SitesBLAST
Comparing WP_012759542.1 NCBI__GCF_000023185.1:WP_012759542.1 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)
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
34% identity, 96% coverage: 11:283/285 of query aligns to 2:266/269 of Q5HNV1
- SLS 13:15 (≠ SRS 22:24) binding shikimate
- T60 (= T71) binding shikimate
- N85 (= N96) binding shikimate
- D100 (= D111) binding shikimate
- Y211 (= Y227) 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 (= Q255) binding shikimate
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
37% identity, 88% coverage: 14:265/285 of query aligns to 11:252/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (≠ I72), G130 (= G136), G133 (= G139), A134 (= A140), N153 (= N160), R154 (= R161), T155 (= T162), K158 (≠ R165), T188 (= T199), S189 (= S200), V190 (≠ L201), I214 (= I225), M238 (= M251), L239 (= L252)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S22), S21 (= S24), N64 (= N69), T66 (= T71), K70 (= K75), N91 (= N96), D106 (= D111), Y216 (= Y227), L239 (= L252), Q242 (= Q255)
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
37% identity, 88% coverage: 14:265/285 of query aligns to 11:252/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (≠ I72), G132 (= G138), G133 (= G139), A134 (= A140), N153 (= N160), R154 (= R161), T155 (= T162), T188 (= T199), S189 (= S200), V190 (≠ L201)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S22), S21 (= S24), N64 (= N69), K70 (= K75), N91 (= N96), D106 (= D111), Y216 (= Y227), L239 (= L252), Q242 (= Q255)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
37% identity, 88% coverage: 14:265/285 of query aligns to 11:252/269 of O67049
- SLS 19:21 (≠ SRS 22:24) binding shikimate
- D82 (≠ A87) binding NADP(+)
- N91 (= N96) binding shikimate
- D106 (= D111) binding shikimate
- GAGGA 130:134 (= GAGGA 136:140) binding NADP(+)
- I214 (= I225) binding NADP(+)
- Y216 (= Y227) binding shikimate
- G235 (= G248) binding NADP(+)
- Q242 (= Q255) binding shikimate
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
33% identity, 95% coverage: 14:283/285 of query aligns to 5:257/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (= S22), S15 (= S24), N58 (= N69), T60 (= T71), K64 (= K75), N85 (= N96), D100 (= D111), F227 (≠ L252), Q230 (= Q255)
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
36% identity, 89% coverage: 14:266/285 of query aligns to 12:273/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (= A137), G133 (= G138), G134 (= G139), A135 (= A140), N155 (= N160), R156 (= R161), D158 (≠ V163), F160 (vs. gap), T204 (= T199), K205 (≠ S200), V206 (≠ L201), M208 (= M203), C232 (≠ I225), M258 (= M251), L259 (= L252)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
36% identity, 89% coverage: 14:266/285 of query aligns to 12:273/288 of P0A6D5
- S22 (= S24) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (= Y41) 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 (= AGGA 137:140) binding NAD(+)
- NRRD 155:158 (≠ NRTV 160:163) binding NAD(+)
- K205 (≠ S200) binding NAD(+)
- CVYN 232:235 (≠ IVYV 225:228) binding NAD(+)
- G255 (= G248) binding NAD(+)
- Q262 (= Q255) 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)
36% identity, 89% coverage: 14:266/285 of query aligns to 6:267/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (= A137), G127 (= G138), G128 (= G139), A129 (= A140), R150 (= R161), F154 (vs. gap), K199 (≠ S200), V200 (≠ L201), M202 (= M203), C226 (≠ I225), Y228 (= Y227), M252 (= M251), L253 (= L252)
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)
32% identity, 93% coverage: 14:278/285 of query aligns to 11:277/282 of Q58484
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
32% identity, 93% coverage: 14:278/285 of query aligns to 16:282/287 of 1nvtB
- active site: K75 (= K75), D111 (= D111)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (= I72), G135 (≠ F135), G137 (≠ A137), G138 (= G138), A139 (≠ G139), N157 (= N160), R158 (= R161), T159 (= T162), K162 (≠ R165), A200 (≠ T198), T201 (= T199), P202 (≠ S200), I203 (≠ L201), M205 (= M203), L229 (≠ I225), Y231 (= Y227), M255 (= M251), L256 (= L252)
- binding zinc ion: E22 (≠ K20), H23 (= H21)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
32% identity, 93% coverage: 14:278/285 of query aligns to 16:282/287 of 1nvtA
- active site: K75 (= K75), D111 (= D111)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (≠ F135), A139 (≠ G139), N157 (= N160), R158 (= R161), T159 (= T162), K162 (≠ R165), A200 (≠ T198), T201 (= T199), P202 (≠ S200), I203 (≠ L201), M205 (= M203), L229 (≠ I225), Y231 (= Y227), G252 (= G248), M255 (= M251), L256 (= L252)
Q9KVT3 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
34% identity, 93% coverage: 14:277/285 of query aligns to 10:270/278 of Q9KVT3
- SKS 18:20 (≠ SRS 22:24) binding shikimate
- N90 (= N96) binding shikimate
- D106 (= D111) binding shikimate
- NRTFAK 154:159 (≠ NRTVER 160:165) binding NADP(+)
- Q248 (= Q255) binding shikimate
3pgjA 2.49 angstrom resolution crystal structure of shikimate 5- dehydrogenase (aroe) from vibrio cholerae o1 biovar eltor str. N16961 in complex with shikimate
34% identity, 93% coverage: 14:277/285 of query aligns to 6:266/272 of 3pgjA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S14 (= S22), S16 (= S24), N59 (= N69), T61 (= T71), K65 (= K75), N86 (= N96), D102 (= D111), Q244 (= Q255)
P15770 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Escherichia coli (strain K12) (see paper)
38% identity, 93% coverage: 14:277/285 of query aligns to 6:266/272 of P15770
Q8ZPR4 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
36% identity, 89% coverage: 14:266/285 of query aligns to 12:273/288 of Q8ZPR4
1nytA Shikimate dehydrogenase aroe complexed with NADP+ (see paper)
38% identity, 93% coverage: 14:277/285 of query aligns to 6:266/271 of 1nytA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K65 (= K75), D102 (= D111), G128 (= G138), G129 (= G139), A130 (= A140), N149 (= N160), R150 (= R161), T151 (= T162), R154 (= R165), T188 (= T199), S189 (= S200), S190 (≠ L201), M213 (≠ I225), G237 (= G248), M240 (= M251), L241 (= L252)
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
34% identity, 89% coverage: 18:271/285 of query aligns to 22:284/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G136), A138 (= A137), G139 (= G138), G140 (= G139), A141 (= A140), N161 (= N160), R162 (= R161), D164 (vs. gap), F166 (vs. gap), T210 (= T199), G211 (≠ S200), V212 (≠ L201), M214 (= M203), F217 (vs. gap), V238 (≠ I225), Y240 (= Y227), G261 (= G248), M264 (= M251), M265 (≠ L252)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
34% identity, 89% coverage: 18:271/285 of query aligns to 22:284/291 of Q8Y9N5
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
34% identity, 89% coverage: 18:271/285 of query aligns to 19:281/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (≠ I72), G134 (= G136), A135 (= A137), G136 (= G138), G137 (= G139), A138 (= A140), N158 (= N160), R159 (= R161), D161 (vs. gap), F163 (vs. gap), T207 (= T199), V209 (≠ L201), M211 (= M203), F214 (vs. gap), V235 (≠ I225), Y237 (= Y227), M261 (= M251), M262 (≠ L252)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (= S22), S25 (= S24), N68 (= N69), S70 (≠ T71), K74 (= K75), N95 (= N96), D110 (= D111), Q265 (= Q255)
2ev9B Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP(h) and shikimate (see paper)
37% identity, 93% coverage: 14:277/285 of query aligns to 6:261/263 of 2ev9B
- active site: K64 (= K75), D100 (= D111)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S14 (= S22), S16 (= S24), N58 (= N69), T60 (= T71), K64 (= K75), N85 (= N96), D100 (= D111), Q235 (= Q255)
Query Sequence
>WP_012759542.1 NCBI__GCF_000023185.1:WP_012759542.1
MGDSRETLGPKAFVTGFPIKHSRSPLIHGYWLKTLGLPGSYRAHEVAPEAFADFIHSLKD
GSSGFTGGNVTIPHKELAFRLADEPDALSRELGAANTLWLEDGALHATNTDGRGFIANLD
ERHPGWDRHGTAVVFGAGGASRAIIQAVRDRGFKEIHVVNRTVERARELADRFGPRVQAH
PAGALAEVMKGAGLFINTTSLGMDGEAAPQLDFSPLAADAVVTDIVYVPLKTPILAQAEE
QGFPIVDGLGMLLHQAVPGFEQWFGRRPIVDAALRALVIADMEAH
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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