ge1A
Q5HGD2 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Staphylococcus aureus (strain COL)
24% identity, 89% coverage: 3:441/493 of query aligns to 6:451/498 of Q5HGD2
- T12 (= T9) binding
- R16 (≠ K13) binding
- R82 (≠ M79) binding
- E83 (≠ H80) binding
- Y134 (≠ G128) binding
- D244 (= D236) binding
- Q245 (≠ N237) binding
- T266 (= T258) binding
- G309 (≠ A298) binding
- Q313 (≠ R302) binding
- G410 (= G399) binding
- N414 (≠ S403) binding
1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
23% identity, 93% coverage: 3:459/493 of query aligns to 4:462/489 of 1gldG
- binding adenosine-5'-diphosphate: R14 (≠ K13), G256 (= G260), T257 (≠ V261), G300 (≠ A298), A316 (≠ I319), G401 (= G399), A402 (≠ G400), N405 (≠ S403)
- binding glyceraldehyde-3-phosphate: T10 (= T9), R80 (≠ M79), E81 (≠ H80), Y132 (≠ G128), D235 (= D236), F260 (≠ V264)
- 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)
23% identity, 93% coverage: 3:459/493 of query aligns to 4:462/489 of 1glcG
- binding adenosine-5'-diphosphate: G256 (= G260), T257 (≠ V261), G300 (≠ A298), A316 (≠ I319), G401 (= G399), A402 (≠ G400), N405 (≠ S403)
- binding glyceraldehyde-3-phosphate: T10 (= T9), R80 (≠ M79), E81 (≠ H80), W100 (= W98), Y132 (≠ G128), D235 (= D236), F260 (≠ V264)
1glbG Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase (see paper)
23% identity, 93% coverage: 3:459/493 of query aligns to 4:462/489 of 1glbG
- binding adenosine-5'-diphosphate: R14 (≠ K13), G256 (= G260), T257 (≠ V261), G300 (≠ A298), I303 (≠ L301), A316 (≠ I319), G401 (= G399), A402 (≠ G400), N405 (≠ S403)
- binding glycerol: R80 (≠ M79), E81 (≠ H80), W100 (= W98), Y132 (≠ G128), D235 (= D236), F260 (≠ V264)
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)
24% identity, 93% coverage: 3:459/493 of query aligns to 6:471/498 of 1glfO
- binding adenosine-5'-diphosphate: R16 (≠ K13), G265 (= G260), T266 (≠ V261), G309 (≠ A298), G410 (= G399), A411 (≠ G400)
- binding glycerol: R82 (≠ M79), E83 (≠ H80), Y134 (≠ G128), D244 (= D236)
- binding phosphate ion: G232 (≠ D226), G233 (= G227), R235 (≠ I229)
1bo5O Crystal structure of the complex between escherichia coli glycerol kinase and the allosteric regulator fructose 1,6-bisphosphate. (see paper)
24% identity, 93% coverage: 3:459/493 of query aligns to 6:471/498 of 1bo5O
P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
24% identity, 93% coverage: 3:459/493 of query aligns to 8:473/502 of P0A6F3
- T14 (= T9) binding ; binding
- R18 (≠ K13) binding
- S59 (≠ T54) 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 (= A61) 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 (≠ M79) binding ; binding
- E85 (≠ H80) binding ; binding
- Y136 (≠ G128) binding ; binding
- G231 (= G223) 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 (≠ S225) modified: N6-malonyllysine
- G235 (= G227) binding
- R237 (≠ I229) 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 (= D236) binding ; binding
- Q247 (≠ N237) binding
- T268 (≠ V261) binding
- G305 (≠ S292) mutation to S: In glpK22; abolishes glucose control of glycerol utilization.
- G311 (≠ A298) binding
- G412 (= G399) binding
- N416 (≠ S403) 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.
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
23% identity, 93% coverage: 3:459/493 of query aligns to 6:467/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T9), T13 (≠ S10), G261 (= G260), T262 (≠ V261), G305 (≠ A298), I308 (≠ L301), Q309 (≠ R302), A321 (≠ I319), G406 (= G399), N410 (≠ S403)
- binding glycerol: R82 (≠ M79), E83 (≠ H80), Y134 (≠ G128), D240 (= D236), Q241 (≠ N237), F265 (≠ V264)
1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
23% identity, 93% coverage: 3:459/493 of query aligns to 6:467/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: T12 (= T9), T13 (≠ S10), G261 (= G260), T262 (≠ V261), G305 (≠ A298), Q309 (≠ R302), A321 (≠ I319), G406 (= G399), A407 (≠ G400)
- binding glycerol: R82 (≠ M79), E83 (≠ H80), W102 (= W98), Y134 (≠ G128), D240 (= D236), F265 (≠ V264)
Query Sequence
>BPHYT_RS16080 FitnessBrowser__BFirm:BPHYT_RS16080
MYLGIDLGTSEVKVLLLASDGRVIGTAGSPFTVSRPHQRWAEQNPEDWWAGTRTALAALR
AKHPDEFAQIRGIGLSGQMHGAVLLDAQDRVLRPAILWNDMRSDKECAELTERAPELHSV
AGNLAMPGFTAPKLLWVARHEPEIFAQTACVLLPKDYLRLQLTGGKVSDPSDAAGTLWLD
VAKRDWSDSLLAACNMSRAQMPSLAEGSEPSGTLLPSVAREFGLSDGVIVAAGGGDNATS
AIGIGATQPGDGFVSLGTSGVLCVVGDSFRPNPASAVHAFCHAIPDRWHQMSVVLSAASC
LRWVCKLTSTDEPTLLAEIEALPADALNTAPLFLPYLSGERTPHNDPYAQGVFFGMTHAT
DRALLGYAVLEGVTLALTDGLDALRAAGTEAKALSLLGGGARSDYWAQLLADALDTATRK
HGGGETGAALGAARLGWLAAGGDPATVLTKPPIAKEFTPNPRRHAELRARLEAYRALYRH
VRPLFDPARQPLA
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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