SitesBLAST
Comparing GFF3462 FitnessBrowser__Phaeo:GFF3462 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)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
35% identity, 98% coverage: 1:272/277 of query aligns to 1:262/269 of O67049
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
34% identity, 98% coverage: 1:272/277 of query aligns to 1:262/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (≠ I67), G130 (= G133), G133 (= G136), A134 (= A137), N153 (= N157), R154 (= R158), T155 (= T159), K158 (≠ R162), T188 (= T196), S189 (= S197), V190 (≠ L198), I214 (≠ L222), M238 (= M248), L239 (= L249)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S19), S21 (= S21), N64 (= N64), T66 (= T66), K70 (= K70), N91 (= N91), D106 (= D107), Y216 (= Y224), L239 (= L249), Q242 (= Q252)
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
34% identity, 98% coverage: 1:272/277 of query aligns to 1:262/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (≠ I67), G132 (= G135), G133 (= G136), A134 (= A137), N153 (= N157), R154 (= R158), T155 (= T159), T188 (= T196), S189 (= S197), V190 (≠ L198)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S19), S21 (= S21), N64 (= N64), K70 (= K70), N91 (= N91), D106 (= D107), Y216 (= Y224), L239 (= L249), Q242 (= Q252)
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
31% identity, 94% coverage: 10:269/277 of query aligns to 4:256/269 of Q5HNV1
- SLS 13:15 (≠ SRS 19:21) binding
- T60 (= T66) binding
- N85 (= N91) binding
- D100 (= D107) binding
- Y211 (= Y224) 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 (= Q252) binding
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
30% identity, 94% coverage: 10:269/277 of query aligns to 4:247/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (= S19), S15 (= S21), N58 (= N64), T60 (= T66), K64 (= K70), N85 (= N91), D100 (= D107), F227 (≠ L249), Q230 (= Q252)
Q9KVT3 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
34% identity, 97% coverage: 4:273/277 of query aligns to 3:269/278 of Q9KVT3
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)
34% identity, 97% coverage: 1:268/277 of query aligns to 1:270/282 of Q58484
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
32% identity, 94% coverage: 8:268/277 of query aligns to 12:281/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (≠ I67), G134 (= G133), A135 (= A134), G136 (= G135), G137 (= G136), A138 (= A137), N158 (= N157), R159 (= R158), D161 (vs. gap), F163 (vs. gap), T207 (= T196), V209 (≠ L198), M211 (= M200), F214 (vs. gap), V235 (≠ L222), Y237 (= Y224), M261 (= M248), M262 (≠ L249)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (= S19), S25 (= S21), N68 (= N64), S70 (≠ T66), K74 (= K70), N95 (= N91), D110 (= D107), Q265 (= Q252)
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
32% identity, 94% coverage: 8:268/277 of query aligns to 15:284/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G133), A138 (= A134), G139 (= G135), G140 (= G136), A141 (= A137), N161 (= N157), R162 (= R158), D164 (vs. gap), F166 (vs. gap), T210 (= T196), G211 (≠ S197), V212 (≠ L198), M214 (= M200), F217 (vs. gap), V238 (≠ L222), Y240 (= Y224), G261 (= G245), M264 (= M248), M265 (≠ L249)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
32% identity, 94% coverage: 8:268/277 of query aligns to 15:284/291 of Q8Y9N5
3pgjA 2.49 angstrom resolution crystal structure of shikimate 5- dehydrogenase (aroe) from vibrio cholerae o1 biovar eltor str. N16961 in complex with shikimate
34% identity, 95% coverage: 11:273/277 of query aligns to 6:265/272 of 3pgjA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S14 (= S19), S16 (= S21), N59 (= N64), T61 (= T66), K65 (= K70), N86 (= N91), D102 (= D107), Q244 (= Q252)
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
34% identity, 97% coverage: 1:268/277 of query aligns to 6:275/287 of 1nvtB
- active site: K75 (= K70), D111 (= D107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (= I67), G135 (= G133), G137 (= G135), G138 (= G136), A139 (= A137), N157 (= N157), R158 (= R158), T159 (= T159), K162 (≠ R162), A200 (≠ T195), T201 (= T196), P202 (≠ S197), I203 (≠ L198), M205 (= M200), L229 (= L222), Y231 (= Y224), M255 (= M248), L256 (= L249)
- binding zinc ion: E22 (≠ A17), H23 (= H18)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
34% identity, 97% coverage: 1:268/277 of query aligns to 6:275/287 of 1nvtA
- active site: K75 (= K70), D111 (= D107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (= G133), A139 (= A137), N157 (= N157), R158 (= R158), T159 (= T159), K162 (≠ R162), A200 (≠ T195), T201 (= T196), P202 (≠ S197), I203 (≠ L198), M205 (= M200), L229 (= L222), Y231 (= Y224), G252 (= G245), M255 (= M248), L256 (= L249)
1nytA Shikimate dehydrogenase aroe complexed with NADP+ (see paper)
32% identity, 95% coverage: 11:273/277 of query aligns to 6:265/271 of 1nytA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K65 (= K70), D102 (= D107), G128 (= G135), G129 (= G136), A130 (= A137), N149 (= N157), R150 (= R158), T151 (= T159), R154 (= R162), T188 (= T196), S189 (= S197), S190 (≠ L198), M213 (≠ L222), G237 (= G245), M240 (= M248), L241 (= L249)
P15770 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Escherichia coli (strain K12) (see paper)
32% identity, 95% coverage: 11:273/277 of query aligns to 6:265/272 of P15770
3sefA 2.4 angstrom resolution crystal structure of shikimate 5-dehydrogenase (aroe) from vibrio cholerae o1 biovar eltor str. N16961 in complex with shikimate and NADPH
34% identity, 95% coverage: 11:273/277 of query aligns to 6:261/268 of 3sefA
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
31% identity, 94% coverage: 5:263/277 of query aligns to 6:273/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (= A134), G133 (= G135), G134 (= G136), A135 (= A137), N155 (= N157), R156 (= R158), D158 (≠ R160), F160 (≠ R162), T204 (= T196), K205 (≠ S197), V206 (≠ L198), M208 (= M200), C232 (≠ L222), M258 (= M248), L259 (= L249)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
31% identity, 94% coverage: 5:263/277 of query aligns to 6:273/288 of P0A6D5
- S22 (= S21) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (= Y38) mutation to F: Kinetically unchanged as compared with the wild-type.
- S67 (≠ T66) mutation to A: Reduces activity towards quinate about 6-fold, but has a little effect on shikimate conversion.
- K71 (= K70) 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 (= N91) 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 134:137) binding
- NRRD 155:158 (≠ NRTR 157:160) binding
- K205 (≠ S197) binding
- CVYN 232:235 (≠ LVYT 222:225) binding
- G255 (= G245) binding
- Q262 (= Q252) mutation to A: 3-fold reduction in catalytic efficiency for both substrates.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2o7sA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
35% identity, 94% coverage: 3:262/277 of query aligns to 233:476/500 of 2o7sA
- binding 3-dehydroshikimate: I239 (≠ V11), S247 (= S19), S249 (= S21), T292 (= T66), K296 (= K70), N317 (= N91), D334 (= D107), Y438 (= Y224), Q466 (= Q252), Q470 (≠ G256)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I293 (= I67), P294 (= P68), K296 (= K70), D334 (= D107), G354 (= G135), G355 (= G136), A356 (= A137), N374 (= N157), R375 (= R158), T376 (= T159), R379 (= R162), T409 (= T196), S410 (= S197), M411 (≠ L198), A436 (≠ L222), M462 (= M248), F463 (≠ L249)
Sites not aligning to the query:
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
32% identity, 92% coverage: 8:263/277 of query aligns to 3:267/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (= A134), G127 (= G135), G128 (= G136), A129 (= A137), R150 (= R158), F154 (≠ R162), K199 (≠ S197), V200 (≠ L198), M202 (= M200), C226 (≠ L222), Y228 (= Y224), M252 (= M248), L253 (= L249)
Query Sequence
>GFF3462 FitnessBrowser__Phaeo:GFF3462
MNDTRIPLAGVIGSPVAHSRSPLVHGHWLRTYGIAGHYVPLHVEPGQLEEVVRSLPKMGF
VGANITIPHKEQIMEIADQVTDRATLIGAANTLIFRPDGSILADNTDGYGFITNLHQAAP
DWDPATGPAVVFGAGGASRAVIASLLEAGVPEILLSNRTRERADQFRSEFGSRIQVVDWV
QVGNVIEQAALLVNTTSLGMVGKPRLRVPLDGLRSSTVVTDLVYTPLKTDMLQWAEDIGC
TTVDGLGMLLHQAVPGFERWFGKRPEVDAATREAALA
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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