SitesBLAST
Comparing WP_012050501.1 NCBI__GCF_000016765.1:WP_012050501.1 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)
Q65CJ7 Hydroxyphenylpyruvate reductase; HPPR; EC 1.1.1.237 from Plectranthus scutellarioides (Coleus) (Solenostemon scutellarioides) (see paper)
39% identity, 96% coverage: 10:306/309 of query aligns to 11:309/313 of Q65CJ7
3bazA Structure of hydroxyphenylpyruvate reductase from coleus blumei in complex with NADP+ (see paper)
39% identity, 96% coverage: 10:306/309 of query aligns to 9:307/311 of 3bazA
- active site: L98 (= L97), R230 (= R229), A251 (= A250), D254 (= D253), E259 (= E258), H277 (= H276)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V74 (≠ A73), G149 (= G148), L150 (≠ F149), G151 (= G150), R152 (= R151), I153 (= I152), S172 (= S171), R173 (= R172), S174 (≠ R173), C201 (≠ L200), P202 (= P201), T207 (= T206), I228 (= I227), G229 (≠ A228), R230 (= R229), D254 (= D253), H277 (= H276), G279 (= G278)
5v6qB Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase smc04462 (smghrb) from sinorhizobium meliloti in complex with NADP and malonate (see paper)
46% identity, 80% coverage: 55:301/309 of query aligns to 54:302/319 of 5v6qB
- active site: L96 (= L97), R230 (= R229), D254 (= D253), E259 (= E258), H277 (= H276)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V72 (≠ A73), V100 (= V101), F148 (≠ L147), L150 (≠ F149), G151 (= G150), R152 (= R151), I153 (= I152), T172 (≠ S171), R173 (= R172), V201 (≠ L200), P202 (= P201), S206 (≠ A205), T207 (= T206), V228 (≠ I227), G229 (≠ A228), R230 (= R229), H277 (= H276), A279 (≠ G278)
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)
46% identity, 80% coverage: 55:301/309 of query aligns to 53:301/319 of 5v7nA
- active site: L95 (= L97), R229 (= R229), D253 (= D253), E258 (= E258), H276 (= H276)
- binding 2-keto-D-gluconic acid: G70 (= G72), V71 (≠ A73), G72 (= G74), R229 (= R229), H276 (= H276), S279 (= S279), R285 (= R285)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V71 (≠ A73), V99 (= V101), L149 (≠ F149), G150 (= G150), R151 (= R151), I152 (= I152), T171 (≠ S171), R172 (= R172), V200 (≠ L200), P201 (= P201), S205 (≠ A205), T206 (= T206), V227 (≠ I227), G228 (≠ A228), R229 (= R229), H276 (= H276), A278 (≠ G278)
5j23A Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase smc04462 (smghrb) from sinorhizobium meliloti in complex with 2'-phospho-adp-ribose (see paper)
46% identity, 80% coverage: 55:301/309 of query aligns to 52:300/318 of 5j23A
- active site: L94 (= L97), R228 (= R229), D252 (= D253), E257 (= E258), H275 (= H276)
- 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 (≠ A73), L148 (≠ F149), G149 (= G150), R150 (= R151), I151 (= I152), T170 (≠ S171), R171 (= R172), P200 (= P201), S204 (≠ A205), T205 (= T206), R228 (= R229)
5v7gA Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase smc04462 (smghrb) from sinorhizobium meliloti in complex with NADPH and oxalate (see paper)
46% identity, 80% coverage: 55:301/309 of query aligns to 52:300/317 of 5v7gA
- active site: L94 (= L97), R228 (= R229), D252 (= D253), E257 (= E258), H275 (= H276)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V70 (≠ A73), V98 (= V101), F146 (≠ L147), L148 (≠ F149), G149 (= G150), R150 (= R151), I151 (= I152), T170 (≠ S171), R171 (= R172), V199 (≠ L200), P200 (= P201), S204 (≠ A205), T205 (= T206), V226 (≠ I227), G227 (≠ A228), R228 (= R229), H275 (= H276), A277 (≠ G278)
- binding oxalate ion: G69 (= G72), V70 (≠ A73), G71 (= G74), R228 (= R229), H275 (= H276)
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
39% identity, 88% coverage: 32:302/309 of query aligns to 35:314/334 of 5aovA
- active site: L100 (= L97), R241 (= R229), D265 (= D253), E270 (= E258), H288 (= H276)
- binding glyoxylic acid: M52 (≠ H49), L53 (≠ A50), L53 (≠ A50), Y74 (≠ F71), A75 (≠ G72), V76 (≠ A73), G77 (= G74), R241 (= R229), H288 (= H276)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ A73), T104 (≠ V101), F158 (= F149), G159 (= G150), R160 (= R151), I161 (= I152), S180 (= S171), R181 (= R172), A211 (= A199), V212 (≠ L200), P213 (= P201), T218 (= T206), I239 (= I227), A240 (= A228), R241 (= R229), H288 (= H276), G290 (= G278)
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
40% identity, 88% coverage: 32:302/309 of query aligns to 34:313/332 of 6biiA
- active site: L99 (= L97), R240 (= R229), D264 (= D253), E269 (= E258), H287 (= H276)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V75 (≠ A73), T103 (≠ V101), G156 (= G148), F157 (= F149), G158 (= G150), R159 (= R151), I160 (= I152), A179 (vs. gap), R180 (≠ H170), S181 (= S171), K183 (≠ R173), V211 (≠ L200), P212 (= P201), E216 (≠ A205), T217 (= T206), V238 (≠ I227), A239 (= A228), R240 (= R229), D264 (= D253), H287 (= H276), G289 (= G278)
2dbqA Crystal structure of glyoxylate reductase (ph0597) from pyrococcus horikoshii ot3, complexed with NADP (i41) (see paper)
39% identity, 89% coverage: 27:302/309 of query aligns to 30:314/333 of 2dbqA
- active site: L100 (= L97), R241 (= R229), D265 (= D253), E270 (= E258), H288 (= H276)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ A73), T104 (≠ V101), L158 (≠ F149), G159 (= G150), R160 (= R151), I161 (= I152), S180 (= S171), R181 (= R172), T182 (≠ R173), A211 (= A199), V212 (≠ L200), P213 (= P201), T218 (= T206), I239 (= I227), A240 (= A228), R241 (= R229), D265 (= D253), H288 (= H276), G290 (= G278)
O58320 Glyoxylate reductase; EC 1.1.1.26 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
39% identity, 89% coverage: 27:302/309 of query aligns to 30:314/334 of O58320
2gcgA Ternary crystal structure of human glyoxylate reductase/hydroxypyruvate reductase (see paper)
36% identity, 78% coverage: 65:305/309 of query aligns to 71:318/324 of 2gcgA
- active site: L103 (= L97), R241 (= R229), D265 (= D253), E270 (= E258), H289 (= H276)
- binding (2r)-2,3-dihydroxypropanoic acid: S78 (≠ G72), V79 (≠ A73), G80 (= G74), R241 (= R229), H289 (= H276)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V79 (≠ A73), T107 (≠ V101), G156 (= G148), G158 (= G150), I160 (= I152), G180 (≠ S171), R181 (= R172), R184 (≠ V175), C212 (≠ L200), S213 (≠ P201), T218 (= T206), I239 (= I227), R241 (= R229), D265 (= D253), H289 (= H276), G291 (= G278)
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)
36% identity, 78% coverage: 65:305/309 of query aligns to 75:322/328 of Q9UBQ7
- VG 83:84 (≠ AG 73:74) binding substrate
- GRI 162:164 (= GRI 150:152) binding NADP(+)
- RQPR 185:188 (≠ RRPV 172:175) binding NADP(+)
- S217 (≠ P201) binding NADP(+)
- I243 (= I227) binding NADP(+)
- R245 (= R229) binding substrate
- D269 (= D253) binding substrate
- HIGS 293:296 (≠ HVGS 276:279) binding substrate
- G295 (= G278) binding NADP(+)
4e5mA Thermostable phosphite dehydrogenase e175a/a176r in complex with NADP (see paper)
39% identity, 81% coverage: 56:305/309 of query aligns to 59:322/329 of 4e5mA
- active site: L100 (= L97), R237 (= R229), D261 (= D253), E266 (= E258), H292 (= H276)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K76 (≠ A73), L100 (= L97), T104 (≠ V101), G154 (= G150), A155 (≠ R151), I156 (= I152), R176 (= R172), L208 (= L200), P209 (= P201), T214 (= T206), P235 (≠ I227), C236 (≠ A228), R237 (= R229), H292 (= H276), G294 (= G278)
4e5pA Thermostable phosphite dehydrogenase a176r variant in complex with nad (see paper)
39% identity, 81% coverage: 56:305/309 of query aligns to 59:322/332 of 4e5pA
- active site: L100 (= L97), R237 (= R229), D261 (= D253), E266 (= E258), H292 (= H276)
- binding nicotinamide-adenine-dinucleotide: K76 (≠ A73), L100 (= L97), T104 (≠ V101), G154 (= G150), A155 (≠ R151), I156 (= I152), A175 (≠ S171), R176 (= R172), L208 (= L200), P209 (= P201), T214 (= T206), P235 (≠ I227), C236 (≠ A228), R237 (= R229), H292 (= H276)
4e5kA Thermostable phosphite dehydrogenase in complex with NAD and sulfite (see paper)
38% identity, 81% coverage: 56:305/309 of query aligns to 59:322/329 of 4e5kA
- active site: L100 (= L97), R237 (= R229), D261 (= D253), E266 (= E258), H292 (= H276)
- binding nicotinamide-adenine-dinucleotide: K76 (≠ A73), G77 (= G74), L100 (= L97), T104 (≠ V101), G152 (= G148), G154 (= G150), A155 (≠ R151), I156 (= I152), H174 (= H170), E175 (≠ S171), A176 (≠ R172), A207 (= A199), L208 (= L200), P209 (= P201), P235 (≠ I227), C236 (≠ A228), R237 (= R229), D261 (= D253), H292 (= H276), G294 (= G278)
- binding sulfite ion: L75 (≠ G72), K76 (≠ A73), G77 (= G74), L100 (= L97), R237 (= R229), H292 (= H276)
Sites not aligning to the query:
2w2lA Crystal structure of the holo forms of rhodotorula graminis d- mandelate dehydrogenase at 2.5a.
35% identity, 81% coverage: 56:306/309 of query aligns to 71:335/346 of 2w2lA
- active site: G113 (= G94), R257 (= R229), D281 (= D253), E286 (= E258), H304 (= H276)
- binding nicotinamide-adenine-dinucleotide: T117 (= T98), G172 (= G150), A173 (≠ R151), I174 (= I152), D194 (≠ S171), V228 (≠ L200), P229 (= P201), T234 (= T206), T255 (≠ I227), A256 (= A228), R257 (= R229), H304 (= H276), G306 (= G278), G307 (≠ S279)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
32% identity, 90% coverage: 25:302/309 of query aligns to 25:304/304 of 1wwkA
- active site: S96 (≠ L97), R230 (= R229), D254 (= D253), E259 (= E258), H278 (= H276)
- binding nicotinamide-adenine-dinucleotide: V100 (= V101), G146 (= G148), F147 (= F149), G148 (= G150), R149 (= R151), I150 (= I152), Y168 (≠ H170), D169 (≠ S171), P170 (≠ R172), V201 (≠ L200), P202 (= P201), T207 (= T206), T228 (≠ I227), S229 (≠ A228), D254 (= D253), H278 (= H276), G280 (= G278)
P87228 Putative D-3-phosphoglycerate dehydrogenase; 3-PGDH; 2-oxoglutarate reductase; EC 1.1.1.95; EC 1.1.1.399 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
30% identity, 80% coverage: 64:309/309 of query aligns to 119:377/466 of P87228
- S258 (≠ G203) modified: Phosphoserine
Sites not aligning to the query:
- 87 modified: Phosphoserine
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)
28% identity, 85% coverage: 46:309/309 of query aligns to 51:316/533 of O43175
- T78 (≠ A73) binding NAD(+)
- R135 (≠ K130) 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 (≠ S171) binding NAD(+)
- T207 (≠ L200) binding NAD(+)
- CAR 234:236 (≠ IAR 227:229) binding NAD(+)
- D260 (= D253) binding NAD(+)
- V261 (= V254) 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 (≠ HVGS 276:279) 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
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
35% identity, 80% coverage: 56:303/309 of query aligns to 56:305/525 of 3ddnB
Query Sequence
>WP_012050501.1 NCBI__GCF_000016765.1:WP_012050501.1
MTILQVTPLPAPRQPSELLDRPVPIFDRLDDPEGWLAEHGGSVQCLITHAMRGPPAGLLA
RLPALKLIANFGAGIDLIDLDTARARGIAVTASGDLLTHDVADLALWQMLTLLRGLGGAD
GFVRAGQWSKGPPPLGRSARGRKLGVLGFGRIGQAIARRGEAVGMEIAYHSRRPVAEVAD
RYESDPLALARWADIVVIALPGGGATQSLVDRAFLDALGPDGLLVNIARGSVVDEEALVA
ALRDGRVGGAALDVFRNEPTIAPALLEAPNLLLTPHVGSATHDVRLAMADHVVTNIRAFL
EGRPLIGLV
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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