SitesBLAST
Comparing WP_019868369.1 NCBI__GCF_000384075.1:WP_019868369.1 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)
7colA Crystal structure of 5-ketofructose reductase complexed with NADPH (see paper)
38% identity, 93% coverage: 12:276/286 of query aligns to 7:270/280 of 7colA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G128 (= G134), G130 (= G136), G131 (= G137), A132 (= A138), N152 (≠ T158), R153 (= R159), K157 (≠ Q163), T195 (= T201), S196 (≠ H202), I197 (≠ L203), V222 (= V228), Q252 (≠ L258)
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
34% identity, 95% coverage: 9:280/286 of query aligns to 10:281/287 of 1nvtB
- active site: K75 (= K75), D111 (= D111)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (≠ V72), G135 (= G134), G137 (= G136), G138 (= G137), A139 (= A138), N157 (≠ H153), R158 (≠ L154), T159 (= T155), K162 (≠ R159), A200 (= A200), T201 (= T201), P202 (≠ H202), I203 (≠ L203), M205 (≠ A205), L229 (≠ V228), Y231 (≠ T230), M255 (= M254), L256 (= L255)
- binding zinc ion: E22 (≠ A21), H23 (≠ E22)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
34% identity, 95% coverage: 9:280/286 of query aligns to 10:281/287 of 1nvtA
- active site: K75 (= K75), D111 (= D111)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (= G134), A139 (= A138), N157 (≠ H153), R158 (≠ L154), T159 (= T155), K162 (≠ R159), A200 (= A200), T201 (= T201), P202 (≠ H202), I203 (≠ L203), M205 (≠ A205), L229 (≠ V228), Y231 (≠ T230), G252 (= G251), M255 (= M254), L256 (= L255)
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)
34% identity, 95% coverage: 9:280/286 of query aligns to 5:276/282 of Q58484
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
31% identity, 91% coverage: 9:268/286 of query aligns to 5:252/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (= V72), G130 (= G134), G133 (= G137), A134 (= A138), N153 (= N160), R154 (≠ E161), T155 (= T162), K158 (= K165), T188 (= T201), S189 (≠ H202), V190 (≠ L203), I214 (≠ V228), M238 (= M254), L239 (= L255)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (≠ N23), S21 (≠ I25), N64 (≠ C69), T66 (= T71), K70 (= K75), N91 (= N96), D106 (= D111), Y216 (≠ T230), L239 (= L255), Q242 (≠ L258)
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
31% identity, 91% coverage: 9:268/286 of query aligns to 5:252/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (= V72), G132 (= G136), G133 (= G137), A134 (= A138), N153 (= N160), R154 (≠ E161), T155 (= T162), T188 (= T201), S189 (≠ H202), V190 (≠ L203)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (≠ N23), S21 (≠ I25), N64 (≠ C69), K70 (= K75), N91 (= N96), D106 (= D111), Y216 (≠ T230), L239 (= L255), Q242 (≠ L258)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
30% identity, 91% coverage: 9:268/286 of query aligns to 5:252/269 of O67049
- SLS 19:21 (≠ NPI 23:25) binding shikimate
- D82 (≠ Q87) binding NADP(+)
- N91 (= N96) binding shikimate
- D106 (= D111) binding shikimate
- GAGGA 130:134 (= GAGGA 134:138) binding NADP(+)
- I214 (≠ V228) binding NADP(+)
- Y216 (≠ T230) binding shikimate
- G235 (= G251) binding NADP(+)
- Q242 (≠ L258) binding shikimate
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
28% identity, 76% coverage: 67:284/286 of query aligns to 56:265/269 of Q5HNV1
- T60 (= T71) binding shikimate
- N85 (= N96) binding shikimate
- D100 (= D111) binding shikimate
- Y211 (≠ T230) 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 (≠ L258) binding shikimate
Sites not aligning to the query:
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
27% identity, 76% coverage: 67:284/286 of query aligns to 56:256/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: N58 (≠ C69), T60 (= T71), K64 (= K75), N85 (= N96), D100 (= D111), F227 (≠ L255), Q230 (≠ L258)
Sites not aligning to the query:
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
25% identity, 90% coverage: 11:267/286 of query aligns to 14:277/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G134), A138 (= A135), G139 (= G136), G140 (= G137), A141 (= A138), N161 (≠ T158), R162 (= R159), D164 (≠ E161), F166 (vs. gap), T210 (= T201), G211 (≠ H202), V212 (≠ L203), M214 (≠ A205), F217 (≠ E208), V238 (= V228), Y240 (≠ T230), G261 (= G251), M264 (= M254), M265 (≠ L255)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
25% identity, 90% coverage: 11:267/286 of query aligns to 14:277/291 of Q8Y9N5
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
25% identity, 90% coverage: 11:267/286 of query aligns to 11:274/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (≠ V72), G134 (= G134), A135 (= A135), G136 (= G136), G137 (= G137), A138 (= A138), N158 (≠ T158), R159 (= R159), D161 (≠ E161), F163 (vs. gap), T207 (= T201), V209 (≠ L203), M211 (≠ A205), F214 (≠ E208), V235 (= V228), Y237 (≠ T230), M261 (= M254), M262 (≠ L255)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (≠ N23), S25 (≠ I25), N68 (≠ C69), S70 (≠ T71), K74 (= K75), N95 (= N96), D110 (= D111), Q265 (≠ L258)
2gptA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate (see paper)
28% identity, 96% coverage: 4:277/286 of query aligns to 228:484/498 of 2gptA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: I239 (≠ M15), S247 (vs. gap), S249 (≠ N23), T292 (= T71), K296 (= K75), N317 (= N96), D334 (= D111), Y436 (≠ T230), Q464 (≠ L258), Q468 (≠ I262)
Sites not aligning to the query:
4k28A 2.15 angstrom resolution crystal structure of a shikimate dehydrogenase family protein from pseudomonas putida kt2440 in complex with NAD+ (see paper)
30% identity, 92% coverage: 11:273/286 of query aligns to 5:266/266 of 4k28A
- binding manganese (ii) ion: C153 (≠ I157), C164 (≠ A168), V176 (≠ W184), F180 (≠ V188)
- binding nicotinamide-adenine-dinucleotide: I129 (≠ L133), G130 (= G134), G132 (= G136), G133 (= G137), V134 (≠ A138), C153 (≠ I157), D154 (≠ T158), P155 (≠ R159), R159 (≠ Q163), S193 (≠ T201), P194 (vs. gap), V222 (= V228), G245 (= G251), M248 (= M254), A249 (vs. gap)
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
26% identity, 93% coverage: 11:277/286 of query aligns to 8:282/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (= A135), G133 (= G136), G134 (= G137), A135 (= A138), N155 (≠ T158), R156 (= R159), D158 (≠ E161), F160 (≠ Q163), T204 (= T201), K205 (≠ H202), V206 (≠ L203), M208 (≠ A205), C232 (≠ V228), M258 (= M254), L259 (= L255)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
26% identity, 93% coverage: 11:277/286 of query aligns to 8:282/288 of P0A6D5
- S22 (≠ I25) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (≠ F42) 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 (≠ N110) 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 (= AGGA 135:138) binding NAD(+)
- NRRD 155:158 (≠ TRNE 158:161) binding NAD(+)
- K205 (≠ H202) binding NAD(+)
- CVYN 232:235 (≠ VITN 228:231) binding NAD(+)
- G255 (= G251) binding NAD(+)
- Q262 (≠ L258) 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)
26% identity, 93% coverage: 11:277/286 of query aligns to 2:276/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (= A135), G127 (= G136), G128 (= G137), A129 (= A138), R150 (= R159), F154 (≠ Q163), K199 (≠ H202), V200 (≠ L203), M202 (≠ A205), C226 (≠ V228), Y228 (≠ T230), M252 (= M254), L253 (= L255)
6bmqA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase (t381g mutant) in complex with tartrate and shikimate (see paper)
28% identity, 96% coverage: 4:277/286 of query aligns to 228:484/498 of 6bmqA
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: S247 (vs. gap), S249 (≠ N23), C291 (≠ I70), K296 (= K75), N317 (= N96), D334 (= D111), Y436 (≠ T230), Q464 (≠ L258)
Sites not aligning to the query:
2o7sA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
28% identity, 96% coverage: 4:277/286 of query aligns to 228:486/500 of 2o7sA
- binding 3-dehydroshikimate: I239 (≠ M15), S247 (vs. gap), S249 (≠ N23), T292 (= T71), K296 (= K75), N317 (= N96), D334 (= D111), Y438 (≠ T230), Q466 (≠ L258), Q470 (≠ I262)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I293 (≠ V72), P294 (= P73), K296 (= K75), D334 (= D111), G354 (= G136), G355 (= G137), A356 (= A138), N374 (≠ T158), R375 (= R159), T376 (≠ N160), R379 (≠ Q163), T409 (= T201), S410 (≠ H202), M411 (≠ L203), A436 (≠ V228), M462 (= M254), F463 (≠ L255)
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)
28% identity, 96% coverage: 4:277/286 of query aligns to 317:598/603 of Q9SQT8
- S336 (vs. gap) binding shikimate; mutation to A: 13-fold decrease in substrate affinity but almost no change in activity.
- S338 (≠ N23) binding shikimate; mutation to A: 10-fold decrease in activity, and 9-fold decrease in substrate affinity.
- T381 (= T71) binding shikimate
- K385 (= K75) 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 (= N96) binding shikimate
- D423 (= D111) binding shikimate; mutation to A: Loss of shikimate dehydrogenase activity.; mutation to N: Reduced shikimate dehydrogenase activity, but no change in substrate affinity.
- A461 (= A135) binding NADP(+)
- G463 (= G137) binding NADP(+)
- A464 (= A138) binding NADP(+)
- N483 (= N160) binding NADP(+)
- T485 (= T162) binding NADP(+)
- R488 (≠ K165) binding NADP(+)
- M525 (≠ A205) binding NADP(+)
- A548 (≠ V228) binding NADP(+)
- Y550 (≠ T230) binding shikimate; mutation Y->F,A: 100-fold decrease in activity, and 2-fold decrease in substrate affinity.
- G571 (= G251) binding NADP(+)
- Q578 (≠ L258) binding shikimate
- Q582 (≠ I262) 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_019868369.1 NCBI__GCF_000384075.1:WP_019868369.1
MSTRPFPPQKQMTGMLGHPVAENPIDRMFDAVYAHYGLNWQFWKSDIASTHELMAAIHGA
KALGYAGFCITVPYKVASIPALDAVDQDVQDIGAANYVTIEQGRTIGHNNDGKGVVKAIS
KVSPIAGKRVAMLGAGGAGRAMAAEIARAGAAHLTVITRNETQGKEVAEMVRRVTGIPVA
WLHWEGDVTIPEGTQILLNATHLGAAPELGQVPVDWDSIGASITVVDVITNPRITPFLET
ARNKGCPIANGVEMLVQLAMQIFQAWTGIIPEEAVFQDAVSKALAE
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