SitesBLAST
Comparing 15811 FitnessBrowser__Keio:15811 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)
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
100% identity, 100% coverage: 1:288/288 of query aligns to 1:288/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (= A132), G133 (= G133), G134 (= G134), A135 (= A135), N155 (= N155), R156 (= R156), D158 (= D158), F160 (= F160), T204 (= T204), K205 (= K205), V206 (= V206), M208 (= M208), C232 (= C232), M258 (= M258), L259 (= L259)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
100% identity, 100% coverage: 1:288/288 of query aligns to 1:288/288 of P0A6D5
- M1 (= M1) modified: Initiator methionine, Removed
- S22 (= S22) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (= Y39) mutation to F: Kinetically unchanged as compared with the wild-type.
- S67 (= S67) mutation to A: Reduces activity towards quinate about 6-fold, but has a little effect on shikimate conversion.
- K71 (= K71) 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 (= N92) mutation to A: Alters protein structure. Loss of activity for both substrates.
- T106 (= T106) 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 (= D107) mutation to A: Loss of activity towards quinate. 20000-fold decrease in the affinity for shikimate.
- AGGA 132:135 (= AGGA 132:135) binding
- NRRD 155:158 (= NRRD 155:158) binding
- K205 (= K205) binding
- CVYN 232:235 (= CVYN 232:235) binding
- G255 (= G255) binding
- Q262 (= Q262) mutation to A: 3-fold reduction in catalytic efficiency for both substrates.
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
100% identity, 97% coverage: 7:286/288 of query aligns to 1:280/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (= A132), G127 (= G133), G128 (= G134), A129 (= A135), R150 (= R156), F154 (= F160), K199 (= K205), V200 (= V206), M202 (= M208), C226 (= C232), Y228 (= Y234), M252 (= M258), L253 (= L259)
Q8ZPR4 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
91% identity, 100% coverage: 1:288/288 of query aligns to 1:288/288 of Q8ZPR4
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
49% identity, 98% coverage: 3:284/288 of query aligns to 9:290/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G131), A138 (= A132), G139 (= G133), G140 (= G134), A141 (= A135), N161 (= N155), R162 (= R156), D164 (= D158), F166 (= F160), T210 (= T204), G211 (≠ K205), V212 (= V206), M214 (= M208), F217 (≠ L211), V238 (≠ C232), Y240 (= Y234), G261 (= G255), M264 (= M258), M265 (≠ L259)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
49% identity, 98% coverage: 3:284/288 of query aligns to 9:290/291 of Q8Y9N5
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
49% identity, 98% coverage: 3:284/288 of query aligns to 6:287/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (= M68), G134 (= G131), A135 (= A132), G136 (= G133), G137 (= G134), A138 (= A135), N158 (= N155), R159 (= R156), D161 (= D158), F163 (= F160), T207 (= T204), V209 (= V206), M211 (= M208), F214 (≠ L211), V235 (≠ C232), Y237 (= Y234), M261 (= M258), M262 (≠ L259)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (= S20), S25 (= S22), N68 (≠ G65), S70 (= S67), K74 (= K71), N95 (= N92), D110 (= D107), Q265 (= Q262)
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
35% identity, 95% coverage: 3:276/288 of query aligns to 2:256/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (≠ M68), G130 (= G131), G133 (= G134), A134 (= A135), N153 (= N155), R154 (= R156), T155 (≠ R157), K158 (= K163), T188 (= T204), S189 (≠ K205), V190 (= V206), I214 (≠ C232), M238 (= M258), L239 (= L259)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S20), S21 (= S22), N64 (≠ G65), T66 (≠ S67), K70 (= K71), N91 (= N92), D106 (= D107), Y216 (= Y234), L239 (= L259), Q242 (= Q262)
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
35% identity, 95% coverage: 3:276/288 of query aligns to 2:256/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (≠ M68), G132 (= G133), G133 (= G134), A134 (= A135), N153 (= N155), R154 (= R156), T155 (≠ R157), T188 (= T204), S189 (≠ K205), V190 (= V206)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S20), S21 (= S22), N64 (≠ G65), K70 (= K71), N91 (= N92), D106 (= D107), Y216 (= Y234), L239 (= L259), Q242 (= Q262)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
35% identity, 95% coverage: 3:276/288 of query aligns to 2:256/269 of O67049
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)
36% identity, 98% coverage: 3:284/288 of query aligns to 2:276/282 of Q58484
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
36% identity, 98% coverage: 3:284/288 of query aligns to 7:281/287 of 1nvtB
- active site: K75 (= K71), D111 (= D107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (≠ M68), G135 (= G131), G137 (= G133), G138 (= G134), A139 (= A135), N157 (= N155), R158 (= R156), T159 (≠ R157), K162 (= K163), A200 (≠ G203), T201 (= T204), P202 (≠ K205), I203 (≠ V206), M205 (= M208), L229 (≠ C232), Y231 (= Y234), M255 (= M258), L256 (= L259)
- binding zinc ion: E22 (≠ R18), H23 (= H19)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
36% identity, 98% coverage: 3:284/288 of query aligns to 7:281/287 of 1nvtA
- active site: K75 (= K71), D111 (= D107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (= G131), A139 (= A135), N157 (= N155), R158 (= R156), T159 (≠ R157), K162 (= K163), A200 (≠ G203), T201 (= T204), P202 (≠ K205), I203 (≠ V206), M205 (= M208), L229 (≠ C232), Y231 (= Y234), G252 (= G255), M255 (= M258), L256 (= L259)
2ev9B Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP(h) and shikimate (see paper)
30% identity, 91% coverage: 10:272/288 of query aligns to 4:245/263 of 2ev9B
- active site: K64 (= K71), D100 (= D107)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S14 (= S20), S16 (= S22), N58 (≠ G65), T60 (≠ S67), K64 (= K71), N85 (= N92), D100 (= D107), Q235 (= Q262)
2cy0A Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP (see paper)
30% identity, 91% coverage: 10:272/288 of query aligns to 4:245/262 of 2cy0A
- active site: K64 (= K71), D100 (= D107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G123 (≠ L130), G126 (≠ A135), A127 (≠ S136), N146 (= N155), R147 (= R156), T148 (≠ R157), R151 (≠ K163), T179 (= T204), R180 (≠ K205), V181 (= V206), L205 (≠ C232), L232 (= L259)
Q5SJF8 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
30% identity, 91% coverage: 10:272/288 of query aligns to 4:245/263 of Q5SJF8
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
31% identity, 97% coverage: 6:284/288 of query aligns to 2:261/269 of Q5HNV1
- SLS 13:15 (= SLS 20:22) binding
- T60 (≠ S67) binding
- N85 (= N92) binding
- D100 (= D107) binding
- Y211 (= Y234) 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 (= Q262) binding
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
30% identity, 97% coverage: 6:284/288 of query aligns to 2:252/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (= S20), S15 (= S22), N58 (≠ G65), T60 (≠ S67), K64 (= K71), N85 (= N92), D100 (= D107), F227 (≠ L259), Q230 (= Q262)
P44774 Shikimate dehydrogenase-like protein HI_0607; SDH-L; EC 1.1.1.25 from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) (see paper)
30% identity, 91% coverage: 25:287/288 of query aligns to 23:267/271 of P44774
- K67 (= K71) mutation K->A,H,N: Loss of activity.
- D103 (= D107) mutation D->A,N: Loss of activity.
2o7sA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
31% identity, 97% coverage: 8:285/288 of query aligns to 235:489/500 of 2o7sA
- binding 3-dehydroshikimate: I239 (≠ L12), S247 (= S20), S249 (= S22), T292 (≠ S67), K296 (= K71), N317 (= N92), D334 (= D107), Y438 (= Y234), Q466 (= Q262), Q470 (= Q266)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I293 (≠ M68), P294 (= P69), K296 (= K71), D334 (= D107), G354 (= G133), G355 (= G134), A356 (= A135), N374 (= N155), R375 (= R156), T376 (≠ R157), R379 (≠ K163), T409 (= T204), S410 (≠ K205), M411 (≠ V206), A436 (≠ C232), M462 (= M258), F463 (≠ L259)
Sites not aligning to the query:
Query Sequence
>15811 FitnessBrowser__Keio:15811
MDVTAKYELIGLMAYPIRHSLSPEMQNKALEKAGLPFTYMAFEVDNDSFPGAIEGLKALK
MRGTGVSMPNKQLACEYVDELTPAAKLVGAINTIVNDDGYLRGYNTDGTGHIRAIKESGF
DIKGKTMVLLGAGGASTAIGAQGAIEGLKEIKLFNRRDEFFDKALAFAQRVNENTDCVVT
VTDLADQQAFAEALASADILTNGTKVGMKPLENESLVNDISLLHPGLLVTECVYNPHMTK
LLQQAQQAGCKTIDGYGMLLWQGAEQFTLWTGKDFPLEYVKQVMGFGA
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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