SitesBLAST
Comparing WP_013683138.1 NCBI__GCF_000194625.1:WP_013683138.1 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)
2o7qA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
31% identity, 92% coverage: 2:183/197 of query aligns to 18:215/501 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)
31% identity, 92% coverage: 2:183/197 of query aligns to 18:215/498 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
2gptA Crystal structure of arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase in complex with tartrate and shikimate (see paper)
31% identity, 92% coverage: 2:183/197 of query aligns to 18:215/498 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
2o7sA Crystal structure of the a. Thaliana dhq-dehydroshikimate-sdh- shikimate-NADP(h)
31% identity, 92% coverage: 2:183/197 of query aligns to 18:215/500 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
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)
31% identity, 92% coverage: 2:183/197 of query aligns to 107:304/603 of Q9SQT8
- E124 (= E21) binding
- R126 (= R23) binding
- R155 (= R48) binding
- K241 (= K123) binding
- R279 (= R160) binding
- S300 (≠ V179) binding
- Q304 (= Q183) binding
Sites not aligning to the query:
- 336 binding ; S→A: 13-fold decrease in substrate affinity but almost no change in activity.
- 338 binding ; S→A: 10-fold decrease in activity, and 9-fold decrease in substrate affinity.
- 381 binding
- 385 binding ; 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
- 423 binding ; D→A: Loss of shikimate dehydrogenase activity.; D→N: Reduced shikimate dehydrogenase activity, but no change in substrate affinity.
- 461 binding
- 463 binding
- 464 binding
- 483 binding
- 485 binding
- 488 binding
- 525 binding
- 548 binding
- 550 binding ; mutation Y->F,A: 100-fold decrease in activity, and 2-fold decrease in substrate affinity.
- 571 binding
- 578 binding
- 582 binding
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, 90% coverage: 7:184/197 of query aligns to 13:204/219 of O66440
- R61 (= R48) binding
- H116 (= H99) active site, Proton donor/acceptor
- K142 (= K123) active site, Schiff-base intermediate with substrate
- R180 (= R160) binding
1sfjA 2.4a crystal structure of staphylococcus aureus type i 3- dehydroquinase, with 3-dehydroquinate bound (see paper)
26% identity, 86% coverage: 18:186/197 of query aligns to 26:217/227 of 1sfjA
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)
25% identity, 86% coverage: 18:186/197 of query aligns to 32:228/238 of Q6GII7
- R70 (= R48) binding
- H133 (= H99) active site, Proton donor/acceptor
- K160 (= K123) active site, Schiff-base intermediate with substrate
- R202 (= R160) binding
- Q225 (= Q183) binding
6sfhA Crystal structure of dhq1 from staphylococcus aureus covalently modified by ligand 7 (see paper)
24% identity, 86% coverage: 18:186/197 of query aligns to 31:227/237 of 6sfhA
- active site: Q73 (≠ E52), H132 (= H99), K159 (= K123)
- binding (1~{S},3~{S},4~{S},5~{R})-3-(aminomethyl)-3,4,5-tris(hydroxyl)cyclohexane-1-carboxylic acid: E34 (= E21), R36 (= R23), R69 (= R48), H132 (= H99), K159 (= K123), R201 (= R160), Y213 (= Y172), A221 (= A180), Q224 (= Q183)
8b2aBBB 3-dehydroquinate dehydratase (see paper)
24% identity, 86% coverage: 18:186/197 of query aligns to 32:228/238 of 8b2aBBB
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)
27% identity, 97% coverage: 5:196/197 of query aligns to 30:249/252 of P05194
- H143 (= H99) active site, Proton donor/acceptor; mutation to A: Loss of dehydratase activity.
- H146 (≠ S102) mutation to A: It retains full catalytic activity.
- K170 (= K123) active site, Schiff-base intermediate with substrate; mutation to A: Loss of dehydratase activity, but it is still able to bind substrate.
- M205 (= M152) mutation to L: It has little effect on the catalytic efficiency and affinity for 3-dehydroquinate.
4gujA 1.50 angstrom crystal structure of the salmonella enterica 3- dehydroquinate dehydratase (arod) in complex with shikimate (see paper)
26% identity, 97% coverage: 5:196/197 of query aligns to 29:248/251 of 4gujA
- active site: E85 (= E52), H142 (= H99), K169 (= K123)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: E45 (= E21), R47 (= R23), R81 (= R48), H142 (= H99), R212 (= R160), F224 (≠ Y172), S231 (≠ V179), A232 (= A180), Q235 (= Q183)
4guiA 1.78 angstrom crystal structure of the salmonella enterica 3- dehydroquinate dehydratase (arod) in complex with quinate (see paper)
26% identity, 97% coverage: 5:196/197 of query aligns to 29:248/251 of 4guiA
- active site: E85 (= E52), H142 (= H99), K169 (= K123)
- binding (1S,3R,4S,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid: E45 (= E21), R47 (= R23), R81 (= R48), H142 (= H99), K169 (= K123), M204 (= M152), R212 (= R160), F224 (≠ Y172), A232 (= A180), Q235 (= Q183)
3m7wA Crystal structure of type i 3-dehydroquinate dehydratase (arod) from salmonella typhimurium lt2 in covalent complex with dehydroquinate (see paper)
26% identity, 97% coverage: 5:196/197 of query aligns to 29:248/251 of 3m7wA
- active site: E85 (= E52), H142 (= H99), K169 (= K123)
- binding 1,3,4-trihydroxy-5-oxo-cyclohexanecarboxylic acid: E45 (= E21), R47 (= R23), H142 (= H99), K169 (= K123), M202 (≠ F150), M204 (= M152), R212 (= R160), F224 (≠ Y172), A232 (= A180), Q235 (= Q183)
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)
26% identity, 97% coverage: 5:196/197 of query aligns to 30:249/252 of P58687
- EWR 46:48 (≠ ELR 21:23) binding
- R82 (= R48) binding
- E86 (= E52) 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 (= H99) active site, Proton donor/acceptor
- K170 (= K123) 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 (= R160) binding
- S232 (≠ V179) binding ; mutation to A: Reduces enzyme activity 50-fold.
- Q236 (= Q183) binding ; mutation to A: Nearly abolishes enzyme activity.
Sites not aligning to the query:
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)
26% identity, 97% coverage: 5:196/197 of query aligns to 43:262/265 of 4guhB
- active site: A99 (≠ E52), H156 (= H99), K183 (= K123)
- binding (4S,5R)-4,5-dihydroxy-3-oxocyclohex-1-ene-1-carboxylic acid: E59 (= E21), R61 (= R23), R95 (= R48), K183 (= K123), M216 (≠ F150), R226 (= R160), F238 (≠ Y172), A246 (= A180), Q249 (= Q183)
8b2cAAA 3-dehydroquinate dehydratase (see paper)
24% identity, 97% coverage: 5:196/197 of query aligns to 30:249/252 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 (= E21), R48 (= R23), H143 (= H99), K170 (= K123), M205 (= M152), R213 (= R160), F225 (≠ Y172), A233 (= A180), Q236 (= Q183)
8b2bAAA 3-dehydroquinate dehydratase (see paper)
24% identity, 97% coverage: 5:196/197 of query aligns to 30:249/252 of 8b2bAAA
- binding (4R,5R)-3-amino-4,5-dihydroxy-cyclohexene-1-carboxylic acid: E46 (= E21), R48 (= R23), H143 (= H99), K170 (= K123), R213 (= R160), F225 (≠ Y172), S232 (≠ V179), A233 (= A180), Q236 (= Q183)
6sfeA Crystal structure of dhq1 from salmonella typhi covalently modified by compound 7 (see paper)
24% identity, 97% coverage: 5:196/197 of query aligns to 30:249/252 of 6sfeA
- active site: E86 (= E52), H143 (= H99), K170 (= K123)
- binding (1~{S},3~{S},4~{S},5~{R})-3-(aminomethyl)-3,4,5-tris(hydroxyl)cyclohexane-1-carboxylic acid: E46 (= E21), R48 (= R23), R82 (= R48), H143 (= H99), K170 (= K123), R213 (= R160), F225 (≠ Y172), S232 (≠ V179), A233 (= A180), Q236 (= Q183)
6h5jA Crystal structure of dhq1 from salmonella typhi covalently modified by ligand 4
24% identity, 97% coverage: 5:196/197 of query aligns to 30:249/252 of 6h5jA
- active site: E86 (= E52), H143 (= H99), K170 (= K123)
- binding (3~{R})-3,4,5-tris(hydroxyl)cyclohexane-1-carboxylic acid: E46 (= E21), R48 (= R23), R82 (= R48), H143 (= H99), K170 (= K123), R213 (= R160), F225 (≠ Y172), S232 (≠ V179), A233 (= A180), Q236 (= Q183)
Query Sequence
>WP_013683138.1 NCBI__GCF_000194625.1:WP_013683138.1
MKIVVSARSLQEAKADCDVVELRLDLFDRLPAISEVEAISKEKIVTVRRKDEGGLFEGSE
EERLELMRKYATVANYVDVECDAHDDFFDMPCKIIESYHNFSETPPFETLRDMIEGRRGD
IFKIATLGRDKRDVLTIVRILCEYDNVVAFLMGEKFAYTRILAVMLGSPFIYCHAGNAVA
PGQLEAGKARKILEMLL
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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