SitesBLAST
Comparing AZOBR_RS01310 FitnessBrowser__azobra:AZOBR_RS01310 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
2e37C Structure of tt0471 protein from thermus thermophilus
65% identity, 97% coverage: 1:304/313 of query aligns to 1:304/310 of 2e37C
- active site: R85 (= R85), D145 (= D145), R148 (= R148), H172 (= H172)
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), M10 (≠ A10), V11 (= V11), D32 (= D32), L33 (≠ M33), A75 (= A75), G76 (= G76), V77 (= V77), V95 (= V95), A226 (≠ H226), T227 (= T227)
Q5SJA1 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
65% identity, 97% coverage: 1:304/313 of query aligns to 1:304/310 of Q5SJA1
3vphA L-lactate dehydrogenase from thermus caldophilus gk24 complexed with oxamate, nadh and fbp (see paper)
65% identity, 97% coverage: 1:304/313 of query aligns to 1:304/310 of 3vphA
- active site: R85 (= R85), D145 (= D145), R148 (= R148), H172 (= H172)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: R150 (= R150), Q162 (≠ K162), H165 (= H165), Y167 (≠ H167)
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), M10 (≠ A10), V11 (= V11), D32 (= D32), L33 (≠ M33), Y62 (= Y62), A75 (= A75), G76 (= G76), V99 (≠ I99), A115 (= A115), N117 (= N117), H172 (= H172), T227 (= T227), I231 (= I231)
P06150 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Thermus caldophilus (see 2 papers)
65% identity, 97% coverage: 1:304/313 of query aligns to 1:304/310 of P06150
- MV 10:11 (≠ AV 10:11) binding
- D32 (= D32) binding
- L46 (≠ A46) 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 (= H47) 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 (= Y62) binding
- GV 76:77 (= GV 76:77) binding
- ATN 115:117 (= ATN 115:117) binding
- S140 (= S140) binding
- R150 (= R150) 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 (≠ D155) 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 (= H165) mutation to F: The strong stimulatory effect of fructose 1,6-bisphosphate (FBP) is abolished.
- R197 (≠ L197) 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 (= A216) 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)
65% identity, 97% coverage: 1:304/313 of query aligns to 1:304/310 of 3zznA
2xxbA Penta-mutant of thermus thermophilus lactate dehydrogenase, complex with amp
65% identity, 97% coverage: 1:304/313 of query aligns to 1:304/310 of 2xxbA
- active site: R85 (= R85), D145 (= D145), R148 (= R148), H172 (= H172)
- binding adenosine monophosphate: G7 (= G7), G9 (= G9), M10 (≠ A10), D32 (= D32), L33 (≠ M33), Y62 (= Y62), A75 (= A75), G76 (= G76)
1a5zA Lactate dehydrogenase from thermotoga maritima (tmldh) (see paper)
45% identity, 98% coverage: 1:308/313 of query aligns to 1:307/312 of 1a5zA
- active site: R85 (= R85), D145 (= D145), R148 (= R148), H172 (= H172)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: E39 (≠ A39), Y58 (≠ R58), D61 (≠ G61), D64 (≠ A64), R150 (= R150), S163 (= S163), H165 (= H165), G186 (≠ A186)
- binding nicotinamide-adenine-dinucleotide: G7 (= G7), G9 (= G9), R10 (≠ A10), V11 (= V11), D32 (= D32), V33 (≠ M33), A75 (= A75), G76 (= G76), T116 (= T116), N117 (= N117), A225 (≠ H226), T226 (= T227)
P16115 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
45% identity, 98% coverage: 1:308/313 of query aligns to 1:307/319 of P16115
4ln1B Crystal structure of l-lactate dehydrogenase from bacillus cereus atcc 14579 complexed with calcium, nysgrc target 029452
43% identity, 98% coverage: 2:308/313 of query aligns to 14:320/321 of 4ln1B
Sites not aligning to the query:
P13714 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Bacillus subtilis (strain 168) (see paper)
41% identity, 96% coverage: 2:303/313 of query aligns to 7:308/320 of P13714
1ldnA Structure of a ternary complex of an allosteric lactate dehydrogenase from bacillus stearothermophilus at 2.5 angstroms resolution (see paper)
43% identity, 96% coverage: 2:302/313 of query aligns to 8:308/316 of 1ldnA
- active site: R92 (= R85), D152 (= D145), R155 (= R148), H179 (= H172)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: Q169 (≠ K162), N170 (≠ S163), H172 (= H165)
- binding nicotinamide-adenine-dinucleotide: G15 (= G9), F16 (≠ A10), V17 (= V11), D38 (= D32), A39 (≠ M33), C81 (≠ A74), A82 (= A75), G83 (= G76), A84 (≠ V77), N85 (≠ A78), A122 (= A115), N124 (= N117), H179 (= H172), T233 (= T227), I237 (= I231)
P00344 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see 3 papers)
43% identity, 96% coverage: 2:302/313 of query aligns to 8:308/317 of P00344
- FV 16:17 (≠ AV 10:11) binding
- D38 (= D32) binding
- ATN 122:124 (= ATN 115:117) binding
- S147 (= S140) binding
- R157 (= R150) 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 (≠ KSVH 162:165) binding
3pqdB Crystal structure of l-lactate dehydrogenase from bacillus subtilis complexed with fbp and NAD+
41% identity, 96% coverage: 2:303/313 of query aligns to 4:305/312 of 3pqdB
8ab3A Crystal structure of the lactate dehydrogenase of cyanobacterium aponinum in complex with oxamate, nadh and fbp. (see paper)
41% identity, 97% coverage: 5:309/313 of query aligns to 25:330/330 of 8ab3A
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: R171 (= R150), R183 (≠ K162), H186 (= H165)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G29 (= G9), Q30 (≠ A10), V31 (= V11), D52 (= D32), I53 (≠ M33), T95 (≠ A74), A96 (= A75), G97 (= G76), V98 (= V77), A99 (= A78), V136 (≠ A115), N138 (= N117), H193 (= H172), I252 (= I231)
Q5HJD7 L-lactate dehydrogenase 1; L-LDH 1; EC 1.1.1.27 from Staphylococcus aureus (strain COL)
41% identity, 99% coverage: 2:310/313 of query aligns to 8:315/317 of Q5HJD7
3h3jB Crystal structure of lactate dehydrogenase mutant (a85r) from staphylococcus aureus complexed with NAD and pyruvate
40% identity, 99% coverage: 2:310/313 of query aligns to 5:312/314 of 3h3jB
- active site: R89 (= R85), D149 (= D145), R152 (= R148), H176 (= H172)
- binding nicotinamide-adenine-dinucleotide: G12 (= G9), A13 (= A10), V14 (= V11), D35 (= D32), L36 (≠ M33), C78 (≠ A74), A79 (= A75), G80 (= G76), A81 (≠ V77), R82 (≠ A78), A119 (= A115), N121 (= N117), H176 (= H172), T229 (= T227), V233 (≠ I231)
- binding pyruvic acid: R89 (= R85), N121 (= N117), L148 (= L144), R152 (= R148), H176 (= H172), A219 (= A217), T229 (= T227)
3wswA Crystal structure of minor l-lactate dehydrogenase from enterococcus mundtii in the ligands-bound form (see paper)
41% identity, 98% coverage: 2:308/313 of query aligns to 5:311/316 of 3wswA
- active site: R89 (= R85), D149 (= D145), R152 (= R148), H176 (= H172)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: R154 (= R150), R166 (≠ K162), H169 (= H165)
- binding nicotinamide-adenine-dinucleotide: G12 (= G9), F13 (≠ A10), V14 (= V11), D35 (= D32), V36 (≠ M33), T78 (≠ A74), A79 (= A75), G80 (= G76), I99 (≠ V95), A119 (= A115), S120 (≠ T116), N121 (= N117), L148 (= L144), I234 (= I231)
6j9tB Complex structure of lactobacillus casei lactate dehydrogenase with fructose-1,6-bisphosphate
39% identity, 98% coverage: 2:307/313 of query aligns to 9:313/316 of 6j9tB
P00343 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Lacticaseibacillus casei (Lactobacillus casei) (see 3 papers)
39% identity, 98% coverage: 2:307/313 of query aligns to 11:315/326 of P00343
- R94 (= R85) binding
- R159 (= R150) binding
- R171 (≠ K162) 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 (≠ KSVH 162:165) binding
- H174 (= H165) 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 (= T227) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1llcA Structure determination of the allosteric l-lactate dehydrogenase from lactobacillus casei at 3.0 angstroms resolution
39% identity, 98% coverage: 2:307/313 of query aligns to 10:314/320 of 1llcA
- active site: R93 (= R85), D153 (= D145), R156 (= R148), H180 (= H172)
- binding 1,6-di-O-phosphono-alpha-D-fructofuranose: T154 (= T146), R158 (= R150), H173 (= H165), Y175 (≠ H167), R244 (= R237), V256 (= V249), L257 (= L250)
Sites not aligning to the query:
Query Sequence
>AZOBR_RS01310 FitnessBrowser__azobra:AZOBR_RS01310
MKVGIVGAGAVGATAGFAMVMSGAASEVVLVDMNEKLAAAQAQDIAHAVPFARAAQVRHG
GYAALAGAGVVVLAAGVAQRPGETRLQLLERNAAVFGAIIPAVLAAAPDAILLVATNPLD
VMTQIATRISGLPPSRVIGSGTILDTARFRALLADRLGVTPKSVHAHVVGEHGDSEVLLW
SGATVACLPVDRGAERLKRPLTAEDRAAIDEGVRRAAYHIIDGKGHTAFGIGGGLSRIVA
AIAGDERAVLTCSILNDEVLGVPDVALSLPRVIGAGGVLETVMPDLSEEEAAALKRSAEI
LKEAVTSVEKSLP
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