SitesBLAST
Comparing WP_012709967.1 NCBI__GCF_000018545.1:WP_012709967.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
45% identity, 97% coverage: 6:329/334 of query aligns to 2:321/334 of 5aovA
- active site: L100 (= L105), R241 (= R246), D265 (= D270), E270 (= E275), H288 (= H296)
- binding glyoxylic acid: M52 (≠ T56), L53 (≠ V57), L53 (≠ V57), Y74 (≠ F79), A75 (≠ S80), V76 (≠ N81), G77 (= G82), R241 (= R246), H288 (= H296)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ N81), T104 (= T109), F158 (≠ M161), G159 (= G162), R160 (= R163), I161 (= I164), S180 (≠ N183), R181 (= R184), A211 (≠ N216), V212 (≠ C217), P213 (= P218), T218 (= T223), I239 (≠ T244), A240 (= A245), R241 (= R246), H288 (= H296), G290 (≠ S298)
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
43% identity, 96% coverage: 6:326/334 of query aligns to 1:317/332 of 6biiA
- active site: L99 (= L105), R240 (= R246), D264 (= D270), E269 (= E275), H287 (= H296)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V75 (≠ N81), T103 (= T109), G156 (= G160), F157 (≠ M161), G158 (= G162), R159 (= R163), I160 (= I164), A179 (≠ N183), R180 (= R184), S181 (≠ H185), K183 (= K188), V211 (≠ C217), P212 (= P218), E216 (≠ A222), T217 (= T223), V238 (≠ T244), A239 (= A245), R240 (= R246), D264 (= D270), H287 (= H296), G289 (≠ S298)
O58320 Glyoxylate reductase; EC 1.1.1.26 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
43% identity, 96% coverage: 6:326/334 of query aligns to 2:318/334 of O58320
2dbqA Crystal structure of glyoxylate reductase (ph0597) from pyrococcus horikoshii ot3, complexed with NADP (i41) (see paper)
43% identity, 96% coverage: 6:326/334 of query aligns to 2:318/333 of 2dbqA
- active site: L100 (= L105), R241 (= R246), D265 (= D270), E270 (= E275), H288 (= H296)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ N81), T104 (= T109), L158 (≠ M161), G159 (= G162), R160 (= R163), I161 (= I164), S180 (≠ N183), R181 (= R184), T182 (≠ H185), A211 (≠ N216), V212 (≠ C217), P213 (= P218), T218 (= T223), I239 (≠ T244), A240 (= A245), R241 (= R246), D265 (= D270), H288 (= H296), G290 (≠ S298)
Q65CJ7 Hydroxyphenylpyruvate reductase; HPPR; EC 1.1.1.237 from Plectranthus scutellarioides (Coleus) (Solenostemon scutellarioides) (see paper)
42% identity, 78% coverage: 62:322/334 of query aligns to 58:305/313 of Q65CJ7
3bazA Structure of hydroxyphenylpyruvate reductase from coleus blumei in complex with NADP+ (see paper)
42% identity, 78% coverage: 62:322/334 of query aligns to 56:303/311 of 3bazA
- active site: L98 (= L105), R230 (= R246), A251 (= A267), D254 (= D270), E259 (= E275), H277 (= H296)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V74 (≠ N81), G149 (= G160), L150 (≠ M161), G151 (= G162), R152 (= R163), I153 (= I164), S172 (≠ N183), R173 (= R184), S174 (≠ H185), C201 (= C217), P202 (= P218), T207 (= T223), I228 (≠ T244), G229 (≠ A245), R230 (= R246), D254 (= D270), H277 (= H296), G279 (≠ S298)
5v6qB Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase smc04462 (smghrb) from sinorhizobium meliloti in complex with NADP and malonate (see paper)
39% identity, 95% coverage: 5:321/334 of query aligns to 2:302/319 of 5v6qB
- active site: L96 (= L105), R230 (= R246), D254 (= D270), E259 (= E275), H277 (= H296)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V72 (≠ N81), V100 (≠ T109), F148 (≠ V159), L150 (≠ M161), G151 (= G162), R152 (= R163), I153 (= I164), T172 (≠ N183), R173 (= R184), V201 (≠ C217), P202 (= P218), S206 (≠ A222), T207 (= T223), V228 (≠ T244), G229 (≠ A245), R230 (= R246), H277 (= H296), A279 (≠ S298)
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)
39% identity, 95% coverage: 5:321/334 of query aligns to 1:301/319 of 5v7nA
- active site: L95 (= L105), R229 (= R246), D253 (= D270), E258 (= E275), H276 (= H296)
- binding 2-keto-D-gluconic acid: G70 (≠ S80), V71 (≠ N81), G72 (= G82), R229 (= R246), H276 (= H296), S279 (= S299), R285 (= R305)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V71 (≠ N81), V99 (≠ T109), L149 (≠ M161), G150 (= G162), R151 (= R163), I152 (= I164), T171 (≠ N183), R172 (= R184), V200 (≠ C217), P201 (= P218), S205 (≠ A222), T206 (= T223), V227 (≠ T244), G228 (≠ A245), R229 (= R246), H276 (= H296), A278 (≠ S298)
5v7gA Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase smc04462 (smghrb) from sinorhizobium meliloti in complex with NADPH and oxalate (see paper)
39% identity, 95% coverage: 6:321/334 of query aligns to 1:300/317 of 5v7gA
- active site: L94 (= L105), R228 (= R246), D252 (= D270), E257 (= E275), H275 (= H296)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V70 (≠ N81), V98 (≠ T109), F146 (≠ V159), L148 (≠ M161), G149 (= G162), R150 (= R163), I151 (= I164), T170 (≠ N183), R171 (= R184), V199 (≠ C217), P200 (= P218), S204 (≠ A222), T205 (= T223), V226 (≠ T244), G227 (≠ A245), R228 (= R246), H275 (= H296), A277 (≠ S298)
- binding oxalate ion: G69 (≠ S80), V70 (≠ N81), G71 (= G82), R228 (= R246), H275 (= H296)
5j23A Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase smc04462 (smghrb) from sinorhizobium meliloti in complex with 2'-phospho-adp-ribose (see paper)
39% identity, 95% coverage: 6:321/334 of query aligns to 1:300/318 of 5j23A
- active site: L94 (= L105), R228 (= R246), D252 (= D270), E257 (= E275), H275 (= H296)
- 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 (≠ N81), L148 (≠ M161), G149 (= G162), R150 (= R163), I151 (= I164), T170 (≠ N183), R171 (= R184), P200 (= P218), S204 (≠ A222), T205 (= T223), R228 (= R246)
Q9UBQ7 Glyoxylate reductase/hydroxypyruvate reductase; EC 1.1.1.79; EC 1.1.1.81 from Homo sapiens (Human) (see paper)
32% identity, 96% coverage: 9:329/334 of query aligns to 9:326/328 of Q9UBQ7
- VG 83:84 (≠ NG 81:82) binding substrate
- GRI 162:164 (= GRI 162:164) binding NADP(+)
- RQPR 185:188 (≠ HRVK 185:188) binding NADP(+)
- S217 (≠ P218) binding NADP(+)
- I243 (≠ T244) binding NADP(+)
- R245 (= R246) binding substrate
- D269 (= D270) binding substrate
- HIGS 293:296 (≠ HMSS 296:299) binding substrate
- G295 (≠ S298) binding NADP(+)
2gcgA Ternary crystal structure of human glyoxylate reductase/hydroxypyruvate reductase (see paper)
32% identity, 96% coverage: 9:329/334 of query aligns to 5:322/324 of 2gcgA
- active site: L103 (= L105), R241 (= R246), D265 (= D270), E270 (= E275), H289 (= H296)
- binding (2r)-2,3-dihydroxypropanoic acid: L55 (≠ V57), S78 (= S80), V79 (≠ N81), G80 (= G82), R241 (= R246), H289 (= H296)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V79 (≠ N81), T107 (= T109), G156 (= G160), G158 (= G162), I160 (= I164), G180 (≠ R184), R181 (≠ H185), R184 (≠ K188), C212 (= C217), S213 (≠ P218), T218 (= T223), I239 (≠ T244), R241 (= R246), D265 (= D270), H289 (= H296), G291 (≠ S298)
6ih6A Phosphite dehydrogenase mutant i151r/p176r/m207a from ralstonia sp. 4506 in complex with non-natural cofactor nicotinamide cytosine dinucleotide
34% identity, 96% coverage: 6:325/334 of query aligns to 2:322/330 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 (= T109), R151 (≠ V159), G154 (= G162), A155 (≠ R163), V156 (≠ I164), D175 (≠ N183), A207 (≠ N216), V208 (≠ C217), P209 (= P218), T214 (= T223), A235 (≠ T244), C236 (≠ A245), R237 (= R246)
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
32% identity, 89% coverage: 26:322/334 of query aligns to 20:320/334 of 3kb6B
- active site: S97 (≠ L105), R231 (= R246), D255 (= D270), E260 (= E275), H294 (= H296)
- binding lactic acid: F49 (≠ T56), S72 (= S80), V73 (≠ N81), G74 (= G82), Y96 (≠ V104), R231 (= R246), H294 (= H296)
- binding nicotinamide-adenine-dinucleotide: V73 (≠ N81), Y96 (≠ V104), V101 (≠ T109), G150 (= G162), R151 (= R163), I152 (= I164), D171 (≠ N183), V172 (≠ R184), P203 (= P218), T229 (= T244), A230 (= A245), R231 (= R246), H294 (= H296), A296 (≠ S298), Y297 (≠ S299)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
38% identity, 88% coverage: 20:313/334 of query aligns to 11:299/304 of 1wwkA
- active site: S96 (≠ L105), R230 (= R246), D254 (= D270), E259 (= E275), H278 (= H296)
- binding nicotinamide-adenine-dinucleotide: V100 (≠ T109), G146 (= G160), F147 (≠ M161), G148 (= G162), R149 (= R163), I150 (= I164), Y168 (vs. gap), D169 (vs. gap), P170 (vs. gap), V201 (≠ C217), P202 (= P218), T207 (= T223), T228 (= T244), S229 (≠ A245), D254 (= D270), H278 (= H296), G280 (≠ S298)
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
36% identity, 86% coverage: 42:329/334 of query aligns to 35:311/525 of 3ddnB
4e5mA Thermostable phosphite dehydrogenase e175a/a176r in complex with NADP (see paper)
29% identity, 97% coverage: 7:329/334 of query aligns to 3:325/329 of 4e5mA
- active site: L100 (= L105), R237 (= R246), D261 (= D270), E266 (= E275), H292 (= H296)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K76 (≠ N81), L100 (= L105), T104 (= T109), G154 (= G162), A155 (≠ R163), I156 (= I164), R176 (= R184), L208 (≠ C217), P209 (= P218), T214 (= T223), P235 (≠ T244), C236 (≠ A245), R237 (= R246), H292 (= H296), G294 (≠ S298)
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
36% identity, 86% coverage: 42:329/334 of query aligns to 34:310/526 of 3dc2A
Sites not aligning to the query:
4e5pA Thermostable phosphite dehydrogenase a176r variant in complex with nad (see paper)
29% identity, 97% coverage: 7:329/334 of query aligns to 3:325/332 of 4e5pA
- active site: L100 (= L105), R237 (= R246), D261 (= D270), E266 (= E275), H292 (= H296)
- binding nicotinamide-adenine-dinucleotide: K76 (≠ N81), L100 (= L105), T104 (= T109), G154 (= G162), A155 (≠ R163), I156 (= I164), A175 (≠ N183), R176 (= R184), L208 (≠ C217), P209 (= P218), T214 (= T223), P235 (≠ T244), C236 (≠ A245), R237 (= R246), H292 (= H296)
4e5kA Thermostable phosphite dehydrogenase in complex with NAD and sulfite (see paper)
29% identity, 97% coverage: 7:329/334 of query aligns to 3:325/329 of 4e5kA
- active site: L100 (= L105), R237 (= R246), D261 (= D270), E266 (= E275), H292 (= H296)
- binding nicotinamide-adenine-dinucleotide: K76 (≠ N81), G77 (= G82), L100 (= L105), T104 (= T109), G152 (= G160), G154 (= G162), A155 (≠ R163), I156 (= I164), H174 (= H182), E175 (≠ N183), A176 (≠ R184), A207 (≠ N216), L208 (≠ C217), P209 (= P218), P235 (≠ T244), C236 (≠ A245), R237 (= R246), D261 (= D270), H292 (= H296), G294 (≠ S298)
- binding sulfite ion: M53 (≠ V57), L75 (≠ S80), K76 (≠ N81), G77 (= G82), L100 (= L105), R237 (= R246), H292 (= H296)
Query Sequence
>WP_012709967.1 NCBI__GCF_000018545.1:WP_012709967.1
MTSKKKPTVYITRKLPDVVETRMRELFDAELNIDDTPRSQPELVAAVKRVDVLVPTVTDR
IDAALIEQAGPQLKLIAAFSNGVDNIDVDTAARKGITVTNTPNVLTEDTADMTMALILAV
PRRLAEGAQVLTDRKGEWAGWSPTWMLGRRIAGKRIGIVGMGRIGTAVARRARAFGLSIH
YHNRHRVKRETEEMLEATYWDSLDQMLARVDIVSVNCPSTPATYHLLSARRLALMRPDSY
IVNTARGDVIDETAMIKCLREGKIAGAGLDVFENEPAVNPKLIKLAGEGKVVLLPHMSSA
TLEGRIDMGEKVVINIRTFFDGHRPPDRVLPGRD
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