SitesBLAST
Comparing WP_092057095.1 NCBI__GCF_900111775.1:WP_092057095.1 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)
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)
39% identity, 99% coverage: 3:285/287 of query aligns to 2:281/282 of Q58484
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
39% identity, 99% coverage: 3:285/287 of query aligns to 7:286/287 of 1nvtB
- active site: K75 (= K71), D111 (= D107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (≠ V68), G135 (= G132), G137 (= G134), G138 (= G135), A139 (= A136), N157 (= N156), R158 (= R157), T159 (= T158), K162 (≠ R161), A200 (≠ S201), T201 (≠ S202), P202 (≠ A203), I203 (≠ L204), M205 (≠ L206), L229 (≠ M228), Y231 (= Y230), M255 (= M254), L256 (= L255)
- binding zinc ion: E22 (≠ K18), H23 (= H19)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
39% identity, 99% coverage: 3:285/287 of query aligns to 7:286/287 of 1nvtA
- active site: K75 (= K71), D111 (= D107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (= G132), A139 (= A136), N157 (= N156), R158 (= R157), T159 (= T158), K162 (≠ R161), A200 (≠ S201), T201 (≠ S202), P202 (≠ A203), I203 (≠ L204), M205 (≠ L206), L229 (≠ M228), Y231 (= Y230), G252 (= G251), M255 (= M254), L256 (= L255)
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
40% identity, 95% coverage: 3:275/287 of query aligns to 2:259/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (= V68), G130 (= G132), G133 (= G135), A134 (= A136), N153 (= N156), R154 (= R157), T155 (= T158), K158 (≠ R161), T188 (≠ S202), S189 (≠ A203), V190 (≠ L204), I214 (≠ M228), M238 (= M254), L239 (= L255)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S20), S21 (= S22), N64 (= N65), T66 (= T67), K70 (= K71), N91 (= N92), D106 (= D107), 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)
40% identity, 95% coverage: 3:275/287 of query aligns to 2:259/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (= V68), G132 (= G134), G133 (= G135), A134 (= A136), N153 (= N156), R154 (= R157), T155 (= T158), T188 (≠ S202), S189 (≠ A203), V190 (≠ L204)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S20), S21 (= S22), N64 (= N65), K70 (= K71), N91 (= N92), D106 (= D107), Y216 (= Y230), L239 (= L255), Q242 (= Q258)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
39% identity, 95% coverage: 3:275/287 of query aligns to 2:259/269 of O67049
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
36% identity, 93% coverage: 12:277/287 of query aligns to 5:258/269 of Q5HNV1
- SLS 13:15 (= SLS 20:22) binding
- T60 (= T67) binding
- N85 (= N92) binding
- D100 (= D107) 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
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
36% identity, 97% coverage: 1:277/287 of query aligns to 1:281/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (= A133), G133 (= G134), G134 (= G135), A135 (= A136), N155 (= N156), R156 (= R157), D158 (≠ P159), F160 (≠ R161), T204 (≠ S202), K205 (≠ A203), V206 (≠ L204), M208 (vs. gap), C232 (≠ M228), 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)
36% identity, 97% coverage: 1:277/287 of query aligns to 1:281/288 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 (≠ T67) 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 133:136) binding
- NRRD 155:158 (≠ NRTP 156:159) binding
- K205 (≠ A203) binding
- CVYN 232:235 (≠ MVYG 228:231) binding
- G255 (= G251) binding
- Q262 (= Q258) mutation to A: 3-fold reduction in catalytic efficiency for both substrates.
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
36% identity, 93% coverage: 12:277/287 of query aligns to 5:249/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (= S20), S15 (= S22), N58 (= N65), T60 (= T67), K64 (= K71), N85 (= N92), D100 (= D107), F227 (≠ L255), Q230 (= Q258)
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
37% identity, 94% coverage: 8:277/287 of query aligns to 2:275/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (= A133), G127 (= G134), G128 (= G135), A129 (= A136), R150 (= R157), F154 (≠ R161), K199 (≠ A203), V200 (≠ L204), M202 (vs. gap), C226 (≠ M228), Y228 (= Y230), M252 (= M254), L253 (= L255)
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
34% identity, 98% coverage: 2:281/287 of query aligns to 5:288/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (≠ V68), G134 (= G132), A135 (= A133), G136 (= G134), G137 (= G135), A138 (= A136), N158 (= N156), R159 (= R157), D161 (≠ P159), F163 (≠ R161), T207 (≠ S202), V209 (≠ L204), M211 (≠ L206), F214 (vs. gap), V235 (≠ M228), Y237 (= Y230), M261 (= M254), M262 (≠ L255)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (= S20), S25 (= S22), N68 (= N65), S70 (≠ T67), K74 (= K71), N95 (= N92), D110 (= D107), Q265 (= Q258)
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
34% identity, 98% coverage: 2:281/287 of query aligns to 8:291/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G132), A138 (= A133), G139 (= G134), G140 (= G135), A141 (= A136), N161 (= N156), R162 (= R157), D164 (≠ P159), F166 (≠ R161), T210 (≠ S202), G211 (≠ A203), V212 (≠ L204), M214 (≠ L206), F217 (vs. gap), V238 (≠ M228), 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, 98% coverage: 2:281/287 of query aligns to 8:291/291 of Q8Y9N5
Q8ZPR4 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
36% identity, 97% coverage: 1:277/287 of query aligns to 1:281/288 of Q8ZPR4
2ev9B Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP(h) and shikimate (see paper)
43% identity, 94% coverage: 10:278/287 of query aligns to 4:256/263 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 (= N65), T60 (= T67), K64 (= K71), N85 (= N92), D100 (= D107), Q235 (= Q258)
Q5SJF8 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
43% identity, 94% coverage: 10:278/287 of query aligns to 4:256/263 of Q5SJF8
2cy0A Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP (see paper)
43% identity, 94% coverage: 10:278/287 of query aligns to 4:256/262 of 2cy0A
- active site: K64 (= K71), D100 (= D107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G123 (= G132), G126 (= G135), A127 (= A136), N146 (= N156), R147 (= R157), T148 (= T158), R151 (= R161), T179 (≠ S202), R180 (≠ A203), V181 (≠ L204), L205 (≠ M228), L232 (= L255)
7colA Crystal structure of 5-ketofructose reductase complexed with NADPH (see paper)
38% identity, 95% coverage: 9:280/287 of query aligns to 7:274/280 of 7colA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G128 (= G132), G130 (= G134), G131 (= G135), A132 (= A136), N152 (= N156), R153 (= R157), K157 (≠ R161), T195 (≠ S202), S196 (≠ A203), I197 (≠ L204), V222 (≠ M228), Q252 (= Q258)
1nytA Shikimate dehydrogenase aroe complexed with NADP+ (see paper)
38% identity, 91% coverage: 12:271/287 of query aligns to 6:257/271 of 1nytA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K65 (= K71), D102 (= D107), G128 (= G134), G129 (= G135), A130 (= A136), N149 (= N156), R150 (= R157), T151 (= T158), R154 (= R161), T188 (≠ S202), S189 (≠ A203), S190 (≠ L204), M213 (= M228), G237 (= G251), M240 (= M254), L241 (= L255)
Query Sequence
>WP_092057095.1 NCBI__GCF_900111775.1:WP_092057095.1
MKISGTTRIIGIFGDPVKHSLSPLMHNAALTGIGYDAVYVPFHVLPDALPTAVEAIRILD
LLGVNLTVPHKERVCPLLDEIDPQARLIGAVNTVVNRQGRLIGYNTDGIGFLRSLAEDLG
FDPAGRRILLLGAGGASRAALVALAEAGAAAIVVANRTPERAAALVAEFRPVFSGTSFAS
CSLATEDLAAHLAGVDLVVNSSALGLGGEALPGFPWEKLPVFAVVYDMVYGFEPTPFLRE
AATRGHAGADGLGMLAAQGEEGFRLWTGQTPPSGVMKARLLAAVAAR
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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