SitesBLAST
Comparing WP_022529344.1 NCBI__GCF_000469325.1:WP_022529344.1 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)
3ll3A The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
42% identity, 96% coverage: 3:500/521 of query aligns to 3:488/492 of 3ll3A
- binding adenosine-5'-triphosphate: G259 (= G262), T260 (= T263), G299 (= G302), P316 (≠ T319), L320 (≠ M323), G400 (= G412), G401 (= G413), F402 (= F414)
- binding 1-deoxy-d-xylulose-5-phosphate: H128 (= H131), N296 (= N299), E342 (= E354), A349 (= A361)
- binding d-xylulose: Q78 (≠ A81), M79 (= M82), H80 (= H83), D238 (= D241), R343 (= R355)
3ll3B The crystal structure of ligand bound xylulose kinase from lactobacillus acidophilus
42% identity, 96% coverage: 3:500/521 of query aligns to 2:486/490 of 3ll3B
- binding adenosine-5'-diphosphate: G258 (= G262), T259 (= T263), G298 (= G302), P314 (≠ Y328), G399 (= G413), F400 (= F414), K402 (≠ R416)
- binding 1-deoxy-d-xylulose-5-phosphate: H127 (= H131), N295 (= N299), G338 (= G352), E340 (= E354), A347 (= A361)
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)
29% identity, 94% coverage: 6:496/521 of query aligns to 3:479/484 of P09099
- D6 (= D9) mutation to A: Loss of activity.
- MH 77:78 (= MH 82:83) binding substrate
- D233 (= D241) mutation to A: Loss of activity.
2itmA Crystal structure of the e. Coli xylulose kinase complexed with xylulose (see paper)
29% identity, 94% coverage: 6:496/521 of query aligns to 3:471/476 of 2itmA
5ya1A Crystal structure of lsrk-hpr complex with atp (see paper)
27% identity, 92% coverage: 4:484/521 of query aligns to 4:474/478 of 5ya1A
5ya2A Crystal structure of lsrk-hpr complex with adp (see paper)
27% identity, 92% coverage: 4:484/521 of query aligns to 4:474/478 of 5ya2A
6udeB Crystal structure of glycerol kinase from elizabethkingia anophelis nuhp1 in complex with adp and glycerol
27% identity, 88% coverage: 5:463/521 of query aligns to 5:457/495 of 6udeB
- binding adenosine-5'-diphosphate: R16 (≠ K16), G262 (= G262), T263 (= T263), G306 (= G302), I309 (≠ F305), S323 (≠ Y328), G406 (= G412), G407 (= G413), A408 (≠ F414)
- binding magnesium ion: G11 (= G11), T12 (= T12), T13 (= T13), S14 (= S14)
1gldG Cation promoted association (cpa) of a regulatory and target protein is controlled by phosphorylation (see paper)
27% identity, 91% coverage: 3:474/521 of query aligns to 1:462/489 of 1gldG
- binding adenosine-5'-diphosphate: R14 (≠ K16), G256 (= G262), T257 (= T263), G300 (= G302), A316 (≠ Q322), G401 (= G413), A402 (≠ F414), N405 (≠ S417)
- binding glyceraldehyde-3-phosphate: T10 (= T12), R80 (≠ M82), E81 (≠ H83), Y132 (≠ M133), D235 (= D241), F260 (≠ A266)
- 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, 91% coverage: 3:474/521 of query aligns to 1:462/489 of 1glcG
- binding adenosine-5'-diphosphate: G256 (= G262), T257 (= T263), G300 (= G302), A316 (≠ Q322), G401 (= G413), A402 (≠ F414), N405 (≠ S417)
- binding glyceraldehyde-3-phosphate: T10 (= T12), R80 (≠ M82), E81 (≠ H83), W100 (= W101), Y132 (≠ M133), D235 (= D241), F260 (≠ A266)
1glbG Structure of the regulatory complex of escherichia coli iiiglc with glycerol kinase (see paper)
27% identity, 91% coverage: 3:474/521 of query aligns to 1:462/489 of 1glbG
- binding adenosine-5'-diphosphate: R14 (≠ K16), G256 (= G262), T257 (= T263), G300 (= G302), I303 (≠ F305), A316 (≠ Q322), G401 (= G413), A402 (≠ F414), N405 (≠ S417)
- binding glycerol: R80 (≠ M82), E81 (≠ H83), W100 (= W101), Y132 (≠ M133), D235 (= D241), F260 (≠ A266)
P18157 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Bacillus subtilis (strain 168) (see paper)
25% identity, 91% coverage: 1:475/521 of query aligns to 1:472/496 of P18157
- H230 (vs. gap) mutation to R: Increased activity.
- F232 (≠ I229) mutation to S: Increased activity.
Q5HGD2 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Staphylococcus aureus (strain COL)
28% identity, 87% coverage: 1:455/521 of query aligns to 1:452/498 of Q5HGD2
- T12 (= T12) binding ADP
- R16 (≠ K16) binding ADP
- R82 (≠ M82) binding glycerol
- E83 (≠ H83) binding glycerol
- Y134 (≠ M133) binding glycerol
- D244 (= D241) binding glycerol
- Q245 (≠ G242) binding glycerol
- T266 (= T263) binding ADP
- G309 (= G302) binding ADP
- Q313 (≠ R306) binding ADP
- G410 (= G413) binding ADP
- N414 (≠ S417) binding ADP
3ge1A 2.7 angstrom crystal structure of glycerol kinase (glpk) from staphylococcus aureus in complex with adp and glycerol
28% identity, 87% coverage: 1:455/521 of query aligns to 2:453/499 of 3ge1A
1gllO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
27% identity, 91% coverage: 3:474/521 of query aligns to 3:467/494 of 1gllO
- binding phosphomethylphosphonic acid adenylate ester: T12 (= T12), T13 (= T13), G261 (= G262), T262 (= T263), G305 (= G302), I308 (≠ F305), Q309 (≠ R306), A321 (≠ Q322), G406 (= G413), N410 (≠ S417)
- binding glycerol: R82 (≠ M82), E83 (≠ H83), Y134 (≠ M133), D240 (= D241), Q241 (≠ G242), F265 (≠ A266)
1gljO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
27% identity, 91% coverage: 3:474/521 of query aligns to 3:467/494 of 1gljO
- binding gamma-arsono-beta, gamma-methyleneadenosine-5'-diphosphate: T12 (= T12), T13 (= T13), G261 (= G262), T262 (= T263), G305 (= G302), Q309 (≠ R306), A321 (≠ Q322), G406 (= G413), A407 (≠ F414)
- binding glycerol: R82 (≠ M82), E83 (≠ H83), W102 (= W101), Y134 (≠ M133), D240 (= D241), F265 (≠ A266)
1bwfO Escherichia coli glycerol kinase mutant with bound atp analog showing substantial domain motion (see paper)
27% identity, 91% coverage: 3:474/521 of query aligns to 3:467/494 of 1bwfO
- binding phosphodifluoromethylphosphonic acid-adenylate ester: T12 (= T12), T13 (= T13), T262 (= T263), G305 (= G302), I308 (≠ F305), Q309 (≠ R306), A321 (≠ Q322), G406 (= G413), N410 (≠ S417)
- binding glycerol: R82 (≠ M82), E83 (≠ H83), W102 (= W101), Y134 (≠ M133), D240 (= D241), Q241 (≠ G242), F265 (≠ A266)
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, 91% coverage: 3:474/521 of query aligns to 3:471/499 of 1bu6Y
O34154 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Enterococcus faecalis (strain ATCC 700802 / V583) (see 2 papers)
27% identity, 88% coverage: 3:463/521 of query aligns to 5:461/501 of O34154
- H231 (≠ A224) 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.
28% identity, 85% coverage: 5:449/521 of query aligns to 1:431/485 of 6k76A
P0A6F3 Glycerol kinase; ATP:glycerol 3-phosphotransferase; Glycerokinase; GK; EC 2.7.1.30 from Escherichia coli (strain K12) (see 10 papers)
27% identity, 91% coverage: 3:474/521 of query aligns to 5:473/502 of P0A6F3
- T14 (= T12) binding ADP; binding sn-glycerol 3-phosphate
- R18 (≠ K16) binding ADP
- S59 (≠ A57) 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 (≠ R64) 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 (≠ M82) binding glycerol; binding sn-glycerol 3-phosphate
- E85 (≠ H83) binding glycerol; binding sn-glycerol 3-phosphate
- Y136 (≠ M133) binding glycerol; binding sn-glycerol 3-phosphate
- G231 (≠ N220) 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 (≠ A224) binding beta-D-fructose 1,6-bisphosphate
- R237 (≠ S232) 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 (= D241) binding glycerol; binding sn-glycerol 3-phosphate
- Q247 (≠ G242) binding glycerol
- T268 (= T263) 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
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 Zn(2+)
- 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.
Query Sequence
>WP_022529344.1 NCBI__GCF_000469325.1:WP_022529344.1
MTNYLIGVDLGTTSTKVVLFDTRGQVVASANTPYPLYQDTPDMAEEDPEEIFDATIAGLT
AVMRRAHLKPGELAGVSFSAAMHSLILMGQDNTPLTRVITWADNRAAQYATELKDSGLGM
QLFKNTGVPTHPMSPLVKLRWLNAEHPDLMRQTAHVIGIKDYILHRLFGRYVQDYSLANA
TGLFNIHTMDWDDQALAVAQVTRDQLPELVDTDYQLTGLNPAYADVIGIDSSVPFIIGAS
DGTLSNLGVNAIDPGVLAVTIGTSGAVRVVTDKPVVDPQGRLFTYYLAPGRWVVGGPVNN
GGIVFRWVRDQLFAPEKLTAEQMDVDSYELLTTIASKIPAGADGLLFHPYLGGERAPIWD
ANARGSFFGLTRQHTRAHMVRATLEGIVYNLYMVMLMIEGITGKPQAIQATGGFARSALW
RQMLADIFEQDVNIPESFESSALGAVVIAMKRLGLIDDLSAVKDMVGVTNTHHPDPSVFP
IYRELLPIWIRLTRELSTEYTAIADFQRRHPDPTARIAPED
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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