SitesBLAST
Comparing WP_012968942.1 NCBI__GCF_000025465.1:WP_012968942.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
8b2cAAA 3-dehydroquinate dehydratase (see paper)
57% identity, 98% coverage: 5:250/251 of query aligns to 4:249/252 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 (= E47), R48 (= R49), H143 (= H144), K170 (= K171), M205 (= M206), R213 (= R214), F225 (= F226), A233 (= A234), Q236 (= Q237)
8b2bAAA 3-dehydroquinate dehydratase (see paper)
57% identity, 98% coverage: 5:250/251 of query aligns to 4:249/252 of 8b2bAAA
- binding (4R,5R)-3-amino-4,5-dihydroxy-cyclohexene-1-carboxylic acid: E46 (= E47), R48 (= R49), H143 (= H144), K170 (= K171), R213 (= R214), F225 (= F226), S232 (= S233), A233 (= A234), Q236 (= Q237)
6sfeA Crystal structure of dhq1 from salmonella typhi covalently modified by compound 7 (see paper)
57% identity, 98% coverage: 5:250/251 of query aligns to 4:249/252 of 6sfeA
- active site: E86 (= E87), H143 (= H144), K170 (= K171)
- binding (1~{S},3~{S},4~{S},5~{R})-3-(aminomethyl)-3,4,5-tris(hydroxyl)cyclohexane-1-carboxylic acid: E46 (= E47), R48 (= R49), R82 (= R83), H143 (= H144), K170 (= K171), R213 (= R214), F225 (= F226), S232 (= S233), A233 (= A234), Q236 (= Q237)
6h5jA Crystal structure of dhq1 from salmonella typhi covalently modified by ligand 4
57% identity, 98% coverage: 5:250/251 of query aligns to 4:249/252 of 6h5jA
- active site: E86 (= E87), H143 (= H144), K170 (= K171)
- binding (3~{R})-3,4,5-tris(hydroxyl)cyclohexane-1-carboxylic acid: E46 (= E47), R48 (= R49), R82 (= R83), H143 (= H144), K170 (= K171), R213 (= R214), F225 (= F226), S232 (= S233), A233 (= A234), Q236 (= Q237)
6h5gA Crystal structure of dhq1 from salmonella typhi covalently modified by ligand 3
57% identity, 98% coverage: 5:250/251 of query aligns to 4:249/252 of 6h5gA
- active site: E86 (= E87), H143 (= H144), K170 (= K171)
- binding (1~{R},3~{S},4~{R},5~{R})-3-methyl-4,5-bis(hydroxyl)cyclohexane-1-carboxylic acid: E46 (= E47), R48 (= R49), R82 (= R83), K170 (= K171), M203 (= M204), R213 (= R214), F225 (= F226), S232 (= S233), A233 (= A234), Q236 (= Q237)
6h5cA Crystal structure of dhq1 from salmonella typhi covalently modified by ligand 1
57% identity, 98% coverage: 5:250/251 of query aligns to 4:249/252 of 6h5cA
- active site: E86 (= E87), H143 (= H144), K170 (= K171)
- binding (1~{S},3~{R},4~{S},5~{R})-3-methyl-3,4,5-tris(hydroxyl)cyclohexane-1-carboxylic Acid: E46 (= E47), R48 (= R49), R82 (= R83), H143 (= H144), K170 (= K171), R213 (= R214), F225 (= F226), S232 (= S233), A233 (= A234), Q236 (= Q237)
4cnpA Structure of the salmonella typhi type i dehydroquinase inhibited by a 3-epiquinic acid derivative
57% identity, 98% coverage: 5:250/251 of query aligns to 4:249/252 of 4cnpA
- active site: E86 (= E87), H143 (= H144), K170 (= K171)
- binding (2s)-2-hydroxy-3-epiquinic acid: E46 (= E47), R48 (= R49), R82 (= R83), K170 (= K171), M203 (= M204), R213 (= R214), F225 (= F226), S232 (= S233), A233 (= A234), Q236 (= Q237)
P24670 3-dehydroquinate dehydratase; 3-dehydroquinase; Type I DHQase; Type I dehydroquinase; DHQ1; EC 4.2.1.10 from Salmonella typhi (see 3 papers)
57% identity, 98% coverage: 5:250/251 of query aligns to 4:249/252 of P24670
- S21 (≠ P22) binding
- EWR 46:48 (= EWR 47:49) binding
- R82 (= R83) binding
- K170 (= K171) active site, Schiff-base intermediate with substrate
- R213 (= R214) binding
- S232 (= S233) binding
- Q236 (= Q237) binding
4clmB Structure of salmonella typhi type i dehydroquinase irreversibly inhibited with a 1,3,4-trihydroxyciclohexane-1-carboxylic acid derivative (see paper)
57% identity, 98% coverage: 5:250/251 of query aligns to 3:248/251 of 4clmB
- active site: E85 (= E87), H142 (= H144), K169 (= K171)
- binding (1~{S},3~{S},4~{R},5~{R})-3-methyl-1,4,5-tris(hydroxyl)cyclohexane-1-carboxylic acid: E45 (= E47), R47 (= R49), R81 (= R83), K169 (= K171), M204 (= M206), R212 (= R214), F224 (= F226), S231 (= S233), A232 (= A234), Q235 (= Q237)
4uioA Structure of the salmonella typhi type i dehydroquinase covalently inhibited by a 3-dehydroquinic acid derivative (see paper)
57% identity, 98% coverage: 5:250/251 of query aligns to 2:247/250 of 4uioA
- active site: E84 (= E87), H141 (= H144), K168 (= K171)
- binding (1~{R},3~{R},4~{S},5~{R})-3-methyl-1,3,4,5-tetrakis(oxidanyl)cyclohexane-1-carboxylic acid: E44 (= E47), R46 (= R49), R80 (= R83), H141 (= H144), K168 (= K171), M203 (= M206), R211 (= R214), F223 (= F226), A231 (= A234), Q234 (= Q237)
1l9wA Crystal structure of 3-dehydroquinase from salmonella typhi complexed with reaction product (see paper)
57% identity, 98% coverage: 5:250/251 of query aligns to 4:249/252 of 1l9wA
- active site: E86 (= E87), H143 (= H144), K170 (= K171)
- binding 3-amino-4,5-dihydroxy-cyclohex-1-enecarboxylate: E46 (= E47), R48 (= R49), R82 (= R83), H143 (= H144), K170 (= K171), R213 (= R214), F225 (= F226), S232 (= S233), A233 (= A234), Q236 (= Q237)
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)
57% identity, 98% coverage: 5:250/251 of query aligns to 4:249/252 of P05194
- H143 (= H144) active site, Proton donor/acceptor; mutation to A: Loss of dehydratase activity.
- H146 (= H147) mutation to A: It retains full catalytic activity.
- K170 (= K171) active site, Schiff-base intermediate with substrate; mutation to A: Loss of dehydratase activity, but it is still able to bind substrate.
- M205 (= M206) mutation to L: It has little effect on the catalytic efficiency and affinity for 3-dehydroquinate.
P58687 3-dehydroquinate dehydratase; 3-dehydroquinase; DHQD; Type I DHQase; Type I dehydroquinase; DHQ1; EC 4.2.1.10 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 4 papers)
56% identity, 98% coverage: 5:250/251 of query aligns to 4:249/252 of P58687
- S21 (≠ P22) binding
- EWR 46:48 (= EWR 47:49) binding
- R82 (= R83) binding
- E86 (= E87) mutation to A: Very strong reduction of the catalytic efficiency and almost the same affinity for 3-dehydroquinate.; mutation to Q: Strong reduction of the catalytic efficiency and slight increase of the affinity for 3-dehydroquinate.
- H143 (= H144) active site, Proton donor/acceptor
- K170 (= K171) active site, Schiff-base intermediate with substrate; mutation to M: Abolishes enzyme activity and 1.5-fold reduction of the affinity for 3-dehydroquinate.
- R213 (= R214) binding
- S232 (= S233) binding ; mutation to A: Reduces enzyme activity 50-fold.
- Q236 (= Q237) binding ; mutation to A: Nearly abolishes enzyme activity.
4gujA 1.50 angstrom crystal structure of the salmonella enterica 3- dehydroquinate dehydratase (arod) in complex with shikimate (see paper)
56% identity, 98% coverage: 5:250/251 of query aligns to 3:248/251 of 4gujA
- active site: E85 (= E87), H142 (= H144), K169 (= K171)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: E45 (= E47), R47 (= R49), R81 (= R83), H142 (= H144), R212 (= R214), F224 (= F226), S231 (= S233), A232 (= A234), Q235 (= Q237)
4guiA 1.78 angstrom crystal structure of the salmonella enterica 3- dehydroquinate dehydratase (arod) in complex with quinate (see paper)
56% identity, 98% coverage: 5:250/251 of query aligns to 3:248/251 of 4guiA
- active site: E85 (= E87), H142 (= H144), K169 (= K171)
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: E45 (= E47), R47 (= R49), R81 (= R83), H142 (= H144), K169 (= K171), M204 (= M206), R212 (= R214), F224 (= F226), A232 (= A234), Q235 (= Q237)
3m7wA Crystal structure of type i 3-dehydroquinate dehydratase (arod) from salmonella typhimurium lt2 in covalent complex with dehydroquinate (see paper)
56% identity, 98% coverage: 5:250/251 of query aligns to 3:248/251 of 3m7wA
- active site: E85 (= E87), H142 (= H144), K169 (= K171)
- binding 1,3,4-trihydroxy-5-oxo-cyclohexanecarboxylic acid: E45 (= E47), R47 (= R49), H142 (= H144), K169 (= K171), M202 (= M204), M204 (= M206), R212 (= R214), F224 (= F226), A232 (= A234), Q235 (= Q237)
4guhB 1.95 angstrom crystal structure of the salmonella enterica 3- dehydroquinate dehydratase (arod) e86a mutant in complex with dehydroshikimate (crystal form #2) (see paper)
55% identity, 98% coverage: 5:250/251 of query aligns to 17:262/265 of 4guhB
- active site: A99 (≠ E87), H156 (= H144), K183 (= K171)
- binding (4S,5R)-4,5-dihydroxy-3-oxocyclohex-1-ene-1-carboxylic acid: E59 (= E47), R61 (= R49), R95 (= R83), K183 (= K171), M216 (= M204), R226 (= R214), F238 (= F226), A246 (= A234), Q249 (= Q237)
Q186A6 3-dehydroquinate dehydratase; 3-dehydroquinase; Type I DHQase; Type I dehydroquinase; DHQ1; EC 4.2.1.10 from Clostridioides difficile (strain 630) (Peptoclostridium difficile) (see paper)
54% identity, 100% coverage: 1:250/251 of query aligns to 1:250/255 of Q186A6
- EWR 47:49 (= EWR 47:49) binding
- R83 (= R83) binding
- H144 (= H144) active site, Proton donor/acceptor
- K171 (= K171) active site, Schiff-base intermediate with substrate
- R214 (= R214) binding
- S233 (= S233) binding
- Q237 (= Q237) binding
4h3dB 1.95 angstrom crystal structure of of type i 3-dehydroquinate dehydratase (arod) from clostridium difficile with covalent modified comenic acid.
54% identity, 100% coverage: 1:250/251 of query aligns to 1:250/254 of 4h3dB
3js3A Crystal structure of type i 3-dehydroquinate dehydratase (arod) from clostridium difficile with covalent reaction intermediate (see paper)
54% identity, 100% coverage: 1:250/251 of query aligns to 1:250/253 of 3js3A
- active site: E87 (= E87), H144 (= H144), K171 (= K171)
- binding 3-amino-4,5-dihydroxy-cyclohex-1-enecarboxylate: E47 (= E47), R49 (= R49), K171 (= K171), M204 (= M204), R214 (= R214), F226 (= F226), S233 (= S233), A234 (= A234)
Query Sequence
>WP_012968942.1 NCBI__GCF_000025465.1:WP_012968942.1
MTNAVTVKNITFQEGETLICVPLIGKTLDEILGNAHGLVDAGADIIEWRVDHFTQVRDMT
QVMAALAEIRGALKALPLLFTFRSKKEGGETEISDEAYFALNREAARSGLVDVIDIELFN
DEAQIRALVDDAHAAGVKVIMSNHDFHKTPAQEDIIYRLRRMQDLGADLPKIAVMPQSPQ
DVLTLLAATLTMKEKYATRPLITMSMGKSGGVSRVTGRLFGSAMTFGTVGQASAPGQIAI
AKLREVMDILS
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