SitesBLAST
Comparing WP_012966712.1 NCBI__GCF_000025505.1:WP_012966712.1 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)
2o7sA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
32% identity, 82% coverage: 22:188/204 of query aligns to 31:215/500 of 2o7sA
Sites not aligning to the query:
- binding 3-dehydroshikimate: 239, 247, 249, 292, 296, 317, 334, 438, 466, 470
- binding nadp nicotinamide-adenine-dinucleotide phosphate: 293, 294, 296, 334, 354, 355, 356, 374, 375, 376, 379, 409, 410, 411, 436, 462, 463
2o7qA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
32% identity, 82% coverage: 22:188/204 of query aligns to 31:215/501 of 2o7qA
Sites not aligning to the query:
6bmqA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase (t381g mutant) in complex with tartrate and shikimate (see paper)
32% identity, 82% coverage: 22:188/204 of query aligns to 31:215/498 of 6bmqA
Sites not aligning to the query:
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: 247, 249, 291, 296, 317, 334, 436, 464
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)
32% identity, 82% coverage: 22:188/204 of query aligns to 120:304/603 of Q9SQT8
- E124 (= E26) binding 3-dehydroshikimate
- R126 (= R28) binding 3-dehydroshikimate
- R155 (= R52) binding 3-dehydroshikimate
- K241 (= K128) binding 3-dehydroshikimate
- R279 (= R165) binding 3-dehydroshikimate
- S300 (≠ V184) binding 3-dehydroshikimate
- Q304 (= Q188) binding 3-dehydroshikimate
Sites not aligning to the query:
- 336 binding shikimate; S→A: 13-fold decrease in substrate affinity but almost no change in activity.
- 338 binding shikimate; S→A: 10-fold decrease in activity, and 9-fold decrease in substrate affinity.
- 381 binding shikimate
- 385 binding shikimate; K→A: Strongly reduced shikimate dehydrogenase activity, but minor change in substrate affinity.; K→N: Strongly reduced shikimate dehydrogenase activity, but no change in substrate affinity.
- 406 binding shikimate
- 423 binding shikimate; D→A: Loss of shikimate dehydrogenase activity.; D→N: Reduced shikimate dehydrogenase activity, but no change in substrate affinity.
- 461 binding NADP(+)
- 463 binding NADP(+)
- 464 binding NADP(+)
- 483 binding NADP(+)
- 485 binding NADP(+)
- 488 binding NADP(+)
- 525 binding NADP(+)
- 548 binding NADP(+)
- 550 binding shikimate; mutation Y->F,A: 100-fold decrease in activity, and 2-fold decrease in substrate affinity.
- 571 binding NADP(+)
- 578 binding shikimate
- 582 binding shikimate
2gptA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate (see paper)
32% identity, 82% coverage: 22:188/204 of query aligns to 31:215/498 of 2gptA
Sites not aligning to the query:
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: 239, 247, 249, 292, 296, 317, 334, 436, 464, 468
O66440 3-dehydroquinate dehydratase; 3-dehydroquinase; Type I DHQase; Type I dehydroquinase; DHQ1; EC 4.2.1.10 from Aquifex aeolicus (strain VF5) (see paper)
31% identity, 87% coverage: 22:199/204 of query aligns to 24:214/219 of O66440
- R61 (= R52) binding 3-dehydroquinate
- H116 (= H104) active site, Proton donor/acceptor
- K142 (= K128) active site, Schiff-base intermediate with substrate
- R180 (= R165) binding 3-dehydroquinate
1l9wA Crystal structure of 3-dehydroquinase from salmonella typhi complexed with reaction product (see paper)
24% identity, 83% coverage: 23:191/204 of query aligns to 43:239/252 of 1l9wA
- active site: E86 (≠ D56), H143 (= H104), K170 (= K128)
- binding 3-amino-4,5-dihydroxy-cyclohex-1-enecarboxylate: E46 (= E26), R48 (= R28), R82 (= R52), H143 (= H104), K170 (= K128), R213 (= R165), F225 (≠ Y177), S232 (≠ V184), A233 (= A185), Q236 (= Q188)
4uioA Structure of the salmonella typhi type i dehydroquinase covalently inhibited by a 3-dehydroquinic acid derivative (see paper)
25% identity, 83% coverage: 23:191/204 of query aligns to 41:237/250 of 4uioA
- active site: E84 (≠ D56), H141 (= H104), K168 (= K128)
- binding (1~{R},3~{R},4~{S},5~{R})-3-methyl-1,3,4,5-tetrakis(oxidanyl)cyclohexane-1-carboxylic acid: E44 (= E26), R46 (= R28), R80 (= R52), H141 (= H104), K168 (= K128), M203 (= M157), R211 (= R165), F223 (≠ Y177), A231 (= A185), Q234 (= Q188)
8b2cAAA 3-dehydroquinate dehydratase (see paper)
25% identity, 83% coverage: 23:191/204 of query aligns to 43:239/252 of 8b2cAAA
- binding (1~{S},2~{R},4~{R},5~{S},6~{S})-2,4,5-trihydroxy-7-oxabicyclo[4.1.0]heptane-2-carboxylic acid: E46 (= E26), R48 (= R28), H143 (= H104), K170 (= K128), M205 (= M157), R213 (= R165), F225 (≠ Y177), A233 (= A185), Q236 (= Q188)
8b2bAAA 3-dehydroquinate dehydratase (see paper)
25% identity, 83% coverage: 23:191/204 of query aligns to 43:239/252 of 8b2bAAA
- binding (4R,5R)-3-amino-4,5-dihydroxy-cyclohexene-1-carboxylic acid: E46 (= E26), R48 (= R28), H143 (= H104), K170 (= K128), R213 (= R165), F225 (≠ Y177), S232 (≠ V184), A233 (= A185), Q236 (= Q188)
6sfeA Crystal structure of dhq1 from salmonella typhi covalently modified by compound 7 (see paper)
25% identity, 83% coverage: 23:191/204 of query aligns to 43:239/252 of 6sfeA
- active site: E86 (≠ D56), H143 (= H104), K170 (= K128)
- binding (1~{S},3~{S},4~{S},5~{R})-3-(aminomethyl)-3,4,5-tris(hydroxyl)cyclohexane-1-carboxylic acid: E46 (= E26), R48 (= R28), R82 (= R52), H143 (= H104), K170 (= K128), R213 (= R165), F225 (≠ Y177), S232 (≠ V184), A233 (= A185), Q236 (= Q188)
6h5jA Crystal structure of dhq1 from salmonella typhi covalently modified by ligand 4
25% identity, 83% coverage: 23:191/204 of query aligns to 43:239/252 of 6h5jA
- active site: E86 (≠ D56), H143 (= H104), K170 (= K128)
- binding (3~{R})-3,4,5-tris(hydroxyl)cyclohexane-1-carboxylic acid: E46 (= E26), R48 (= R28), R82 (= R52), H143 (= H104), K170 (= K128), R213 (= R165), F225 (≠ Y177), S232 (≠ V184), A233 (= A185), Q236 (= Q188)
6h5gA Crystal structure of dhq1 from salmonella typhi covalently modified by ligand 3
25% identity, 83% coverage: 23:191/204 of query aligns to 43:239/252 of 6h5gA
- active site: E86 (≠ D56), H143 (= H104), K170 (= K128)
- binding (1~{R},3~{S},4~{R},5~{R})-3-methyl-4,5-bis(hydroxyl)cyclohexane-1-carboxylic acid: E46 (= E26), R48 (= R28), R82 (= R52), K170 (= K128), M203 (≠ F155), R213 (= R165), F225 (≠ Y177), S232 (≠ V184), A233 (= A185), Q236 (= Q188)
6h5cA Crystal structure of dhq1 from salmonella typhi covalently modified by ligand 1
25% identity, 83% coverage: 23:191/204 of query aligns to 43:239/252 of 6h5cA
- active site: E86 (≠ D56), H143 (= H104), K170 (= K128)
- binding (1~{S},3~{R},4~{S},5~{R})-3-methyl-3,4,5-tris(hydroxyl)cyclohexane-1-carboxylic Acid: E46 (= E26), R48 (= R28), R82 (= R52), H143 (= H104), K170 (= K128), R213 (= R165), F225 (≠ Y177), S232 (≠ V184), A233 (= A185), Q236 (= Q188)
4cnpA Structure of the salmonella typhi type i dehydroquinase inhibited by a 3-epiquinic acid derivative
25% identity, 83% coverage: 23:191/204 of query aligns to 43:239/252 of 4cnpA
- active site: E86 (≠ D56), H143 (= H104), K170 (= K128)
- binding (2s)-2-hydroxy-3-epiquinic acid: E46 (= E26), R48 (= R28), R82 (= R52), K170 (= K128), M203 (≠ F155), R213 (= R165), F225 (≠ Y177), S232 (≠ V184), A233 (= A185), Q236 (= Q188)
4clmB Structure of salmonella typhi type i dehydroquinase irreversibly inhibited with a 1,3,4-trihydroxyciclohexane-1-carboxylic acid derivative (see paper)
25% identity, 83% coverage: 23:191/204 of query aligns to 42:238/251 of 4clmB
- active site: E85 (≠ D56), H142 (= H104), K169 (= K128)
- binding (1~{S},3~{S},4~{R},5~{R})-3-methyl-1,4,5-tris(hydroxyl)cyclohexane-1-carboxylic acid: E45 (= E26), R47 (= R28), R81 (= R52), K169 (= K128), M204 (= M157), R212 (= R165), F224 (≠ Y177), S231 (≠ V184), A232 (= A185), Q235 (= Q188)
P24670 3-dehydroquinate dehydratase; 3-dehydroquinase; Type I DHQase; Type I dehydroquinase; DHQ1; EC 4.2.1.10 from Salmonella typhi (see 3 papers)
25% identity, 83% coverage: 23:191/204 of query aligns to 43:239/252 of P24670
- EWR 46:48 (≠ EFR 26:28) binding 3-dehydroquinate
- R82 (= R52) binding 3-dehydroquinate
- K170 (= K128) active site, Schiff-base intermediate with substrate
- R213 (= R165) binding 3-dehydroquinate
- S232 (≠ V184) binding 3-dehydroquinate
- Q236 (= Q188) binding 3-dehydroquinate
Sites not aligning to the query:
- 21 binding 3-dehydroquinate
1sfjA 2.4a crystal structure of staphylococcus aureus type i 3- dehydroquinase, with 3-dehydroquinate bound (see paper)
24% identity, 92% coverage: 4:191/204 of query aligns to 3:217/227 of 1sfjA
P05194 3-dehydroquinate dehydratase; 3-dehydroquinase; Type I DHQase; Type I dehydroquinase; DHQ1; EC 4.2.1.10 from Escherichia coli (strain K12) (see 3 papers)
24% identity, 83% coverage: 23:191/204 of query aligns to 43:239/252 of P05194
- H143 (= H104) active site, Proton donor/acceptor; mutation to A: Loss of dehydratase activity.
- H146 (≠ S107) mutation to A: It retains full catalytic activity.
- K170 (= K128) active site, Schiff-base intermediate with substrate; mutation to A: Loss of dehydratase activity, but it is still able to bind substrate.
- M205 (= M157) mutation to L: It has little effect on the catalytic efficiency and affinity for 3-dehydroquinate.
Q6GII7 3-dehydroquinate dehydratase; 3-dehydroquinase; Type I DHQase; Type I dehydroquinase; DHQ1; EC 4.2.1.10 from Staphylococcus aureus (strain MRSA252) (see paper)
23% identity, 83% coverage: 23:191/204 of query aligns to 32:228/238 of Q6GII7
- R70 (= R52) binding 3-dehydroquinate
- H133 (= H104) active site, Proton donor/acceptor
- K160 (= K128) active site, Schiff-base intermediate with substrate
- R202 (= R165) binding 3-dehydroquinate
- Q225 (= Q188) binding 3-dehydroquinate
Query Sequence
>WP_012966712.1 NCBI__GCF_000025505.1:WP_012966712.1
MKGKVIATVKNFAEVSKVLRVADGVEFRIDLFRKPPEPKSVRIEKISIVTIRKPEDGGKY
SGDEEERLKLLEKYSKFCDYVDLEYYLADEVFEKMSCKVIESYHNFSETPDYEFLKGIVE
NRRGDIVKIATLGKSKRDVEKIVKLLCDYENVVAFLMGEEFAFTRIFSLFLGSPFIYCGV
GESVAPGQYDVFKAVKILKGLGYR
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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