SitesBLAST
Comparing WP_057508481.1 NCBI__GCF_001431535.1:WP_057508481.1 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)
3js3A Crystal structure of type i 3-dehydroquinate dehydratase (arod) from clostridium difficile with covalent reaction intermediate (see paper)
42% identity, 89% coverage: 28:278/283 of query aligns to 3:253/253 of 3js3A
- active site: E87 (= E113), H144 (= H170), K171 (= K197)
- binding 3-amino-4,5-dihydroxy-cyclohex-1-enecarboxylate: E47 (= E73), R49 (= R75), K171 (= K197), M204 (= M229), R214 (= R239), F226 (= F251), S233 (= S258), A234 (= A259)
4h3dB 1.95 angstrom crystal structure of of type i 3-dehydroquinate dehydratase (arod) from clostridium difficile with covalent modified comenic acid.
42% identity, 89% coverage: 28:278/283 of query aligns to 3:253/254 of 4h3dB
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)
42% identity, 89% coverage: 28:278/283 of query aligns to 3:253/255 of Q186A6
- EWR 47:49 (= EWR 73:75) binding
- R83 (= R109) binding
- H144 (= H170) active site, Proton donor/acceptor
- K171 (= K197) active site, Schiff-base intermediate with substrate
- R214 (= R239) binding
- S233 (= S258) binding
- Q237 (= Q262) binding
1l9wA Crystal structure of 3-dehydroquinase from salmonella typhi complexed with reaction product (see paper)
44% identity, 88% coverage: 27:276/283 of query aligns to 1:250/252 of 1l9wA
- active site: E86 (= E113), H143 (= H170), K170 (= K197)
- binding 3-amino-4,5-dihydroxy-cyclohex-1-enecarboxylate: E46 (= E73), R48 (= R75), R82 (= R109), H143 (= H170), K170 (= K197), R213 (= R239), F225 (= F251), S232 (= S258), A233 (= A259), Q236 (= Q262)
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)
43% identity, 88% coverage: 27:276/283 of query aligns to 1:250/252 of P05194
- H143 (= H170) active site, Proton donor/acceptor; mutation to A: Loss of dehydratase activity.
- H146 (= H173) mutation to A: It retains full catalytic activity.
- K170 (= K197) active site, Schiff-base intermediate with substrate; mutation to A: Loss of dehydratase activity, but it is still able to bind substrate.
- M205 (= M231) mutation to L: It has little effect on the catalytic efficiency and affinity for 3-dehydroquinate.
8b2cAAA 3-dehydroquinate dehydratase (see paper)
44% identity, 88% coverage: 27:276/283 of query aligns to 1:250/252 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 (= E73), R48 (= R75), H143 (= H170), K170 (= K197), M205 (= M231), R213 (= R239), F225 (= F251), A233 (= A259), Q236 (= Q262)
8b2bAAA 3-dehydroquinate dehydratase (see paper)
44% identity, 88% coverage: 27:276/283 of query aligns to 1:250/252 of 8b2bAAA
- binding (4R,5R)-3-amino-4,5-dihydroxy-cyclohexene-1-carboxylic acid: E46 (= E73), R48 (= R75), H143 (= H170), K170 (= K197), R213 (= R239), F225 (= F251), S232 (= S258), A233 (= A259), Q236 (= Q262)
6sfeA Crystal structure of dhq1 from salmonella typhi covalently modified by compound 7 (see paper)
44% identity, 88% coverage: 27:276/283 of query aligns to 1:250/252 of 6sfeA
- active site: E86 (= E113), H143 (= H170), K170 (= K197)
- binding (1~{S},3~{S},4~{S},5~{R})-3-(aminomethyl)-3,4,5-tris(hydroxyl)cyclohexane-1-carboxylic acid: E46 (= E73), R48 (= R75), R82 (= R109), H143 (= H170), K170 (= K197), R213 (= R239), F225 (= F251), S232 (= S258), A233 (= A259), Q236 (= Q262)
6h5jA Crystal structure of dhq1 from salmonella typhi covalently modified by ligand 4
44% identity, 88% coverage: 27:276/283 of query aligns to 1:250/252 of 6h5jA
- active site: E86 (= E113), H143 (= H170), K170 (= K197)
- binding (3~{R})-3,4,5-tris(hydroxyl)cyclohexane-1-carboxylic acid: E46 (= E73), R48 (= R75), R82 (= R109), H143 (= H170), K170 (= K197), R213 (= R239), F225 (= F251), S232 (= S258), A233 (= A259), Q236 (= Q262)
6h5gA Crystal structure of dhq1 from salmonella typhi covalently modified by ligand 3
44% identity, 88% coverage: 27:276/283 of query aligns to 1:250/252 of 6h5gA
- active site: E86 (= E113), H143 (= H170), K170 (= K197)
- binding (1~{R},3~{S},4~{R},5~{R})-3-methyl-4,5-bis(hydroxyl)cyclohexane-1-carboxylic acid: E46 (= E73), R48 (= R75), R82 (= R109), K170 (= K197), M203 (= M229), R213 (= R239), F225 (= F251), S232 (= S258), A233 (= A259), Q236 (= Q262)
6h5cA Crystal structure of dhq1 from salmonella typhi covalently modified by ligand 1
44% identity, 88% coverage: 27:276/283 of query aligns to 1:250/252 of 6h5cA
- active site: E86 (= E113), H143 (= H170), K170 (= K197)
- binding (1~{S},3~{R},4~{S},5~{R})-3-methyl-3,4,5-tris(hydroxyl)cyclohexane-1-carboxylic Acid: E46 (= E73), R48 (= R75), R82 (= R109), H143 (= H170), K170 (= K197), R213 (= R239), F225 (= F251), S232 (= S258), A233 (= A259), Q236 (= Q262)
4cnpA Structure of the salmonella typhi type i dehydroquinase inhibited by a 3-epiquinic acid derivative
44% identity, 88% coverage: 27:276/283 of query aligns to 1:250/252 of 4cnpA
- active site: E86 (= E113), H143 (= H170), K170 (= K197)
- binding (2s)-2-hydroxy-3-epiquinic acid: E46 (= E73), R48 (= R75), R82 (= R109), K170 (= K197), M203 (= M229), R213 (= R239), F225 (= F251), S232 (= S258), A233 (= A259), Q236 (= Q262)
P24670 3-dehydroquinate dehydratase; 3-dehydroquinase; Type I DHQase; Type I dehydroquinase; DHQ1; EC 4.2.1.10 from Salmonella typhi (see 3 papers)
44% identity, 88% coverage: 27:276/283 of query aligns to 1:250/252 of P24670
- S21 (≠ P47) binding
- EWR 46:48 (= EWR 73:75) binding
- R82 (= R109) binding
- K170 (= K197) active site, Schiff-base intermediate with substrate
- R213 (= R239) binding
- S232 (= S258) binding
- Q236 (= Q262) binding
4clmB Structure of salmonella typhi type i dehydroquinase irreversibly inhibited with a 1,3,4-trihydroxyciclohexane-1-carboxylic acid derivative (see paper)
44% identity, 88% coverage: 28:276/283 of query aligns to 1:249/251 of 4clmB
- active site: E85 (= E113), H142 (= H170), K169 (= K197)
- binding (1~{S},3~{S},4~{R},5~{R})-3-methyl-1,4,5-tris(hydroxyl)cyclohexane-1-carboxylic acid: E45 (= E73), R47 (= R75), R81 (= R109), K169 (= K197), M204 (= M231), R212 (= R239), F224 (= F251), S231 (= S258), A232 (= A259), Q235 (= Q262)
4uioA Structure of the salmonella typhi type i dehydroquinase covalently inhibited by a 3-dehydroquinic acid derivative (see paper)
45% identity, 87% coverage: 32:276/283 of query aligns to 4:248/250 of 4uioA
- active site: E84 (= E113), H141 (= H170), K168 (= K197)
- binding (1~{R},3~{R},4~{S},5~{R})-3-methyl-1,3,4,5-tetrakis(oxidanyl)cyclohexane-1-carboxylic acid: E44 (= E73), R46 (= R75), R80 (= R109), H141 (= H170), K168 (= K197), M203 (= M231), R211 (= R239), F223 (= F251), A231 (= A259), Q234 (= Q262)
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)
41% identity, 88% coverage: 27:276/283 of query aligns to 1:250/252 of P58687
- S21 (≠ P47) binding
- EWR 46:48 (= EWR 73:75) binding
- R82 (= R109) binding
- E86 (= E113) 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 (= H170) active site, Proton donor/acceptor
- K170 (= K197) 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 (= R239) binding
- S232 (= S258) binding ; mutation to A: Reduces enzyme activity 50-fold.
- Q236 (= Q262) 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)
42% identity, 88% coverage: 28:276/283 of query aligns to 1:249/251 of 4gujA
- active site: E85 (= E113), H142 (= H170), K169 (= K197)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: E45 (= E73), R47 (= R75), R81 (= R109), H142 (= H170), R212 (= R239), F224 (= F251), S231 (= S258), A232 (= A259), Q235 (= Q262)
4guiA 1.78 angstrom crystal structure of the salmonella enterica 3- dehydroquinate dehydratase (arod) in complex with quinate (see paper)
42% identity, 88% coverage: 28:276/283 of query aligns to 1:249/251 of 4guiA
- active site: E85 (= E113), H142 (= H170), K169 (= K197)
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: E45 (= E73), R47 (= R75), R81 (= R109), H142 (= H170), K169 (= K197), M204 (= M231), R212 (= R239), F224 (= F251), A232 (= A259), Q235 (= Q262)
3m7wA Crystal structure of type i 3-dehydroquinate dehydratase (arod) from salmonella typhimurium lt2 in covalent complex with dehydroquinate (see paper)
42% identity, 88% coverage: 28:276/283 of query aligns to 1:249/251 of 3m7wA
- active site: E85 (= E113), H142 (= H170), K169 (= K197)
- binding 1,3,4-trihydroxy-5-oxo-cyclohexanecarboxylic acid: E45 (= E73), R47 (= R75), H142 (= H170), K169 (= K197), M202 (= M229), M204 (= M231), R212 (= R239), F224 (= F251), A232 (= A259), Q235 (= Q262)
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)
41% identity, 89% coverage: 26:276/283 of query aligns to 13:263/265 of 4guhB
- active site: A99 (≠ E113), H156 (= H170), K183 (= K197)
- binding (4S,5R)-4,5-dihydroxy-3-oxocyclohex-1-ene-1-carboxylic acid: E59 (= E73), R61 (= R75), R95 (= R109), K183 (= K197), M216 (= M229), R226 (= R239), F238 (= F251), A246 (= A259), Q249 (= Q262)
Query Sequence
>WP_057508481.1 NCBI__GCF_001431535.1:WP_057508481.1
MRALMPLLLAMACATSIPAVQAAPPAIRPLQIGTMRIGEGMPKTIVPITAATAEQALQQA
KVIAASASTDIAEWRIDYLDIATDGTALLALGKRIEQALAGKPLIVTFRTQAEGGSKAIS
DADYGALYATLLRGGFVQMLDVEMFRDRQVVQSLVDAAHGAGAKVVMSSHDFHATPPREE
IVARLLRQQAMGADVLKIAVMPRDAGDVLALLDATWQVRQQSDRPLLTMAMGGTGVVSRL
AGETFGQAMTFGMIGTPSAPGQVEVEQLQSVLQVIHASGQAGR
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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