SitesBLAST
Comparing BPHYT_RS11290 FitnessBrowser__BFirm:BPHYT_RS11290 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)
48% 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 (≠ S48), 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)
44% 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 (= E209), T217 (= T210), V238 (≠ A231), A239 (≠ S232), R240 (= R233), D264 (= D257), H287 (= H281), G289 (= G283)
2dbqA Crystal structure of glyoxylate reductase (ph0597) from pyrococcus horikoshii ot3, complexed with NADP (i41) (see paper)
44% 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)
O58320 Glyoxylate reductase; EC 1.1.1.26 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
44% identity, 99% coverage: 3:320/321 of query aligns to 4:327/334 of O58320
2gcgA Ternary crystal structure of human glyoxylate reductase/hydroxypyruvate reductase (see paper)
45% 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)
45% identity, 76% coverage: 63:307/321 of query aligns to 75:319/328 of Q9UBQ7
Q65CJ7 Hydroxyphenylpyruvate reductase; HPPR; EC 1.1.1.237 from Plectranthus scutellarioides (Coleus) (Solenostemon scutellarioides) (see paper)
42% 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)
42% 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
40% 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, 100% coverage: 1:320/321 of query aligns to 6:322/533 of O43175
- T78 (≠ V71) binding
- R135 (≠ H128) 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
- D175 (≠ N172) binding
- T207 (≠ V204) binding
- CAR 234:236 (≠ ASR 231:233) binding
- D260 (= D257) binding
- 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
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
6plfA Crystal structure of human phgdh complexed with compound 1 (see paper)
33% identity, 96% coverage: 1:307/321 of query aligns to 2:305/305 of 6plfA
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
40% identity, 89% coverage: 23:307/321 of query aligns to 23:304/304 of 1wwkA
- active site: S96 (≠ L95), R230 (= R233), D254 (= D257), E259 (= E262), H278 (= H281)
- binding nicotinamide-adenine-dinucleotide: V100 (≠ T99), G146 (= G148), F147 (≠ L149), G148 (= G150), R149 (= R151), I150 (= I152), Y168 (= Y170), D169 (≠ T171), P170 (≠ N172), V201 (= V204), P202 (= P205), T207 (= T210), T228 (≠ A231), S229 (= S232), D254 (= D257), H278 (= H281), G280 (= G283)
7dkmA Phgdh covalently linked to oridonin (see paper)
33% identity, 94% coverage: 1:302/321 of query aligns to 2:300/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (≠ V71), A102 (≠ T99), G148 (= G148), R151 (= R151), I152 (= I152), Y170 (≠ T171), D171 (≠ N172), P172 (≠ R173), I173 (≠ S174), H202 (≠ Q203), T203 (≠ V204), P204 (= P205), T209 (= T210), C230 (≠ A231), A231 (≠ S232), R232 (= R233), H279 (= H281), G281 (= G283)
- binding (1beta,6beta,7beta,8alpha,9beta,10alpha,13alpha,14R,16beta)-1,6,7,14-tetrahydroxy-7,20-epoxykauran-15-one: C14 (≠ D13), K17 (≠ A16), I18 (≠ Y17), E293 (≠ R295)
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
33% identity, 94% coverage: 1:302/321 of query aligns to 1:299/301 of 6rj5A
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
33% identity, 94% coverage: 1:302/321 of query aligns to 1:299/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (≠ V147), G147 (= G148), L148 (= L149), G149 (= G150), R150 (= R151), I151 (= I152), G152 (= G153), D170 (≠ N172), H201 (≠ Q203), T202 (≠ V204), P203 (= P205)
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
33% identity, 94% coverage: 1:302/321 of query aligns to 1:299/302 of 6rihA
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
33% identity, 94% coverage: 1:302/321 of query aligns to 1:299/303 of 6plgA
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
33% identity, 94% coverage: 2:302/321 of query aligns to 1:298/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (≠ L95), A100 (≠ T99), R149 (= R151), I150 (= I152), Y168 (≠ T171), D169 (≠ N172), P170 (≠ R173), I171 (≠ S174), H200 (≠ Q203), T201 (≠ V204), P202 (= P205), T207 (= T210), C228 (≠ A231), A229 (≠ S232), R230 (= R233), H277 (= H281), G279 (= G283)
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
34% identity, 90% coverage: 2:290/321 of query aligns to 1:286/297 of 6rj3A
6rj2A Crystal structure of phgdh in complex with compound 40 (see paper)
34% identity, 87% coverage: 23:302/321 of query aligns to 21:296/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (= G150), I148 (= I152), Y166 (≠ T171), D167 (≠ N172), P168 (≠ R173), I169 (≠ S174), I170 (≠ A175), H198 (≠ Q203), T199 (≠ V204), L208 (= L213), R228 (= R233)
Query Sequence
>BPHYT_RS11290 FitnessBrowser__BFirm:BPHYT_RS11290
MKKIVAWKSLPEDVLAYLQQHAQVVQVDATQHDAFVAALKDADGGIGSSVKITPAMLEGA
TRLKALSTISVGFDQFDVADLTRRGIVLANTPDVLTESTADTVFSLILASARRVVELAEW
VKAGHWQHSIGPALFGVDVQGKTLGIVGLGRIGGAVARRAALGFNMKVLYTNRSANPQAE
EAYGARRVELAELLATADFVCLQVPLTPETKHLIGAAELKSMKKSAILINASRGATVDEK
ALIEALQNGTIHGAGLDVFETEPLPSDSPLLKLANVVALPHIGSATHETRHAMARNAAEN
LVAALDGTLTSNIVNREVLSK
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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