SitesBLAST
Comparing WP_008485733.1 NCBI__GCF_000299915.1:WP_008485733.1 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)
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
48% identity, 78% coverage: 60:323/337 of query aligns to 62:325/334 of 5aovA
- active site: L100 (= L98), R241 (= R239), D265 (= D263), E270 (= E268), H288 (= H286)
- binding glyoxylic acid: Y74 (≠ V72), A75 (≠ S73), V76 (= V74), G77 (= G75), R241 (= R239), H288 (= H286)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (= V74), T104 (= T102), F158 (≠ L152), G159 (= G153), R160 (= R154), I161 (= I155), S180 (≠ G175), R181 (≠ N176), A211 (≠ V209), V212 (= V210), P213 (= P211), T218 (= T216), I239 (≠ L237), A240 (= A238), R241 (= R239), H288 (= H286), G290 (= G288)
Sites not aligning to the query:
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
50% identity, 77% coverage: 63:323/337 of query aligns to 64:324/332 of 6biiA
- active site: L99 (= L98), R240 (= R239), D264 (= D263), E269 (= E268), H287 (= H286)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V75 (= V74), T103 (= T102), G156 (= G151), F157 (≠ L152), G158 (= G153), R159 (= R154), I160 (= I155), A179 (≠ G175), R180 (≠ N176), S181 (= S177), K183 (= K182), V211 (= V210), P212 (= P211), E216 (= E215), T217 (= T216), V238 (≠ L237), A239 (= A238), R240 (= R239), D264 (= D263), H287 (= H286), G289 (= G288)
2dbqA Crystal structure of glyoxylate reductase (ph0597) from pyrococcus horikoshii ot3, complexed with NADP (i41) (see paper)
42% identity, 96% coverage: 1:323/337 of query aligns to 1:325/333 of 2dbqA
- active site: L100 (= L98), R241 (= R239), D265 (= D263), E270 (= E268), H288 (= H286)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (= V74), T104 (= T102), L158 (= L152), G159 (= G153), R160 (= R154), I161 (= I155), S180 (≠ G175), R181 (≠ N176), T182 (≠ S177), A211 (≠ V209), V212 (= V210), P213 (= P211), T218 (= T216), I239 (≠ L237), A240 (= A238), R241 (= R239), D265 (= D263), H288 (= H286), G290 (= G288)
O58320 Glyoxylate reductase; EC 1.1.1.26 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
42% identity, 96% coverage: 1:323/337 of query aligns to 1:325/334 of O58320
Q9UBQ7 Glyoxylate reductase/hydroxypyruvate reductase; EC 1.1.1.79; EC 1.1.1.81 from Homo sapiens (Human) (see paper)
43% identity, 75% coverage: 61:313/337 of query aligns to 70:320/328 of Q9UBQ7
- VG 83:84 (= VG 74:75) binding substrate
- GRI 162:164 (= GRI 153:155) binding NADP(+)
- RQPR 185:188 (≠ RNSR 178:181) binding NADP(+)
- S217 (≠ P211) binding NADP(+)
- I243 (≠ L237) binding NADP(+)
- R245 (= R239) binding substrate
- D269 (= D263) binding substrate
- HIGS 293:296 (≠ HLGS 286:289) binding substrate
- G295 (= G288) binding NADP(+)
2gcgA Ternary crystal structure of human glyoxylate reductase/hydroxypyruvate reductase (see paper)
43% identity, 75% coverage: 61:313/337 of query aligns to 66:316/324 of 2gcgA
- active site: L103 (= L98), R241 (= R239), D265 (= D263), E270 (= E268), H289 (= H286)
- binding (2r)-2,3-dihydroxypropanoic acid: S78 (= S73), V79 (= V74), G80 (= G75), R241 (= R239), H289 (= H286)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V79 (= V74), T107 (= T102), G156 (= G151), G158 (= G153), I160 (= I155), G180 (= G175), R181 (= R178), R184 (= R181), C212 (≠ V210), S213 (≠ P211), T218 (= T216), I239 (≠ L237), R241 (= R239), D265 (= D263), H289 (= H286), G291 (= G288)
Sites not aligning to the query:
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
38% identity, 94% coverage: 3:320/337 of query aligns to 2:311/526 of 3dc2A
Sites not aligning to the query:
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
38% identity, 94% coverage: 3:320/337 of query aligns to 3:312/525 of 3ddnB
3bazA Structure of hydroxyphenylpyruvate reductase from coleus blumei in complex with NADP+ (see paper)
37% identity, 80% coverage: 45:313/337 of query aligns to 44:304/311 of 3bazA
- active site: L98 (= L98), R230 (= R239), A251 (= A260), D254 (= D263), E259 (= E268), H277 (= H286)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V74 (= V74), G149 (= G151), L150 (= L152), G151 (= G153), R152 (= R154), I153 (= I155), S172 (≠ G175), R173 (≠ N176), S174 (= S177), C201 (≠ V210), P202 (= P211), T207 (= T216), I228 (≠ L237), G229 (≠ A238), R230 (= R239), D254 (= D263), H277 (= H286), G279 (= G288)
Q65CJ7 Hydroxyphenylpyruvate reductase; HPPR; EC 1.1.1.237 from Plectranthus scutellarioides (Coleus) (Solenostemon scutellarioides) (see paper)
37% identity, 80% coverage: 45:313/337 of query aligns to 46:306/313 of Q65CJ7
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)
35% identity, 79% coverage: 63:327/337 of query aligns to 67:324/533 of O43175
- T78 (≠ V74) binding NAD(+)
- R135 (= R131) 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 154:155) binding NAD(+)
- D175 (vs. gap) binding NAD(+)
- T207 (≠ V210) binding NAD(+)
- CAR 234:236 (≠ LAR 237:239) binding NAD(+)
- D260 (= D263) binding NAD(+)
- V261 (= V264) 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 (≠ HLGS 286:289) 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
4e5mA Thermostable phosphite dehydrogenase e175a/a176r in complex with NADP (see paper)
32% identity, 95% coverage: 1:320/337 of query aligns to 1:326/329 of 4e5mA
- active site: L100 (= L98), R237 (= R239), D261 (= D263), E266 (= E268), H292 (= H286)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K76 (≠ V74), L100 (= L98), T104 (= T102), G154 (= G153), A155 (≠ R154), I156 (= I155), R176 (= R178), L208 (≠ V210), P209 (= P211), T214 (= T216), P235 (≠ L237), C236 (≠ A238), R237 (= R239), H292 (= H286), G294 (= G288)
4e5pA Thermostable phosphite dehydrogenase a176r variant in complex with nad (see paper)
32% identity, 95% coverage: 1:320/337 of query aligns to 1:326/332 of 4e5pA
- active site: L100 (= L98), R237 (= R239), D261 (= D263), E266 (= E268), H292 (= H286)
- binding nicotinamide-adenine-dinucleotide: K76 (≠ V74), L100 (= L98), T104 (= T102), G154 (= G153), A155 (≠ R154), I156 (= I155), A175 (≠ S177), R176 (= R178), L208 (≠ V210), P209 (= P211), T214 (= T216), P235 (≠ L237), C236 (≠ A238), R237 (= R239), H292 (= H286)
6plfA Crystal structure of human phgdh complexed with compound 1 (see paper)
35% identity, 74% coverage: 63:312/337 of query aligns to 63:305/305 of 6plfA
7dkmA Phgdh covalently linked to oridonin (see paper)
35% identity, 74% coverage: 63:313/337 of query aligns to 63:306/306 of 7dkmA