SitesBLAST
Comparing WP_011372908.1 NCBI__GCF_000012965.1:WP_011372908.1 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)
P56119 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
44% identity, 94% coverage: 1:248/263 of query aligns to 3:250/263 of P56119
3phiA Shikimate 5-dehydrogenase (aroe) from helicobacter pylori in complex with shikimate and NADPH
44% identity, 94% coverage: 1:248/263 of query aligns to 3:247/259 of 3phiA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: L66 (≠ V60), P67 (= P61), K69 (= K63), G124 (= G122), G125 (= G123), S126 (≠ T124), R146 (= R144), T177 (= T177), S178 (= S178), A179 (= A179), L181 (= L181), P186 (= P187), L205 (≠ V206), Y207 (= Y208), G227 (= G228), M230 (= M231), L231 (= L232)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S16 (= S14), S18 (= S16), N63 (= N57), K69 (= K63), N90 (= N84), D105 (= D99), Y207 (= Y208), Q234 (= Q235)
4fosA Crystal structure of shikimate dehydrogenase (aroe) q237a mutant from helicobacter pylori in complex with shikimate
44% identity, 94% coverage: 1:248/263 of query aligns to 3:250/263 of 4fosA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S16 (= S14), S18 (= S16), N63 (= N57), V64 (≠ I58), T65 (= T59), K69 (= K63), N90 (= N84), D105 (= D99), Y210 (= Y208), L234 (= L232)
3phjA Shikimate 5-dehydrogenase (aroe) from helicobacter pylori in complex with 3-dehydroshikimate
43% identity, 94% coverage: 1:248/263 of query aligns to 3:242/255 of 3phjA
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
36% identity, 94% coverage: 2:248/263 of query aligns to 7:255/269 of O67049
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
36% identity, 94% coverage: 2:248/263 of query aligns to 7:255/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (= V60), G130 (= G120), G133 (= G123), A134 (≠ T124), N153 (= N143), R154 (= R144), T155 (≠ S145), K158 (≠ R148), T188 (= T177), S189 (= S178), V190 (≠ A179), I214 (≠ V206), M238 (= M231), L239 (= L232)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S14), S21 (= S16), N64 (= N57), T66 (= T59), K70 (= K63), N91 (= N84), D106 (= D99), Y216 (= Y208), L239 (= L232), Q242 (= Q235)
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
36% identity, 94% coverage: 2:248/263 of query aligns to 7:255/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (= V60), G132 (= G122), G133 (= G123), A134 (≠ T124), N153 (= N143), R154 (= R144), T155 (≠ S145), T188 (= T177), S189 (= S178), V190 (≠ A179)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S14), S21 (= S16), N64 (= N57), K70 (= K63), N91 (= N84), D106 (= D99), Y216 (= Y208), L239 (= L232), Q242 (= Q235)
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
32% identity, 93% coverage: 4:247/263 of query aligns to 3:251/269 of Q5HNV1
- SLS 13:15 (≠ SRS 14:16) binding
- T60 (= T59) binding
- N85 (= N84) binding
- D100 (= D99) binding
- Y211 (= Y208) 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 (= Q235) binding
1nytA Shikimate dehydrogenase aroe complexed with NADP+ (see paper)
32% identity, 89% coverage: 1:235/263 of query aligns to 1:244/271 of 1nytA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K65 (= K63), D102 (= D99), G128 (= G122), G129 (= G123), A130 (≠ T124), N149 (= N143), R150 (= R144), T151 (≠ S145), R154 (= R148), T188 (= T177), S189 (= S178), S190 (≠ A179), M213 (≠ V206), G237 (= G228), M240 (= M231), L241 (= L232)
2cy0A Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP (see paper)
36% identity, 93% coverage: 1:245/263 of query aligns to 1:245/262 of 2cy0A
- active site: K64 (= K63), D100 (= D99)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G123 (= G120), G126 (= G123), A127 (≠ T124), N146 (= N143), R147 (= R144), T148 (≠ S145), R151 (= R148), T179 (= T177), R180 (≠ S178), V181 (≠ A179), L205 (≠ V206), L232 (= L232)
2ev9B Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP(h) and shikimate (see paper)
36% identity, 93% coverage: 1:245/263 of query aligns to 1:245/263 of 2ev9B
- active site: K64 (= K63), D100 (= D99)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S14 (= S14), S16 (= S16), N58 (= N57), T60 (= T59), K64 (= K63), N85 (= N84), D100 (= D99), Q235 (= Q235)
Q5SJF8 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
36% identity, 93% coverage: 1:245/263 of query aligns to 1:245/263 of Q5SJF8
P15770 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Escherichia coli (strain K12) (see paper)
32% identity, 89% coverage: 1:235/263 of query aligns to 1:244/272 of P15770
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
31% identity, 93% coverage: 4:247/263 of query aligns to 3:242/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (= S14), S15 (= S16), N58 (= N57), T60 (= T59), K64 (= K63), N85 (= N84), D100 (= D99), F227 (≠ L232), Q230 (= Q235)
2gptA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate (see paper)
32% identity, 98% coverage: 2:259/263 of query aligns to 235:488/498 of 2gptA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: I239 (= I6), S247 (= S14), S249 (= S16), T292 (= T59), K296 (= K63), N317 (= N84), D334 (= D99), Y436 (= Y208), Q464 (= Q235), Q468 (≠ A239)
Sites not aligning to the query:
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)
30% identity, 98% coverage: 2:259/263 of query aligns to 324:602/603 of Q9SQT8
- S336 (= S14) binding ; mutation to A: 13-fold decrease in substrate affinity but almost no change in activity.
- S338 (= S16) binding ; mutation to A: 10-fold decrease in activity, and 9-fold decrease in substrate affinity.
- T381 (= T59) binding
- K385 (= K63) binding ; 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 (= N84) binding
- D423 (= D99) binding ; mutation to A: Loss of shikimate dehydrogenase activity.; mutation to N: Reduced shikimate dehydrogenase activity, but no change in substrate affinity.
- A461 (= A121) binding
- G463 (= G123) binding
- A464 (≠ T124) binding
- N483 (= N143) binding
- T485 (≠ S145) binding
- R488 (= R148) binding
- M525 (≠ L181) binding
- A548 (≠ V206) binding
- Y550 (= Y208) binding ; mutation Y->F,A: 100-fold decrease in activity, and 2-fold decrease in substrate affinity.
- G571 (= G228) binding
- Q578 (= Q235) binding
- Q582 (≠ A239) binding
Sites not aligning to the query:
- 124 binding
- 126 binding
- 155 binding
- 241 binding
- 279 binding
- 300 binding
- 304 binding
6bmqA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase (t381g mutant) in complex with tartrate and shikimate (see paper)
32% identity, 98% coverage: 2:259/263 of query aligns to 235:488/498 of 6bmqA
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: S247 (= S14), S249 (= S16), C291 (≠ I58), K296 (= K63), N317 (= N84), D334 (= D99), Y436 (= Y208), Q464 (= Q235)
Sites not aligning to the query:
2o7qA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
32% identity, 98% coverage: 2:259/263 of query aligns to 235:491/501 of 2o7qA
Sites not aligning to the query:
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
30% identity, 97% coverage: 2:257/263 of query aligns to 11:287/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (≠ V60), G134 (= G120), A135 (= A121), G136 (= G122), G137 (= G123), A138 (≠ T124), N158 (= N143), R159 (= R144), D161 (= D146), F163 (vs. gap), T207 (= T177), V209 (≠ A179), M211 (≠ L181), F214 (≠ K184), V235 (= V206), Y237 (= Y208), M261 (= M231), M262 (≠ L232)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (= S14), S25 (= S16), N68 (= N57), S70 (≠ T59), K74 (= K63), N95 (= N84), D110 (= D99), Q265 (= Q235)
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
30% identity, 97% coverage: 2:257/263 of query aligns to 14:290/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G120), A138 (= A121), G139 (= G122), G140 (= G123), A141 (≠ T124), N161 (= N143), R162 (= R144), D164 (= D146), F166 (vs. gap), T210 (= T177), G211 (≠ S178), V212 (≠ A179), M214 (≠ L181), F217 (≠ K184), V238 (= V206), Y240 (= Y208), G261 (= G228), M264 (= M231), M265 (≠ L232)
Query Sequence
>WP_011372908.1 NCBI__GCF_000012965.1:WP_011372908.1
MKLFAIFGDPVAHSRSPLMHNSVFKNLNYKACYTRIHLQDGSKLKETFLSLKLSGANITV
PHKEAAYAACDEVRGFAKKVGVVNTIVNENGRLIGYNTDADGFMFAIKEFGDVKNILILG
AGGTAKALASKFIDSGIKVSVMNRSDSRLSYFKELGCECFNWDNFEIKKYDLVLNSTSAG
LKDKEFPAPLALIEQILNNTSFVAEVIYGKITPFLKLAKEKNITCKDGADMLLAQGILAN
ELFVNSELKSDDIEHYMSKSFTL
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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