SitesBLAST
Comparing PP_2406 FitnessBrowser__Putida:PP_2406 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)
52% identity, 99% coverage: 3:281/282 of query aligns to 2:283/283 of Q9X5C9
- S17 (= S18) binding
- SRT 17:19 (= SRT 18:20) binding
- T69 (= T70) binding ; binding
- K73 (= K74) active site, Proton acceptor; binding ; binding
- N94 (= N95) binding ; binding
- D110 (= D110) binding ; binding
- GV 137:138 (≠ GA 137:138) binding
- D158 (≠ E158) binding
- R163 (= R163) binding
- PMGM 203:206 (≠ PVGM 201:204) binding
- A213 (≠ P211) binding
- V228 (≠ I226) binding
- G251 (= G249) binding
- Q258 (= Q256) binding ; binding
3jyqA Quinate dehydrogenase from corynebacterium glutamicum in complex with shikimate and nadh (see paper)
52% identity, 99% coverage: 3:281/282 of query aligns to 1:282/282 of 3jyqA
- binding nicotinamide-adenine-dinucleotide: V132 (≠ M133), G135 (= G136), G136 (= G137), V137 (≠ A138), D157 (≠ E158), L158 (≠ V159), R162 (= R163), T201 (= T200), P202 (= P201), M205 (= M204), V227 (≠ I226), A254 (= A253)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S16 (= S18), N66 (= N68), T68 (= T70), N93 (= N95), D109 (= D110), Q257 (= Q256)
3jypA Quinate dehydrogenase from corynebacterium glutamicum in complex with quinate and nadh (see paper)
52% identity, 99% coverage: 3:281/282 of query aligns to 1:282/282 of 3jypA
- binding nicotinamide-adenine-dinucleotide: V132 (≠ M133), G135 (= G136), V137 (≠ A138), D157 (≠ E158), L158 (≠ V159), R162 (= R163), T201 (= T200), P202 (= P201), M205 (= M204), A212 (≠ P211), V227 (≠ I226), Y229 (= Y228), A254 (= A253)
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: S16 (= S18), T18 (= T20), N66 (= N68), T68 (= T70), K72 (= K74), N93 (= N95), D109 (= D110), Q257 (= Q256)
3jyoA Quinate dehydrogenase from corynebacterium glutamicum in complex with NAD (see paper)
52% identity, 99% coverage: 3:281/282 of query aligns to 1:282/282 of 3jyoA
- binding nicotinamide-adenine-dinucleotide: V132 (≠ M133), G135 (= G136), V137 (≠ A138), D157 (≠ E158), L158 (≠ V159), R162 (= R163), T201 (= T200), P202 (= P201), M205 (= M204), V227 (≠ I226), Y229 (= Y228), A254 (= A253)
2hk9B Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
32% identity, 94% coverage: 1:266/282 of query aligns to 2:252/267 of 2hk9B
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V67 (≠ Y71), G130 (= G134), G133 (= G137), A134 (= A138), N153 (≠ D160), R154 (≠ A161), T155 (= T162), K158 (≠ Q165), T188 (= T200), S189 (≠ P201), V190 (= V202), I214 (= I226), M238 (= M252), L239 (≠ A253)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S18), S21 (≠ T20), N64 (= N68), T66 (= T70), K70 (= K74), N91 (= N95), D106 (= D110), Y216 (= Y228), L239 (≠ A253), Q242 (= Q256)
2hk9A Crystal structure of shikimate dehydrogenase from aquifex aeolicus in complex with shikimate and NADP+ at 2.2 angstrom resolution (see paper)
32% identity, 94% coverage: 1:266/282 of query aligns to 2:252/269 of 2hk9A
- binding 2'-monophosphoadenosine-5'-diphosphate: V67 (≠ Y71), G132 (= G136), G133 (= G137), A134 (= A138), N153 (≠ D160), R154 (≠ A161), T155 (= T162), T188 (= T200), S189 (≠ P201), V190 (= V202)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S19 (= S18), S21 (≠ T20), N64 (= N68), K70 (= K74), N91 (= N95), D106 (= D110), Y216 (= Y228), L239 (≠ A253), Q242 (= Q256)
O67049 Shikimate dehydrogenase (NADP(+)); SD; SDH; EC 1.1.1.25 from Aquifex aeolicus (strain VF5) (see paper)
31% identity, 94% coverage: 1:266/282 of query aligns to 2:252/269 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)
33% identity, 93% coverage: 7:267/282 of query aligns to 9:273/288 of 1npdB
- binding nicotinamide-adenine-dinucleotide: A132 (= A135), G133 (= G136), G134 (= G137), A135 (= A138), N155 (≠ E158), R156 (vs. gap), D158 (vs. gap), F160 (vs. gap), T204 (= T200), K205 (≠ P201), V206 (= V202), M208 (= M204), C232 (≠ I226), M258 (= M252), L259 (≠ A253)
P0A6D5 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Escherichia coli (strain K12) (see 4 papers)
33% identity, 93% coverage: 7:267/282 of query aligns to 9:273/288 of P0A6D5
- S22 (≠ T20) mutation to A: Kinetically unchanged as compared with the wild-type.
- Y39 (= Y37) 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 (= T109) 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 (= D110) mutation to A: Loss of activity towards quinate. 20000-fold decrease in the affinity for shikimate.
- AGGA 132:135 (= AGGA 135:138) binding
- NRRD 155:158 (≠ E--- 158) binding
- K205 (≠ P201) binding
- CVYN 232:235 (≠ IIYF 226:229) binding
- G255 (= G249) binding
- Q262 (= Q256) 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)
33% identity, 93% coverage: 7:267/282 of query aligns to 3:267/280 of 1o9bA
- binding 1,4-dihydronicotinamide adenine dinucleotide: A126 (= A135), G127 (= G136), G128 (= G137), A129 (= A138), R150 (vs. gap), F154 (vs. gap), K199 (≠ P201), V200 (= V202), M202 (= M204), C226 (≠ I226), Y228 (= Y228), M252 (= M252), L253 (≠ A253)
3tnlA 1.45 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with shikimate and NAD.
31% identity, 93% coverage: 7:268/282 of query aligns to 12:277/288 of 3tnlA
- binding nicotinamide-adenine-dinucleotide: M71 (≠ Y71), G134 (= G134), A135 (= A135), G136 (= G136), G137 (= G137), A138 (= A138), N158 (≠ E158), R159 (≠ V159), D161 (vs. gap), F163 (vs. gap), T207 (= T200), V209 (= V202), M211 (= M204), F214 (≠ L207), V235 (≠ I226), Y237 (= Y228), M261 (= M252), M262 (≠ A253)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (= S18), S25 (≠ T20), N68 (= N68), S70 (≠ T70), K74 (= K74), N95 (= N95), D110 (= D110), Q265 (= Q256)
3tozA 2.2 angstrom crystal structure of shikimate 5-dehydrogenase from listeria monocytogenes in complex with NAD.
31% identity, 93% coverage: 7:268/282 of query aligns to 15:280/291 of 3tozA
- binding nicotinamide-adenine-dinucleotide: G137 (= G134), A138 (= A135), G139 (= G136), G140 (= G137), A141 (= A138), N161 (≠ E158), R162 (≠ V159), D164 (vs. gap), F166 (vs. gap), T210 (= T200), G211 (≠ P201), V212 (= V202), M214 (= M204), F217 (≠ L207), V238 (≠ I226), Y240 (= Y228), G261 (= G249), M264 (= M252), M265 (≠ A253)
Q8Y9N5 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
31% identity, 93% coverage: 7:268/282 of query aligns to 15:280/291 of Q8Y9N5
Q5HNV1 Shikimate dehydrogenase (NADP(+)); SDH; EC 1.1.1.25 from Staphylococcus epidermidis (strain ATCC 35984 / RP62A) (see paper)
28% identity, 94% coverage: 10:275/282 of query aligns to 5:258/269 of Q5HNV1
- SLS 13:15 (≠ SRT 18:20) binding
- T60 (= T70) binding
- N85 (= N95) binding
- D100 (= D110) binding
- Y211 (= Y228) 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 (= Q256) binding
1nvtB Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
32% identity, 98% coverage: 1:275/282 of query aligns to 7:278/287 of 1nvtB
- active site: K75 (= K74), D111 (= D110)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I72 (≠ Y71), G135 (= G134), G137 (= G136), G138 (= G137), A139 (= A138), N157 (≠ E158), R158 (≠ V159), T159 (≠ D160), K162 (≠ R163), A200 (≠ T199), T201 (= T200), P202 (= P201), I203 (≠ V202), M205 (= M204), L229 (≠ I226), Y231 (= Y228), M255 (= M252), L256 (≠ A253)
- binding zinc ion: E22 (≠ Q16), H23 (≠ L17)
1nvtA Crystal structure of shikimate dehydrogenase (aroe or mj1084) in complex with NADP+ (see paper)
32% identity, 98% coverage: 1:275/282 of query aligns to 7:278/287 of 1nvtA
- active site: K75 (= K74), D111 (= D110)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G135 (= G134), A139 (= A138), N157 (≠ E158), R158 (≠ V159), T159 (≠ D160), K162 (≠ R163), A200 (≠ T199), T201 (= T200), P202 (= P201), I203 (≠ V202), M205 (= M204), L229 (≠ I226), Y231 (= Y228), G252 (= G249), M255 (= M252), L256 (≠ A253)
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, 98% coverage: 1:275/282 of query aligns to 2:273/282 of Q58484
3dooA Crystal structure of shikimate dehydrogenase from staphylococcus epidermidis complexed with shikimate (see paper)
27% identity, 94% coverage: 10:275/282 of query aligns to 5:249/258 of 3dooA
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S13 (= S18), S15 (≠ T20), N58 (= N68), T60 (= T70), K64 (= K74), N85 (= N95), D100 (= D110), F227 (≠ A253), Q230 (= Q256)
Q8ZPR4 Quinate/shikimate dehydrogenase; NAD-dependent shikimate 5-dehydrogenase; EC 1.1.1.282 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
32% identity, 93% coverage: 7:267/282 of query aligns to 9:273/288 of Q8ZPR4
7colA Crystal structure of 5-ketofructose reductase complexed with NADPH (see paper)
36% identity, 85% coverage: 35:274/282 of query aligns to 28:270/280 of 7colA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G128 (= G134), G130 (= G136), G131 (= G137), A132 (= A138), N152 (≠ E158), R153 (≠ V159), K157 (≠ R163), T195 (= T200), S196 (≠ P201), I197 (≠ V202), V222 (≠ I226), Q252 (= Q256)
Query Sequence
>PP_2406 FitnessBrowser__Putida:PP_2406
MSQQAILAGLIGRGIQLSRTPALHEHEGDAQALRYLYRLIDADQLQLDDSALPGLLEAAQ
HTGFTGLNITYPFKQAILPLLDELSDEARGIGAVNTVVLKDGKRVGHNTDCLGFAEGLRR
GLPDVARRQVVQMGAGGAGSAVAHALLGEGVERLVLFEVDATRAQALVDNLNTHFGAERA
VLGTDLATALAEADGLVNTTPVGMAKLPGTPLPVELLHPRLWVAEIIYFPLETELLRAAR
ALGCRTLDGSNMAVFQAVKAFELFSGRQADAARMQAHFASFT
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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