SitesBLAST
Comparing Synpcc7942_2467 FitnessBrowser__SynE:Synpcc7942_2467 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)
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
34% identity, 97% coverage: 4:281/288 of query aligns to 9:290/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G132), A138 (≠ C133), G139 (= G134), G140 (= G135), A141 (= A136), N161 (≠ A159), R162 (≠ Q160), D164 (≠ G162), F166 (≠ A164), T210 (= T198), G211 (≠ P199), V212 (≠ L200), M214 (= M202), F217 (≠ H205), V238 (≠ L228), Y240 (= Y230), G261 (= G251), M264 (= M254), M265 (≠ L255)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
34% identity, 97% coverage: 4:281/288 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.
34% identity, 97% coverage: 4:281/288 of query aligns to 6:287/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (≠ I69), G134 (= G132), A135 (≠ C133), G136 (= G134), G137 (= G135), A138 (= A136), N158 (≠ A159), R159 (≠ Q160), D161 (≠ G162), F163 (≠ A164), T207 (= T198), V209 (≠ L200), M211 (= M202), F214 (≠ H205), V235 (≠ L228), Y237 (= Y230), M261 (= M254), M262 (≠ L255)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (= S21), S25 (= S23), N68 (= N66), S70 (≠ T68), K74 (= K72), N95 (= N93), D110 (= D108), Q265 (= Q258)
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
35% identity, 97% coverage: 2:281/288 of query aligns to 5:281/287 of 1nvtB
- active site: K75 (= K72), D111 (= D108)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (= I69), G135 (= G132), G137 (= G134), G138 (= G135), A139 (= A136), N157 (≠ T154), R158 (= R157), T159 (≠ D158), K162 (= K161), A200 (≠ T197), T201 (= T198), P202 (= P199), I203 (≠ L200), M205 (= M202), L229 (= L228), Y231 (= Y230), M255 (= M254), L256 (= L255)
- binding zinc ion: E22 (= E19), H23 (= H20)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
35% identity, 97% coverage: 2:281/288 of query aligns to 5:281/287 of 1nvtA
- active site: K75 (= K72), D111 (= D108)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (= G132), A139 (= A136), N157 (≠ T154), R158 (= R157), T159 (≠ D158), K162 (= K161), A200 (≠ T197), T201 (= T198), P202 (= P199), I203 (≠ L200), M205 (= M202), L229 (= L228), Y231 (= Y230), G252 (= G251), M255 (= M254), L256 (= L255)
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)
35% identity, 97% coverage: 4:281/288 of query aligns to 2:276/282 of Q58484
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
34% identity, 96% coverage: 4:280/288 of query aligns to 2:264/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (≠ I69), G130 (= G132), G133 (= G135), A134 (= A136), N153 (≠ V156), R154 (= R157), T155 (≠ D158), K158 (= K161), T188 (= T198), S189 (≠ P199), V190 (≠ L200), I214 (≠ L228), M238 (= M254), L239 (= L255)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S21), S21 (= S23), N64 (= N66), T66 (= T68), K70 (= K72), N91 (= N93), D106 (= D108), Y216 (= Y230), L239 (= L255), Q242 (= Q258)
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
34% identity, 96% coverage: 4:280/288 of query aligns to 2:264/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (≠ I69), G132 (= G134), G133 (= G135), A134 (= A136), N153 (≠ V156), R154 (= R157), T155 (≠ D158), T188 (= T198), S189 (≠ P199), V190 (≠ L200)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S21), S21 (= S23), N64 (= N66), K70 (= K72), N91 (= N93), D106 (= D108), Y216 (= Y230), L239 (= L255), Q242 (= Q258)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
34% identity, 96% coverage: 4:280/288 of query aligns to 2:264/269 of O67049
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
33% identity, 97% coverage: 4:281/288 of query aligns to 3:284/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (≠ C133), G133 (= G134), G134 (= G135), A135 (= A136), N155 (≠ V156), R156 (= R157), D158 (≠ A159), F160 (≠ K161), T204 (= T198), K205 (≠ P199), V206 (≠ L200), M208 (= M202), C232 (≠ L228), M258 (= M254), L259 (= L255)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
33% identity, 97% coverage: 4:281/288 of query aligns to 3:284/288 of P0A6D5
- S22 (= S23) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (= Y40) mutation to F: Kinetically unchanged as compared with the wild-type.
- S67 (≠ T68) mutation to A: Reduces activity towards quinate about 6-fold, but has a little effect on shikimate conversion.
- K71 (= K72) 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 (= N93) mutation to A: Alters protein structure. Loss of activity for both substrates.
- T106 (= T107) 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 (= D108) mutation to A: Loss of activity towards quinate. 20000-fold decrease in the affinity for shikimate.
- AGGA 132:135 (≠ CGGA 133:136) binding
- NRRD 155:158 (≠ VRDA 156:159) binding
- K205 (≠ P199) binding
- CVYN 232:235 (≠ LIYT 228:231) binding
- G255 (= G251) binding
- Q262 (= Q258) mutation to A: 3-fold reduction in catalytic efficiency for both substrates.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Q8ZPR4 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
34% identity, 97% coverage: 4:281/288 of query aligns to 3:284/288 of Q8ZPR4
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
33% identity, 95% coverage: 9:281/288 of query aligns to 2:278/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (≠ C133), G127 (= G134), G128 (= G135), A129 (= A136), R150 (= R157), F154 (≠ K161), K199 (≠ P199), V200 (≠ L200), M202 (= M202), C226 (≠ L228), Y228 (= Y230), M252 (= M254), L253 (= L255)
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
30% identity, 94% coverage: 11:281/288 of query aligns to 3:261/269 of Q5HNV1
- SLS 13:15 (= SLS 21:23) binding
- T60 (= T68) binding
- N85 (= N93) binding
- D100 (= D108) binding
- Y211 (= Y230) 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 (= Q258) binding
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
29% identity, 94% coverage: 11:281/288 of query aligns to 3:252/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (= S21), S15 (= S23), N58 (= N66), T60 (= T68), K64 (= K72), N85 (= N93), D100 (= D108), F227 (≠ L255), Q230 (= Q258)
7colA Crystal structure of 5-ketofructose reductase complexed with NADPH (see paper)
37% identity, 91% coverage: 7:268/288 of query aligns to 4:262/280 of 7colA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G128 (= G132), G130 (= G134), G131 (= G135), A132 (= A136), N152 (≠ V156), R153 (= R157), K157 (= K161), T195 (= T198), S196 (≠ P199), I197 (≠ L200), V222 (≠ L228), Q252 (= Q258)
2o7qA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
32% identity, 91% coverage: 8:268/288 of query aligns to 234:477/501 of 2o7qA
Sites not aligning to the query:
2o7sA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
31% identity, 92% coverage: 8:271/288 of query aligns to 234:479/500 of 2o7sA
- binding 3-dehydroshikimate: I239 (= I13), S247 (= S21), S249 (= S23), T292 (= T68), K296 (= K72), N317 (= N93), D334 (= D108), Y438 (= Y230), Q466 (= Q258), Q470 (≠ G262)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I293 (= I69), P294 (= P70), K296 (= K72), D334 (= D108), G354 (= G134), G355 (= G135), A356 (= A136), N374 (≠ T154), R375 (= R157), T376 (≠ D158), R379 (≠ K161), T409 (= T198), S410 (≠ P199), M411 (≠ L200), A436 (≠ L228), M462 (= M254), F463 (≠ L255)
Sites not aligning to the query:
2gptA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate (see paper)
30% identity, 91% coverage: 8:268/288 of query aligns to 234:474/498 of 2gptA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: I239 (= I13), S247 (= S21), S249 (= S23), T292 (= T68), K296 (= K72), N317 (= N93), D334 (= D108), Y436 (= Y230), Q464 (= Q258), Q468 (≠ G262)
Sites not aligning to the query:
6bmqA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase (t381g mutant) in complex with tartrate and shikimate (see paper)
29% identity, 91% coverage: 8:268/288 of query aligns to 234:474/498 of 6bmqA
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: S247 (= S21), S249 (= S23), C291 (≠ V67), K296 (= K72), N317 (= N93), D334 (= D108), Y436 (= Y230), Q464 (= Q258)
Sites not aligning to the query:
Query Sequence
>Synpcc7942_2467 FitnessBrowser__SynE:Synpcc7942_2467
MSALTGRTRLLGIIGDPIEHSLSPLIQNAAIAELGLDYCYVPFPVKGADLATALAGLAAI
GVQGFNVTIPHKQAVMPLLSQVSELAQSVGSVNTVWQTEQGWVGTNTDVLGFLAPLQTLR
SDWSGCRVVLLGCGGAARAVVAGCLQLGCSAIATVVRDAQKGDAFQQSWGDRADSLTIHD
WSDIPDVLSTADLVVNTTPLGMDPHIERSPLDNSAAQQLRPETIAYDLIYTPSPTRFLQQ
AIAQGCHAIDGLEMLVQQGAAGLKIWTGAEAVPVDTMRSVLNAHLGLA
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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