SitesBLAST
Comparing WP_012282307.1 NCBI__GCF_000019165.1:WP_012282307.1 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)
53% identity, 99% coverage: 5:328/328 of query aligns to 1:327/334 of 5aovA
- active site: L100 (= L104), R241 (= R241), D265 (= D265), E270 (= E270), H288 (= H289)
- binding glyoxylic acid: M52 (= M56), L53 (≠ I57), L53 (≠ I57), Y74 (= Y78), A75 (≠ G79), V76 (= V80), G77 (= G81), R241 (= R241), H288 (= H289)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (= V80), T104 (= T108), F158 (≠ L158), G159 (= G159), R160 (= R160), I161 (= I161), S180 (≠ A180), R181 (= R181), A211 (≠ H211), V212 (≠ T212), P213 (= P213), T218 (= T218), I239 (≠ T239), A240 (= A240), R241 (= R241), H288 (= H289), G290 (= G291)
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
54% identity, 98% coverage: 6:328/328 of query aligns to 1:326/332 of 6biiA
- active site: L99 (= L104), R240 (= R241), D264 (= D265), E269 (= E270), H287 (= H289)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V75 (= V80), T103 (= T108), G156 (= G157), F157 (≠ L158), G158 (= G159), R159 (= R160), I160 (= I161), A179 (= A180), R180 (= R181), S181 (≠ R182), K183 (≠ N184), V211 (≠ T212), P212 (= P213), E216 (= E217), T217 (= T218), V238 (≠ T239), A239 (= A240), R240 (= R241), D264 (= D265), H287 (= H289), G289 (= G291)
O58320 Glyoxylate reductase; EC 1.1.1.26 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
53% identity, 99% coverage: 5:328/328 of query aligns to 1:327/334 of O58320
2dbqA Crystal structure of glyoxylate reductase (ph0597) from pyrococcus horikoshii ot3, complexed with NADP (i41) (see paper)
53% identity, 99% coverage: 5:328/328 of query aligns to 1:327/333 of 2dbqA
- active site: L100 (= L104), R241 (= R241), D265 (= D265), E270 (= E270), H288 (= H289)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (= V80), T104 (= T108), L158 (= L158), G159 (= G159), R160 (= R160), I161 (= I161), S180 (≠ A180), R181 (= R181), T182 (≠ R182), A211 (≠ H211), V212 (≠ T212), P213 (= P213), T218 (= T218), I239 (≠ T239), A240 (= A240), R241 (= R241), D265 (= D265), H288 (= H289), G290 (= G291)
2gcgA Ternary crystal structure of human glyoxylate reductase/hydroxypyruvate reductase (see paper)
41% identity, 95% coverage: 8:320/328 of query aligns to 4:320/324 of 2gcgA
- active site: L103 (= L104), R241 (= R241), D265 (= D265), E270 (= E270), H289 (= H289)
- binding (2r)-2,3-dihydroxypropanoic acid: L55 (≠ I57), S78 (≠ G79), V79 (= V80), G80 (= G81), R241 (= R241), H289 (= H289)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V79 (= V80), T107 (= T108), G156 (= G157), G158 (= G159), I160 (= I161), G180 (≠ A180), R181 (= R181), R184 (≠ N184), C212 (≠ T212), S213 (≠ P213), T218 (= T218), I239 (≠ T239), R241 (= R241), D265 (= D265), H289 (= H289), G291 (= G291)
Q9UBQ7 Glyoxylate reductase/hydroxypyruvate reductase; EC 1.1.1.79; EC 1.1.1.81 from Homo sapiens (Human) (see paper)
41% identity, 95% coverage: 8:320/328 of query aligns to 8:324/328 of Q9UBQ7
- VG 83:84 (= VG 80:81) binding substrate
- GRI 162:164 (= GRI 159:161) binding NADP(+)
- RQPR 185:188 (≠ RRRN 181:184) binding NADP(+)
- S217 (≠ P213) binding NADP(+)
- I243 (≠ T239) binding NADP(+)
- R245 (= R241) binding substrate
- D269 (= D265) binding substrate
- HIGS 293:296 (= HIGS 289:292) binding substrate
- G295 (= G291) binding NADP(+)
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
42% identity, 87% coverage: 38:323/328 of query aligns to 31:312/525 of 3ddnB
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
42% identity, 87% coverage: 38:323/328 of query aligns to 30:311/526 of 3dc2A
Sites not aligning to the query:
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
40% identity, 94% coverage: 8:315/328 of query aligns to 2:304/304 of 1wwkA
- active site: S96 (≠ L104), R230 (= R241), D254 (= D265), E259 (= E270), H278 (= H289)
- binding nicotinamide-adenine-dinucleotide: V100 (≠ T108), G146 (= G157), F147 (≠ L158), G148 (= G159), R149 (= R160), I150 (= I161), Y168 (≠ T179), D169 (≠ A180), P170 (≠ R181), V201 (≠ T212), P202 (= P213), T207 (= T218), T228 (= T239), S229 (≠ A240), D254 (= D265), H278 (= H289), G280 (= G291)
4e5mA Thermostable phosphite dehydrogenase e175a/a176r in complex with NADP (see paper)
36% identity, 97% coverage: 7:323/328 of query aligns to 3:326/329 of 4e5mA
- active site: L100 (= L104), R237 (= R241), D261 (= D265), E266 (vs. gap), H292 (= H289)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K76 (≠ V80), L100 (= L104), T104 (= T108), G154 (= G159), A155 (≠ R160), I156 (= I161), R176 (= R181), L208 (≠ T212), P209 (= P213), T214 (= T218), P235 (≠ T239), C236 (≠ A240), R237 (= R241), H292 (= H289), G294 (= G291)
4e5pA Thermostable phosphite dehydrogenase a176r variant in complex with nad (see paper)
36% identity, 97% coverage: 7:323/328 of query aligns to 3:326/332 of 4e5pA
- active site: L100 (= L104), R237 (= R241), D261 (= D265), E266 (vs. gap), H292 (= H289)
- binding nicotinamide-adenine-dinucleotide: K76 (≠ V80), L100 (= L104), T104 (= T108), G154 (= G159), A155 (≠ R160), I156 (= I161), A175 (= A180), R176 (= R181), L208 (≠ T212), P209 (= P213), T214 (= T218), P235 (≠ T239), C236 (≠ A240), R237 (= R241), H292 (= H289)
4e5kA Thermostable phosphite dehydrogenase in complex with NAD and sulfite (see paper)
36% identity, 97% coverage: 7:323/328 of query aligns to 3:326/329 of 4e5kA
- active site: L100 (= L104), R237 (= R241), D261 (= D265), E266 (vs. gap), H292 (= H289)
- binding nicotinamide-adenine-dinucleotide: K76 (≠ V80), G77 (= G81), L100 (= L104), T104 (= T108), G152 (= G157), G154 (= G159), A155 (≠ R160), I156 (= I161), H174 (vs. gap), E175 (≠ T179), A176 (= A180), A207 (≠ H211), L208 (≠ T212), P209 (= P213), P235 (≠ T239), C236 (≠ A240), R237 (= R241), D261 (= D265), H292 (= H289), G294 (= G291)
- binding sulfite ion: M53 (≠ I57), L75 (≠ G79), K76 (≠ V80), G77 (= G81), L100 (= L104), R237 (= R241), H292 (= H289)
Q65CJ7 Hydroxyphenylpyruvate reductase; HPPR; EC 1.1.1.237 from Plectranthus scutellarioides (Coleus) (Solenostemon scutellarioides) (see paper)
40% identity, 78% coverage: 62:316/328 of query aligns to 58:306/313 of Q65CJ7
3bazA Structure of hydroxyphenylpyruvate reductase from coleus blumei in complex with NADP+ (see paper)
40% identity, 78% coverage: 62:316/328 of query aligns to 56:304/311 of 3bazA
- active site: L98 (= L104), R230 (= R241), A251 (= A262), D254 (= D265), E259 (= E270), H277 (= H289)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V74 (= V80), G149 (= G157), L150 (= L158), G151 (= G159), R152 (= R160), I153 (= I161), S172 (≠ A180), R173 (= R181), S174 (≠ R182), C201 (≠ T212), P202 (= P213), T207 (= T218), I228 (≠ T239), G229 (≠ A240), R230 (= R241), D254 (= D265), H277 (= H289), G279 (= G291)
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)
36% identity, 88% coverage: 39:328/328 of query aligns to 37:322/533 of O43175
- T78 (≠ V80) binding NAD(+)
- R135 (≠ P140) 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 160:161) binding NAD(+)
- D175 (≠ A180) binding NAD(+)
- T207 (= T212) binding NAD(+)
- CAR 234:236 (≠ TAR 239:241) binding NAD(+)
- D260 (= D265) binding NAD(+)
- V261 (= V266) 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 289:292) 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
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
38% identity, 80% coverage: 40:302/328 of query aligns to 32:290/297 of 6rj3A
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
38% identity, 80% coverage: 40:302/328 of query aligns to 32:290/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (≠ L104), A100 (≠ T108), R149 (= R160), I150 (= I161), Y168 (≠ T179), D169 (≠ A180), P170 (≠ R181), I171 (≠ R182), H200 (= H211), T201 (= T212), P202 (= P213), T207 (= T218), C228 (≠ T239), A229 (= A240), R230 (= R241), H277 (= H289), G279 (= G291)
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
38% identity, 80% coverage: 40:302/328 of query aligns to 33:291/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (≠ V156), G147 (= G157), L148 (= L158), G149 (= G159), R150 (= R160), I151 (= I161), G152 (= G162), D170 (≠ A180), H201 (= H211), T202 (= T212), P203 (= P213)
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
38% identity, 80% coverage: 40:302/328 of query aligns to 33:291/301 of 6rj5A
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
38% identity, 80% coverage: 40:302/328 of query aligns to 33:291/302 of 6rihA
Query Sequence
>WP_012282307.1 NCBI__GCF_000019165.1:WP_012282307.1
MNHSLRPKVLVTREIPQPALDRIKEFARLDLWPAFPPPEKGELQRMLADADALLCMITDP
IDDDVIEAGKKLRVIANYGVGYDNIDIAAATRRRIAVTNTPDALTEATADLAFALLLATA
RNLIAADRFTRDGFWIAWHPQLLLGRDVFGSTLGIVGLGRIGEAVARRARGFNMHVLYTA
RRRNPKAEAELGIEYCTLEELLRRSDFVSLHTPLTLETRHLIGAKELNMMKPTAILINTA
RGGVVDQEALTEALQQGVIGGAGLDVFAEEPVAPEEALLELPNVVVSPHIGSATVEARTR
MGLMAVENIQAVLEGRRPPNLVNSELFS
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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