SitesBLAST
Comparing BWI76_RS15220 FitnessBrowser__Koxy:BWI76_RS15220 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
42% identity, 99% coverage: 1:311/314 of query aligns to 8:318/321 of 4ln1B
Q5HJD7 L-lactate dehydrogenase 1; L-LDH 1; EC 1.1.1.27 from Staphylococcus aureus (strain COL)
41% identity, 99% coverage: 1:312/314 of query aligns to 1:312/317 of Q5HJD7
3h3jB Crystal structure of lactate dehydrogenase mutant (a85r) from staphylococcus aureus complexed with NAD and pyruvate
41% identity, 98% coverage: 4:312/314 of query aligns to 2:309/314 of 3h3jB
- active site: R89 (= R92), D149 (= D152), R152 (= R155), H176 (= H179)
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), A13 (≠ N15), V14 (= V16), D35 (= D37), L36 (= L38), C78 (≠ T80), A79 (≠ S82), G80 (= G83), A81 (≠ G84), R82 (≠ A85), A119 (= A122), N121 (= N124), H176 (= H179), T229 (= T232), V233 (= V236)
- binding pyruvic acid: R89 (= R92), N121 (= N124), L148 (= L151), R152 (= R155), H176 (= H179), A219 (≠ G222), T229 (= T232)
P13714 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Bacillus subtilis (strain 168) (see paper)
42% identity, 98% coverage: 1:307/314 of query aligns to 1:307/320 of P13714
3pqdB Crystal structure of l-lactate dehydrogenase from bacillus subtilis complexed with fbp and NAD+
42% identity, 96% coverage: 6:307/314 of query aligns to 3:304/312 of 3pqdB
P00343 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Lacticaseibacillus casei (Lactobacillus casei) (see 3 papers)
40% identity, 96% coverage: 6:307/314 of query aligns to 10:310/326 of P00343
- R94 (= R92) binding
- R159 (= R157) binding
- R171 (≠ Q169) 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 (≠ QSID 169:172) binding
- H174 (≠ D172) 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 (= T232) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3wswA Crystal structure of minor l-lactate dehydrogenase from enterococcus mundtii in the ligands-bound form (see paper)
40% identity, 97% coverage: 5:308/314 of query aligns to 3:306/316 of 3wswA
- active site: R89 (= R92), D149 (= D152), R152 (= R155), H176 (= H179)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: R154 (= R157), R166 (≠ Q169), H169 (≠ D172)
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), F13 (≠ N15), V14 (= V16), D35 (= D37), V36 (≠ L38), T78 (= T80), A79 (≠ S82), G80 (= G83), I99 (= I102), A119 (= A122), S120 (≠ T123), N121 (= N124), L148 (= L151), I234 (≠ V236)
6j9tB Complex structure of lactobacillus casei lactate dehydrogenase with fructose-1,6-bisphosphate
40% identity, 96% coverage: 6:307/314 of query aligns to 8:308/316 of 6j9tB
1ldnA Structure of a ternary complex of an allosteric lactate dehydrogenase from bacillus stearothermophilus at 2.5 angstroms resolution (see paper)
39% identity, 99% coverage: 2:312/314 of query aligns to 3:313/316 of 1ldnA
- active site: R92 (= R92), D152 (= D152), R155 (= R155), H179 (= H179)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: Q169 (= Q169), N170 (≠ S170), H172 (≠ D172)
- binding nicotinamide-adenine-dinucleotide: G15 (= G14), F16 (≠ N15), V17 (= V16), D38 (= D37), A39 (≠ L38), C81 (≠ T80), A82 (≠ S82), G83 (= G83), A84 (≠ G84), N85 (≠ A85), A122 (= A122), N124 (= N124), H179 (= H179), T233 (= T232), I237 (≠ V236)
P00344 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see 3 papers)
39% identity, 99% coverage: 2:312/314 of query aligns to 3:313/317 of P00344
- FV 16:17 (≠ NV 15:16) binding
- D38 (= D37) binding
- ATN 122:124 (= ATN 122:124) binding
- S147 (≠ T147) binding
- R157 (= R157) 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 (≠ QSID 169:172) binding
1llcA Structure determination of the allosteric l-lactate dehydrogenase from lactobacillus casei at 3.0 angstroms resolution
39% identity, 96% coverage: 6:307/314 of query aligns to 9:309/320 of 1llcA
- active site: R93 (= R92), D153 (= D152), R156 (= R155), H180 (= H179)
- binding 1,6-di-O-phosphono-alpha-D-fructofuranose: T154 (= T153), R158 (= R157), H173 (≠ D172), Y175 (≠ F174), R244 (≠ E242), V256 (≠ A254), L257 (= L255)
Sites not aligning to the query:
3pqdD Crystal structure of l-lactate dehydrogenase from bacillus subtilis complexed with fbp and NAD+
40% identity, 96% coverage: 6:307/314 of query aligns to 3:294/301 of 3pqdD
- active site: D138 (= D152), R141 (= R155), H165 (= H179)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: R143 (= R157), Q155 (= Q169), N156 (≠ S170), H158 (≠ D172)
- binding nicotinamide-adenine-dinucleotide: G11 (= G14), F12 (≠ N15), V13 (= V16), D34 (= D37), V35 (≠ L38), C77 (≠ T80), A78 (≠ V81), I92 (≠ L106), T109 (= T123), N110 (= N124), H165 (= H179), T219 (= T232), V223 (= V236)
6j9uA Complex structure of lactobacillus casei lactate dehydrogenase penta mutant with pyruvate
40% identity, 96% coverage: 6:307/314 of query aligns to 7:302/306 of 6j9uA
P56511 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Lactiplantibacillus pentosus (Lactobacillus pentosus) (see 3 papers)
37% identity, 96% coverage: 6:307/314 of query aligns to 8:307/320 of P56511
- D39 (= D37) binding
- R44 (= R42) binding
- GA 83:84 (≠ GG 83:84) binding
- S105 (= S105) binding
- AAN 122:124 (≠ ATN 122:124) binding
- S147 (≠ T147) binding
- D172 (= D172) 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)
37% identity, 96% coverage: 6:307/314 of query aligns to 6:305/318 of 1ez4B
- active site: R90 (= R92), D150 (= D152), R153 (= R155), H177 (= H179)
- binding nicotinamide-adenine-dinucleotide: G14 (= G14), A15 (≠ N15), V16 (= V16), D37 (= D37), T79 (= T80), A80 (≠ S82), G81 (= G83), I100 (= I102), A120 (= A122), N122 (= N124), V124 (≠ C126), S145 (≠ T147), H177 (= H179), I234 (≠ V236)
2ldbA Structure determination and refinement of bacillus stearothermophilus lactate dehydrogenase (see paper)
37% identity, 99% coverage: 2:312/314 of query aligns to 3:297/301 of 2ldbA
- active site: D142 (= D152), R145 (= R155), H169 (= H179)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: Q159 (= Q169), H162 (≠ D172)
- binding nicotinamide-adenine-dinucleotide: G15 (= G14), F16 (≠ N15), V17 (= V16), D38 (= D37), A39 (≠ L38), A80 (≠ V81), A112 (= A122), T113 (= T123), N114 (= N124), H169 (= H179), I221 (≠ V236)
- binding sulfate ion: G29 (≠ S28), A31 (≠ C30), D32 (≠ E31), L141 (= L151), R145 (= R155), H169 (= H179), T217 (= T232)
1ldbA Structure determination and refinement of bacillus stearothermophilus lactate dehydrogenase (see paper)
37% identity, 99% coverage: 2:312/314 of query aligns to 3:290/294 of 1ldbA
2e37C Structure of tt0471 protein from thermus thermophilus
37% identity, 96% coverage: 7:307/314 of query aligns to 2:302/310 of 2e37C
- active site: R85 (= R92), D145 (= D152), R148 (= R155), H172 (= H179)
- binding nicotinamide-adenine-dinucleotide: G9 (= G14), M10 (≠ N15), V11 (= V16), D32 (= D37), L33 (= L38), A75 (≠ S82), G76 (= G83), V77 (≠ G84), V95 (≠ I102), A226 (≠ C231), T227 (= T232)
Q5SJA1 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
37% identity, 96% coverage: 7:307/314 of query aligns to 2:302/310 of Q5SJA1
3vphA L-lactate dehydrogenase from thermus caldophilus gk24 complexed with oxamate, nadh and fbp (see paper)
36% identity, 96% coverage: 7:307/314 of query aligns to 2:302/310 of 3vphA
- active site: R85 (= R92), D145 (= D152), R148 (= R155), H172 (= H179)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: R150 (= R157), Q162 (= Q169), H165 (≠ D172), Y167 (≠ F174)
- binding nicotinamide-adenine-dinucleotide: G9 (= G14), M10 (≠ N15), V11 (= V16), D32 (= D37), L33 (= L38), Y62 (≠ C71), A75 (≠ S82), G76 (= G83), V99 (≠ L106), A115 (= A122), N117 (= N124), H172 (= H179), T227 (= T232), I231 (≠ V236)
Query Sequence
>BWI76_RS15220 FitnessBrowser__Koxy:BWI76_RS15220
MNTKARKVMIIGAGNVGASAAYALLNQSVCEELILVDLNKPRAEAHAQDLSDAAAYMPGM
MTISTREASDCADVDIAVITVSGGALKPGQTRLDELTNTAKIVKSLVPQMMNGGFNGIFL
VATNPCDIITWQVWQLSGLPRGQVLGTGVWLDTTRLRRVLAQALDIGAQSIDAFILGEHG
DAQFPVWSHSAVYGSAIADVYQKHTGKALDRDLIADKVRKLGFEIYAGKGCTEYGVAGTI
AEICRNIFTGSHRALAVSCILDGEYGVTGAAAGVPAVLTQSGVQQIIELQLADDEAEKFR
HAIEVIKASIARLP
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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