SitesBLAST
Comparing WP_015738681.1 NCBI__GCF_000024605.1:WP_015738681.1 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)
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
40% identity, 95% coverage: 2:283/297 of query aligns to 8:290/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G131), A138 (= A132), G139 (= G133), G140 (= G134), A141 (= A135), N161 (= N155), R162 (= R156), D164 (≠ F158), F166 (vs. gap), T210 (= T203), G211 (≠ S204), V212 (≠ L205), M214 (= M207), F217 (≠ R210), V238 (≠ L231), Y240 (= Y233), G261 (= G254), M264 (= M257), M265 (≠ L258)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
40% identity, 95% coverage: 2:283/297 of query aligns to 8:290/291 of Q8Y9N5
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
40% identity, 95% coverage: 2:283/297 of query aligns to 5:287/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (≠ V68), G134 (= G131), A135 (= A132), G136 (= G133), G137 (= G134), A138 (= A135), N158 (= N155), R159 (= R156), D161 (≠ F158), F163 (vs. gap), T207 (= T203), V209 (≠ L205), M211 (= M207), F214 (≠ R210), V235 (≠ L231), Y237 (= Y233), M261 (= M257), M262 (≠ L258)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (≠ T20), S25 (= S22), N68 (= N65), S70 (≠ T67), K74 (= K71), N95 (= N92), D110 (= D107), Q265 (= Q261)
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)
43% identity, 96% coverage: 3:287/297 of query aligns to 2:280/282 of Q58484
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
43% identity, 96% coverage: 3:287/297 of query aligns to 7:285/287 of 1nvtB
- active site: K75 (= K71), D111 (= D107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (≠ V68), G135 (= G131), G137 (= G133), G138 (= G134), A139 (= A135), N157 (= N155), R158 (= R156), T159 (= T157), K162 (≠ R160), A200 (≠ T202), T201 (= T203), P202 (≠ S204), I203 (≠ L205), M205 (= M207), L229 (= L231), Y231 (= Y233), M255 (= M257), L256 (= L258)
- binding zinc ion: E22 (≠ A18), H23 (= H19)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
43% identity, 96% coverage: 3:287/297 of query aligns to 7:285/287 of 1nvtA
- active site: K75 (= K71), D111 (= D107)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (= G131), A139 (= A135), N157 (= N155), R158 (= R156), T159 (= T157), K162 (≠ R160), A200 (≠ T202), T201 (= T203), P202 (≠ S204), I203 (≠ L205), M205 (= M207), L229 (= L231), Y231 (= Y233), G252 (= G254), M255 (= M257), L256 (= L258)
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
37% identity, 95% coverage: 1:283/297 of query aligns to 1:284/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (= A132), G133 (= G133), G134 (= G134), A135 (= A135), N155 (= N155), R156 (= R156), D158 (vs. gap), F160 (vs. gap), T204 (= T203), K205 (≠ S204), V206 (≠ L205), M208 (= M207), C232 (≠ L231), M258 (= M257), L259 (= L258)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
37% identity, 95% coverage: 1:283/297 of query aligns to 1:284/288 of P0A6D5
- M1 (= M1) modified: Initiator methionine, Removed
- S22 (= S22) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (= Y39) 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 (= AGGA 132:135) binding
- NRRD 155:158 (≠ NRT- 155:157) binding
- K205 (≠ S204) binding
- CVYN 232:235 (≠ LVYR 231:234) binding
- G255 (= G254) binding
- Q262 (= Q261) mutation to A: 3-fold reduction in catalytic efficiency for both substrates.
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
38% identity, 93% coverage: 8:283/297 of query aligns to 2:278/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (= A132), G127 (= G133), G128 (= G134), A129 (= A135), R150 (= R156), F154 (vs. gap), K199 (≠ S204), V200 (≠ L205), M202 (= M207), C226 (≠ L231), Y228 (= Y233), M252 (= M257), L253 (= L258)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
37% identity, 96% coverage: 3:288/297 of query aligns to 2:269/269 of O67049
2hk9A 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: 3:288/297 of query aligns to 2:269/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (= V68), G132 (= G133), G133 (= G134), A134 (= A135), N153 (= N155), R154 (= R156), T155 (= T157), T188 (= T203), S189 (= S204), V190 (≠ L205)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (≠ T20), S21 (= S22), N64 (= N65), K70 (= K71), N91 (= N92), D106 (= D107), Y216 (= Y233), L239 (= L258), Q242 (= Q261)
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
38% identity, 93% coverage: 3:278/297 of query aligns to 2:259/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (= V68), G130 (= G131), G133 (= G134), A134 (= A135), N153 (= N155), R154 (= R156), T155 (= T157), K158 (≠ R160), T188 (= T203), S189 (= S204), V190 (≠ L205), I214 (≠ L231), M238 (= M257), L239 (= L258)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (≠ T20), S21 (= S22), N64 (= N65), T66 (= T67), K70 (= K71), N91 (= N92), D106 (= D107), Y216 (= Y233), L239 (= L258), Q242 (= Q261)
Q8ZPR4 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
38% identity, 95% coverage: 1:283/297 of query aligns to 1:284/288 of Q8ZPR4
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
33% identity, 93% coverage: 12:287/297 of query aligns to 5:265/269 of Q5HNV1
- SLS 13:15 (≠ TLS 20:22) binding
- T60 (= T67) binding
- N85 (= N92) binding
- D100 (= D107) binding
- Y211 (= Y233) 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 (= Q261) binding
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
33% identity, 93% coverage: 12:287/297 of query aligns to 5:256/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (≠ T20), S15 (= S22), N58 (= N65), T60 (= T67), K64 (= K71), N85 (= N92), D100 (= D107), F227 (≠ L258), Q230 (= Q261)
P15770 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Escherichia coli (strain K12) (see paper)
36% identity, 93% coverage: 12:287/297 of query aligns to 6:270/272 of P15770
1nytA Shikimate dehydrogenase aroe complexed with NADP+ (see paper)
36% identity, 93% coverage: 12:287/297 of query aligns to 6:270/271 of 1nytA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K65 (= K71), D102 (= D107), G128 (= G133), G129 (= G134), A130 (= A135), N149 (= N155), R150 (= R156), T151 (= T157), R154 (= R160), T188 (= T203), S189 (= S204), S190 (≠ L205), M213 (≠ L231), G237 (= G254), M240 (= M257), L241 (= L258)
7colA Crystal structure of 5-ketofructose reductase complexed with NADPH (see paper)
36% identity, 94% coverage: 9:288/297 of query aligns to 7:279/280 of 7colA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G128 (= G131), G130 (= G133), G131 (= G134), A132 (= A135), N152 (= N155), R153 (= R156), K157 (≠ R160), T195 (= T203), S196 (= S204), I197 (≠ L205), V222 (≠ L231), Q252 (= Q261)
2o7qA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
33% identity, 93% coverage: 2:278/297 of query aligns to 229:484/501 of 2o7qA
Sites not aligning to the query:
2ev9B Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP(h) and shikimate (see paper)
43% identity, 94% coverage: 12:289/297 of query aligns to 6:263/263 of 2ev9B
- active site: K64 (= K71), D100 (= D107)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S14 (≠ T20), S16 (= S22), N58 (= N65), T60 (= T67), K64 (= K71), N85 (= N92), D100 (= D107), Q235 (= Q261)
Query Sequence
>WP_015738681.1 NCBI__GCF_000024605.1:WP_015738681.1
MQIDGNTRIVGIFGDPIAHTLSPHMHNAAFRALNLNYIYVPFWVRREELAEATAAIRALN
LAGVNVTVPHKEAIIPYLDELEEEACLIGAVNTVVNQGGKLWGSNTDASGFLAALQEEGF
APAKKKVAVLGAGGAARAVGVALARSQVEEITFFNRTFDRAAELAAYLEERTGVRARALP
WEEMGSFRGIEFLQAADLIVQTTSLGMHPREGEMPPVAEEAFRPGQLVIDLVYRPLKTRF
LSLAQKRGAKTASGLGMLLYQGALAFSLWTGVPAPLEVMRAALEEALGVGQGRGENA
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