SitesBLAST
Comparing 209544 MicrobesOnline__882:209544 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)
4ln1B Crystal structure of l-lactate dehydrogenase from bacillus cereus atcc 14579 complexed with calcium, nysgrc target 029452
44% identity, 100% coverage: 1:309/309 of query aligns to 12:320/321 of 4ln1B
Sites not aligning to the query:
3wswA Crystal structure of minor l-lactate dehydrogenase from enterococcus mundtii in the ligands-bound form (see paper)
45% identity, 97% coverage: 3:302/309 of query aligns to 5:304/316 of 3wswA
- active site: R89 (= R86), D149 (= D146), R152 (= R149), H176 (= H173)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: R154 (= R151), R166 (= R163), H169 (= H166)
- binding nicotinamide-adenine-dinucleotide: G12 (= G10), F13 (≠ N11), V14 (= V12), D35 (= D33), V36 (≠ A34), T78 (= T75), A79 (= A76), G80 (= G77), I99 (= I96), A119 (= A116), S120 (≠ T117), N121 (= N118), L148 (= L145), I234 (= I232)
P13714 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Bacillus subtilis (strain 168) (see paper)
44% identity, 98% coverage: 1:302/309 of query aligns to 5:306/320 of P13714
3pqdB Crystal structure of l-lactate dehydrogenase from bacillus subtilis complexed with fbp and NAD+
44% identity, 98% coverage: 1:302/309 of query aligns to 2:303/312 of 3pqdB
P00343 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Lacticaseibacillus casei (Lactobacillus casei) (see 3 papers)
41% identity, 99% coverage: 3:307/309 of query aligns to 11:314/326 of P00343
- R94 (= R86) binding
- R159 (= R151) binding
- R171 (= R163) mutation to Q: Exhibits no significant catalytic activity toward pyruvate up to 50 mM at pH 5.0 in the absence of fructose 1,6-bisphosphate (FBP). In the presence of 5 mM fructose 1,6-bisphosphate (FBP), it exhibits marked catalytic activity.
- RSVH 171:174 (≠ RGVH 163:166) binding
- H174 (= H166) mutation to D: Shows a lower thermoresistance than the wild-type, even in the absence of fructose 1,6-bisphosphate (FBP). Not thermostabilized in the presence of fructose 1,6-bisphosphate (FBP), Mn(2+) or both. Under acidic conditions, the mutant does not show a positive allosteric regulation by fructose 1,6-bisphosphate (FBP), which even inhibits the stimulative effects of the alternative activation factors. In addition, Mn(2+) ions also show greatly reduced inhibitory effects on the mutant enzyme. Under neutral conditions, the reaction of the mutant is slightly enhanced by fructose 1,6-bisphosphate (FBP), but not further stimulates by additional Mn(2+) ions, unlike the case of the wild-type.
- T235 (= T228) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6j9tB Complex structure of lactobacillus casei lactate dehydrogenase with fructose-1,6-bisphosphate
41% identity, 99% coverage: 2:307/309 of query aligns to 8:312/316 of 6j9tB
1ldnA Structure of a ternary complex of an allosteric lactate dehydrogenase from bacillus stearothermophilus at 2.5 angstroms resolution (see paper)
43% identity, 99% coverage: 3:307/309 of query aligns to 8:312/316 of 1ldnA
- active site: R92 (= R86), D152 (= D146), R155 (= R149), H179 (= H173)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: Q169 (≠ R163), N170 (≠ G164), H172 (= H166)
- binding nicotinamide-adenine-dinucleotide: G15 (= G10), F16 (≠ N11), V17 (= V12), D38 (= D33), A39 (= A34), C81 (≠ T75), A82 (= A76), G83 (= G77), A84 (= A78), N85 (≠ K79), A122 (= A116), N124 (= N118), H179 (= H173), T233 (= T228), I237 (= I232)
P00344 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see 3 papers)
43% identity, 99% coverage: 3:307/309 of query aligns to 8:312/317 of P00344
- FV 16:17 (≠ NV 11:12) binding
- D38 (= D33) binding
- ATN 122:124 (= ATN 116:118) binding
- S147 (= S141) binding
- R157 (= R151) binding ; mutation to Q: This mutant undergoes a reversible subunit assembly from dimer to tetramer. However, the tetramer mutant is much more stable than the wild type, and is destabilized rather than stabilized by binding the allosteric regulator, fructose 1,6-bisphosphate (FBP). The mutation weakens the binding of fructose 1,6-bisphosphate (FBP) to both the dimeric and tetrameric forms, and almost abolishes any stimulatory effect.
- QNVH 169:172 (≠ RGVH 163:166) binding
1llcA Structure determination of the allosteric l-lactate dehydrogenase from lactobacillus casei at 3.0 angstroms resolution
40% identity, 99% coverage: 3:307/309 of query aligns to 10:313/320 of 1llcA
- active site: R93 (= R86), D153 (= D146), R156 (= R149), H180 (= H173)
- binding 1,6-di-O-phosphono-alpha-D-fructofuranose: T154 (≠ S147), R158 (= R151), H173 (= H166), Y175 (≠ H168), R244 (= R238), V256 (= V250), L257 (= L251)
Sites not aligning to the query:
P56511 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Lactiplantibacillus pentosus (Lactobacillus pentosus) (see 3 papers)
41% identity, 100% coverage: 2:309/309 of query aligns to 8:317/320 of P56511
- D39 (= D33) binding
- R44 (= R38) binding
- GA 83:84 (= GA 77:78) binding
- S105 (≠ D99) binding
- AAN 122:124 (≠ ATN 116:118) binding
- S147 (= S141) binding
- D172 (≠ H166) mutation to H: Shows a significant FBP-induced thermostabilization as in the cases of many allosteric LDHs, indicating the binding of fructose 1,6-bisphosphate (FBP). However, the mutant is still a non-allosteric enzyme and shows essentially the same FBP-independent catalytic activity as the wild-type.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1ez4B Crystal structure of non-allosteric l-lactate dehydrogenase from lactobacillus pentosus at 2.3 angstrom resolution (see paper)
41% identity, 100% coverage: 2:309/309 of query aligns to 6:315/318 of 1ez4B
- active site: R90 (= R86), D150 (= D146), R153 (= R149), H177 (= H173)
- binding nicotinamide-adenine-dinucleotide: G14 (= G10), A15 (≠ N11), V16 (= V12), D37 (= D33), T79 (= T75), A80 (= A76), G81 (= G77), I100 (= I96), A120 (= A116), N122 (= N118), V124 (= V120), S145 (= S141), H177 (= H173), I234 (= I232)
2e37C Structure of tt0471 protein from thermus thermophilus
44% identity, 99% coverage: 3:309/309 of query aligns to 2:308/310 of 2e37C
- active site: R85 (= R86), D145 (= D146), R148 (= R149), H172 (= H173)
- binding nicotinamide-adenine-dinucleotide: G9 (= G10), M10 (≠ N11), V11 (= V12), D32 (= D33), L33 (≠ A34), A75 (= A76), G76 (= G77), V77 (≠ A78), V95 (≠ I96), A226 (= A227), T227 (= T228)
Q5SJA1 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
44% identity, 99% coverage: 3:309/309 of query aligns to 2:308/310 of Q5SJA1
1lthR T and r states in the crystals of bacterial l-lactate dehydrogenase reveal the mechanism for allosteric control (see paper)
42% identity, 99% coverage: 3:309/309 of query aligns to 3:311/313 of 1lthR
- active site: H174 (= H173)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: R152 (= R151), K164 (≠ R163), N165 (≠ G164), H167 (= H166)
- binding nicotinamide-adenine-dinucleotide: G10 (= G10), A11 (≠ N11), V12 (= V12), D33 (= D33), I34 (≠ A34), T76 (= T75), A77 (= A76), P79 (≠ A78), R80 (≠ K79), I97 (= I96), I101 (= I100), I117 (≠ A116), N119 (= N118), H174 (= H173), T230 (= T228), I234 (= I232)
1lldA Molecular basis of allosteric activation of bacterial l-lactate dehydrogenase (see paper)
42% identity, 99% coverage: 3:309/309 of query aligns to 3:311/313 of 1lldA
- active site: R87 (= R86), D147 (= D146), R150 (= R149), H174 (= H173)
- binding nicotinamide-adenine-dinucleotide: G10 (= G10), A11 (≠ N11), V12 (= V12), D33 (= D33), I34 (≠ A34), R38 (= R38), T76 (= T75), A77 (= A76), I101 (= I100), N119 (= N118), H174 (= H173), I224 (= I222), I234 (= I232)
E8ME30 L-lactate dehydrogenase 2; L-LDH 2; FBP-dependent LDH; EC 1.1.1.27 from Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) (see 2 papers)
42% identity, 99% coverage: 3:309/309 of query aligns to 10:318/320 of E8ME30
3vphA L-lactate dehydrogenase from thermus caldophilus gk24 complexed with oxamate, nadh and fbp (see paper)
44% identity, 99% coverage: 3:309/309 of query aligns to 2:308/310 of 3vphA
- active site: R85 (= R86), D145 (= D146), R148 (= R149), H172 (= H173)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: R150 (= R151), Q162 (≠ R163), H165 (= H166), Y167 (≠ H168)
- binding nicotinamide-adenine-dinucleotide: G9 (= G10), M10 (≠ N11), V11 (= V12), D32 (= D33), L33 (≠ A34), Y62 (= Y63), A75 (= A76), G76 (= G77), V99 (≠ I100), A115 (= A116), N117 (= N118), H172 (= H173), T227 (= T228), I231 (= I232)
P06150 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Thermus caldophilus (see 2 papers)
44% identity, 99% coverage: 3:309/309 of query aligns to 2:308/310 of P06150
- MV 10:11 (≠ NV 11:12) binding
- D32 (= D33) binding
- L46 (≠ A47) mutation to E: Increases the thermal stability of the enzyme. In the absence of fructose 1,6-bisphosphate (FBP), the Q4(R) mutant exhibits a 4-fold increased Vmax value and a 5-fold increase of the affinity for pyruvate; when associated with D-47; K-155 and R-216.
- H47 (≠ D48) mutation to D: Increases the thermal stability of the enzyme. In the absence of fructose 1,6-bisphosphate (FBP), the Q4(R) mutant exhibits a 4-fold increased Vmax value and a 5-fold increase of the affinity for pyruvate; when associated with E-46; K-155 and R-216.
- Y62 (= Y63) binding
- GV 76:77 (≠ GA 77:78) binding
- ATN 115:117 (= ATN 116:118) binding
- S140 (= S141) binding
- R150 (= R151) binding ; mutation to Q: Increases the thermal stability of the enzyme. In the absence of fructose 1,6-bisphosphate (FBP), the P2 mutant does not exhibit a markedly increased Vmax value, but shows a strong affinity for pyruvate, and additively increases the FBP-independent activity of the enzyme; when associated with L-197.; mutation to Q: The strong stimulatory effect of fructose 1,6-bisphosphate (FBP) is abolished.
- E155 (= E156) mutation to K: Increases the thermal stability of the enzyme. In the absence of fructose 1,6-bisphosphate (FBP), the Q4(R) mutant exhibits a 4-fold increased Vmax value and a 5-fold increase of the affinity for pyruvate; when associated with E-46; D-47 and R-216.
- H165 (= H166) mutation to F: The strong stimulatory effect of fructose 1,6-bisphosphate (FBP) is abolished.
- R197 (= R198) mutation to L: Increases the thermal stability of the enzyme. In the absence of fructose 1,6-bisphosphate (FBP), the P2 mutant does not exhibit a markedly increased Vmax value, but shows a strong affinity for pyruvate, and additively increases the FBP-independent activity of the enzyme; when associated with Q-150.
- A216 (= A217) mutation to R: Increases the thermal stability of the enzyme. In the absence of fructose 1,6-bisphosphate (FBP), the Q4(R) mutant exhibits a 4-fold increased Vmax value and a 5-fold increase of the affinity for pyruvate; when associated with E-46; D-47 and K-155.
3zznA 5-mutant (r79w, r151a, e279a, e299a,e313a) lactate-dehydrogenase from thermus thermophillus (see paper)
44% identity, 99% coverage: 3:309/309 of query aligns to 2:308/310 of 3zznA
2xxbA Penta-mutant of thermus thermophilus lactate dehydrogenase, complex with amp
44% identity, 99% coverage: 3:309/309 of query aligns to 2:308/310 of 2xxbA
- active site: R85 (= R86), D145 (= D146), R148 (= R149), H172 (= H173)
- binding adenosine monophosphate: G7 (= G8), G9 (= G10), M10 (≠ N11), D32 (= D33), L33 (≠ A34), Y62 (= Y63), A75 (= A76), G76 (= G77)
Query Sequence
>209544 MicrobesOnline__882:209544
MNRIAVIGVGNVGMAFAYAAAIKRLANDIVLIDANAARAEGESMDLADAMALVGPVQIRS
GGYEQCEGARIVVVTAGAKQMPGQSRLDLVRVNAGITRDILTAVMQYADDPLYIMATNPV
DVLTHVARTVTGVAPGRVIGSGTVLDSARFRGHVAEILGVDVRGVHAHIVGEHGDSEVAL
WSRANVSGIPVAEMCARRGIAYDAAFREKALGHVRHAAYEIIGRKGATGYGIGMSLCRIV
EAILHDEHSVLTVSCPVAGHYGLGDVSLSLPCVIGSDGIEEVLDAPIAEDEQAALAASAR
VLGEHLAAL
Or try a new SitesBLAST search
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