SitesBLAST
Comparing 209045 FitnessBrowser__DvH:209045 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)
38% identity, 86% coverage: 35:293/301 of query aligns to 7:262/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (≠ I95), G130 (= G156), G133 (= G159), A134 (= A160), N153 (= N180), R154 (= R181), T155 (= T182), K158 (= K185), T188 (= T215), S189 (≠ P216), V190 (≠ C217), I214 (≠ L243), M238 (= M269), L239 (≠ F270)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (≠ T47), S21 (= S49), N64 (≠ S92), T66 (= T94), K70 (= K98), N91 (= N119), D106 (= D134), Y216 (= Y245), L239 (≠ F270), Q242 (= Q273)
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
38% identity, 86% coverage: 35:293/301 of query aligns to 7:262/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (≠ I95), G132 (= G158), G133 (= G159), A134 (= A160), N153 (= N180), R154 (= R181), T155 (= T182), T188 (= T215), S189 (≠ P216), V190 (≠ C217)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (≠ T47), S21 (= S49), N64 (≠ S92), K70 (= K98), N91 (= N119), D106 (= D134), Y216 (= Y245), L239 (≠ F270), Q242 (= Q273)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
37% identity, 88% coverage: 35:300/301 of query aligns to 7:269/269 of O67049
- SLS 19:21 (≠ TLS 47:49) binding shikimate
- D82 (= D110) binding NADP(+)
- N91 (= N119) binding shikimate
- D106 (= D134) binding shikimate
- GAGGA 130:134 (= GAGGA 156:160) binding NADP(+)
- I214 (≠ L243) binding NADP(+)
- Y216 (= Y245) binding shikimate
- G235 (= G266) binding NADP(+)
- Q242 (= Q273) binding shikimate
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / DSM 28319 / BCRC 17069 / CCUG 31568 / BM 3577 / RP62A) (see paper)
32% identity, 87% coverage: 37:299/301 of query aligns to 3:265/269 of Q5HNV1
- SLS 13:15 (≠ TLS 47:49) binding shikimate
- T60 (= T94) binding shikimate
- N85 (= N119) binding shikimate
- D100 (= D134) binding shikimate
- Y211 (= Y245) 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 (= Q273) binding shikimate
2o7qA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
38% identity, 85% coverage: 35:289/301 of query aligns to 235:483/501 of 2o7qA
Sites not aligning to the query:
2ev9B Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP(h) and shikimate (see paper)
44% identity, 85% coverage: 37:293/301 of query aligns to 4:259/263 of 2ev9B
- active site: K64 (= K98), D100 (= D134)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S14 (≠ T47), S16 (= S49), N58 (≠ S92), T60 (= T94), K64 (= K98), N85 (= N119), D100 (= D134), Q235 (= Q273)
Q5SJF8 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
44% identity, 85% coverage: 37:293/301 of query aligns to 4:259/263 of Q5SJF8
- SLS 14:16 (≠ TLS 47:49) binding shikimate
- T60 (= T94) binding shikimate
- K64 (= K98) active site, Proton acceptor
- N85 (= N119) binding shikimate
- D100 (= D134) binding shikimate
- GAGGA 123:127 (= GAGGA 156:160) binding NADP(+)
- NRTPQR 146:151 (≠ NRTHDK 180:185) binding NADP(+)
- L205 (= L243) binding NADP(+)
- Y207 (= Y245) binding shikimate
- G228 (= G266) binding NADP(+)
- Q235 (= Q273) binding shikimate
2cy0A Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP (see paper)
44% identity, 85% coverage: 37:293/301 of query aligns to 4:259/262 of 2cy0A
- active site: K64 (= K98), D100 (= D134)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G123 (= G156), G126 (= G159), A127 (= A160), N146 (= N180), R147 (= R181), T148 (= T182), R151 (≠ K185), T179 (= T215), R180 (≠ P216), V181 (≠ C217), L205 (= L243), L232 (≠ F270)
2o7sA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
39% identity, 85% coverage: 35:289/301 of query aligns to 235:482/500 of 2o7sA
- binding 3-dehydroshikimate: I239 (= I39), S247 (≠ T47), S249 (= S49), T292 (= T94), K296 (= K98), N317 (= N119), D334 (= D134), Y438 (= Y245), Q466 (= Q273), Q470 (= Q277)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I293 (= I95), P294 (= P96), K296 (= K98), D334 (= D134), G354 (= G158), G355 (= G159), A356 (= A160), N374 (= N180), R375 (= R181), T376 (= T182), R379 (≠ K185), T409 (= T215), S410 (≠ P216), M411 (≠ C217), A436 (≠ L243), M462 (= M269), F463 (= F270)
Sites not aligning to the query:
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
30% identity, 87% coverage: 37:299/301 of query aligns to 3:256/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (≠ T47), S15 (= S49), N58 (≠ S92), T60 (= T94), K64 (= K98), N85 (= N119), D100 (= D134), F227 (= F270), Q230 (= Q273)
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)
36% identity, 85% coverage: 35:289/301 of query aligns to 324:594/603 of Q9SQT8
- S336 (≠ T47) binding shikimate; mutation to A: 13-fold decrease in substrate affinity but almost no change in activity.
- S338 (= S49) binding shikimate; mutation to A: 10-fold decrease in activity, and 9-fold decrease in substrate affinity.
- T381 (= T94) binding shikimate
- K385 (= K98) binding shikimate; 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 (= N119) binding shikimate
- D423 (= D134) binding shikimate; mutation to A: Loss of shikimate dehydrogenase activity.; mutation to N: Reduced shikimate dehydrogenase activity, but no change in substrate affinity.
- A461 (= A157) binding NADP(+)
- G463 (= G159) binding NADP(+)
- A464 (= A160) binding NADP(+)
- N483 (= N180) binding NADP(+)
- T485 (= T182) binding NADP(+)
- R488 (≠ K185) binding NADP(+)
- M525 (= M219) binding NADP(+)
- A548 (≠ L243) binding NADP(+)
- Y550 (= Y245) binding shikimate; mutation Y->F,A: 100-fold decrease in activity, and 2-fold decrease in substrate affinity.
- G571 (= G266) binding NADP(+)
- Q578 (= Q273) binding shikimate
- Q582 (= Q277) binding shikimate
Sites not aligning to the query:
- 124 binding 3-dehydroshikimate
- 126 binding 3-dehydroshikimate
- 155 binding 3-dehydroshikimate
- 241 binding 3-dehydroshikimate
- 279 binding 3-dehydroshikimate
- 300 binding 3-dehydroshikimate
- 304 binding 3-dehydroshikimate
2gptA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate (see paper)
39% identity, 85% coverage: 35:289/301 of query aligns to 235:480/498 of 2gptA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: I239 (= I39), S247 (≠ T47), S249 (= S49), T292 (= T94), K296 (= K98), N317 (= N119), D334 (= D134), Y436 (= Y245), Q464 (= Q273), Q468 (= Q277)
Sites not aligning to the query:
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
34% identity, 87% coverage: 35:295/301 of query aligns to 2:278/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (= A157), G127 (= G158), G128 (= G159), A129 (= A160), R150 (= R181), F154 (vs. gap), K199 (≠ P216), V200 (≠ C217), M202 (= M219), C226 (≠ L243), Y228 (= Y245), M252 (= M269), L253 (≠ F270)
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
34% identity, 87% coverage: 35:295/301 of query aligns to 8:284/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (= A157), G133 (= G158), G134 (= G159), A135 (= A160), N155 (= N180), R156 (= R181), D158 (≠ H183), F160 (vs. gap), T204 (= T215), K205 (≠ P216), V206 (≠ C217), M208 (= M219), C232 (≠ L243), M258 (= M269), L259 (≠ F270)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
34% identity, 87% coverage: 35:295/301 of query aligns to 8:284/288 of P0A6D5
- S22 (= S49) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (= Y66) mutation to F: Kinetically unchanged as compared with the wild-type.
- S67 (≠ T94) mutation to A: Reduces activity towards quinate about 6-fold, but has a little effect on shikimate conversion.
- K71 (= K98) 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 (= N119) mutation to A: Alters protein structure. Loss of activity for both substrates.
- T106 (= T133) 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 (= D134) mutation to A: Loss of activity towards quinate. 20000-fold decrease in the affinity for shikimate.
- AGGA 132:135 (= AGGA 157:160) binding NAD(+)
- NRRD 155:158 (≠ NRTH 180:183) binding NAD(+)
- K205 (≠ P216) binding NAD(+)
- CVYN 232:235 (≠ LVYN 243:246) binding NAD(+)
- G255 (= G266) binding NAD(+)
- Q262 (= Q273) mutation to A: 3-fold reduction in catalytic efficiency for both substrates.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3pgjA 2.49 angstrom resolution crystal structure of shikimate 5- dehydrogenase (aroe) from vibrio cholerae o1 biovar eltor str. N16961 in complex with shikimate
36% identity, 82% coverage: 37:284/301 of query aligns to 4:255/272 of 3pgjA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S14 (≠ T47), S16 (= S49), N59 (≠ S92), T61 (= T94), K65 (= K98), N86 (= N119), D102 (= D134), Q244 (= Q273)
Q9KVT3 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
36% identity, 82% coverage: 37:284/301 of query aligns to 8:259/278 of Q9KVT3
- SKS 18:20 (≠ TLS 47:49) binding shikimate
- N90 (= N119) binding shikimate
- D106 (= D134) binding shikimate
- NRTFAK 154:159 (≠ NRTHDK 180:185) binding NADP(+)
- Q248 (= Q273) binding shikimate
6bmqA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase (t381g mutant) in complex with tartrate and shikimate (see paper)
38% identity, 85% coverage: 35:289/301 of query aligns to 235:480/498 of 6bmqA
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: S247 (≠ T47), S249 (= S49), C291 (≠ V93), K296 (= K98), N317 (= N119), D334 (= D134), Y436 (= Y245), Q464 (= Q273)
Sites not aligning to the query:
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)
31% identity, 88% coverage: 35:299/301 of query aligns to 7:280/282 of Q58484
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
31% identity, 88% coverage: 35:299/301 of query aligns to 12:285/287 of 1nvtB
- active site: K75 (= K98), D111 (= D134)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (= I95), G135 (= G158), G137 (≠ A160), G138 (≠ A161), A139 (≠ R162), N157 (= N180), R158 (= R181), T159 (= T182), K162 (= K185), A200 (≠ T214), T201 (= T215), P202 (= P216), I203 (≠ C217), M205 (= M219), L229 (= L243), Y231 (= Y245), M255 (= M269), L256 (≠ F270)
- binding zinc ion: E22 (≠ G45), H23 (= H46)
Query Sequence
>209045 FitnessBrowser__DvH:209045
MSAPIPTRSVKLSQSPCAADSSESAHRVPFRIPERLYGIVGHPLGHTLSPLLHNWGFALH
SLPAVYMAWPVPPGRFASFMEAVRTLPVHGASVTIPHKEEALRLCDRVTDRARAVGAVNT
LFLEDGVVCGENTDVTGFLAPLRARGVRIDEALVLGAGGAARAVLAGLVELGVRRVRISN
RTHDKAMELAGAFGADVVPWDERGSAAAGLVVNTTPCGMQGARMGESPLPEGAFSGRGMA
YDLVYNPLTTRFLADARAAGWETQDGLGMFVEQGREQFRIWTGLDLPAEGARRLIAEALG
L
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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