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Comparing H281DRAFT_03216 FitnessBrowser__Burk376:H281DRAFT_03216 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)
Q9X5C9 Quinate/shikimate dehydrogenase (NAD(+)); QSDH; EC 1.1.1.-; EC 1.1.1.24 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
50% identity, 93% coverage: 20:297/300 of query aligns to 3:283/283 of Q9X5C9
- S17 (= S34) binding
- SRT 17:19 (≠ SLS 34:36) binding
- T69 (= T86) binding ; binding
- K73 (= K90) active site, Proton acceptor; binding ; binding
- N94 (= N111) binding ; binding
- D110 (= D126) binding ; binding
- GV 137:138 (≠ GA 153:154) binding
- D158 (= D174) binding
- R163 (= R179) binding
- PMGM 203:206 (≠ PTGM 217:220) binding
- A213 (≠ P227) binding
- V228 (≠ I242) binding
- G251 (= G265) binding
- Q258 (= Q272) binding ; binding
3jyqA Quinate dehydrogenase from corynebacterium glutamicum in complex with shikimate and nadh (see paper)
50% identity, 93% coverage: 20:297/300 of query aligns to 2:282/282 of 3jyqA
- binding nicotinamide-adenine-dinucleotide: V132 (≠ L149), G135 (= G152), G136 (= G153), V137 (≠ A154), D157 (= D174), L158 (≠ V175), R162 (= R179), T201 (= T216), P202 (= P217), M205 (= M220), V227 (≠ I242), A254 (= A269)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S16 (= S34), N66 (= N84), T68 (= T86), N93 (= N111), D109 (= D126), Q257 (= Q272)
3jypA Quinate dehydrogenase from corynebacterium glutamicum in complex with quinate and nadh (see paper)
50% identity, 93% coverage: 20:297/300 of query aligns to 2:282/282 of 3jypA
- binding nicotinamide-adenine-dinucleotide: V132 (≠ L149), G135 (= G152), V137 (≠ A154), D157 (= D174), L158 (≠ V175), R162 (= R179), T201 (= T216), P202 (= P217), M205 (= M220), A212 (≠ P227), V227 (≠ I242), Y229 (= Y244), A254 (= A269)
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: S16 (= S34), T18 (≠ S36), N66 (= N84), T68 (= T86), K72 (= K90), N93 (= N111), D109 (= D126), Q257 (= Q272)
3jyoA Quinate dehydrogenase from corynebacterium glutamicum in complex with NAD (see paper)
50% identity, 93% coverage: 20:297/300 of query aligns to 2:282/282 of 3jyoA
- binding nicotinamide-adenine-dinucleotide: V132 (≠ L149), G135 (= G152), V137 (≠ A154), D157 (= D174), L158 (≠ V175), R162 (= R179), T201 (= T216), P202 (= P217), M205 (= M220), V227 (≠ I242), Y229 (= Y244), A254 (= A269)
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
34% identity, 91% coverage: 12:284/300 of query aligns to 4:280/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G150), A138 (= A151), G139 (= G152), G140 (= G153), A141 (= A154), N161 (≠ D174), R162 (≠ V175), D164 (≠ A177), F166 (≠ R179), T210 (= T216), G211 (≠ P217), V212 (≠ T218), M214 (= M220), F217 (≠ L223), V238 (≠ I242), Y240 (= Y244), G261 (= G265), M264 (= M268), M265 (≠ A269)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
34% identity, 91% coverage: 12:284/300 of query aligns to 4:280/291 of Q8Y9N5
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
34% identity, 91% coverage: 12:284/300 of query aligns to 1:277/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (≠ Y87), G134 (= G150), A135 (= A151), G136 (= G152), G137 (= G153), A138 (= A154), N158 (≠ D174), R159 (≠ V175), D161 (≠ A177), F163 (≠ R179), T207 (= T216), V209 (≠ T218), M211 (= M220), F214 (≠ L223), V235 (≠ I242), Y237 (= Y244), M261 (= M268), M262 (≠ A269)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (= S34), S25 (= S36), N68 (= N84), S70 (≠ T86), K74 (= K90), N95 (= N111), D110 (= D126), Q265 (= Q272)
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
33% identity, 88% coverage: 26:288/300 of query aligns to 5:255/269 of Q5HNV1
- SLS 13:15 (= SLS 34:36) binding
- T60 (= T86) binding
- N85 (= N111) binding
- D100 (= D126) binding
- Y211 (= Y244) 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 (= Q272) binding
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
33% identity, 95% coverage: 4:288/300 of query aligns to 2:275/287 of 1nvtB
- active site: K75 (= K90), D111 (= D126)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (≠ Y87), G135 (≠ A151), G137 (= G153), G138 (≠ A154), A139 (≠ G155), N157 (vs. gap), R158 (vs. gap), T159 (≠ L172), K162 (≠ V175), A200 (= A215), T201 (= T216), P202 (= P217), I203 (≠ T218), M205 (= M220), L229 (≠ I242), Y231 (= Y244), M255 (= M268), L256 (≠ A269)
- binding zinc ion: E22 (≠ G32), H23 (≠ G33)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
33% identity, 95% coverage: 4:288/300 of query aligns to 2:275/287 of 1nvtA
- active site: K75 (= K90), D111 (= D126)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (≠ A151), A139 (≠ G155), N157 (vs. gap), R158 (vs. gap), T159 (≠ L172), K162 (≠ V175), A200 (= A215), T201 (= T216), P202 (= P217), I203 (≠ T218), M205 (= M220), L229 (≠ I242), Y231 (= Y244), G252 (= G265), M255 (= M268), L256 (≠ A269)
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, 90% coverage: 18:288/300 of query aligns to 3:270/282 of Q58484
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
32% identity, 88% coverage: 26:288/300 of query aligns to 5:246/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (= S34), S15 (= S36), N58 (= N84), T60 (= T86), K64 (= K90), N85 (= N111), D100 (= D126), F227 (≠ A269), Q230 (= Q272)
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
31% identity, 89% coverage: 18:284/300 of query aligns to 3:254/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (≠ Y87), G130 (= G150), G133 (= G153), A134 (= A154), N153 (≠ A178), R154 (= R179), T155 (≠ A180), K158 (≠ L183), T188 (= T216), S189 (≠ P217), V190 (≠ T218), I214 (= I242), M238 (= M268), L239 (≠ A269)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S34), S21 (= S36), N64 (= N84), T66 (= T86), K70 (= K90), N91 (= N111), D106 (= D126), Y216 (= Y244), L239 (≠ A269), Q242 (= Q272)
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
31% identity, 89% coverage: 18:284/300 of query aligns to 3:254/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (≠ Y87), G132 (= G152), G133 (= G153), A134 (= A154), N153 (≠ A178), R154 (= R179), T155 (≠ A180), T188 (= T216), S189 (≠ P217), V190 (≠ T218)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S34), S21 (= S36), N64 (= N84), K70 (= K90), N91 (= N111), D106 (= D126), Y216 (= Y244), L239 (≠ A269), Q242 (= Q272)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
30% identity, 89% coverage: 18:284/300 of query aligns to 3:254/269 of O67049
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
32% identity, 91% coverage: 18:290/300 of query aligns to 4:280/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (= A151), G133 (= G152), G134 (= G153), A135 (= A154), N155 (vs. gap), R156 (vs. gap), D158 (= D174), F160 (≠ D176), T204 (= T216), K205 (≠ P217), V206 (≠ T218), M208 (= M220), C232 (≠ I242), M258 (= M268), L259 (≠ A269)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
32% identity, 91% coverage: 18:290/300 of query aligns to 4:280/288 of P0A6D5
- S22 (= S36) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (= Y53) mutation to F: Kinetically unchanged as compared with the wild-type.
- S67 (≠ T86) mutation to A: Reduces activity towards quinate about 6-fold, but has a little effect on shikimate conversion.
- K71 (= K90) 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 (= N111) mutation to A: Alters protein structure. Loss of activity for both substrates.
- T106 (= T125) 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 (= D126) mutation to A: Loss of activity towards quinate. 20000-fold decrease in the affinity for shikimate.
- AGGA 132:135 (= AGGA 151:154) binding
- NRRD 155:158 (≠ ---D 174) binding
- K205 (≠ P217) binding
- CVYN 232:235 (≠ IVYF 242:245) binding
- G255 (= G265) binding
- Q262 (= Q272) 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)
32% identity, 89% coverage: 23:290/300 of query aligns to 3:274/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (= A151), G127 (= G152), G128 (= G153), A129 (= A154), R150 (vs. gap), F154 (≠ D176), K199 (≠ P217), V200 (≠ T218), M202 (= M220), C226 (≠ I242), Y228 (= Y244), M252 (= M268), L253 (≠ A269)
2ev9B Crystal structure of shikimate 5-dehydrogenase (aroe) from thermus thermophilus hb8 in complex with NADP(h) and shikimate (see paper)
33% identity, 87% coverage: 26:286/300 of query aligns to 6:249/263 of 2ev9B
- active site: K64 (= K90), D100 (= D126)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S14 (= S34), S16 (= S36), N58 (= N84), T60 (= T86), K64 (= K90), N85 (= N111), D100 (= D126), Q235 (= Q272)
Q5SJF8 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
33% identity, 87% coverage: 26:286/300 of query aligns to 6:249/263 of Q5SJF8
Query Sequence
>H281DRAFT_03216 FitnessBrowser__Burk376:H281DRAFT_03216
MNVPMNEQANAKTSARASANSYLVGLIGSGIGGSLSPAMHEEEGSKLGLHYVYRRIDLEA
LKLDVAALPDLLVAAERMGYNGLNITYPCKQAVIPLLDELSDDARALGAVNTVLFKDGKR
IGHNTDWSGFARAFRRGLPDVALDRVVQLGAGGAGAAVAHAALAMGTQTLTLFDVDAARA
ASLAAELQKRFADRTVTAGTSLGETLAAANGLIHATPTGMAKLPGLPLPAELLHSGLWVA
DIVYFPIRTALLQAAEALGCRTLSGGGMAVYQAVDAMRIFTGLEPDAERVYTHFQSLLER
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