SitesBLAST
Comparing WP_011736222.1 NCBI__GCF_000015045.1:WP_011736222.1 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)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
34% identity, 96% coverage: 8:272/277 of query aligns to 7:266/269 of O67049
- SLS 19:21 (= SLS 20:22) binding shikimate
- D82 (= D83) binding NADP(+)
- N91 (= N92) binding shikimate
- D106 (= D107) binding shikimate
- GAGGA 130:134 (≠ GAGGV 131:135) binding NADP(+)
- I214 (= I219) binding NADP(+)
- Y216 (= Y221) binding shikimate
- G235 (= G242) binding NADP(+)
- Q242 (= Q249) binding shikimate
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
33% identity, 96% coverage: 8:272/277 of query aligns to 7:266/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (≠ I68), G130 (= G131), G133 (= G134), A134 (≠ V135), N153 (≠ D155), R154 (≠ I156), T155 (≠ V157), K158 (≠ S160), T188 (= T190), S189 (≠ P191), V190 (≠ L192), I214 (= I219), M238 (= M245), L239 (≠ F246)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S20), S21 (= S22), N64 (≠ C65), T66 (= T67), K70 (= K71), N91 (= N92), D106 (= D107), Y216 (= Y221), L239 (≠ F246), Q242 (= Q249)
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
33% identity, 96% coverage: 8:272/277 of query aligns to 7:266/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (≠ I68), G132 (= G133), G133 (= G134), A134 (≠ V135), N153 (≠ D155), R154 (≠ I156), T155 (≠ V157), T188 (= T190), S189 (≠ P191), V190 (≠ L192)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S20), S21 (= S22), N64 (≠ C65), K70 (= K71), N91 (= N92), D106 (= D107), Y216 (= Y221), L239 (≠ F246), Q242 (= Q249)
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
31% identity, 92% coverage: 8:263/277 of query aligns to 14:282/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G131), A138 (= A132), G139 (= G133), G140 (= G134), A141 (≠ V135), N161 (vs. gap), R162 (vs. gap), D164 (vs. gap), F166 (vs. gap), T210 (= T190), G211 (≠ P191), V212 (≠ L192), M214 (= M194), F217 (= F198), V238 (≠ I219), Y240 (= Y221), G261 (= G242), M264 (= M245), M265 (≠ F246)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
31% identity, 92% coverage: 8:263/277 of query aligns to 14:282/291 of Q8Y9N5
- SLS 26:28 (= SLS 20:22) binding shikimate
- NRKD 161:164 (vs. gap) binding NAD(+)
- M214 (= M194) binding NADP(+)
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
31% identity, 92% coverage: 8:263/277 of query aligns to 11:279/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (≠ I68), G134 (= G131), A135 (= A132), G136 (= G133), G137 (= G134), A138 (≠ V135), N158 (vs. gap), R159 (vs. gap), D161 (vs. gap), F163 (vs. gap), T207 (= T190), V209 (≠ L192), M211 (= M194), F214 (= F198), V235 (≠ I219), Y237 (= Y221), M261 (= M245), M262 (≠ F246)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (= S20), S25 (= S22), N68 (≠ C65), S70 (≠ T67), K74 (= K71), N95 (= N92), D110 (= D107), Q265 (= Q249)
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: 1:263/277 of query aligns to 1:276/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (= A132), G133 (= G133), G134 (= G134), A135 (≠ V135), N155 (vs. gap), R156 (vs. gap), D158 (vs. gap), F160 (vs. gap), T204 (= T190), K205 (≠ P191), V206 (≠ L192), M208 (= M194), C232 (≠ I219), M258 (= M245), L259 (≠ F246)
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: 1:263/277 of query aligns to 1:276/288 of P0A6D5
- M1 (= M1) modified: Initiator methionine, Removed
- S22 (= S22) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (≠ L39) 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 (≠ AGGV 132:135) binding NAD(+)
- NRRD 155:158 (vs. gap) binding NAD(+)
- K205 (≠ P191) binding NAD(+)
- CVYN 232:235 (≠ IVYT 219:222) binding NAD(+)
- G255 (= G242) binding NAD(+)
- Q262 (= Q249) mutation to A: 3-fold reduction in catalytic efficiency for both substrates.
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
30% identity, 92% coverage: 8:263/277 of query aligns to 2:270/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (= A132), G127 (= G133), G128 (= G134), A129 (≠ V135), R150 (vs. gap), F154 (vs. gap), K199 (≠ P191), V200 (≠ L192), M202 (= M194), C226 (≠ I219), Y228 (= Y221), M252 (= M245), L253 (≠ F246)
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
31% identity, 96% coverage: 10:274/277 of query aligns to 3:265/269 of Q5HNV1
- SLS 13:15 (= SLS 20:22) binding shikimate
- T60 (= T67) binding shikimate
- N85 (= N92) binding shikimate
- D100 (= D107) binding shikimate
- Y211 (= Y221) 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 (= Q249) binding shikimate
2ev9B Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP(h) and shikimate (see paper)
36% identity, 94% coverage: 10:270/277 of query aligns to 4:261/263 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 (≠ C65), T60 (= T67), K64 (= K71), N85 (= N92), D100 (= D107), Q235 (= Q249)
Q5SJF8 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
36% identity, 94% coverage: 10:270/277 of query aligns to 4:261/263 of Q5SJF8
- SLS 14:16 (= SLS 20:22) binding shikimate
- T60 (= T67) binding shikimate
- K64 (= K71) active site, Proton acceptor
- N85 (= N92) binding shikimate
- D100 (= D107) binding shikimate
- GAGGA 123:127 (≠ GAGGV 131:135) binding NADP(+)
- NRTPQR 146:151 (≠ DIVDAS 155:160) binding NADP(+)
- L205 (≠ I219) binding NADP(+)
- Y207 (= Y221) binding shikimate
- G228 (= G242) binding NADP(+)
- Q235 (= Q249) binding shikimate
2cy0A Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP (see paper)
36% identity, 94% coverage: 10:270/277 of query aligns to 4:261/262 of 2cy0A
- active site: K64 (= K71), D100 (= D107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G123 (= G131), G126 (= G134), A127 (≠ V135), N146 (≠ D155), R147 (≠ I156), T148 (≠ V157), R151 (≠ S160), T179 (= T190), R180 (≠ P191), V181 (≠ L192), L205 (≠ I219), L232 (≠ F246)
2o7qA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
35% identity, 93% coverage: 8:264/277 of query aligns to 235:482/501 of 2o7qA
Sites not aligning to the query:
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
33% identity, 97% coverage: 8:275/277 of query aligns to 12:286/287 of 1nvtB
- active site: K75 (= K71), D111 (= D107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (= I68), G135 (= G131), G137 (= G133), G138 (= G134), A139 (≠ V135), N157 (vs. gap), R158 (vs. gap), T159 (vs. gap), K162 (≠ I156), A200 (≠ T189), T201 (= T190), P202 (= P191), I203 (≠ L192), M205 (= M194), L229 (≠ I219), Y231 (= Y221), M255 (= M245), L256 (≠ F246)
- binding zinc ion: E22 (≠ G18), H23 (= H19)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
33% identity, 97% coverage: 8:275/277 of query aligns to 12:286/287 of 1nvtA
- active site: K75 (= K71), D111 (= D107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (= G131), A139 (≠ V135), N157 (vs. gap), R158 (vs. gap), T159 (vs. gap), K162 (≠ I156), A200 (≠ T189), T201 (= T190), P202 (= P191), I203 (≠ L192), M205 (= M194), L229 (≠ I219), Y231 (= Y221), G252 (= G242), M255 (= M245), L256 (≠ F246)
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, 98% coverage: 5:275/277 of query aligns to 4:281/282 of Q58484
2o7sA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
35% identity, 93% coverage: 8:264/277 of query aligns to 235:481/500 of 2o7sA
- binding 3-dehydroshikimate: I239 (≠ V12), S247 (= S20), S249 (= S22), T292 (= T67), K296 (= K71), N317 (= N92), D334 (= D107), Y438 (= Y221), Q466 (= Q249), Q470 (= Q253)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I293 (= I68), P294 (= P69), K296 (= K71), D334 (= D107), G354 (= G133), G355 (= G134), A356 (≠ V135), N374 (≠ D155), R375 (≠ I156), T376 (≠ V157), R379 (≠ S160), T409 (= T190), S410 (≠ P191), M411 (≠ L192), A436 (≠ I219), M462 (= M245), F463 (= F246)
Sites not aligning to the query:
2gptA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate (see paper)
35% identity, 93% coverage: 8:264/277 of query aligns to 235:479/498 of 2gptA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: I239 (≠ V12), S247 (= S20), S249 (= S22), T292 (= T67), K296 (= K71), N317 (= N92), D334 (= D107), Y436 (= Y221), Q464 (= Q249), Q468 (= Q253)
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, 92% coverage: 9:264/277 of query aligns to 325:593/603 of Q9SQT8
- S336 (= S20) binding shikimate; mutation to A: 13-fold decrease in substrate affinity but almost no change in activity.
- S338 (= S22) binding shikimate; mutation to A: 10-fold decrease in activity, and 9-fold decrease in substrate affinity.
- T381 (= T67) binding shikimate
- K385 (= K71) 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 (= N92) binding shikimate
- D423 (= D107) binding shikimate; mutation to A: Loss of shikimate dehydrogenase activity.; mutation to N: Reduced shikimate dehydrogenase activity, but no change in substrate affinity.
- A461 (= A132) binding NADP(+)
- G463 (= G134) binding NADP(+)
- A464 (≠ V135) binding NADP(+)
- N483 (≠ D155) binding NADP(+)
- T485 (≠ V157) binding NADP(+)
- R488 (≠ S160) binding NADP(+)
- M525 (= M194) binding NADP(+)
- A548 (≠ I219) binding NADP(+)
- Y550 (= Y221) binding shikimate; mutation Y->F,A: 100-fold decrease in activity, and 2-fold decrease in substrate affinity.
- G571 (= G242) binding NADP(+)
- Q578 (= Q249) binding shikimate
- Q582 (= Q253) 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
Query Sequence
>WP_011736222.1 NCBI__GCF_000015045.1:WP_011736222.1
MNPCSTPSLYGVIGYPLGHSLSPLLHNTAFRELGIPGVLLPWSIEPERLPAFIQSVRLLN
IRGACVTIPHKQSIIPLLDRVTDRVKALGAANTLYWDGDLLCGDNTDILGFMSPLQADPP
SAEQTRVLVLGAGGVARAAVAGLKSLGLNQITITDIVDASSATLAETFDLKTIPWSQRSE
VDAHILINTTPLGMKGKFEEESPYPTEALAARQGIAYDIVYTPFVTRFLREARAAGWKTI
GGLEMFISQADHQFLTWTGRNLPQAAKQAVIDALTAT
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