SitesBLAST
Comparing H281DRAFT_05213 FitnessBrowser__Burk376:H281DRAFT_05213 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)
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
47% identity, 90% coverage: 32:320/321 of query aligns to 36:327/334 of 5aovA
- active site: L100 (= L95), R241 (= R233), D265 (= D257), E270 (= E262), H288 (= H281)
- binding glyoxylic acid: M52 (≠ A48), L53 (vs. gap), L53 (vs. gap), Y74 (≠ I69), A75 (≠ S70), V76 (= V71), G77 (= G72), R241 (= R233), H288 (= H281)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (= V71), T104 (= T99), F158 (≠ L149), G159 (= G150), R160 (= R151), I161 (= I152), S180 (≠ N172), R181 (= R173), A211 (≠ Q203), V212 (= V204), P213 (= P205), T218 (= T210), I239 (≠ A231), A240 (≠ S232), R241 (= R233), H288 (= H281), G290 (= G283)
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
45% identity, 99% coverage: 3:320/321 of query aligns to 3:326/332 of 6biiA
- active site: L99 (= L95), R240 (= R233), D264 (= D257), E269 (= E262), H287 (= H281)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V75 (= V71), T103 (= T99), G156 (= G148), F157 (≠ L149), G158 (= G150), R159 (= R151), I160 (= I152), A179 (≠ N172), R180 (= R173), S181 (= S174), K183 (≠ N176), V211 (= V204), P212 (= P205), E216 (≠ Q209), T217 (= T210), V238 (≠ A231), A239 (≠ S232), R240 (= R233), D264 (= D257), H287 (= H281), G289 (= G283)
O58320 Glyoxylate reductase; EC 1.1.1.26 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
43% identity, 99% coverage: 3:320/321 of query aligns to 4:327/334 of O58320
2dbqA Crystal structure of glyoxylate reductase (ph0597) from pyrococcus horikoshii ot3, complexed with NADP (i41) (see paper)
43% identity, 99% coverage: 3:320/321 of query aligns to 4:327/333 of 2dbqA
- active site: L100 (= L95), R241 (= R233), D265 (= D257), E270 (= E262), H288 (= H281)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (= V71), T104 (= T99), L158 (= L149), G159 (= G150), R160 (= R151), I161 (= I152), S180 (≠ N172), R181 (= R173), T182 (≠ S174), A211 (≠ Q203), V212 (= V204), P213 (= P205), T218 (= T210), I239 (≠ A231), A240 (≠ S232), R241 (= R233), D265 (= D257), H288 (= H281), G290 (= G283)
2gcgA Ternary crystal structure of human glyoxylate reductase/hydroxypyruvate reductase (see paper)
44% identity, 76% coverage: 63:307/321 of query aligns to 71:315/324 of 2gcgA
- active site: L103 (= L95), R241 (= R233), D265 (= D257), E270 (= E262), H289 (= H281)
- binding (2r)-2,3-dihydroxypropanoic acid: S78 (= S70), V79 (= V71), G80 (= G72), R241 (= R233), H289 (= H281)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V79 (= V71), T107 (= T99), G156 (= G148), G158 (= G150), I160 (= I152), G180 (≠ N172), R181 (= R173), R184 (≠ N176), C212 (≠ V204), S213 (≠ P205), T218 (= T210), I239 (≠ A231), R241 (= R233), D265 (= D257), H289 (= H281), G291 (= G283)
Sites not aligning to the query:
Q9UBQ7 Glyoxylate reductase/hydroxypyruvate reductase; EC 1.1.1.79; EC 1.1.1.81 from Homo sapiens (Human) (see paper)
44% identity, 76% coverage: 63:307/321 of query aligns to 75:319/328 of Q9UBQ7
- VG 83:84 (= VG 71:72) binding substrate
- GRI 162:164 (= GRI 150:152) binding NADP(+)
- RQPR 185:188 (≠ RSAN 173:176) binding NADP(+)
- S217 (≠ P205) binding NADP(+)
- I243 (≠ A231) binding NADP(+)
- R245 (= R233) binding substrate
- D269 (= D257) binding substrate
- HIGS 293:296 (= HIGS 281:284) binding substrate
- G295 (= G283) binding NADP(+)
Q65CJ7 Hydroxyphenylpyruvate reductase; HPPR; EC 1.1.1.237 from Plectranthus scutellarioides (Coleus) (Solenostemon scutellarioides) (see paper)
40% identity, 79% coverage: 56:307/321 of query aligns to 61:305/313 of Q65CJ7
3bazA Structure of hydroxyphenylpyruvate reductase from coleus blumei in complex with NADP+ (see paper)
40% identity, 79% coverage: 56:307/321 of query aligns to 59:303/311 of 3bazA
- active site: L98 (= L95), R230 (= R233), A251 (= A254), D254 (= D257), E259 (= E262), H277 (= H281)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V74 (= V71), G149 (= G148), L150 (= L149), G151 (= G150), R152 (= R151), I153 (= I152), S172 (≠ N172), R173 (= R173), S174 (= S174), C201 (≠ V204), P202 (= P205), T207 (= T210), I228 (≠ A231), G229 (≠ S232), R230 (= R233), D254 (= D257), H277 (= H281), G279 (= G283)
6ih6A Phosphite dehydrogenase mutant i151r/p176r/m207a from ralstonia sp. 4506 in complex with non-natural cofactor nicotinamide cytosine dinucleotide
38% identity, 88% coverage: 36:316/321 of query aligns to 40:328/330 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 (= T99), R151 (≠ V147), G154 (= G150), A155 (≠ R151), V156 (≠ I152), D175 (≠ N172), A207 (≠ Q203), V208 (= V204), P209 (= P205), T214 (= T210), A235 (= A231), C236 (≠ S232), R237 (= R233)
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)
32% identity, 99% coverage: 1:319/321 of query aligns to 6:321/533 of O43175
- T78 (≠ V71) binding NAD(+)
- R135 (≠ Q128) 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 (= RI 151:152) binding NAD(+)
- D175 (≠ N172) binding NAD(+)
- T207 (≠ V204) binding NAD(+)
- CAR 234:236 (≠ ASR 231:233) binding NAD(+)
- D260 (= D257) binding NAD(+)
- V261 (= V258) 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 281:284) binding NAD(+)
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
5j23A Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase smc04462 (smghrb) from sinorhizobium meliloti in complex with 2'-phospho-adp-ribose (see paper)
38% identity, 90% coverage: 14:303/321 of query aligns to 14:297/318 of 5j23A
- active site: L94 (= L95), R228 (= R233), D252 (= D257), E257 (= E262), H275 (= H281)
- binding [(2r,3r,4r,5r)-5-(6-amino-9h-purin-9-yl)-3-hydroxy-4-(phosphonooxy)tetrahydrofuran-2-yl]methyl [(2r,3s,4r,5r)-3,4,5-trihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate: V70 (= V71), L148 (= L149), G149 (= G150), R150 (= R151), I151 (= I152), T170 (≠ N172), R171 (= R173), P200 (= P205), S204 (≠ Q209), T205 (= T210), R228 (= R233)
5v7nA Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase smc04462 (smghrb) from sinorhizobium meliloti in complex with NADP and 2-keto-d-gluconic acid (see paper)
38% identity, 90% coverage: 14:303/321 of query aligns to 15:298/319 of 5v7nA
- active site: L95 (= L95), R229 (= R233), D253 (= D257), E258 (= E262), H276 (= H281)
- binding 2-keto-D-gluconic acid: G70 (≠ S70), V71 (= V71), G72 (= G72), R229 (= R233), H276 (= H281), S279 (= S284), R285 (= R290)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V71 (= V71), V99 (≠ T99), L149 (= L149), G150 (= G150), R151 (= R151), I152 (= I152), T171 (≠ N172), R172 (= R173), V200 (= V204), P201 (= P205), S205 (≠ Q209), T206 (= T210), V227 (≠ A231), G228 (≠ S232), R229 (= R233), H276 (= H281), A278 (≠ G283)
5v7gA Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase smc04462 (smghrb) from sinorhizobium meliloti in complex with NADPH and oxalate (see paper)
38% identity, 90% coverage: 14:303/321 of query aligns to 14:297/317 of 5v7gA
- active site: L94 (= L95), R228 (= R233), D252 (= D257), E257 (= E262), H275 (= H281)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V70 (= V71), V98 (≠ T99), F146 (≠ V147), L148 (= L149), G149 (= G150), R150 (= R151), I151 (= I152), T170 (≠ N172), R171 (= R173), V199 (= V204), P200 (= P205), S204 (≠ Q209), T205 (= T210), V226 (≠ A231), G227 (≠ S232), R228 (= R233), H275 (= H281), A277 (≠ G283)
- binding oxalate ion: G69 (≠ S70), V70 (= V71), G71 (= G72), R228 (= R233), H275 (= H281)
5v6qB Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase smc04462 (smghrb) from sinorhizobium meliloti in complex with NADP and malonate (see paper)
38% identity, 90% coverage: 14:303/321 of query aligns to 16:299/319 of 5v6qB
- active site: L96 (= L95), R230 (= R233), D254 (= D257), E259 (= E262), H277 (= H281)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V72 (= V71), V100 (≠ T99), F148 (≠ V147), L150 (= L149), G151 (= G150), R152 (= R151), I153 (= I152), T172 (≠ N172), R173 (= R173), V201 (= V204), P202 (= P205), S206 (≠ Q209), T207 (= T210), V228 (≠ A231), G229 (≠ S232), R230 (= R233), H277 (= H281), A279 (≠ G283)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
39% identity, 89% coverage: 22:307/321 of query aligns to 22:304/304 of 1wwkA