SitesBLAST
Comparing WP_005347030.1 NCBI__GCF_000173975.1:WP_005347030.1 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)
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
37% identity, 96% coverage: 7:280/286 of query aligns to 9:288/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (≠ K69), G134 (= G134), A135 (≠ S135), G136 (= G136), G137 (= G137), A138 (= A138), N158 (vs. gap), R159 (vs. gap), D161 (= D158), F163 (= F160), T207 (≠ S200), V209 (≠ I202), M211 (= M204), F214 (≠ H207), V235 (≠ A227), Y237 (= Y229), M261 (= M253), M262 (≠ S254)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (= S21), S25 (≠ A23), N68 (≠ A66), S70 (≠ T68), K74 (= K72), N95 (= N93), D110 (= D109), Q265 (= Q257)
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
37% identity, 96% coverage: 7:280/286 of query aligns to 12:291/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G134), A138 (≠ S135), G139 (= G136), G140 (= G137), A141 (= A138), N161 (vs. gap), R162 (vs. gap), D164 (= D158), F166 (= F160), T210 (≠ S200), G211 (= G201), V212 (≠ I202), M214 (= M204), F217 (≠ H207), V238 (≠ A227), Y240 (= Y229), G261 (= G250), M264 (= M253), M265 (≠ S254)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
37% identity, 96% coverage: 7:280/286 of query aligns to 12:291/291 of Q8Y9N5
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)
36% identity, 99% coverage: 4:285/286 of query aligns to 2:282/282 of Q58484
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
36% identity, 99% coverage: 4:285/286 of query aligns to 7:287/287 of 1nvtB
- active site: K75 (= K72), D111 (= D109)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (≠ K69), G135 (≠ A138), G137 (≠ R140), G138 (≠ A141), A139 (≠ M142), N157 (≠ D158), R158 (≠ V159), T159 (≠ F160), K162 (≠ S163), A200 (= A199), T201 (≠ S200), P202 (≠ G201), I203 (= I202), M205 (= M204), L229 (≠ A227), Y231 (= Y229), M255 (= M253), L256 (≠ S254)
- binding zinc ion: E22 (≠ K19), H23 (≠ Q20)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
36% identity, 99% coverage: 4:285/286 of query aligns to 7:287/287 of 1nvtA
- active site: K75 (= K72), D111 (= D109)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (≠ A138), A139 (≠ M142), N157 (≠ D158), R158 (≠ V159), T159 (≠ F160), K162 (≠ S163), A200 (= A199), T201 (≠ S200), P202 (≠ G201), I203 (= I202), M205 (= M204), L229 (≠ A227), Y231 (= Y229), G252 (= G250), M255 (= M253), L256 (≠ S254)
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
33% identity, 96% coverage: 4:277/286 of query aligns to 1:282/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (≠ S135), G133 (= G136), G134 (= G137), A135 (= A138), N155 (vs. gap), R156 (vs. gap), D158 (= D158), F160 (= F160), T204 (≠ S206), K205 (≠ H207), V206 (≠ I208), M208 (≠ E210), C232 (≠ A227), M258 (= M253), L259 (≠ S254)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
33% identity, 96% coverage: 4:277/286 of query aligns to 1:282/288 of P0A6D5
- M1 (≠ V4) modified: Initiator methionine, Removed
- S22 (≠ A23) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (= Y40) mutation to F: Kinetically unchanged as compared with the wild-type.
- S67 (≠ T68) mutation to A: Reduces activity towards quinate about 6-fold, but has a little effect on shikimate conversion.
- K71 (= K72) 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 (= N93) mutation to A: Alters protein structure. Loss of activity for both substrates.
- T106 (= T108) 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 (= D109) mutation to A: Loss of activity towards quinate. 20000-fold decrease in the affinity for shikimate.
- AGGA 132:135 (≠ SGGA 135:138) binding NAD(+)
- NRRD 155:158 (≠ --TD 157:158) binding NAD(+)
- K205 (≠ H207) binding NAD(+)
- CVYN 232:235 (≠ ACYN 227:230) binding NAD(+)
- G255 (= G250) binding NAD(+)
- Q262 (= Q257) mutation to A: 3-fold reduction in catalytic efficiency for both substrates.
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
33% identity, 94% coverage: 9:277/286 of query aligns to 2:276/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (≠ S135), G127 (= G136), G128 (= G137), A129 (= A138), R150 (vs. gap), F154 (= F160), K199 (≠ H207), V200 (≠ I208), M202 (≠ E210), C226 (≠ A227), Y228 (= Y229), M252 (= M253), L253 (≠ S254)
Q8ZPR4 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
33% identity, 96% coverage: 4:277/286 of query aligns to 1:282/288 of Q8ZPR4
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
31% identity, 98% coverage: 4:282/286 of query aligns to 2:267/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (≠ K69), G132 (= G136), G133 (= G137), A134 (= A138), N153 (≠ D158), R154 (≠ V159), T155 (≠ F160), T188 (≠ S200), S189 (≠ G201), V190 (≠ I202)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S21), S21 (≠ A23), N64 (≠ A66), K70 (= K72), N91 (= N93), D106 (= D109), Y216 (= Y229), L239 (≠ S254), Q242 (= Q257)
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
31% identity, 98% coverage: 4:282/286 of query aligns to 2:267/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (≠ K69), G130 (= G134), G133 (= G137), A134 (= A138), N153 (≠ D158), R154 (≠ V159), T155 (≠ F160), K158 (≠ S163), T188 (≠ S200), S189 (≠ G201), V190 (≠ I202), I214 (≠ A227), M238 (= M253), L239 (≠ S254)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S21), S21 (≠ A23), N64 (≠ A66), T66 (= T68), K70 (= K72), N91 (= N93), D106 (= D109), Y216 (= Y229), L239 (≠ S254), Q242 (= Q257)
7colA Crystal structure of 5-ketofructose reductase complexed with NADPH (see paper)
32% identity, 93% coverage: 17:282/286 of query aligns to 14:277/280 of 7colA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G128 (≠ C132), G130 (= G134), G131 (≠ S135), A132 (≠ G136), N152 (≠ D158), R153 (≠ V159), K157 (≠ S163), T195 (≠ S200), S196 (≠ G201), I197 (= I202), V222 (≠ A227), Q252 (= Q257)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
30% identity, 98% coverage: 4:282/286 of query aligns to 2:267/269 of O67049
- SLS 19:21 (≠ SFA 21:23) binding shikimate
- D82 (≠ P84) binding NADP(+)
- N91 (= N93) binding shikimate
- D106 (= D109) binding shikimate
- GAGGA 130:134 (≠ GSGGA 134:138) binding NADP(+)
- I214 (≠ A227) binding NADP(+)
- Y216 (= Y229) binding shikimate
- G235 (= G250) binding NADP(+)
- Q242 (= Q257) binding shikimate
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
28% identity, 94% coverage: 13:280/286 of query aligns to 5:262/269 of Q5HNV1
- SLS 13:15 (≠ SFA 21:23) binding shikimate
- T60 (= T68) binding shikimate
- N85 (= N93) binding shikimate
- D100 (= D109) binding shikimate
- Y211 (= Y229) 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 (= Q257) binding shikimate
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
28% identity, 94% coverage: 13:280/286 of query aligns to 5:253/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (= S21), S15 (≠ A23), N58 (≠ A66), T60 (= T68), K64 (= K72), N85 (= N93), D100 (= D109), F227 (≠ S254), Q230 (= Q257)
2gptA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate (see paper)
31% identity, 96% coverage: 3:277/286 of query aligns to 229:484/498 of 2gptA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: I239 (≠ L13), S247 (= S21), S249 (≠ A23), T292 (= T68), K296 (= K72), N317 (= N93), D334 (= D109), Y436 (= Y229), Q464 (= Q257), Q468 (= Q261)
Sites not aligning to the query:
2o7sA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
31% identity, 96% coverage: 3:277/286 of query aligns to 229:486/500 of 2o7sA
- binding 3-dehydroshikimate: I239 (≠ L13), S247 (= S21), S249 (≠ A23), T292 (= T68), K296 (= K72), N317 (= N93), D334 (= D109), Y438 (= Y229), Q466 (= Q257), Q470 (= Q261)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I293 (≠ K69), P294 (= P70), K296 (= K72), D334 (= D109), G354 (= G136), G355 (= G137), A356 (= A138), N374 (≠ D158), R375 (≠ V159), T376 (≠ F160), R379 (≠ S163), T409 (≠ S200), S410 (≠ G201), M411 (≠ I202), A436 (= A227), M462 (= M253), F463 (≠ S254)
Sites not aligning to the query:
2o7qA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
28% identity, 96% coverage: 3:277/286 of query aligns to 229:487/501 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)
31% identity, 96% coverage: 3:277/286 of query aligns to 229:484/498 of 6bmqA
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: S247 (= S21), S249 (≠ A23), C291 (≠ V67), K296 (= K72), N317 (= N93), D334 (= D109), Y436 (= Y229), Q464 (= Q257)
Sites not aligning to the query:
Query Sequence
>WP_005347030.1 NCBI__GCF_000173975.1:WP_005347030.1
MAKVDINTKMITLLGDPLKQSFAAQMQNCGYEAAGLNMIYFYTEVNNEHLADVVNGIRYM
NFAGFAVTKPNKVKVLEYLDELDPLCEKMGASNTVVKTPEGKLVGYNTDGIGFIRSMERD
GNVKIDENIYFCIGSGGAGRAMCSALAYYGAKKIYITDVFEESSKSLVEDINKNFAPVAE
FCPAGDFSKVKEATVVLNASGIGMGSHIGENPLPKEFISKDQFYFDACYNPAKTQFLLDA
EEAGATILNGLGMSLYQGAAQIEYWTGQEPPIEAMRQKLLDIISEK
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