SitesBLAST
Comparing WP_084057311.1 NCBI__GCF_900176285.1:WP_084057311.1 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)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
40% identity, 96% coverage: 4:270/278 of query aligns to 3:269/269 of O67049
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
40% identity, 96% coverage: 4:270/278 of query aligns to 3:269/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (≠ I66), G132 (= G130), G133 (= G131), A134 (= A132), N153 (= N151), R154 (= R152), T155 (= T153), T188 (= T186), S189 (≠ A187), V190 (≠ G188)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S20), S21 (= S22), N64 (≠ S63), K70 (= K69), N91 (= N90), D106 (= D105), Y216 (= Y215), L239 (= L240), Q242 (= Q243)
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: 4:267/278 of query aligns to 3:266/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (≠ I66), G130 (= G128), G133 (= G131), A134 (= A132), N153 (= N151), R154 (= R152), T155 (= T153), K158 (= K156), T188 (= T186), S189 (≠ A187), V190 (≠ G188), I214 (= I213), M238 (= M239), L239 (= L240)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S20), S21 (= S22), N64 (≠ S63), T66 (= T65), K70 (= K69), N91 (= N90), D106 (= D105), Y216 (= Y215), L239 (= L240), Q242 (= Q243)
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
34% identity, 87% coverage: 10:251/278 of query aligns to 3:247/269 of Q5HNV1
- SLS 13:15 (= SLS 20:22) binding
- T60 (= T65) binding
- N85 (= N90) binding
- D100 (= D105) binding
- Y211 (= Y215) 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 (= Q243) 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)
31% identity, 95% coverage: 1:265/278 of query aligns to 1:284/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (= A129), G133 (= G130), G134 (= G131), A135 (= A132), N155 (= N151), R156 (= R152), D158 (≠ E154), F160 (vs. gap), T204 (= T186), K205 (≠ A187), V206 (≠ G188), M208 (≠ L190), C232 (≠ I213), M258 (= M239), L259 (= L240)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
31% identity, 95% coverage: 1:265/278 of query aligns to 1:284/288 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 (≠ T65) mutation to A: Reduces activity towards quinate about 6-fold, but has a little effect on shikimate conversion.
- K71 (= K69) 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 (= N90) mutation to A: Alters protein structure. Loss of activity for both substrates.
- T106 (= T104) 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 (= D105) mutation to A: Loss of activity towards quinate. 20000-fold decrease in the affinity for shikimate.
- AGGA 132:135 (= AGGA 129:132) binding
- NRRD 155:158 (≠ NRTE 151:154) binding
- K205 (≠ A187) binding
- CVYN 232:235 (≠ IVYS 213:216) binding
- G255 (= G236) binding
- Q262 (= Q243) mutation to A: 3-fold reduction in catalytic efficiency for both substrates.
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
32% identity, 93% coverage: 7:265/278 of query aligns to 1:278/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (= A129), G127 (= G130), G128 (= G131), A129 (= A132), R150 (= R152), F154 (vs. gap), K199 (≠ A187), V200 (≠ G188), M202 (≠ L190), C226 (≠ I213), Y228 (= Y215), M252 (= M239), L253 (= L240)
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
34% identity, 87% coverage: 10:251/278 of query aligns to 3:238/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (= S20), S15 (= S22), N58 (≠ S63), T60 (= T65), K64 (= K69), N85 (= N90), D100 (= D105), F227 (≠ L240), Q230 (= Q243)
Q8ZPR4 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
32% identity, 95% coverage: 1:265/278 of query aligns to 1:284/288 of Q8ZPR4
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)
33% identity, 92% coverage: 11:267/278 of query aligns to 10:278/282 of Q58484
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
33% identity, 92% coverage: 11:267/278 of query aligns to 15:283/287 of 1nvtB
- active site: K75 (= K69), D111 (= D105)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (= I66), G135 (= G128), G137 (= G130), G138 (= G131), A139 (= A132), N157 (= N151), R158 (= R152), T159 (= T153), K162 (vs. gap), A200 (≠ C185), T201 (= T186), P202 (≠ A187), I203 (≠ G188), M205 (≠ L190), L229 (≠ I213), Y231 (= Y215), M255 (= M239), L256 (= L240)
- binding zinc ion: E22 (≠ R18), H23 (= H19)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
33% identity, 92% coverage: 11:267/278 of query aligns to 15:283/287 of 1nvtA
- active site: K75 (= K69), D111 (= D105)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (= G128), A139 (= A132), N157 (= N151), R158 (= R152), T159 (= T153), K162 (vs. gap), A200 (≠ C185), T201 (= T186), P202 (≠ A187), I203 (≠ G188), M205 (≠ L190), L229 (≠ I213), Y231 (= Y215), G252 (= G236), M255 (= M239), L256 (= L240)
2o7qA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
32% identity, 91% coverage: 9:260/278 of query aligns to 236:484/501 of 2o7qA
Sites not aligning to the query:
P56119 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
32% identity, 92% coverage: 10:266/278 of query aligns to 6:260/263 of P56119
3phiA Shikimate 5-dehydrogenase (aroe) from helicobacter pylori in complex with shikimate and NADPH
32% identity, 92% coverage: 10:266/278 of query aligns to 6:257/259 of 3phiA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: L66 (≠ I66), P67 (= P67), K69 (= K69), G124 (= G130), G125 (= G131), S126 (≠ A132), R146 (= R152), T177 (= T186), S178 (≠ A187), A179 (≠ G188), L181 (= L190), P186 (= P203), L205 (≠ I213), Y207 (= Y215), G227 (= G236), M230 (= M239), L231 (= L240)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S16 (= S20), S18 (= S22), N63 (≠ S63), K69 (= K69), N90 (= N90), D105 (= D105), Y207 (= Y215), Q234 (= Q243)
4fosA Crystal structure of shikimate dehydrogenase (aroe) q237a mutant from helicobacter pylori in complex with shikimate
31% identity, 92% coverage: 10:266/278 of query aligns to 6:260/263 of 4fosA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S16 (= S20), S18 (= S22), N63 (≠ S63), V64 (= V64), T65 (= T65), K69 (= K69), N90 (= N90), D105 (= D105), Y210 (= Y215), L234 (= L240)
2gptA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate (see paper)
35% identity, 91% coverage: 9:260/278 of query aligns to 236:481/498 of 2gptA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: I239 (≠ V12), S247 (= S20), S249 (= S22), T292 (= T65), K296 (= K69), N317 (= N90), D334 (= D105), Y436 (= Y215), Q464 (= Q243), Q468 (= Q247)
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)
33% identity, 91% coverage: 9:260/278 of query aligns to 325:595/603 of Q9SQT8
- S336 (= S20) binding ; mutation to A: 13-fold decrease in substrate affinity but almost no change in activity.
- S338 (= S22) binding ; mutation to A: 10-fold decrease in activity, and 9-fold decrease in substrate affinity.
- T381 (= T65) binding
- K385 (= K69) 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 (= N90) binding
- D423 (= D105) binding ; mutation to A: Loss of shikimate dehydrogenase activity.; mutation to N: Reduced shikimate dehydrogenase activity, but no change in substrate affinity.
- A461 (= A129) binding
- G463 (= G131) binding
- A464 (= A132) binding
- N483 (= N151) binding
- T485 (= T153) binding
- R488 (≠ K156) binding
- M525 (≠ L190) binding
- A548 (≠ I213) binding
- Y550 (= Y215) binding ; mutation Y->F,A: 100-fold decrease in activity, and 2-fold decrease in substrate affinity.
- G571 (= G236) binding
- Q578 (= Q243) binding
- Q582 (= Q247) binding
Sites not aligning to the query:
- 124 binding
- 126 binding
- 155 binding
- 241 binding
- 279 binding
- 300 binding
- 304 binding
3phjA Shikimate 5-dehydrogenase (aroe) from helicobacter pylori in complex with 3-dehydroshikimate
31% identity, 92% coverage: 10:266/278 of query aligns to 6:252/255 of 3phjA
2cy0A Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP (see paper)
41% identity, 94% coverage: 10:270/278 of query aligns to 4:262/262 of 2cy0A
- active site: K64 (= K69), D100 (= D105)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G123 (= G128), G126 (= G131), A127 (= A132), N146 (= N151), R147 (= R152), T148 (= T153), R151 (≠ K156), T179 (= T186), R180 (≠ A187), V181 (≠ G188), L205 (≠ I213), L232 (= L240)
Query Sequence
>WP_084057311.1 NCBI__GCF_900176285.1:WP_084057311.1
MARSVQHDLYGVVGNPVRHSLSPAMMNAALVHLAVPAFYLALESEDFAQDLEGLVELGLR
GLSVTIPHKETALGLCAWVDEAAREIGAVNTLRWSEKGWEGRNTDWIGAVRALQSAVELG
GQRALVLGAGGAAKAVIYGLVRSGLQVTVANRTEAKARDLAARFGCHWVPLAHMKEVSVD
LVVHCTAGGLRGRSYAFALEEVPFRPGAVVMDIVYSPLDTPFLQAARAAGASVVDGLEML
LHQGVEQLSWWLGRPAPESVMRRALRDAAGGREGREGA
Or try a new SitesBLAST search
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