SitesBLAST
Comparing Ac3H11_1226 FitnessBrowser__acidovorax_3H11:Ac3H11_1226 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)
47% identity, 90% coverage: 25:298/303 of query aligns to 5:283/283 of Q9X5C9
- S17 (= S37) binding
- SRT 17:19 (≠ SLS 37:39) binding
- T69 (= T89) binding ; binding
- K73 (= K93) active site, Proton acceptor; binding ; binding
- N94 (= N114) binding ; binding
- D110 (= D129) binding ; binding
- GV 137:138 (≠ GA 156:157) binding
- D158 (= D177) binding
- R163 (= R182) binding
- PMGM 203:206 (≠ PTGM 218:221) binding
- A213 (≠ P228) binding
- V228 (= V243) binding
- G251 (= G266) binding
- Q258 (= Q273) binding ; binding
3jyqA Quinate dehydrogenase from corynebacterium glutamicum in complex with shikimate and nadh (see paper)
47% identity, 90% coverage: 25:298/303 of query aligns to 4:282/282 of 3jyqA
- binding nicotinamide-adenine-dinucleotide: V132 (≠ L152), G135 (= G155), G136 (= G156), V137 (≠ A157), D157 (= D177), L158 (≠ A178), R162 (= R182), T201 (= T217), P202 (= P218), M205 (= M221), V227 (= V243), A254 (= A270)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S16 (= S37), N66 (= N87), T68 (= T89), N93 (= N114), D109 (= D129), Q257 (= Q273)
3jypA Quinate dehydrogenase from corynebacterium glutamicum in complex with quinate and nadh (see paper)
47% identity, 90% coverage: 25:298/303 of query aligns to 4:282/282 of 3jypA
- binding nicotinamide-adenine-dinucleotide: V132 (≠ L152), G135 (= G155), V137 (≠ A157), D157 (= D177), L158 (≠ A178), R162 (= R182), T201 (= T217), P202 (= P218), M205 (= M221), A212 (≠ P228), V227 (= V243), Y229 (= Y245), A254 (= A270)
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: S16 (= S37), T18 (≠ S39), N66 (= N87), T68 (= T89), K72 (= K93), N93 (= N114), D109 (= D129), Q257 (= Q273)
3jyoA Quinate dehydrogenase from corynebacterium glutamicum in complex with NAD (see paper)
47% identity, 90% coverage: 25:298/303 of query aligns to 4:282/282 of 3jyoA
- binding nicotinamide-adenine-dinucleotide: V132 (≠ L152), G135 (= G155), V137 (≠ A157), D157 (= D177), L158 (≠ A178), R162 (= R182), T201 (= T217), P202 (= P218), M205 (= M221), V227 (= V243), Y229 (= Y245), A254 (= A270)
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
29% identity, 87% coverage: 29:291/303 of query aligns to 5:257/269 of Q5HNV1
- SLS 13:15 (= SLS 37:39) binding
- T60 (= T89) binding
- N85 (= N114) binding
- D100 (= D129) binding
- Y211 (= Y245) 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 (= Q273) binding
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
29% identity, 87% coverage: 29:291/303 of query aligns to 5:248/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (= S37), S15 (= S39), N58 (= N87), T60 (= T89), K64 (= K93), N85 (= N114), D100 (= D129), F227 (≠ A270), Q230 (= Q273)
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
33% identity, 85% coverage: 26:282/303 of query aligns to 15:277/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G153), A138 (= A154), G139 (= G155), G140 (= G156), A141 (= A157), N161 (≠ D177), R162 (≠ A178), D164 (≠ P180), F166 (vs. gap), T210 (= T217), G211 (≠ P218), V212 (≠ T219), M214 (= M221), F217 (≠ L224), V238 (= V243), Y240 (= Y245), G261 (= G266), M264 (= M269), M265 (≠ A270)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
33% identity, 85% coverage: 26:282/303 of query aligns to 15:277/291 of Q8Y9N5
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
33% identity, 85% coverage: 26:282/303 of query aligns to 12:274/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (≠ Y90), G134 (= G153), A135 (= A154), G136 (= G155), G137 (= G156), A138 (= A157), N158 (≠ D177), R159 (≠ A178), D161 (≠ P180), F163 (vs. gap), T207 (= T217), V209 (≠ T219), M211 (= M221), F214 (≠ L224), V235 (= V243), Y237 (= Y245), M261 (= M269), M262 (≠ A270)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (= S37), S25 (= S39), N68 (= N87), S70 (≠ T89), K74 (= K93), N95 (= N114), D110 (= D129), Q265 (= Q273)
7colA Crystal structure of 5-ketofructose reductase complexed with NADPH (see paper)
37% identity, 83% coverage: 39:291/303 of query aligns to 18:270/280 of 7colA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G128 (= G153), G130 (= G155), G131 (= G156), A132 (= A157), N152 (≠ D177), R153 (≠ A178), K157 (≠ R182), T195 (= T217), S196 (≠ P218), I197 (≠ T219), V222 (= V243), Q252 (= Q273)
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
29% identity, 90% coverage: 18:291/303 of query aligns to 5:277/287 of 1nvtB
- active site: K75 (= K93), D111 (= D129)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (≠ Y90), G135 (= G153), G137 (= G155), G138 (= G156), A139 (= A157), N157 (≠ D177), R158 (≠ A178), T159 (≠ Q179), K162 (≠ R182), A200 (= A216), T201 (= T217), P202 (= P218), I203 (≠ T219), M205 (= M221), L229 (≠ V243), Y231 (= Y245), M255 (= M269), L256 (≠ A270)
- binding zinc ion: E22 (≠ Q35), H23 (≠ K36)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
29% identity, 90% coverage: 18:291/303 of query aligns to 5:277/287 of 1nvtA
- active site: K75 (= K93), D111 (= D129)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (= G153), A139 (= A157), N157 (≠ D177), R158 (≠ A178), T159 (≠ Q179), K162 (≠ R182), A200 (= A216), T201 (= T217), P202 (= P218), I203 (≠ T219), M205 (= M221), L229 (≠ V243), Y231 (= Y245), G252 (= G266), M255 (= M269), L256 (≠ A270)
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, 85% coverage: 26:284/303 of query aligns to 9:273/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (= A154), G133 (= G155), G134 (= G156), A135 (= A157), N155 (≠ D177), R156 (≠ A178), D158 (≠ P180), F160 (vs. gap), T204 (= T217), K205 (≠ P218), V206 (≠ T219), M208 (= M221), C232 (≠ V243), M258 (= M269), L259 (≠ A270)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
32% identity, 85% coverage: 26:284/303 of query aligns to 9:273/288 of P0A6D5
- S22 (= S39) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (= Y56) mutation to F: Kinetically unchanged as compared with the wild-type.
- S67 (≠ T89) mutation to A: Reduces activity towards quinate about 6-fold, but has a little effect on shikimate conversion.
- K71 (= K93) 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 (= N114) mutation to A: Alters protein structure. Loss of activity for both substrates.
- T106 (= T128) 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 (= D129) mutation to A: Loss of activity towards quinate. 20000-fold decrease in the affinity for shikimate.
- AGGA 132:135 (= AGGA 154:157) binding
- NRRD 155:158 (≠ DAQP 177:180) binding
- K205 (≠ P218) binding
- CVYN 232:235 (≠ VVYF 243:246) binding
- G255 (= G266) binding
- Q262 (= Q273) mutation to A: 3-fold reduction in catalytic efficiency for both substrates.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
30% identity, 88% coverage: 26:291/303 of query aligns to 8:272/282 of Q58484
1o9bA Quinate/shikimate dehydrogenase ydib complexed with nadh (see paper)
32% identity, 85% coverage: 26:284/303 of query aligns to 3:267/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (= A154), G127 (= G155), G128 (= G156), A129 (= A157), R150 (≠ A178), F154 (vs. gap), K199 (≠ P218), V200 (≠ T219), M202 (= M221), C226 (≠ V243), Y228 (= Y245), M252 (= M269), L253 (≠ A270)
Q8ZPR4 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
35% identity, 86% coverage: 26:285/303 of query aligns to 9:274/288 of Q8ZPR4
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
28% identity, 86% coverage: 26:286/303 of query aligns to 8:256/269 of O67049
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
28% identity, 86% coverage: 26:286/303 of query aligns to 8:256/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (≠ Y90), G130 (= G153), G133 (= G156), A134 (= A157), N153 (≠ D177), R154 (≠ A178), T155 (≠ Q179), K158 (≠ R182), T188 (= T217), S189 (≠ P218), V190 (≠ T219), I214 (≠ V243), M238 (= M269), L239 (≠ A270)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S37), S21 (= S39), N64 (= N87), T66 (= T89), K70 (= K93), N91 (= N114), D106 (= D129), Y216 (= Y245), L239 (≠ A270), Q242 (= Q273)
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
28% identity, 86% coverage: 26:286/303 of query aligns to 8:256/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (≠ Y90), G132 (= G155), G133 (= G156), A134 (= A157), N153 (≠ D177), R154 (≠ A178), T155 (≠ Q179), T188 (= T217), S189 (≠ P218), V190 (≠ T219)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S37), S21 (= S39), N64 (= N87), K70 (= K93), N91 (= N114), D106 (= D129), Y216 (= Y245), L239 (≠ A270), Q242 (= Q273)
Query Sequence
>Ac3H11_1226 FitnessBrowser__acidovorax_3H11:Ac3H11_1226
MSPQLLDPPVIPTTSTMSSTSPRKVLIGLIGAGIQKSLSPALHEEEARHHGMRLHYQLID
LDRSASSVEHLPTLLSAARIMGYAGCNVTYPCKQAVIPHLDSLSEEARAMGAVNTVVIRD
GQLVGHNTDGSGWAWGFTRALPGADLGRVVLLGAGGAGAAIAHAVLRLGAQHLSIVDAQP
ERAAQLAADVNALYGARAEAGEIRSAMANATGLIHATPTGMDKLPGLPLDVGLLRPAMWV
SEVVYFPLDTALVQAARALGCKVSDGGGMAVGQAVGAFELFTGEAPDATRMDAHFRRLVS
CAR
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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