SitesBLAST
Comparing WP_011372505.1 NCBI__GCF_000012965.1:WP_011372505.1 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)
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
33% identity, 95% coverage: 6:510/529 of query aligns to 4:506/526 of 3dc2A
- active site: N96 (= N100), R230 (= R235), D254 (= D259), E259 (= E264), H277 (= H282)
- binding serine: Y458 (≠ N463), D460 (= D465), R461 (≠ V466), P462 (= P467), G463 (= G468), A464 (≠ V469), L465 (≠ I470), L484 (= L489)
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
33% identity, 95% coverage: 6:510/529 of query aligns to 5:505/525 of 3ddnB
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, 75% coverage: 6:403/529 of query aligns to 9:406/533 of O43175
- T78 (≠ V76) binding
- R135 (= R134) 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 (≠ NI 154:155) binding
- D175 (= D174) binding
- T207 (= T206) binding
- CAR 234:236 (= CAR 233:235) binding
- D260 (= D259) binding
- V261 (= V260) 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 (= HLGA 282:285) binding
- A373 (≠ F371) to T: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs201553627
- G377 (= G375) to S: in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity; dbSNP:rs267606948
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 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)
38% identity, 57% coverage: 6:308/529 of query aligns to 5:305/305 of 6plfA
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
38% identity, 56% coverage: 6:299/529 of query aligns to 3:294/297 of 6rj3A
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
38% identity, 56% coverage: 6:299/529 of query aligns to 3:294/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (= N100), A100 (= A104), R149 (≠ N154), I150 (= I155), Y168 (= Y173), D169 (= D174), P170 (= P175), I171 (≠ Y176), H200 (= H205), T201 (= T206), P202 (= P207), T207 (= T212), C228 (= C233), A229 (= A234), R230 (= R235), H277 (= H282), G279 (= G284)
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
38% identity, 56% coverage: 6:299/529 of query aligns to 4:295/301 of 6rj5A
7dkmA Phgdh covalently linked to oridonin (see paper)
38% identity, 56% coverage: 6:299/529 of query aligns to 5:296/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (≠ V76), A102 (= A104), G148 (= G151), R151 (≠ N154), I152 (= I155), Y170 (= Y173), D171 (= D174), P172 (= P175), I173 (≠ Y176), H202 (= H205), T203 (= T206), P204 (= P207), T209 (= T212), C230 (= C233), A231 (= A234), R232 (= R235), H279 (= H282), G281 (= G284)
- binding (1beta,6beta,7beta,8alpha,9beta,10alpha,13alpha,14R,16beta)-1,6,7,14-tetrahydroxy-7,20-epoxykauran-15-one: C14 (≠ A15), K17 (≠ E18), I18 (≠ M19), E293 (≠ V296)
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
38% identity, 56% coverage: 6:299/529 of query aligns to 4:295/303 of 6plgA
6rj2A Crystal structure of phgdh in complex with compound 40 (see paper)
38% identity, 56% coverage: 6:299/529 of query aligns to 1:292/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (= G153), I148 (= I155), Y166 (= Y173), D167 (= D174), P168 (= P175), I169 (≠ Y176), I170 (= I177), H198 (= H205), T199 (= T206), L208 (≠ M215), R228 (= R235)
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
38% identity, 56% coverage: 6:299/529 of query aligns to 4:295/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (≠ I150), G147 (= G151), L148 (≠ F152), G149 (= G153), R150 (≠ N154), I151 (= I155), G152 (= G156), D170 (= D174), H201 (= H205), T202 (= T206), P203 (= P207)
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
38% identity, 56% coverage: 6:299/529 of query aligns to 4:295/302 of 6rihA
6plfB Crystal structure of human phgdh complexed with compound 1 (see paper)
39% identity, 54% coverage: 12:299/529 of query aligns to 17:286/292 of 6plfB
- binding 4-{(1S)-1-[(5-chloro-6-{[(5S)-2-oxo-1,3-oxazolidin-5-yl]methoxy}-1H-indole-2-carbonyl)amino]-2-hydroxyethyl}benzoic acid: R141 (≠ N154), Y160 (= Y173), D161 (= D174), P162 (= P175), I164 (= I177), L179 (≠ F193), T193 (= T206), P194 (= P207), S198 (≠ E211), L202 (≠ M215)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
35% identity, 57% coverage: 6:308/529 of query aligns to 3:304/304 of 1wwkA
- active site: S96 (≠ N100), R230 (= R235), D254 (= D259), E259 (= E264), H278 (= H282)
- binding nicotinamide-adenine-dinucleotide: V100 (≠ A104), G146 (= G151), F147 (= F152), G148 (= G153), R149 (≠ N154), I150 (= I155), Y168 (= Y173), D169 (= D174), P170 (= P175), V201 (≠ T206), P202 (= P207), T207 (= T212), T228 (≠ C233), S229 (≠ A234), D254 (= D259), H278 (= H282), G280 (= G284)
7cvpA The crystal structure of human phgdh from biortus.
41% identity, 40% coverage: 88:299/529 of query aligns to 39:249/254 of 7cvpA
- binding nicotinamide-adenine-dinucleotide: G101 (= G151), G103 (= G153), R104 (≠ N154), I105 (= I155), Y123 (= Y173), D124 (= D174), P125 (= P175), I126 (≠ Y176), H155 (= H205), T156 (= T206), P157 (= P207), T162 (= T212), C183 (= C233), A184 (= A234), R185 (= R235), H232 (= H282), G234 (= G284)
2p9eA Crystal structure of g336v mutant of e.Coli phosphoglycerate dehydrogenase (see paper)
34% identity, 60% coverage: 3:318/529 of query aligns to 6:324/406 of 2p9eA
- active site: N104 (= N100), R236 (= R235), D260 (= D259), E265 (= E264), H288 (= H282)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G156 (= G153), H157 (≠ N154), I158 (= I155), Y176 (= Y173), D177 (= D174), I178 (vs. gap), H206 (= H205), V207 (≠ T206), P208 (= P207), S212 (≠ E211), A234 (≠ C233), S235 (≠ A234), R236 (= R235), H288 (= H282), G290 (= G284)
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
33% identity, 52% coverage: 36:308/529 of query aligns to 36:314/334 of 5aovA
- active site: L100 (≠ N100), R241 (= R235), D265 (= D259), E270 (= E264), H288 (= H282)
- binding glyoxylic acid: M52 (≠ R52), L53 (≠ S53), L53 (≠ S53), Y74 (≠ A74), A75 (≠ G75), V76 (= V76), G77 (= G77), R241 (= R235), H288 (= H282)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (= V76), T104 (≠ A104), F158 (= F152), G159 (= G153), R160 (≠ N154), I161 (= I155), S180 (≠ D174), R181 (≠ P175), A211 (≠ H205), V212 (≠ T206), P213 (= P207), T218 (= T212), I239 (≠ C233), A240 (= A234), R241 (= R235), H288 (= H282), G290 (= G284)
P0A9T0 D-3-phosphoglycerate dehydrogenase; PGDH; 2-oxoglutarate reductase; EC 1.1.1.95; EC 1.1.1.399 from Escherichia coli (strain K12) (see 2 papers)
34% identity, 60% coverage: 3:318/529 of query aligns to 10:328/410 of P0A9T0
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1ybaA The active form of phosphoglycerate dehydrogenase (see paper)
34% identity, 60% coverage: 3:318/529 of query aligns to 6:324/406 of 1ybaA
- active site: N104 (= N100), R236 (= R235), D260 (= D259), E265 (= E264), H288 (= H282)
- binding 2-oxoglutaric acid: R56 (= R52), S57 (= S53), C79 (≠ G75), I80 (≠ V76)
- binding nicotinamide-adenine-dinucleotide: I80 (≠ V76), F102 (≠ T98), V108 (≠ A104), G154 (= G151), G156 (= G153), H157 (≠ N154), I158 (= I155), Y176 (= Y173), D177 (= D174), I178 (vs. gap), K181 (vs. gap), H206 (= H205), V207 (≠ T206), P208 (= P207), A234 (≠ C233), S235 (≠ A234), R236 (= R235), H288 (= H282), G290 (= G284)
- binding phosphate ion: G81 (= G77), N83 (≠ D79)
1psdA The allosteric ligand site in the vmax-type cooperative enzyme phosphoglycerate dehydrogenase (see paper)
34% identity, 60% coverage: 3:318/529 of query aligns to 4:322/404 of 1psdA
- active site: N102 (= N100), R234 (= R235), D258 (= D259), E263 (= E264), H286 (= H282)
- binding nicotinamide-adenine-dinucleotide: N102 (= N100), H155 (≠ N154), I156 (= I155), D175 (= D174), I176 (vs. gap), K179 (vs. gap), H204 (= H205), V205 (≠ T206), P206 (= P207), A232 (≠ C233), S233 (≠ A234), R234 (= R235), H286 (= H282)
Sites not aligning to the query:
Query Sequence
>WP_011372505.1 NCBI__GCF_000012965.1:WP_011372505.1
MQKYTIVVCDHIHEAGLEMLQNDKNINFIMAADEDKEKLLTIIESADVAITRSSTDVDAK
FIAHAKNMKAIVRAGVGVDNVDIAGCSKEGIIVMNVPTANTIAAVELTMAHMLSCMRMFP
YSHNHLKLDRVWKREKWYGYELKGKKLGVIGFGNIGSRVAKRAQAFEMDIIAYDPYINPS
KVTDLDMVYTKNFEDILSCDIITIHTPKNKETVNMIDVAEIAKMKDGVVLINCARGGLYN
EEALYAGLTSGKIRFAGIDVFMKEPATNHPLLDLDNVTVSPHLGANTYESQYNIGVQAAE
NAIAAAKGISYAHAMNLPIDESKIPPFVKPFLEMGQTIGFLETQLNQSQIVTIKVSGQGE
IAKYVDSLATFVAVGAMSQISDNTINYVNADFVAKEKGIKIETEALLDSTVYKNLITIKL
TTAEGGTTTISATIFDDNVFRIVSIDGFDIEVALKGDMIILKNQDVPGVIGNIGSTLAKH
NVNIADFSLARNDKKQALAVILVDNVISDDTLEELLRIDACSSVQYARL
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