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Comparing BPHYT_RS28720 FitnessBrowser__BFirm:BPHYT_RS28720 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)
4k28A 2.15 angstrom resolution crystal structure of a shikimate dehydrogenase family protein from pseudomonas putida kt2440 in complex with NAD+ (see paper)
35% identity, 92% coverage: 7:262/278 of query aligns to 2:261/266 of 4k28A
- binding manganese (ii) ion: C153 (≠ S158), C164 (≠ A169), V176 (≠ A180), F180 (≠ P184)
- binding nicotinamide-adenine-dinucleotide: I129 (≠ V134), G130 (= G135), G132 (= G137), G133 (= G138), V134 (≠ A139), C153 (≠ S158), D154 (= D159), P155 (≠ V160), R159 (= R164), S193 (≠ T197), P194 (= P198), V222 (≠ I223), G245 (= G246), M248 (= M249), A249 (≠ H250)
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
33% identity, 92% coverage: 5:260/278 of query aligns to 7:266/287 of 1nvtB
- active site: K75 (= K74), D111 (= D111)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (≠ M71), G135 (= G135), G137 (= G137), G138 (= G138), A139 (= A139), N157 (≠ D159), R158 (≠ V160), T159 (≠ D161), K162 (≠ R164), A200 (= A196), T201 (= T197), P202 (= P198), I203 (≠ L199), M205 (= M201), L229 (≠ I223), Y231 (≠ N225), M255 (= M249), L256 (≠ H250)
- binding zinc ion: E22 (≠ T20), H23 (≠ A21)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
33% identity, 92% coverage: 5:260/278 of query aligns to 7:266/287 of 1nvtA
- active site: K75 (= K74), D111 (= D111)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (= G135), A139 (= A139), N157 (≠ D159), R158 (≠ V160), T159 (≠ D161), K162 (≠ R164), A200 (= A196), T201 (= T197), P202 (= P198), I203 (≠ L199), M205 (= M201), L229 (≠ I223), Y231 (≠ N225), G252 (= G246), M255 (= M249), L256 (≠ H250)
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, 92% coverage: 5:260/278 of query aligns to 2:261/282 of Q58484
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
28% identity, 92% coverage: 5:259/278 of query aligns to 2:248/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (≠ M71), G132 (= G137), G133 (= G138), A134 (= A139), N153 (≠ S158), R154 (≠ D159), T155 (≠ V160), T188 (= T197), S189 (≠ P198), V190 (≠ L199)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (≠ A22), S21 (= S24), N64 (≠ L68), K70 (= K74), N91 (= N95), D106 (= D111), Y216 (≠ A227), L239 (≠ H250), Q242 (= Q253)
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
28% identity, 92% coverage: 5:259/278 of query aligns to 2:248/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (≠ M71), G130 (= G135), G133 (= G138), A134 (= A139), N153 (≠ S158), R154 (≠ D159), T155 (≠ V160), K158 (≠ A163), T188 (= T197), S189 (≠ P198), V190 (≠ L199), I214 (= I223), M238 (= M249), L239 (≠ H250)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (≠ A22), S21 (= S24), N64 (≠ L68), T66 (= T70), K70 (= K74), N91 (= N95), D106 (= D111), Y216 (≠ A227), L239 (≠ H250), Q242 (= Q253)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
28% identity, 92% coverage: 5:259/278 of query aligns to 2:248/269 of O67049
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
32% identity, 92% coverage: 5:260/278 of query aligns to 6:272/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (= M71), G134 (= G135), A135 (= A136), G136 (= G137), G137 (= G138), A138 (= A139), N158 (vs. gap), R159 (vs. gap), D161 (= D159), F163 (≠ D161), T207 (= T197), V209 (≠ L199), M211 (= M201), F214 (≠ N204), V235 (≠ I223), Y237 (≠ N225), M261 (= M249), M262 (≠ H250)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (≠ A22), S25 (= S24), N68 (≠ L68), S70 (≠ T70), K74 (= K74), N95 (= N95), D110 (= D111), Q265 (= Q253)
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
32% identity, 92% coverage: 5:260/278 of query aligns to 9:275/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G135), A138 (= A136), G139 (= G137), G140 (= G138), A141 (= A139), N161 (vs. gap), R162 (vs. gap), D164 (= D159), F166 (≠ D161), T210 (= T197), G211 (≠ P198), V212 (≠ L199), M214 (= M201), F217 (≠ N204), V238 (≠ I223), Y240 (≠ N225), G261 (= G246), M264 (= M249), M265 (≠ H250)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
32% identity, 92% coverage: 5:260/278 of query aligns to 9:275/291 of Q8Y9N5
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
29% identity, 89% coverage: 12:258/278 of query aligns to 3:246/269 of Q5HNV1
- SLS 13:15 (≠ AKS 22:24) binding
- T60 (= T70) binding
- N85 (= N95) binding
- D100 (= D111) binding
- Y211 (≠ N225) 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 (≠ R251) binding
1npdB X-ray structure of shikimate dehydrogenase complexed with NAD+ from e.Coli (ydib) northeast structural genomics research consortium (nesg) target er24 (see paper)
31% identity, 88% coverage: 5:249/278 of query aligns to 3:258/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (= A136), G133 (= G137), G134 (= G138), A135 (= A139), N155 (≠ D159), R156 (vs. gap), D158 (= D161), F160 (≠ A163), T204 (= T197), K205 (≠ P198), V206 (≠ L199), M208 (= M201), C232 (≠ I223), M258 (= M249)
Sites not aligning to the query:
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
31% identity, 88% coverage: 5:249/278 of query aligns to 3:258/288 of P0A6D5
- S22 (= S24) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (≠ C41) mutation to F: Kinetically unchanged as compared with the wild-type.
- S67 (≠ T70) mutation to A: Reduces activity towards quinate about 6-fold, but has a little effect on shikimate conversion.
- K71 (= K74) 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 (= N95) mutation to A: Alters protein structure. Loss of activity for both substrates.
- T106 (≠ F110) 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 136:139) binding
- NRRD 155:158 (≠ D-VD 159:161) binding
- K205 (≠ P198) binding
- CVYN 232:235 (≠ IINA 223:226) binding
- G255 (= G246) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 262 Q→A: 3-fold reduction in catalytic efficiency for both substrates.
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
27% identity, 89% coverage: 12:258/278 of query aligns to 3:237/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (≠ A22), S15 (= S24), N58 (≠ L68), T60 (= T70), K64 (= K74), N85 (= N95), D100 (= D111), F227 (vs. gap), Q230 (≠ R251)
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
31% identity, 86% coverage: 10:249/278 of query aligns to 2:252/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (= A136), G127 (= G137), G128 (= G138), A129 (= A139), R150 (vs. gap), F154 (≠ A163), K199 (≠ P198), V200 (≠ L199), M202 (= M201), C226 (≠ I223), Y228 (≠ N225), M252 (= M249)
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)
30% identity, 88% coverage: 9:254/278 of query aligns to 323:579/603 of Q9SQT8
- S336 (≠ A22) binding ; mutation to A: 13-fold decrease in substrate affinity but almost no change in activity.
- S338 (= S24) binding ; mutation to A: 10-fold decrease in activity, and 9-fold decrease in substrate affinity.
- T381 (= T70) binding
- K385 (= K74) binding ; 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 (= N95) binding
- D423 (= D111) binding ; mutation to A: Loss of shikimate dehydrogenase activity.; mutation to N: Reduced shikimate dehydrogenase activity, but no change in substrate affinity.
- A461 (= A136) binding
- G463 (= G138) binding
- A464 (= A139) binding
- N483 (≠ D159) binding
- T485 (≠ D161) binding
- R488 (= R164) binding
- M525 (= M201) binding
- A548 (≠ I223) binding
- Y550 (≠ N225) binding ; mutation Y->F,A: 100-fold decrease in activity, and 2-fold decrease in substrate affinity.
- G571 (= G246) binding
- Q578 (= Q253) binding
Sites not aligning to the query:
- 124 binding
- 126 binding
- 155 binding
- 241 binding
- 279 binding
- 300 binding
- 304 binding
- 582 binding
2o7sA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
31% identity, 88% coverage: 9:254/278 of query aligns to 234:467/500 of 2o7sA
- binding 3-dehydroshikimate: I239 (≠ L14), S247 (≠ A22), S249 (= S24), T292 (= T70), K296 (= K74), N317 (= N95), D334 (= D111), Y438 (≠ N225), Q466 (= Q253)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I293 (≠ M71), P294 (= P72), K296 (= K74), D334 (= D111), G354 (= G137), G355 (= G138), A356 (= A139), N374 (≠ D159), R375 (≠ V160), T376 (≠ D161), R379 (= R164), T409 (= T197), S410 (≠ P198), M411 (≠ L199), A436 (≠ I223), M462 (= M249), F463 (≠ H250)
Sites not aligning to the query:
3jyqA Quinate dehydrogenase from corynebacterium glutamicum in complex with shikimate and nadh (see paper)
32% identity, 91% coverage: 11:264/278 of query aligns to 5:269/282 of 3jyqA
- binding nicotinamide-adenine-dinucleotide: V132 (= V134), G135 (= G137), G136 (= G138), V137 (≠ A139), D157 (= D159), L158 (≠ V160), R162 (= R164), T201 (= T197), P202 (= P198), M205 (= M201), V227 (≠ I223), A254 (≠ H250)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S16 (≠ A22), N66 (≠ L68), T68 (= T70), N93 (= N95), D109 (= D111), Q257 (= Q253)
3jypA Quinate dehydrogenase from corynebacterium glutamicum in complex with quinate and nadh (see paper)
32% identity, 91% coverage: 11:264/278 of query aligns to 5:269/282 of 3jypA
- binding nicotinamide-adenine-dinucleotide: V132 (= V134), G135 (= G137), V137 (≠ A139), D157 (= D159), L158 (≠ V160), R162 (= R164), T201 (= T197), P202 (= P198), M205 (= M201), A212 (≠ P208), V227 (≠ I223), Y229 (≠ N225), A254 (≠ H250)
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: S16 (≠ A22), T18 (≠ S24), N66 (≠ L68), T68 (= T70), K72 (= K74), N93 (= N95), D109 (= D111), Q257 (= Q253)
3jyoA Quinate dehydrogenase from corynebacterium glutamicum in complex with NAD (see paper)
32% identity, 91% coverage: 11:264/278 of query aligns to 5:269/282 of 3jyoA
- binding nicotinamide-adenine-dinucleotide: V132 (= V134), G135 (= G137), V137 (≠ A139), D157 (= D159), L158 (≠ V160), R162 (= R164), T201 (= T197), P202 (= P198), M205 (= M201), V227 (≠ I223), Y229 (≠ N225), A254 (≠ H250)
Query Sequence
>BPHYT_RS28720 FitnessBrowser__BFirm:BPHYT_RS28720
MDPHITGTTRLYGLVGDPLTAAKSPQLLNQLFTEQRVDAVCVPFWVNAANLPAFVSGARA
MGNLSGMLVTMPHKQRMLALVDELDPTARQVGALNVIRCEPDGRWIGAIFDGVGCVLGMQ
WEGNHPANKSVLLVGAGGAGSAIAFAVAAAGASNLTISDVDEARAGGLAASVAAETGCDA
RSGPPDPQGFEIVINATPLGMKANDAMPVDPERLAHGAIVVDIINAAEPTPLRRAAQARG
CRTQDGGPMHRGQAVYALRFLGFDYRPDGRSTPDDGPR
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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