SitesBLAST
Comparing 8501228 FitnessBrowser__Miya:8501228 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)
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
34% identity, 86% coverage: 10:281/315 of query aligns to 7:256/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (≠ I70), G130 (= G134), G133 (= G137), A134 (= A138), N153 (≠ G164), R154 (= R165), T155 (≠ N166), K158 (= K169), T188 (= T199), S189 (≠ P200), V190 (≠ M201), I214 (≠ L237), M238 (= M263), L239 (≠ F264)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (≠ T22), S21 (= S24), N64 (≠ S67), T66 (= T69), K70 (= K73), N91 (= N94), D106 (= D109), Y216 (= Y239), L239 (≠ F264), Q242 (= Q267)
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
34% identity, 86% coverage: 10:281/315 of query aligns to 7:256/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (≠ I70), G132 (= G136), G133 (= G137), A134 (= A138), N153 (≠ G164), R154 (= R165), T155 (≠ N166), T188 (= T199), S189 (≠ P200), V190 (≠ M201)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (≠ T22), S21 (= S24), N64 (≠ S67), K70 (= K73), N91 (= N94), D106 (= D109), Y216 (= Y239), L239 (≠ F264), Q242 (= Q267)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
34% identity, 86% coverage: 10:281/315 of query aligns to 7:256/269 of O67049
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
31% identity, 90% coverage: 12:293/315 of query aligns to 3:265/269 of Q5HNV1
- SLS 13:15 (≠ TMS 22:24) binding
- T60 (= T69) binding
- N85 (= N94) binding
- D100 (= D109) binding
- Y211 (= Y239) Plays a major role in the catalytic process and a minor role in the substrate binding; mutation to F: Leads to a 345-fold decrease in the catalytic efficiency and a 3-fold decrease in the affinity binding for shikimate.
- Q239 (= Q267) binding
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
30% identity, 90% coverage: 12:293/315 of query aligns to 3:256/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (≠ T22), S15 (= S24), N58 (≠ S67), T60 (= T69), K64 (= K73), N85 (= N94), D100 (= D109), F227 (= F264), Q230 (= Q267)
Q58484 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) (see paper)
33% identity, 86% coverage: 10:279/315 of query aligns to 7:266/282 of Q58484
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
33% identity, 86% coverage: 10:279/315 of query aligns to 12:271/287 of 1nvtB
- active site: K75 (= K73), D111 (= D109)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (= I70), G135 (= G137), G137 (≠ A139), G138 (≠ R140), A139 (= A141), N157 (≠ G164), R158 (= R165), T159 (≠ N166), K162 (= K169), A200 (≠ T198), T201 (= T199), P202 (= P200), I203 (≠ M201), M205 (= M203), L229 (= L237), Y231 (= Y239), M255 (= M263), L256 (≠ F264)
- binding zinc ion: E22 (≠ G20), H23 (= H21)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
33% identity, 86% coverage: 10:279/315 of query aligns to 12:271/287 of 1nvtA
- active site: K75 (= K73), D111 (= D109)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (= G137), A139 (= A141), N157 (≠ G164), R158 (= R165), T159 (≠ N166), K162 (= K169), A200 (≠ T198), T201 (= T199), P202 (= P200), I203 (≠ M201), M205 (= M203), L229 (= L237), Y231 (= Y239), G252 (= G260), M255 (= M263), L256 (≠ F264)
2ev9B Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP(h) and shikimate (see paper)
40% identity, 85% coverage: 12:278/315 of query aligns to 4:246/263 of 2ev9B
- active site: K64 (= K73), D100 (= D109)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S14 (≠ T22), S16 (= S24), N58 (≠ S67), T60 (= T69), K64 (= K73), N85 (= N94), D100 (= D109), Q235 (= Q267)
Q5SJF8 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
40% identity, 85% coverage: 12:278/315 of query aligns to 4:246/263 of Q5SJF8
2cy0A Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP (see paper)
40% identity, 85% coverage: 12:278/315 of query aligns to 4:246/262 of 2cy0A
- active site: K64 (= K73), D100 (= D109)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G123 (= G134), G126 (= G137), A127 (= A138), N146 (≠ G164), R147 (= R165), T148 (≠ N166), R151 (≠ K169), T179 (= T199), R180 (≠ P200), V181 (≠ M201), L205 (= L237), L232 (≠ F264)
2o7sA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
34% identity, 87% coverage: 10:283/315 of query aligns to 235:482/500 of 2o7sA
- binding 3-dehydroshikimate: I239 (= I14), S247 (≠ T22), S249 (= S24), T292 (= T69), K296 (= K73), N317 (= N94), D334 (= D109), Y438 (= Y239), Q466 (= Q267), Q470 (= Q271)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I293 (= I70), P294 (= P71), K296 (= K73), D334 (= D109), G354 (= G136), G355 (= G137), A356 (= A138), N374 (≠ G164), R375 (= R165), T376 (≠ N166), R379 (≠ K169), T409 (= T199), S410 (≠ P200), M411 (= M201), A436 (≠ L237), M462 (= M263), F463 (= F264)
Sites not aligning to the query:
2o7qA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
33% identity, 87% coverage: 10:283/315 of query aligns to 235:483/501 of 2o7qA
Sites not aligning to the query:
Q9SQT8 Bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplastic; DHQ-SDH protein; DHQase-SORase; Protein EMBRYO DEFECTIVE 3004; EC 4.2.1.10; EC 1.1.1.25 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
32% identity, 87% coverage: 10:283/315 of query aligns to 324:594/603 of Q9SQT8
- S336 (≠ T22) binding ; mutation to A: 13-fold decrease in substrate affinity but almost no change in activity.
- S338 (= S24) binding ; mutation to A: 10-fold decrease in activity, and 9-fold decrease in substrate affinity.
- T381 (= T69) binding
- K385 (= K73) binding ; mutation to A: Strongly reduced shikimate dehydrogenase activity, but minor change in substrate affinity.; mutation to N: Strongly reduced shikimate dehydrogenase activity, but no change in substrate affinity.
- N406 (= N94) binding
- D423 (= D109) binding ; mutation to A: Loss of shikimate dehydrogenase activity.; mutation to N: Reduced shikimate dehydrogenase activity, but no change in substrate affinity.
- A461 (≠ N135) binding
- G463 (= G137) binding
- A464 (= A138) binding
- N483 (≠ G164) binding
- T485 (≠ N166) binding
- R488 (≠ K169) binding
- M525 (= M203) binding
- A548 (≠ L237) binding
- Y550 (= Y239) binding ; mutation Y->F,A: 100-fold decrease in activity, and 2-fold decrease in substrate affinity.
- G571 (= G260) binding
- Q578 (= Q267) binding
- Q582 (= Q271) binding
Sites not aligning to the query:
- 124 binding
- 126 binding
- 155 binding
- 241 binding
- 279 binding
- 300 binding
- 304 binding
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
30% identity, 89% coverage: 10:289/315 of query aligns to 11:287/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (≠ I70), G134 (= G134), A135 (≠ N135), G136 (= G136), G137 (= G137), A138 (= A138), N158 (≠ G164), R159 (= R165), D161 (vs. gap), F163 (vs. gap), T207 (= T199), V209 (≠ M201), M211 (= M203), F214 (≠ R207), V235 (≠ L237), Y237 (= Y239), M261 (= M263), M262 (≠ F264)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (≠ T22), S25 (= S24), N68 (≠ S67), S70 (≠ T69), K74 (= K73), N95 (= N94), D110 (= D109), Q265 (= Q267)
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
30% identity, 89% coverage: 10:289/315 of query aligns to 14:290/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G134), A138 (≠ N135), G139 (= G136), G140 (= G137), A141 (= A138), N161 (≠ G164), R162 (= R165), D164 (vs. gap), F166 (vs. gap), T210 (= T199), G211 (≠ P200), V212 (≠ M201), M214 (= M203), F217 (≠ R207), V238 (≠ L237), Y240 (= Y239), G261 (= G260), M264 (= M263), M265 (≠ F264)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
30% identity, 89% coverage: 10:289/315 of query aligns to 14:290/291 of Q8Y9N5
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
28% identity, 89% coverage: 10:289/315 of query aligns to 8:284/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (≠ N135), G133 (= G136), G134 (= G137), A135 (= A138), N155 (≠ G150), R156 (≠ P151), D158 (≠ G153), F160 (≠ G155), T204 (= T199), K205 (≠ P200), V206 (≠ M201), M208 (= M203), C232 (≠ L237), M258 (= M263), L259 (≠ F264)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
28% identity, 89% coverage: 10:289/315 of query aligns to 8:284/288 of P0A6D5
- S22 (= S24) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (= Y41) mutation to F: Kinetically unchanged as compared with the wild-type.
- S67 (≠ T69) mutation to A: Reduces activity towards quinate about 6-fold, but has a little effect on shikimate conversion.
- K71 (= K73) mutation to A: 3200-fold decrease in the affinity for quinate. 170-fold decrease in the affinity for shikimate.; mutation to G: 10-fold greater reduction in catalytic efficiency is observed with quinate than with shikimate.
- N92 (= N94) mutation to A: Alters protein structure. Loss of activity for both substrates.
- T106 (= T108) mutation to A: 2000-fold decrease in the affinity for quinate. 70-fold decrease in the affinity for shikimate. 10-fold greater reduction in catalytic efficiency is observed with quinate than with shikimate.
- D107 (= D109) mutation to A: Loss of activity towards quinate. 20000-fold decrease in the affinity for shikimate.
- AGGA 132:135 (≠ NGGA 135:138) binding
- NRRD 155:158 (≠ GPAG 150:153) binding
- K205 (≠ P200) binding
- CVYN 232:235 (≠ LVYN 237:240) binding
- G255 (= G260) binding
- Q262 (= Q267) mutation to A: 3-fold reduction in catalytic efficiency for both substrates.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
28% identity, 89% coverage: 10:289/315 of query aligns to 2:278/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (≠ N135), G127 (= G136), G128 (= G137), A129 (= A138), R150 (≠ P151), F154 (≠ G155), K199 (≠ P200), V200 (≠ M201), M202 (= M203), C226 (≠ L237), Y228 (= Y239), M252 (= M263), L253 (≠ F264)
Query Sequence
>8501228 FitnessBrowser__Miya:8501228
MPAHPFLPRELYGIIGHPLGHTMSPLLHNWGFSLLDVPAVYMAWPLEPGRVGDFITAVRT
LPIRGASVTIPHKQAVLPLLDGVSDRARAVGAVNTLYWRDGQLLGENTDVTGFLAPLRQR
AAAGWRCERALVLGNGGAARAVLAGLRELGPAGDGVVRAVGVTGRNAEKAAPLAAEFGAE
VVDWDARVHWGADLVVNTTPMGMSGERQGDTAFPEQGFAAQGVAAGGDGRRGLAYDLVYN
PLRTRFLSEAADAGWDTQDGLGMFVEQGREQFRLWTGLELPAEGARTLVAVALGLGDVAV
GRVCGQCELPGLGKG
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