SitesBLAST
Comparing GFF427 Psest_0431 Lactate dehydrogenase and related dehydrogenases 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)
4e5kA Thermostable phosphite dehydrogenase in complex with NAD and sulfite (see paper)
96% identity, 98% coverage: 1:329/336 of query aligns to 1:329/329 of 4e5kA
- active site: L100 (= L100), R237 (= R237), D261 (= D261), E266 (= E266), H292 (= H292)
- binding nicotinamide-adenine-dinucleotide: K76 (= K76), G77 (= G77), L100 (= L100), T104 (= T104), G152 (= G152), G154 (= G154), A155 (= A155), I156 (= I156), H174 (= H174), E175 (= E175), A176 (= A176), A207 (= A207), L208 (= L208), P209 (= P209), P235 (= P235), C236 (= C236), R237 (= R237), D261 (= D261), H292 (= H292), G294 (= G294)
- binding sulfite ion: M53 (= M53), L75 (= L75), K76 (= K76), G77 (= G77), L100 (= L100), R237 (= R237), H292 (= H292)
4e5pA Thermostable phosphite dehydrogenase a176r variant in complex with nad (see paper)
95% identity, 99% coverage: 1:332/336 of query aligns to 1:332/332 of 4e5pA
- active site: L100 (= L100), R237 (= R237), D261 (= D261), E266 (= E266), H292 (= H292)
- binding nicotinamide-adenine-dinucleotide: K76 (= K76), L100 (= L100), T104 (= T104), G154 (= G154), A155 (= A155), I156 (= I156), A175 (≠ E175), R176 (≠ A176), L208 (= L208), P209 (= P209), T214 (= T214), P235 (= P235), C236 (= C236), R237 (= R237), H292 (= H292)
4e5mA Thermostable phosphite dehydrogenase e175a/a176r in complex with NADP (see paper)
95% identity, 98% coverage: 1:329/336 of query aligns to 1:329/329 of 4e5mA
- active site: L100 (= L100), R237 (= R237), D261 (= D261), E266 (= E266), H292 (= H292)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K76 (= K76), L100 (= L100), T104 (= T104), G154 (= G154), A155 (= A155), I156 (= I156), R176 (≠ A176), L208 (= L208), P209 (= P209), T214 (= T214), P235 (= P235), C236 (= C236), R237 (= R237), H292 (= H292), G294 (= G294)
6ih6A Phosphite dehydrogenase mutant i151r/p176r/m207a from ralstonia sp. 4506 in complex with non-natural cofactor nicotinamide cytosine dinucleotide
56% identity, 97% coverage: 1:327/336 of query aligns to 1:328/330 of 6ih6A
- binding [[(2S,3S,4R,5S)-5-(3-aminocarbonylpyridin-1-ium-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2S,3S,4R,5S)-5-(4-azanyl-2-oxidanylidene-pyrimidin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl hydrogen phosphate: T104 (= T104), R151 (≠ L151), G154 (= G154), A155 (= A155), V156 (≠ I156), D175 (≠ E175), A207 (= A207), V208 (≠ L208), P209 (= P209), T214 (= T214), A235 (≠ P235), C236 (= C236), R237 (= R237)
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
34% identity, 97% coverage: 1:327/336 of query aligns to 1:323/334 of 5aovA
- active site: L100 (= L100), R241 (= R237), D265 (= D261), E270 (= E266), H288 (= H292)
- binding glyoxylic acid: M52 (≠ F52), L53 (≠ M53), L53 (≠ M53), Y74 (≠ A74), A75 (≠ L75), V76 (≠ K76), G77 (= G77), R241 (= R237), H288 (= H292)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ K76), T104 (= T104), F158 (≠ M153), G159 (= G154), R160 (≠ A155), I161 (= I156), S180 (≠ A176), R181 (≠ K177), A211 (= A207), V212 (≠ L208), P213 (= P209), T218 (= T214), I239 (≠ P235), A240 (≠ C236), R241 (= R237), H288 (= H292), G290 (= G294)
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
36% identity, 97% coverage: 3:327/336 of query aligns to 2:322/332 of 6biiA
- active site: L99 (= L100), R240 (= R237), D264 (= D261), E269 (= E266), H287 (= H292)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V75 (≠ K76), T103 (= T104), G156 (= G152), F157 (≠ M153), G158 (= G154), R159 (≠ A155), I160 (= I156), A179 (= A176), R180 (≠ K177), S181 (≠ A178), K183 (≠ D180), V211 (≠ L208), P212 (= P209), E216 (≠ D213), T217 (= T214), V238 (≠ P235), A239 (≠ C236), R240 (= R237), D264 (= D261), H287 (= H292), G289 (= G294)
O58320 Glyoxylate reductase; EC 1.1.1.26 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
33% identity, 97% coverage: 1:327/336 of query aligns to 1:323/334 of O58320
2dbqA Crystal structure of glyoxylate reductase (ph0597) from pyrococcus horikoshii ot3, complexed with NADP (i41) (see paper)
33% identity, 97% coverage: 1:327/336 of query aligns to 1:323/333 of 2dbqA
- active site: L100 (= L100), R241 (= R237), D265 (= D261), E270 (= E266), H288 (= H292)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ K76), T104 (= T104), L158 (≠ M153), G159 (= G154), R160 (≠ A155), I161 (= I156), S180 (≠ A176), R181 (≠ K177), T182 (≠ A178), A211 (= A207), V212 (≠ L208), P213 (= P209), T218 (= T214), I239 (≠ P235), A240 (≠ C236), R241 (= R237), D265 (= D261), H288 (= H292), G290 (= G294)
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
33% identity, 84% coverage: 33:314/336 of query aligns to 30:297/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (= L151), G147 (= G152), L148 (≠ M153), G149 (= G154), R150 (≠ A155), I151 (= I156), G152 (= G157), D170 (≠ H174), H201 (≠ A207), T202 (≠ L208), P203 (= P209)
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
33% identity, 84% coverage: 33:314/336 of query aligns to 30:297/302 of 6rihA
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
33% identity, 84% coverage: 33:314/336 of query aligns to 30:297/301 of 6rj5A
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
33% identity, 84% coverage: 33:314/336 of query aligns to 30:297/303 of 6plgA
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
33% identity, 84% coverage: 33:314/336 of query aligns to 29:296/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (≠ L100), A100 (≠ T104), R149 (≠ A155), I150 (= I156), Y168 (= Y173), D169 (≠ H174), P170 (≠ K177), I171 (≠ A178), H200 (≠ A207), T201 (≠ L208), P202 (= P209), T207 (= T214), C228 (≠ P235), A229 (≠ C236), R230 (= R237), H277 (= H292), G279 (= G294)
6plfA Crystal structure of human phgdh complexed with compound 1 (see paper)
33% identity, 84% coverage: 33:314/336 of query aligns to 31:298/305 of 6plfA
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
33% identity, 84% coverage: 33:314/336 of query aligns to 29:296/297 of 6rj3A
7dkmA Phgdh covalently linked to oridonin (see paper)
33% identity, 84% coverage: 33:314/336 of query aligns to 31:298/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (≠ K76), A102 (≠ T104), G148 (= G152), R151 (≠ A155), I152 (= I156), Y170 (= Y173), D171 (≠ H174), P172 (≠ K177), I173 (≠ A178), H202 (≠ A207), T203 (≠ L208), P204 (= P209), T209 (= T214), C230 (≠ P235), A231 (≠ C236), R232 (= R237), H279 (= H292), G281 (= G294)
- binding (1beta,6beta,7beta,8alpha,9beta,10alpha,13alpha,14R,16beta)-1,6,7,14-tetrahydroxy-7,20-epoxykauran-15-one: E293 (≠ A309)
Sites not aligning to the query:
- binding (1beta,6beta,7beta,8alpha,9beta,10alpha,13alpha,14R,16beta)-1,6,7,14-tetrahydroxy-7,20-epoxykauran-15-one: 14, 17, 18
6rj2A Crystal structure of phgdh in complex with compound 40 (see paper)
33% identity, 84% coverage: 33:314/336 of query aligns to 27:294/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (= G154), I148 (= I156), Y166 (= Y173), D167 (≠ H174), P168 (≠ K177), I169 (≠ A178), I170 (≠ L179), H198 (≠ A207), T199 (≠ L208), L208 (= L217), R228 (= R237)
O43175 D-3-phosphoglycerate dehydrogenase; 3-PGDH; 2-oxoglutarate reductase; Malate dehydrogenase; EC 1.1.1.95; EC 1.1.1.399; EC 1.1.1.37 from Homo sapiens (Human) (see 3 papers)
33% identity, 84% coverage: 33:314/336 of query aligns to 35:302/533 of O43175
- T78 (≠ K76) binding
- R135 (≠ Q135) to W: in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity; dbSNP:rs267606949
- RI 155:156 (≠ AI 155:156) binding
- D175 (≠ H174) binding
- T207 (≠ L208) binding
- CAR 234:236 (≠ PCR 235:237) binding
- D260 (= D261) binding
- V261 (= V262) to M: in PHGDHD; results in a four-fold decrease in substrate affinity and a slight increase in maximal enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs267606947
- HLGA 283:286 (≠ HIGS 292:295) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 373 A → T: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs201553627
- 377 G → S: in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity; dbSNP:rs267606948
- 425 V → M: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs121907988
- 490 V → M: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs121907987
2gcgA Ternary crystal structure of human glyoxylate reductase/hydroxypyruvate reductase (see paper)
31% identity, 94% coverage: 2:318/336 of query aligns to 2:315/324 of 2gcgA
- active site: L103 (= L100), R241 (= R237), D265 (= D261), E270 (= E266), H289 (= H292)
- binding (2r)-2,3-dihydroxypropanoic acid: L55 (≠ M53), S78 (≠ L75), V79 (≠ K76), G80 (= G77), R241 (= R237), H289 (= H292)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V79 (≠ K76), T107 (= T104), G156 (= G152), G158 (= G154), I160 (= I156), G180 (≠ A176), R181 (≠ K177), R184 (≠ D180), C212 (≠ L208), S213 (≠ P209), T218 (= T214), I239 (≠ P235), R241 (= R237), D265 (= D261), H289 (= H292), G291 (= G294)
Q9UBQ7 Glyoxylate reductase/hydroxypyruvate reductase; EC 1.1.1.79; EC 1.1.1.81 from Homo sapiens (Human) (see paper)
31% identity, 94% coverage: 2:318/336 of query aligns to 6:319/328 of Q9UBQ7
Query Sequence
>GFF427 Psest_0431 Lactate dehydrogenase and related dehydrogenases
MLPKLVITHRVHDEILQLLAPHCELMTNQTDSTLPREEILRRCRDAQAMMAFMPDRVDAD
FLQACPELRVVGCALKGFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLR
AADAFVRSGKFQGWQPQFYGTGLDNATVGILGMGAIGLAMADRLQGWGATLQYHEAKALD
TQTEQRLGLRRVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSV
VDEAAVLAALERGQLGGYAADVFEMEDWARADRPRLIDPALLAHPNTLFTPHIGSAVRAV
RLEIERCAAQNIIQALAGARPINAANRLPKAEPAAC
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