SitesBLAST
Comparing WP_012410575.1 NCBI__GCF_000020025.1:WP_012410575.1 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)
38% identity, 97% coverage: 6:291/295 of query aligns to 1:280/282 of Q58484
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
38% identity, 97% coverage: 6:291/295 of query aligns to 6:285/287 of 1nvtB
- active site: K75 (= K75), D111 (= D111)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (= I72), G135 (≠ A141), G137 (≠ A143), G138 (≠ V144), A139 (≠ V145), N157 (≠ G160), R158 (= R161), T159 (≠ N162), K162 (≠ R165), A200 (≠ T203), T201 (= T204), P202 (= P205), I203 (= I206), M205 (= M208), L229 (= L234), Y231 (= Y236), M255 (= M260), L256 (= L261)
- binding zinc ion: E22 (= E22), H23 (= H23)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
38% identity, 97% coverage: 6:291/295 of query aligns to 6:285/287 of 1nvtA
- active site: K75 (= K75), D111 (= D111)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (≠ A141), A139 (≠ V145), N157 (≠ G160), R158 (= R161), T159 (≠ N162), K162 (≠ R165), A200 (≠ T203), T201 (= T204), P202 (= P205), I203 (= I206), M205 (= M208), L229 (= L234), Y231 (= Y236), G252 (= G257), M255 (= M260), L256 (= L261)
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
34% identity, 96% coverage: 7:288/295 of query aligns to 9:291/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G136), A138 (≠ N137), G139 (= G138), G140 (= G139), A141 (= A140), N161 (≠ G160), R162 (= R161), D164 (vs. gap), F166 (vs. gap), T210 (= T204), G211 (≠ P205), V212 (≠ I206), M214 (= M208), F217 (≠ K211), V238 (≠ L234), Y240 (= Y236), G261 (= G257), M264 (= M260), M265 (≠ L261)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
34% identity, 96% coverage: 7:288/295 of query aligns to 9:291/291 of Q8Y9N5
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
34% identity, 96% coverage: 7:288/295 of query aligns to 6:288/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (≠ I72), G134 (= G136), A135 (≠ N137), G136 (= G138), G137 (= G139), A138 (= A140), N158 (≠ G160), R159 (= R161), D161 (vs. gap), F163 (vs. gap), T207 (= T204), V209 (≠ I206), M211 (= M208), F214 (≠ K211), V235 (≠ L234), Y237 (= Y236), M261 (= M260), M262 (≠ L261)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (= S24), S25 (= S26), N68 (≠ S69), S70 (≠ T71), K74 (= K75), N95 (= N96), D110 (= D111), Q265 (= Q264)
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
37% identity, 97% coverage: 6:292/295 of query aligns to 1:269/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (≠ I72), G132 (= G138), G133 (= G139), A134 (= A140), N153 (≠ G160), R154 (= R161), T155 (≠ N162), T188 (= T204), S189 (≠ P205), V190 (≠ I206)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S24), S21 (= S26), N64 (≠ S69), K70 (= K75), N91 (= N96), D106 (= D111), Y216 (= Y236), L239 (= L261), Q242 (= Q264)
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
37% identity, 96% coverage: 6:289/295 of query aligns to 1:266/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (≠ I72), G130 (= G136), G133 (= G139), A134 (= A140), N153 (≠ G160), R154 (= R161), T155 (≠ N162), K158 (≠ R165), T188 (= T204), S189 (≠ P205), V190 (≠ I206), I214 (≠ L234), M238 (= M260), L239 (= L261)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S24), S21 (= S26), N64 (≠ S69), T66 (= T71), K70 (= K75), N91 (= N96), D106 (= D111), Y216 (= Y236), L239 (= L261), Q242 (= Q264)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
37% identity, 97% coverage: 6:292/295 of query aligns to 1:269/269 of O67049
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
30% identity, 95% coverage: 7:287/295 of query aligns to 3:284/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (≠ N137), G133 (= G138), G134 (= G139), A135 (= A140), N155 (≠ G160), R156 (= R161), D158 (vs. gap), F160 (vs. gap), T204 (= T204), K205 (≠ P205), V206 (≠ I206), M208 (= M208), C232 (≠ L234), M258 (= M260), L259 (= L261)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
30% identity, 95% coverage: 7:287/295 of query aligns to 3:284/288 of P0A6D5
- S22 (= S26) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (= Y43) mutation to F: Kinetically unchanged as compared with the wild-type.
- S67 (≠ T71) mutation to A: Reduces activity towards quinate about 6-fold, but has a little effect on shikimate conversion.
- K71 (= K75) 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 (= N96) mutation to A: Alters protein structure. Loss of activity for both substrates.
- T106 (= T110) 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 (= D111) mutation to A: Loss of activity towards quinate. 20000-fold decrease in the affinity for shikimate.
- AGGA 132:135 (≠ NGGA 137:140) binding
- NRRD 155:158 (≠ GRN- 160:162) binding
- K205 (≠ P205) binding
- CVYN 232:235 (≠ LIYI 234:237) binding
- G255 (= G257) binding
- Q262 (= Q264) 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, 94% coverage: 12:287/295 of query aligns to 2:278/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (≠ N137), G127 (= G138), G128 (= G139), A129 (= A140), R150 (= R161), F154 (vs. gap), K199 (≠ P205), V200 (≠ I206), M202 (= M208), C226 (≠ L234), Y228 (= Y236), M252 (= M260), L253 (= L261)
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
31% identity, 94% coverage: 14:291/295 of query aligns to 3:265/269 of Q5HNV1
- SLS 13:15 (= SLS 24:26) binding
- T60 (= T71) binding
- N85 (= N96) binding
- D100 (= D111) binding
- Y211 (= Y236) 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 (= Q264) binding
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)
31% identity, 92% coverage: 1:272/295 of query aligns to 313:586/603 of Q9SQT8
- S336 (= S24) binding ; mutation to A: 13-fold decrease in substrate affinity but almost no change in activity.
- S338 (= S26) binding ; mutation to A: 10-fold decrease in activity, and 9-fold decrease in substrate affinity.
- T381 (= T71) binding
- K385 (= K75) 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 (= N96) binding
- D423 (= D111) binding ; mutation to A: Loss of shikimate dehydrogenase activity.; mutation to N: Reduced shikimate dehydrogenase activity, but no change in substrate affinity.
- A461 (≠ N137) binding
- G463 (= G139) binding
- A464 (= A140) binding
- N483 (≠ G160) binding
- T485 (≠ N162) binding
- R488 (= R165) binding
- M525 (= M208) binding
- A548 (≠ L234) binding
- Y550 (= Y236) binding ; mutation Y->F,A: 100-fold decrease in activity, and 2-fold decrease in substrate affinity.
- G571 (= G257) binding
- Q578 (= Q264) binding
- Q582 (≠ A268) binding
Sites not aligning to the query:
- 124 binding
- 126 binding
- 155 binding
- 241 binding
- 279 binding
- 300 binding
- 304 binding
2o7qA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
31% identity, 92% coverage: 1:272/295 of query aligns to 224:475/501 of 2o7qA
Sites not aligning to the query:
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
29% identity, 94% coverage: 14:291/295 of query aligns to 3:256/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (= S24), S15 (= S26), N58 (≠ S69), T60 (= T71), K64 (= K75), N85 (= N96), D100 (= D111), F227 (≠ L261), Q230 (= Q264)
2gptA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate (see paper)
32% identity, 92% coverage: 1:272/295 of query aligns to 224:472/498 of 2gptA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: I239 (≠ V16), S247 (= S24), S249 (= S26), T292 (= T71), K296 (= K75), N317 (= N96), D334 (= D111), Y436 (= Y236), Q464 (= Q264), Q468 (≠ A268)
Sites not aligning to the query:
2o7sA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
31% identity, 92% coverage: 1:272/295 of query aligns to 224:474/500 of 2o7sA
- binding 3-dehydroshikimate: I239 (≠ V16), S247 (= S24), S249 (= S26), T292 (= T71), K296 (= K75), N317 (= N96), D334 (= D111), Y438 (= Y236), Q466 (= Q264), Q470 (≠ A268)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I293 (= I72), P294 (= P73), K296 (= K75), D334 (= D111), G354 (= G138), G355 (= G139), A356 (= A140), N374 (≠ G160), R375 (= R161), T376 (≠ N162), R379 (= R165), T409 (= T204), S410 (≠ P205), M411 (≠ I206), A436 (≠ L234), M462 (= M260), F463 (≠ L261)
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)
31% identity, 92% coverage: 1:272/295 of query aligns to 224:472/498 of 6bmqA
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: S247 (= S24), S249 (= S26), C291 (≠ V70), K296 (= K75), N317 (= N96), D334 (= D111), Y436 (= Y236), Q464 (= Q264)
Sites not aligning to the query:
P44774 Shikimate dehydrogenase-like protein HI_0607; SDH-L; EC 1.1.1.25 from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) (see paper)
31% identity, 92% coverage: 6:276/295 of query aligns to 1:254/271 of P44774
- K67 (= K75) mutation K->A,H,N: Loss of activity.
- D103 (= D111) mutation D->A,N: Loss of activity.
Query Sequence
>WP_012410575.1 NCBI__GCF_000020025.1:WP_012410575.1
MANDKLITGKTKLLGVIGHPVEHSLSPAMHNAAIANLGLDYVYLPFPIAPENLEVAIAGF
AVIGVVGFSVTIPHKQAIMPLLSEITPLAQMIGAVNTVSRQNNQWVGTNTDIEGFIAPLQ
TTYKQDWSQKVAVILGNGGAARAVVAGCHQLGFAKIHVVGRNVQRLQEFRDSWSNSPISE
NLQVHQWEELSKLIPQANLLVNTTPIGMYPKVDESPLSIEEIANLPTGAIAYDLIYIPKP
TQFLELAQKQGAIAIDGLEMLVQQGVAALKIWLQQENIPVEVMRQALLNQLGLGK
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