SitesBLAST
Comparing WP_011973284.1 NCBI__GCF_000017185.1:WP_011973284.1 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)
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
41% identity, 97% coverage: 1:505/523 of query aligns to 1:507/526 of 3dc2A
- active site: N96 (≠ S96), R230 (= R230), D254 (= D254), E259 (= E259), H277 (= H277)
- binding serine: Y458 (≠ H456), D460 (= D458), R461 (≠ K459), P462 (= P460), G463 (= G461), A464 (≠ I462), L465 (≠ I463), L484 (≠ V482)
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
41% identity, 97% coverage: 1:505/523 of query aligns to 2:506/525 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)
39% identity, 84% coverage: 3:439/523 of query aligns to 8:449/533 of O43175
- T78 (≠ V72) binding NAD(+)
- R135 (= R129) 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 149:150) binding NAD(+)
- D175 (= D169) binding NAD(+)
- T207 (≠ V201) binding NAD(+)
- CAR 234:236 (= CAR 228:230) binding NAD(+)
- D260 (= D254) binding NAD(+)
- V261 (= V255) 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 (≠ HQGA 277:280) binding NAD(+)
- A373 (≠ S367) to T: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs201553627
- G377 (= G371) to S: in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity; dbSNP:rs267606948
- V425 (≠ I422) to M: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs121907988
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 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)
46% identity, 58% coverage: 1:303/523 of query aligns to 2:305/305 of 6plfA
7dkmA Phgdh covalently linked to oridonin (see paper)
46% identity, 58% coverage: 1:301/523 of query aligns to 2:303/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (≠ V72), A102 (≠ V100), G148 (= G146), R151 (= R149), I152 (= I150), Y170 (= Y168), D171 (= D169), P172 (= P170), I173 (≠ Y171), H202 (= H200), T203 (≠ V201), P204 (= P202), T209 (= T207), C230 (= C228), A231 (= A229), R232 (= R230), H279 (= H277), G281 (= G279)
- binding (1beta,6beta,7beta,8alpha,9beta,10alpha,13alpha,14R,16beta)-1,6,7,14-tetrahydroxy-7,20-epoxykauran-15-one: C14 (≠ A14), K17 (≠ L17), I18 (≠ L18), E293 (≠ T291)
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
46% identity, 58% coverage: 1:301/523 of query aligns to 1:302/303 of 6plgA
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
46% identity, 58% coverage: 1:301/523 of query aligns to 1:302/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (≠ I145), G147 (= G146), L148 (= L147), G149 (= G148), R150 (= R149), I151 (= I150), G152 (= G151), D170 (= D169), H201 (= H200), T202 (≠ V201), P203 (= P202)
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
46% identity, 58% coverage: 1:301/523 of query aligns to 1:302/302 of 6rihA
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
46% identity, 57% coverage: 1:300/523 of query aligns to 1:301/301 of 6rj5A
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
47% identity, 57% coverage: 3:298/523 of query aligns to 2:298/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (≠ S96), A100 (≠ V100), R149 (= R149), I150 (= I150), Y168 (= Y168), D169 (= D169), P170 (= P170), I171 (≠ Y171), H200 (= H200), T201 (≠ V201), P202 (= P202), T207 (= T207), C228 (= C228), A229 (= A229), R230 (= R230), H277 (= H277), G279 (= G279)
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
47% identity, 56% coverage: 3:297/523 of query aligns to 2:297/297 of 6rj3A
6rj2A Crystal structure of phgdh in complex with compound 40 (see paper)
46% identity, 57% coverage: 4:301/523 of query aligns to 1:299/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (= G148), I148 (= I150), Y166 (= Y168), D167 (= D169), P168 (= P170), I169 (≠ Y171), I170 (= I172), H198 (= H200), T199 (≠ V201), L208 (≠ M210), R228 (= R230)
6plfB Crystal structure of human phgdh complexed with compound 1 (see paper)
45% identity, 57% coverage: 3:300/523 of query aligns to 2:292/292 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 (= R149), Y160 (= Y168), D161 (= D169), P162 (= P170), I164 (= I172), L179 (≠ V187), T193 (≠ V201), P194 (= P202), S198 (≠ K206), L202 (≠ M210)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
51% identity, 58% coverage: 3:303/523 of query aligns to 2:304/304 of 1wwkA
- active site: S96 (= S96), R230 (= R230), D254 (= D254), E259 (= E259), H278 (= H277)
- binding nicotinamide-adenine-dinucleotide: V100 (= V100), G146 (= G146), F147 (≠ L147), G148 (= G148), R149 (= R149), I150 (= I150), Y168 (= Y168), D169 (= D169), P170 (= P170), V201 (= V201), P202 (= P202), T207 (= T207), T228 (≠ C228), S229 (≠ A229), D254 (= D254), H278 (= H277), G280 (= G279)
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
40% identity, 59% coverage: 2:311/523 of query aligns to 3:322/334 of 5aovA
- active site: L100 (≠ S96), R241 (= R230), D265 (= D254), E270 (= E259), H288 (= H277)
- binding glyoxylic acid: M52 (≠ R48), L53 (≠ S49), L53 (≠ S49), Y74 (≠ A70), A75 (≠ G71), V76 (= V72), G77 (= G73), R241 (= R230), H288 (= H277)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (= V72), T104 (≠ V100), F158 (≠ L147), G159 (= G148), R160 (= R149), I161 (= I150), S180 (≠ D169), R181 (≠ P170), A211 (≠ H200), V212 (= V201), P213 (= P202), T218 (= T207), I239 (≠ C228), A240 (= A229), R241 (= R230), H288 (= H277), G290 (= G279)
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
41% identity, 59% coverage: 2:311/523 of query aligns to 2:321/332 of 6biiA
- active site: L99 (≠ S96), R240 (= R230), D264 (= D254), E269 (= E259), H287 (= H277)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V75 (= V72), T103 (≠ V100), G156 (= G146), F157 (≠ L147), G158 (= G148), R159 (= R149), I160 (= I150), A179 (≠ D169), R180 (≠ P170), S181 (≠ Y171), K183 (≠ P173), V211 (= V201), P212 (= P202), E216 (≠ K206), T217 (= T207), V238 (≠ C228), A239 (= A229), R240 (= R230), D264 (= D254), H287 (= H277), G289 (= G279)
2p9eA Crystal structure of g336v mutant of e.Coli phosphoglycerate dehydrogenase (see paper)
39% identity, 60% coverage: 3:315/523 of query aligns to 8:326/406 of 2p9eA
- active site: N104 (≠ S96), R236 (= R230), D260 (= D254), E265 (= E259), H288 (= H277)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G156 (= G148), H157 (≠ R149), I158 (= I150), Y176 (= Y168), D177 (= D169), I178 (= I172), H206 (= H200), V207 (= V201), P208 (= P202), S212 (≠ K206), A234 (≠ C228), S235 (≠ A229), R236 (= R230), H288 (= H277), G290 (= G279)
1ybaA The active form of phosphoglycerate dehydrogenase (see paper)
39% identity, 60% coverage: 3:315/523 of query aligns to 8:326/406 of 1ybaA
- active site: N104 (≠ S96), R236 (= R230), D260 (= D254), E265 (= E259), H288 (= H277)
- binding 2-oxoglutaric acid: R56 (= R48), S57 (= S49), C79 (≠ G71), I80 (≠ V72)
- binding nicotinamide-adenine-dinucleotide: I80 (≠ V72), F102 (≠ D94), V108 (= V100), G154 (= G146), G156 (= G148), H157 (≠ R149), I158 (= I150), Y176 (= Y168), D177 (= D169), I178 (= I172), K181 (≠ E175), H206 (= H200), V207 (= V201), P208 (= P202), A234 (≠ C228), S235 (≠ A229), R236 (= R230), H288 (= H277), G290 (= G279)
- binding phosphate ion: G81 (= G73), N83 (≠ D75)
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)
39% identity, 60% coverage: 3:315/523 of query aligns to 12:330/410 of P0A9T0
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1psdA The allosteric ligand site in the vmax-type cooperative enzyme phosphoglycerate dehydrogenase (see paper)
39% identity, 60% coverage: 3:315/523 of query aligns to 6:324/404 of 1psdA
- active site: N102 (≠ S96), R234 (= R230), D258 (= D254), E263 (= E259), H286 (= H277)
- binding nicotinamide-adenine-dinucleotide: N102 (≠ S96), H155 (≠ R149), I156 (= I150), D175 (= D169), I176 (= I172), K179 (≠ E175), H204 (= H200), V205 (= V201), P206 (= P202), A232 (≠ C228), S233 (≠ A229), R234 (= R230), H286 (= H277)
Sites not aligning to the query:
Query Sequence
>WP_011973284.1 NCBI__GCF_000017185.1:WP_011973284.1
MPKILITDSIHDDAVELLKQAGTVEVATDLTVEELKEKIKDADALVIRSGTKATKEIIDA
ADNLKVIARAGVGVDNVDLTAATEKGIIVVNSPDASSISVAELALGLMLSSARNIPQATA
SLKRGEWDRKSFKGMELYGKTLGIIGLGRIGQQIAKRAEAFGMTVVAYDPYIPVEVAKNM
GIELMEVNDLCKVSDFITLHVPLTPKTKHMIGKEQISLMKPNTIIVNCARGGLIDEEALY
DAINNKKIGGAGLDVFEEEPPKDNPLLTLDKFIGTPHQGASTVEAQKSAGTVVAEQVVKI
LAGKPADNIVNLPRMPTDKMNKLNPYMALAEKMGNMIIQLLDKSVEKVELTYSGELASED
TEMVKRSFLMGLLSPILLAGVNLVNAPTIAKNRNIKIVEGTLSECEYGSSIKIKAEGKEE
CISLVGSLVEGAPVLKEINNYKIDIKPEGIVCVIKHMDKPGIIGKASTLLGDYGVNIAGM
QVGRQEPGGESVMVLNLDHVITEEVISKLKNIDNIIDAKIIKL
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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