SitesBLAST
Comparing WP_008412468.1 NCBI__GCF_000315365.1:WP_008412468.1 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)
40% identity, 98% coverage: 4:503/510 of query aligns to 1:483/484 of P09099
- D6 (= D9) mutation to A: Loss of activity.
- MH 77:78 (= MH 81:82) binding substrate
- D233 (= D240) mutation to A: Loss of activity.
2itmA Crystal structure of the e. Coli xylulose kinase complexed with xylulose (see paper)
39% identity, 98% coverage: 4:503/510 of query aligns to 1:475/476 of 2itmA
3ll3B The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
27% identity, 98% coverage: 6:507/510 of query aligns to 5:490/490 of 3ll3B
- binding adenosine-5'-diphosphate: G258 (= G261), T259 (= T262), G298 (= G303), P314 (= P327), G399 (= G413), F400 (≠ G414), K402 (≠ R416)
- binding 1-deoxy-d-xylulose-5-phosphate: H127 (≠ L130), N295 (≠ A300), G338 (≠ S352), E340 (= E354), A347 (≠ P361)
3ll3A The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
28% identity, 98% coverage: 6:507/510 of query aligns to 6:492/492 of 3ll3A
- binding adenosine-5'-triphosphate: G259 (= G261), T260 (= T262), G299 (= G303), P316 (= P327), L320 (≠ M331), G400 (= G412), G401 (= G413), F402 (≠ G414)
- binding 1-deoxy-d-xylulose-5-phosphate: H128 (≠ L130), N296 (≠ A300), E342 (= E354), A349 (≠ P361)
- binding d-xylulose: Q78 (= Q80), M79 (= M81), H80 (= H82), D238 (= D240), R343 (= R355)
P18157 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Bacillus subtilis (strain 168) (see paper)
29% identity, 90% coverage: 1:461/510 of query aligns to 1:458/496 of P18157
- H230 (≠ T226) mutation to R: Increased activity.
- F232 (≠ L228) mutation to S: Increased activity.
6k76A Glycerol kinase form thermococcus kodakarensis, complex structure with substrate.
28% identity, 89% coverage: 6:461/510 of query aligns to 2:443/485 of 6k76A
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)
27% identity, 95% coverage: 2:485/510 of query aligns to 2:482/499 of 1bu6Y
P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
27% identity, 95% coverage: 2:485/510 of query aligns to 4:484/502 of P0A6F3
- T14 (= T12) binding ADP; binding sn-glycerol 3-phosphate
- R18 (≠ K16) binding ADP
- S59 (≠ G57) 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 (≠ S64) 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 (≠ M81) binding glycerol; binding sn-glycerol 3-phosphate
- E85 (≠ H82) binding glycerol; binding sn-glycerol 3-phosphate
- Y136 (≠ A129) binding glycerol; binding sn-glycerol 3-phosphate
- G231 (≠ R221) 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 (≠ A223) modified: N6-malonyllysine
- G235 (≠ E225) binding beta-D-fructose 1,6-bisphosphate
- R237 (≠ G231) binding beta-D-fructose 1,6-bisphosphate; 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 (= D240) binding glycerol; binding sn-glycerol 3-phosphate
- Q247 (≠ N241) binding glycerol
- T268 (= T262) binding ADP
- G305 (= G296) mutation to S: In glpK22; abolishes glucose control of glycerol utilization.
- G311 (= G302) binding ADP
- G412 (= G413) binding ADP
- N416 (≠ S417) binding ADP
- I475 (≠ V476) 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 (≠ Q480) binding Zn(2+)
- R480 (≠ N481) 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)
27% identity, 95% coverage: 2:485/510 of query aligns to 2:482/498 of 1glfO
- binding adenosine-5'-diphosphate: R16 (≠ K16), G265 (= G261), T266 (= T262), G309 (= G302), G410 (= G413), A411 (≠ G414)
- binding glycerol: R82 (≠ M81), E83 (≠ H82), Y134 (≠ A129), D244 (= D240)
- binding phosphate ion: G232 (≠ A224), G233 (≠ E225), R235 (≠ G231)
1bo5O Crystal structure of the complex between escherichia coli glycerol kinase and the allosteric regulator fructose 1,6-bisphosphate. (see paper)
27% identity, 95% coverage: 2:485/510 of query aligns to 2:482/498 of 1bo5O
O34154 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Enterococcus faecalis (strain ATCC 700802 / V583) (see 2 papers)
26% identity, 95% coverage: 2:486/510 of query aligns to 4:484/501 of O34154
- H231 (≠ G222) modified: Phosphohistidine; by HPr
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
27% identity, 95% coverage: 2:485/510 of query aligns to 2:478/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T12), T13 (= T13), G261 (= G261), T262 (= T262), G305 (= G302), I308 (≠ L305), Q309 (≠ R306), A321 (≠ P327), G406 (= G413), N410 (≠ S417)
- binding glycerol: R82 (≠ M81), E83 (≠ H82), Y134 (≠ A129), D240 (= D240), Q241 (≠ N241), F265 (≠ V265)
1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
27% identity, 95% coverage: 2:485/510 of query aligns to 2:478/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: T12 (= T12), T13 (= T13), G261 (= G261), T262 (= T262), G305 (= G302), Q309 (≠ R306), A321 (≠ P327), G406 (= G413), A407 (≠ G414)
- binding glycerol: R82 (≠ M81), E83 (≠ H82), W102 (= W100), Y134 (≠ A129), D240 (= D240), F265 (≠ V265)
1bwfO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
27% identity, 95% coverage: 2:485/510 of query aligns to 2:478/494 of 1bwfO
- binding phosphodifluoromethylphosphonic acid-adenylate ester: T12 (= T12), T13 (= T13), T262 (= T262), G305 (= G302), I308 (≠ L305), Q309 (≠ R306), A321 (≠ P327), G406 (= G413), N410 (≠ S417)
- binding glycerol: R82 (≠ M81), E83 (≠ H82), W102 (= W100), Y134 (≠ A129), D240 (= D240), Q241 (≠ N241), F265 (≠ V265)
3kzbA Crystal structure of xylulokinase from chromobacterium violaceum
31% identity, 87% coverage: 8:451/510 of query aligns to 9:449/498 of 3kzbA
1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
27% identity, 94% coverage: 5:485/510 of query aligns to 3:473/489 of 1gldG
- binding adenosine-5'-diphosphate: R14 (≠ K16), G256 (= G261), T257 (= T262), G300 (= G302), A316 (≠ P327), G401 (= G413), A402 (≠ G414), N405 (≠ S417)
- binding glyceraldehyde-3-phosphate: T10 (= T12), R80 (≠ M81), E81 (≠ H82), Y132 (≠ A129), D235 (= D240), F260 (≠ V265)
- binding manganese (ii) ion: D7 (= D9), R14 (≠ K16)
1glcG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
27% identity, 94% coverage: 5:485/510 of query aligns to 3:473/489 of 1glcG
- binding adenosine-5'-diphosphate: G256 (= G261), T257 (= T262), G300 (= G302), A316 (≠ P327), G401 (= G413), A402 (≠ G414), N405 (≠ S417)
- binding glyceraldehyde-3-phosphate: T10 (= T12), R80 (≠ M81), E81 (≠ H82), W100 (= W100), Y132 (≠ A129), D235 (= D240), F260 (≠ V265)
1glbG Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase (see paper)
27% identity, 94% coverage: 5:485/510 of query aligns to 3:473/489 of 1glbG
- binding adenosine-5'-diphosphate: R14 (≠ K16), G256 (= G261), T257 (= T262), G300 (= G302), I303 (≠ L305), A316 (≠ P327), G401 (= G413), A402 (≠ G414), N405 (≠ S417)
- binding glycerol: R80 (≠ M81), E81 (≠ H82), W100 (= W100), Y132 (≠ A129), D235 (= D240), F260 (≠ V265)
6udeB Crystal structure of glycerol kinase from elizabethkingia anophelis nuhp1 in complex with adp and glycerol
29% identity, 90% coverage: 2:461/510 of query aligns to 2:455/495 of 6udeB
- binding adenosine-5'-diphosphate: R16 (≠ K16), G262 (= G261), T263 (= T262), G306 (= G302), I309 (≠ L305), S323 (= S332), G406 (= G412), G407 (= G413), A408 (≠ G414)
- binding magnesium ion: G11 (= G11), T12 (= T12), T13 (= T13), S14 (≠ G14)
O34153 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Enterococcus casseliflavus (Enterococcus flavescens) (see 3 papers)
27% identity, 95% coverage: 2:486/510 of query aligns to 4:485/506 of O34153
- R84 (≠ M81) binding glycerol
- E85 (≠ H82) binding glycerol
- Y136 (≠ G132) binding glycerol
- H232 (≠ G222) 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 (= D240) binding glycerol
- Q247 (≠ N241) binding glycerol
Query Sequence
>WP_008412468.1 NCBI__GCF_000315365.1:WP_008412468.1
MQSLFLGIDIGTTGVKALVMDEQGRVVAQATREYPLHVPRPGWAEQNPEDWYKAACGAIA
TIISKGISPGQIQGIGLTGQMHGSVFLDAQGKVIREAILWCDQRTADECRQITDLVGESK
LIELVSNPALAGFTAPKILWLRNHEPENYKRVAKVLLPKDYISWRMTGVFATDVSDASGM
LLLDVVNRKWSSEMLAALEIPAAWLAEVFESPDVVGRVSARGAAETGLPEGIPVVAGAGD
NAAGAVGNGIISPGMATASLGTSGVVFTPSQTPAVDRAGRLHTFCHAVPGQWHLMGVTMA
AGGSLRWYRDTFAGEERAVAQLTGRDPYELMSDEAALIEPGADGLIFLPYLSGERTPHAD
PLARGVFVGMNLKHTKGHFVRSIMEGVAFSLKDTLEIMSGLGIALNDLRITGGGGRSAVW
RQILADVFNMPLQVMENSDGPAYGAAILGAVGAGCWQSVTEAVAATCSRQQLQEVVPIPQ
NAARYQKIYQIYIDTYPPLQPLFKRLSEVN
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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