SitesBLAST
Comparing WP_110806898.1 NCBI__GCF_003217355.1:WP_110806898.1 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)
3zznA 5-mutant (r79w, r151a, e279a, e299a,e313a) lactate-dehydrogenase from thermus thermophillus (see paper)
64% identity, 100% coverage: 1:308/309 of query aligns to 1:308/310 of 3zznA
2xxbA Penta-mutant of thermus thermophilus lactate dehydrogenase, complex with amp
64% identity, 100% coverage: 1:308/309 of query aligns to 1:308/310 of 2xxbA
- active site: R85 (= R85), D145 (= D145), R148 (= R148), H172 (= H172)
- binding adenosine monophosphate: G7 (= G7), G9 (= G9), M10 (= M10), D32 (= D32), L33 (≠ R33), Y62 (= Y62), A75 (= A75), G76 (= G76)
2e37C Structure of tt0471 protein from thermus thermophilus
63% identity, 100% coverage: 1:308/309 of query aligns to 1:308/310 of 2e37C
- active site: R85 (= R85), D145 (= D145), R148 (= R148), H172 (= H172)
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), M10 (= M10), V11 (= V11), D32 (= D32), L33 (≠ R33), A75 (= A75), G76 (= G76), V77 (= V77), V95 (= V95), A226 (= A226), T227 (= T227)
Q5SJA1 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
63% identity, 100% coverage: 1:308/309 of query aligns to 1:308/310 of Q5SJA1
- MV 10:11 (= MV 10:11) binding NAD(+)
- D32 (= D32) binding NAD(+)
- Y62 (= Y62) binding NAD(+)
- GV 76:77 (= GV 76:77) binding NAD(+)
- ATN 115:117 (≠ ASN 115:117) binding NAD(+)
- S140 (≠ T140) binding NAD(+)
3vphA L-lactate dehydrogenase from thermus caldophilus gk24 complexed with oxamate, nadh and fbp (see paper)
63% identity, 100% coverage: 1:308/309 of query aligns to 1:308/310 of 3vphA
- active site: R85 (= R85), D145 (= D145), R148 (= R148), H172 (= H172)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: R150 (= R150), Q162 (≠ H162), H165 (= H165), Y167 (≠ F167)
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), M10 (= M10), V11 (= V11), D32 (= D32), L33 (≠ R33), Y62 (= Y62), A75 (= A75), G76 (= G76), V99 (= V99), 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)
63% identity, 100% coverage: 1:308/309 of query aligns to 1:308/310 of P06150
- MV 10:11 (= MV 10:11) binding NAD(+)
- D32 (= D32) binding NAD(+)
- L46 (≠ G46) 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 NAD(+)
- GV 76:77 (= GV 76:77) binding NAD(+)
- ATN 115:117 (≠ ASN 115:117) binding NAD(+)
- S140 (≠ T140) binding NAD(+)
- R150 (= R150) binding beta-D-fructose 1,6-bisphosphate; 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 (≠ G155) 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.
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)
42% identity, 98% coverage: 1:304/309 of query aligns to 1:303/319 of P16115
- RV 10:11 (≠ MV 10:11) binding NAD(+)
- D32 (= D32) binding NAD(+)
- H165 (= H165) binding beta-D-fructose 1,6-bisphosphate
1a5zA Lactate dehydrogenase from thermotoga maritima (tmldh) (see paper)
42% identity, 98% coverage: 1:304/309 of query aligns to 1:303/312 of 1a5zA
- active site: R85 (= R85), D145 (= D145), R148 (= R148), H172 (= H172)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: E39 (≠ Q39), Y58 (≠ G58), D61 (= D61), D64 (≠ V64), R150 (= R150), S163 (= S163), H165 (= H165), G186 (= G186)
- binding nicotinamide-adenine-dinucleotide: G7 (= G7), G9 (= G9), R10 (≠ M10), V11 (= V11), D32 (= D32), V33 (≠ R33), A75 (= A75), G76 (= G76), T116 (≠ S116), N117 (= N117), A225 (= A226), T226 (= T227)
4ln1B Crystal structure of l-lactate dehydrogenase from bacillus cereus atcc 14579 complexed with calcium, nysgrc target 029452
41% identity, 99% coverage: 2:306/309 of query aligns to 14:318/321 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)
40% identity, 98% coverage: 2:303/309 of query aligns to 7:308/320 of P13714
- FV 15:16 (≠ MV 10:11) binding NAD(+)
- D37 (= D32) binding NAD(+)
- GA 82:83 (≠ GV 76:77) binding NAD(+)
- R156 (= R150) binding beta-D-fructose 1,6-bisphosphate
- QNVHA 168:172 (≠ HSVHG 162:166) binding beta-D-fructose 1,6-bisphosphate
- Y223 (= Y218) modified: Phosphotyrosine
3pqdB Crystal structure of l-lactate dehydrogenase from bacillus subtilis complexed with fbp and NAD+
40% identity, 98% coverage: 2:303/309 of query aligns to 4:305/312 of 3pqdB
P00344 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see 3 papers)
40% identity, 97% coverage: 2:302/309 of query aligns to 8:308/317 of P00344
- FV 16:17 (≠ MV 10:11) binding NAD(+)
- D38 (= D32) binding NAD(+)
- ATN 122:124 (≠ ASN 115:117) binding NAD(+)
- S147 (≠ T140) binding NAD(+)
- R157 (= R150) binding beta-D-fructose 1,6-bisphosphate; 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 (≠ HSVH 162:165) binding beta-D-fructose 1,6-bisphosphate
1ldnA Structure of a ternary complex of an allosteric lactate dehydrogenase from bacillus stearothermophilus at 2.5 angstroms resolution (see paper)
40% identity, 97% coverage: 2:302/309 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 (≠ H162), N170 (≠ S163), H172 (= H165)
- binding nicotinamide-adenine-dinucleotide: G15 (= G9), F16 (≠ M10), V17 (= V11), D38 (= D32), A39 (≠ R33), C81 (≠ A74), A82 (= A75), G83 (= G76), A84 (≠ V77), N85 (≠ A78), A122 (= A115), N124 (= N117), H179 (= H172), T233 (= T227), I237 (= I231)
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)
40% identity, 99% coverage: 2:306/309 of query aligns to 10:316/320 of E8ME30
- AV 18:19 (≠ MV 10:11) binding NAD(+)
- D40 (= D32) binding NAD(+)
- R45 (≠ L37) binding NAD(+)
- ITN 124:126 (≠ ASN 115:117) binding NAD(+)
- R159 (= R150) binding beta-D-fructose 1,6-bisphosphate
- KNVHAY 171:176 (≠ HSVHGF 162:167) binding beta-D-fructose 1,6-bisphosphate
1lthR T and r states in the crystals of bacterial l-lactate dehydrogenase reveal the mechanism for allosteric control (see paper)
40% identity, 99% coverage: 2:306/309 of query aligns to 3:309/313 of 1lthR
- active site: H174 (= H172)
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: R152 (= R150), K164 (≠ H162), N165 (≠ S163), H167 (= H165)
- binding nicotinamide-adenine-dinucleotide: G10 (= G9), A11 (≠ M10), V12 (= V11), D33 (= D32), I34 (≠ R33), T76 (≠ A74), A77 (= A75), P79 (≠ V77), R80 (≠ A78), I97 (≠ V95), I101 (≠ V99), I117 (≠ A115), N119 (= N117), H174 (= H172), T230 (= T227), I234 (= I231)
1lldA Molecular basis of allosteric activation of bacterial l-lactate dehydrogenase (see paper)
40% identity, 99% coverage: 2:306/309 of query aligns to 3:309/313 of 1lldA
- active site: R87 (= R85), D147 (= D145), R150 (= R148), H174 (= H172)
- binding nicotinamide-adenine-dinucleotide: G10 (= G9), A11 (≠ M10), V12 (= V11), D33 (= D32), I34 (≠ R33), R38 (≠ L37), T76 (≠ A74), A77 (= A75), I101 (≠ V99), N119 (= N117), H174 (= H172), I224 (= I221), I234 (= I231)
8ab3A Crystal structure of the lactate dehydrogenase of cyanobacterium aponinum in complex with oxamate, nadh and fbp. (see paper)
39% identity, 97% coverage: 5:303/309 of query aligns to 25:324/330 of 8ab3A
- binding 1,6-di-O-phosphono-beta-D-fructofuranose: R171 (= R150), R183 (≠ H162), H186 (= H165)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G29 (= G9), Q30 (≠ M10), V31 (= V11), D52 (= D32), I53 (≠ R33), T95 (≠ A74), A96 (= A75), G97 (= G76), V98 (= V77), A99 (= A78), V136 (≠ A115), N138 (= N117), H193 (= H172), I252 (= I231)
P56511 L-lactate dehydrogenase; L-LDH; EC 1.1.1.27 from Lactiplantibacillus pentosus (Lactobacillus pentosus) (see 3 papers)
40% identity, 97% coverage: 2:302/309 of query aligns to 9:307/320 of P56511
- D39 (= D32) binding NAD(+)
- R44 (≠ L37) binding NAD(+)
- GA 83:84 (≠ GV 76:77) binding NAD(+)
- S105 (≠ E98) binding NAD(+)
- AAN 122:124 (≠ ASN 115:117) binding NAD(+)
- S147 (≠ T140) binding NAD(+)
- D172 (≠ H165) 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)
40% identity, 97% coverage: 2:302/309 of query aligns to 7:305/318 of 1ez4B
- active site: R90 (= R85), D150 (= D145), R153 (= R148), H177 (= H172)
- binding nicotinamide-adenine-dinucleotide: G14 (= G9), A15 (≠ M10), V16 (= V11), D37 (= D32), T79 (≠ A74), A80 (= A75), G81 (= G76), I100 (≠ V95), A120 (= A115), N122 (= N117), V124 (= V119), S145 (≠ T140), H177 (= H172), I234 (= I231)
Q5HJD7 L-lactate dehydrogenase 1; L-LDH 1; EC 1.1.1.27 from Staphylococcus aureus (strain COL)
39% identity, 98% coverage: 2:303/309 of query aligns to 8:308/317 of Q5HJD7
- AV 16:17 (≠ MV 10:11) binding NAD(+)
- D38 (= D32) binding NAD(+)
- GA 83:84 (≠ GV 76:77) binding NAD(+)
- R92 (= R85) binding substrate
- S147 (≠ T140) binding NAD(+)
- T232 (= T227) binding substrate
Query Sequence
>WP_110806898.1 NCBI__GCF_003217355.1:WP_110806898.1
MKVGIVGAGMVGSAAGFAIAMRGGAREVVFVDRNAALAQAQAEDIGHAVPFAHPVKLGAG
DYEVLAGAGIVILAAGVAQKPGESRLSLLARNAEVFSEVIARVRQHAPDALLIVASNPVD
IMTEVAQRASGLPPERVIGTGTLLDSARFRALLAGHLGVAAHSVHGFVLGEHGDSEVLAW
SSARVGAEPLDRIALQLGVAITEEVRAKIDAGVRQAAYRIIAGKGATWYGIGAGLARLVQ
AIRDDQRAVMSVSIRSPEVAGIADVALSLPRVIGAAGVVSTLVPSLDDGEWAALKRSAEV
LKDSTAGLW
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