SitesBLAST
Comparing WP_025274827.1 NCBI__GCF_000527155.1:WP_025274827.1 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)
4p4gA Crystal structure of mycobacterium tuberculosis shikimate dehydrogenase
42% identity, 97% coverage: 2:262/270 of query aligns to 3:261/265 of 4p4gA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S14 (= S13), S16 (= S15), T61 (= T60), K65 (= K64), N86 (= N85), D101 (= D100), Y211 (= Y211), L236 (= L236), Q239 (= Q239)
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
31% identity, 96% coverage: 4:263/270 of query aligns to 10:266/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (≠ M61), G130 (= G123), G133 (= G126), A134 (≠ T127), N153 (≠ R149), R154 (= R150), T155 (= T151), K158 (≠ R154), T188 (≠ V188), S189 (≠ P189), V190 (≠ K190), I214 (≠ V209), M238 (≠ L235), L239 (= L236)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S13), S21 (= S15), N64 (≠ S58), T66 (= T60), K70 (= K64), N91 (= N85), D106 (= D100), Y216 (= Y211), L239 (= L236), Q242 (= Q239)
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
31% identity, 96% coverage: 4:263/270 of query aligns to 10:266/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (≠ M61), G132 (= G125), G133 (= G126), A134 (≠ T127), N153 (≠ R149), R154 (= R150), T155 (= T151), T188 (≠ V188), S189 (≠ P189), V190 (≠ K190)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S13), S21 (= S15), N64 (≠ S58), K70 (= K64), N91 (= N85), D106 (= D100), Y216 (= Y211), L239 (= L236), Q242 (= Q239)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
31% identity, 96% coverage: 4:263/270 of query aligns to 10:266/269 of O67049
- SLS 19:21 (= SLS 13:15) binding shikimate
- D82 (≠ A76) binding NADP(+)
- N91 (= N85) binding shikimate
- D106 (= D100) binding shikimate
- GAGGA 130:134 (≠ GAGGT 123:127) binding NADP(+)
- I214 (≠ V209) binding NADP(+)
- Y216 (= Y211) binding shikimate
- G235 (= G232) binding NADP(+)
- Q242 (= Q239) binding shikimate
2gptA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate (see paper)
33% identity, 91% coverage: 4:249/270 of query aligns to 238:474/498 of 2gptA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: I239 (≠ V5), S247 (= S13), S249 (= S15), T292 (= T60), K296 (= K64), N317 (= N85), D334 (= D100), Y436 (= Y211), Q464 (= Q239), Q468 (= Q243)
Sites not aligning to the query:
7tbvA Crystal structure of the shikimate kinase + 3-dehydroquinate dehydratase + 3-dehydroshikimate dehydrogenase domains of aro1 from candida albicans (see paper)
31% identity, 96% coverage: 5:262/270 of query aligns to 407:679/682 of 7tbvA
Sites not aligning to the query:
2o7sA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
33% identity, 91% coverage: 4:249/270 of query aligns to 238:476/500 of 2o7sA
- binding 3-dehydroshikimate: I239 (≠ V5), S247 (= S13), S249 (= S15), T292 (= T60), K296 (= K64), N317 (= N85), D334 (= D100), Y438 (= Y211), Q466 (= Q239), Q470 (= Q243)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I293 (≠ M61), P294 (= P62), K296 (= K64), D334 (= D100), G354 (≠ T127), G355 (≠ A128), A356 (≠ R129), N374 (≠ R149), R375 (= R150), T376 (= T151), R379 (= R154), T409 (≠ V188), S410 (≠ P189), M411 (≠ K190), A436 (≠ V209), M462 (≠ L235), F463 (≠ L236)
Sites not aligning to the query:
2o7qA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
33% identity, 91% coverage: 4:249/270 of query aligns to 238:477/501 of 2o7qA
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)
33% identity, 91% coverage: 4:249/270 of query aligns to 238:474/498 of 6bmqA
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: S247 (= S13), S249 (= S15), C291 (≠ L59), K296 (= K64), N317 (= N85), D334 (= D100), Y436 (= Y211), Q464 (= Q239)
Sites not aligning to the query:
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
27% identity, 96% coverage: 1:259/270 of query aligns to 1:258/269 of Q5HNV1
- SLS 13:15 (= SLS 13:15) binding shikimate
- T60 (= T60) binding shikimate
- N85 (= N85) binding shikimate
- D100 (= D100) binding shikimate
- Y211 (= Y211) 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 (= Q239) binding shikimate
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
29% identity, 92% coverage: 4:251/270 of query aligns to 11:274/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (= A124), G133 (= G125), G134 (= G126), A135 (= A128), N155 (≠ A147), R156 (= R148), D158 (≠ R150), F160 (≠ P158), T204 (≠ V188), K205 (≠ P189), V206 (≠ K190), M208 (≠ V192), C232 (≠ V209), M258 (≠ L235), L259 (= L236)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
29% identity, 92% coverage: 4:251/270 of query aligns to 11:274/288 of P0A6D5
- S22 (= S15) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (= Y33) mutation to F: Kinetically unchanged as compared with the wild-type.
- S67 (≠ T60) mutation to A: Reduces activity towards quinate about 6-fold, but has a little effect on shikimate conversion.
- K71 (= K64) 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 (= N85) mutation to A: Alters protein structure. Loss of activity for both substrates.
- T106 (= T99) 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 (= D100) mutation to A: Loss of activity towards quinate. 20000-fold decrease in the affinity for shikimate.
- AGG-A 132:135 (≠ AGGTA 124:128) binding NAD(+)
- NRRD 155:158 (≠ ARRR 147:150) binding NAD(+)
- K205 (≠ P189) binding NAD(+)
- CVYN 232:235 (≠ VVYD 209:212) binding NAD(+)
- G255 (= G232) binding NAD(+)
- Q262 (= Q239) mutation to A: 3-fold reduction in catalytic efficiency for both substrates.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
29% identity, 92% coverage: 4:251/270 of query aligns to 5:268/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (= A124), G127 (= G125), G128 (= G126), A129 (= A128), R150 (= R148), F154 (≠ P158), K199 (≠ P189), V200 (≠ K190), M202 (≠ V192), C226 (≠ V209), Y228 (= Y211), M252 (≠ L235), L253 (= L236)
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: 5:249/270 of query aligns to 328:588/603 of Q9SQT8
- S336 (= S13) binding shikimate; mutation to A: 13-fold decrease in substrate affinity but almost no change in activity.
- S338 (= S15) binding shikimate; mutation to A: 10-fold decrease in activity, and 9-fold decrease in substrate affinity.
- T381 (= T60) binding shikimate
- K385 (= K64) binding shikimate; 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 (= N85) binding shikimate
- D423 (= D100) binding shikimate; mutation to A: Loss of shikimate dehydrogenase activity.; mutation to N: Reduced shikimate dehydrogenase activity, but no change in substrate affinity.
- A461 (= A124) binding NADP(+)
- G463 (= G126) binding NADP(+)
- A464 (≠ T127) binding NADP(+)
- N483 (≠ R149) binding NADP(+)
- T485 (= T151) binding NADP(+)
- R488 (= R154) binding NADP(+)
- M525 (≠ V192) binding NADP(+)
- A548 (≠ V209) binding NADP(+)
- Y550 (= Y211) binding shikimate; mutation Y->F,A: 100-fold decrease in activity, and 2-fold decrease in substrate affinity.
- G571 (= G232) binding NADP(+)
- Q578 (= Q239) binding shikimate
- Q582 (= Q243) binding shikimate
Sites not aligning to the query:
- 124 binding 3-dehydroshikimate
- 126 binding 3-dehydroshikimate
- 155 binding 3-dehydroshikimate
- 241 binding 3-dehydroshikimate
- 279 binding 3-dehydroshikimate
- 300 binding 3-dehydroshikimate
- 304 binding 3-dehydroshikimate
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
28% identity, 96% coverage: 1:259/270 of query aligns to 1:249/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (= S13), S15 (= S15), N58 (≠ S58), T60 (= T60), K64 (= K64), N85 (= N85), D100 (= D100), F227 (≠ L236), Q230 (= Q239)
P07547 Pentafunctional AROM polypeptide; EC 4.2.3.4; EC 2.5.1.19; EC 2.7.1.71; EC 4.2.1.10; EC 1.1.1.25 from Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) (see 2 papers)
28% identity, 92% coverage: 2:249/270 of query aligns to 1291:1567/1583 of P07547
Sites not aligning to the query:
- 44:46 binding NAD(+)
- 81:84 binding NAD(+)
- 114:116 binding NAD(+)
- 119 binding NAD(+)
- 139:140 binding NAD(+)
- 161 binding NAD(+)
- 179:182 binding NAD(+)
- 190 binding NAD(+)
- 194 binding Zn(2+)
- 271 binding Zn(2+)
- 287 binding Zn(2+)
2cy0A Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP (see paper)
31% identity, 92% coverage: 1:249/270 of query aligns to 2:245/262 of 2cy0A