SitesBLAST
Comparing WP_034526472.1 NCBI__GCF_000740055.1:WP_034526472.1 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)
P14295 L-2-hydroxyisocaproate dehydrogenase; L-HicDH; EC 1.1.1.- from Weissella confusa (Lactobacillus confusus) (see paper)
46% identity, 99% coverage: 2:304/306 of query aligns to 3:306/310 of P14295
- 34:55 (vs. 33:54, 59% identical) binding NAD(+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1hyhA Crystal structure of l-2-hydroxyisocaproate dehydrogenase from lactobacillus confusus at 2.2 angstroms resolution-an example of strong asymmetry between subunits (see paper)
46% identity, 99% coverage: 2:304/306 of query aligns to 2:293/297 of 1hyhA
- active site: D144 (= D150), R147 (= R153), H171 (= H177)
- binding nicotinamide-adenine-dinucleotide: G8 (= G8), G10 (= G10), N11 (= N11), V12 (= V12), D33 (= D33), A34 (≠ K34), T76 (= T76), L77 (≠ A77), G78 (= G78), I80 (≠ S80), E87 (= E93), M94 (≠ V100), I114 (= I120), N116 (= N122), H171 (= H177), V220 (≠ I231)
P56511 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Lactiplantibacillus pentosus (Lactobacillus pentosus) (see 3 papers)
32% identity, 98% coverage: 2:302/306 of query aligns to 8:311/320 of P56511
- D39 (= D33) binding NAD(+)
- R44 (≠ K38) binding NAD(+)
- G---A 83:84 (≠ GKSSA 78:82) binding NAD(+)
- S105 (≠ D103) binding NAD(+)
- AAN 122:124 (≠ IMN 120:122) binding NAD(+)
- S147 (≠ T145) binding NAD(+)
- D172 (≠ S170) 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)
32% identity, 98% coverage: 2:302/306 of query aligns to 6:309/318 of 1ez4B
- active site: R90 (= R90), D150 (= D150), R153 (= R153), H177 (= H177)
- binding nicotinamide-adenine-dinucleotide: G14 (= G10), A15 (≠ N11), V16 (= V12), D37 (= D33), T79 (= T76), A80 (= A77), G81 (= G78), I100 (≠ V100), A120 (≠ I120), N122 (= N122), V124 (≠ N124), S145 (≠ T145), H177 (= H177), I234 (= I231)
Q5HJD7 L-lactate dehydrogenase 1; L-LDH 1; EC 1.1.1.27 from Staphylococcus aureus (strain COL)
33% identity, 96% coverage: 3:297/306 of query aligns to 8:306/317 of Q5HJD7
- AV 16:17 (≠ NV 11:12) binding NAD(+)
- D38 (= D33) binding NAD(+)
- G---A 83:84 (≠ GKSSA 78:82) binding NAD(+)
- R92 (= R90) binding substrate
- S147 (≠ T145) binding NAD(+)
- T232 (= T227) binding substrate
6j9uA Complex structure of lactobacillus casei lactate dehydrogenase penta mutant with pyruvate
33% identity, 96% coverage: 2:294/306 of query aligns to 7:298/306 of 6j9uA
P00343 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Lacticaseibacillus casei (Lactobacillus casei) (see 3 papers)
33% identity, 96% coverage: 2:294/306 of query aligns to 10:306/326 of P00343
- R94 (= R90) binding substrate
- R159 (≠ Q155) binding beta-D-fructose 1,6-bisphosphate
- R171 (≠ K167) 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 (≠ KNVS 167:170) binding beta-D-fructose 1,6-bisphosphate
- H174 (≠ S170) 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 substrate
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6j9tB Complex structure of lactobacillus casei lactate dehydrogenase with fructose-1,6-bisphosphate
33% identity, 96% coverage: 2:294/306 of query aligns to 8:304/316 of 6j9tB
3h3jB Crystal structure of lactate dehydrogenase mutant (a85r) from staphylococcus aureus complexed with NAD and pyruvate
33% identity, 96% coverage: 3:297/306 of query aligns to 5:303/314 of 3h3jB
- active site: R89 (= R90), D149 (= D150), R152 (= R153), H176 (= H177)
- binding nicotinamide-adenine-dinucleotide: G12 (= G10), A13 (≠ N11), V14 (= V12), D35 (= D33), L36 (≠ K34), C78 (≠ T76), A79 (= A77), G80 (= G78), A81 (= A82), R82 (≠ V83), A119 (≠ I120), N121 (= N122), H176 (= H177), T229 (= T227), V233 (≠ I231)
- binding pyruvic acid: R89 (= R90), N121 (= N122), L148 (= L149), R152 (= R153), H176 (= H177), A219 (≠ G217), T229 (= T227)
2ldbA Structure determination and refinement of bacillus stearothermophilus lactate dehydrogenase (see paper)
32% identity, 96% coverage: 3:297/306 of query aligns to 8:291/301 of 2ldbA
- active site: D142 (= D150), R145 (= R153), H169 (= H177)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: Q159 (≠ K167), H162 (≠ S170)
- binding nicotinamide-adenine-dinucleotide: G15 (= G10), F16 (≠ N11), V17 (= V12), D38 (= D33), A39 (≠ K34), A80 (= A77), A112 (≠ I120), T113 (≠ M121), N114 (= N122), H169 (= H177), I221 (= I231)
- binding sulfate ion: G29 (= G24), A31 (≠ T26), D32 (= D27), L141 (= L149), R145 (= R153), H169 (= H177), T217 (= T227)
6h9sB Crystal dimeric structure of petrotoga mobilis lactate dehydrogenase with nadh
32% identity, 99% coverage: 3:305/306 of query aligns to 2:289/292 of 6h9sB
- binding nicotinamide-adenine-dinucleotide: G9 (= G10), R10 (≠ N11), V11 (= V12), D32 (= D33), L33 (≠ K34), A75 (= A77), G76 (= G78), A77 (≠ S86), I111 (= I120), N113 (= N122), T213 (= T227)
3wswA Crystal structure of minor l-lactate dehydrogenase from enterococcus mundtii in the ligands-bound form (see paper)
31% identity, 98% coverage: 2:301/306 of query aligns to 4:311/316 of 3wswA
- active site: R89 (= R90), D149 (= D150), R152 (= R153), H176 (= H177)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: R154 (≠ Q155), R166 (≠ K167), H169 (≠ S170)
- binding nicotinamide-adenine-dinucleotide: G12 (= G10), F13 (≠ N11), V14 (= V12), D35 (= D33), V36 (≠ K34), T78 (= T76), A79 (= A77), G80 (= G78), I99 (≠ V100), A119 (≠ I120), S120 (≠ M121), N121 (= N122), L148 (= L149), I234 (= I231)
1ldbA Structure determination and refinement of bacillus stearothermophilus lactate dehydrogenase (see paper)
32% identity, 96% coverage: 3:297/306 of query aligns to 8:284/294 of 1ldbA
1llcA Structure determination of the allosteric l-lactate dehydrogenase from lactobacillus casei at 3.0 angstroms resolution
32% identity, 96% coverage: 2:294/306 of query aligns to 9:305/320 of 1llcA
- active site: R93 (= R90), D153 (= D150), R156 (= R153), H180 (= H177)
- binding 1,6-di-O-phosphono-alpha-D-fructofuranose: T154 (= T151), R158 (≠ Q155), H173 (≠ S170), Y175 (≠ V172), R244 (= R237), V256 (≠ A249), L257 (≠ C250)
Sites not aligning to the query:
P13714 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Bacillus subtilis (strain 168) (see paper)
32% identity, 97% coverage: 1:297/306 of query aligns to 5:306/320 of P13714