SitesBLAST
Comparing WP_011024417.1 NCBI__GCF_000007345.1:WP_011024417.1 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)
7tm5B Crystal structure of shikimate-3-phosphate bound 3-phosphoshikimate 1- carboxyvinyltransferase from klebsiella pneumoniae
36% identity, 96% coverage: 8:420/430 of query aligns to 10:423/427 of 7tm5B
- binding shikimate-3-phosphate: K22 (= K20), S23 (= S21), R27 (= R25), S169 (= S163), S170 (= S164), Q171 (= Q165), S197 (= S191), Y200 (= Y194), D313 (= D311), N336 (≠ H334), K340 (= K338)
7tm6A Crystal structure of shikimate-3-phosphate and glyphosate bound 3- phosphoshikimate 1-carboxyvinyltransferase from klebsiella pneumoniae
36% identity, 96% coverage: 8:420/430 of query aligns to 9:422/426 of 7tm6A
- binding glyphosate: K21 (= K20), G95 (= G90), R123 (= R118), Q170 (= Q165), D312 (= D311), E340 (= E339), R343 (= R342), H384 (= H382), R385 (= R383)
- binding shikimate-3-phosphate: S22 (= S21), R26 (= R25), T96 (= T91), S168 (= S163), S169 (= S164), Q170 (= Q165), S196 (= S191), Y199 (= Y194), D312 (= D311), N335 (≠ H334), K339 (= K338)
3nvsA 1.02 angstrom resolution crystal structure of 3-phosphoshikimate 1- carboxyvinyltransferase from vibrio cholerae in complex with shikimate-3-phosphate (partially photolyzed) and glyphosate
38% identity, 77% coverage: 88:420/430 of query aligns to 94:424/426 of 3nvsA
- active site: N94 (= N88), P119 (≠ S113), R124 (= R118), H128 (≠ P122), Q135 (= Q129), Y142 (≠ S136), E144 (≠ R138), A247 (= A241), A255 (= A249), D314 (= D311), E342 (= E339), H386 (= H382), R387 (= R383), K412 (≠ I408)
- binding glyphosate: G96 (= G90), R124 (= R118), Q172 (= Q165), D314 (= D311), E342 (= E339), R345 (= R342), H386 (= H382), R387 (= R383)
- binding magnesium ion: E123 (≠ T117), Q145 (≠ G139)
- binding shikimate-3-phosphate: T97 (= T91), S170 (= S163), S171 (= S164), Q172 (= Q165), S198 (= S191), Y201 (= Y194), D314 (= D311), N337 (≠ H334), K341 (= K338)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: Q172 (= Q165), Y201 (= Y194), D314 (= D311), K341 (= K338)
Sites not aligning to the query:
Q9KRB0 3-phosphoshikimate 1-carboxyvinyltransferase; 5-enolpyruvylshikimate-3-phosphate synthase; EPSP synthase; EPSPS; EC 2.5.1.19 from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
38% identity, 77% coverage: 88:420/430 of query aligns to 94:424/426 of Q9KRB0
Sites not aligning to the query:
2pq9A E. Coli epsps liganded with (r)-difluoromethyl tetrahedral reaction intermediate analog (see paper)
35% identity, 96% coverage: 8:420/430 of query aligns to 10:423/427 of 2pq9A
- active site: K22 (= K20), S23 (= S21), D49 (vs. gap), N94 (= N88), P119 (≠ S113), R124 (= R118), D313 (= D311), E341 (= E339), H385 (= H382), R386 (= R383), K411 (≠ I408)
- binding (3r,4s,5r)-5-[(1r)-1-carboxy-2,2-difluoro-1-(phosphonooxy)ethoxy]-4-hydroxy-3-(phosphonooxy)cyclohex-1-ene-1-carboxylic acid: K22 (= K20), S23 (= S21), R27 (= R25), G96 (= G90), T97 (= T91), R124 (= R118), S169 (= S163), S170 (= S164), Q171 (= Q165), S197 (= S191), Y200 (= Y194), D313 (= D311), N336 (≠ H334), K340 (= K338), R344 (= R342), H385 (= H382), R386 (= R383), K411 (≠ I408)
2aa9A Epsp synthase liganded with shikimate (see paper)
35% identity, 96% coverage: 8:420/430 of query aligns to 10:423/427 of 2aa9A
- active site: K22 (= K20), S23 (= S21), D49 (vs. gap), N94 (= N88), P119 (≠ S113), R124 (= R118), D313 (= D311), E341 (= E339), H385 (= H382), R386 (= R383), K411 (≠ I408)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: K22 (= K20), S23 (= S21), R27 (= R25), T97 (= T91), Q171 (= Q165), Y200 (= Y194), D313 (= D311), K340 (= K338)
1x8tA Epsps liganded with the (r)-phosphonate analog of the tetrahedral reaction intermediate (see paper)
35% identity, 96% coverage: 8:420/430 of query aligns to 10:423/427 of 1x8tA
- active site: K22 (= K20), S23 (= S21), D49 (vs. gap), N94 (= N88), P119 (≠ S113), R124 (= R118), D313 (= D311), E341 (= E339), H385 (= H382), R386 (= R383), K411 (≠ I408)
- binding [3r-[3a,4a,5b(r*)]]-5-(1-carboxy-1-phosphonoethoxy)-4-hydroxy-3-(phosphonooxy)-1-cyclohexene-1-carboxylic acid: K22 (= K20), S23 (= S21), R27 (= R25), T97 (= T91), S169 (= S163), S170 (= S164), Q171 (= Q165), S197 (= S191), Y200 (= Y194), D313 (= D311), N336 (≠ H334), K340 (= K338), R344 (= R342), H385 (= H382), R386 (= R383)
1x8rA Epsps liganded with the (s)-phosphonate analog of the tetrahedral reaction intermediate (see paper)
35% identity, 96% coverage: 8:420/430 of query aligns to 10:423/427 of 1x8rA
- active site: K22 (= K20), S23 (= S21), D49 (vs. gap), N94 (= N88), P119 (≠ S113), R124 (= R118), D313 (= D311), E341 (= E339), H385 (= H382), R386 (= R383), K411 (≠ I408)
- binding [3r-[3a,4a,5b(s*)]]-5-(1-carboxy-1-phosphonoethoxy)-4-hydroxy-3-(phosphonooxy)-1-cyclohexene-1-carboxylic acid: K22 (= K20), S23 (= S21), R27 (= R25), G96 (= G90), T97 (= T91), R124 (= R118), S169 (= S163), S170 (= S164), Q171 (= Q165), S197 (= S191), Y200 (= Y194), D313 (= D311), N336 (≠ H334), K340 (= K338), E341 (= E339), H385 (= H382), K411 (≠ I408)
1g6tA Structure of epsp synthase liganded with shikimate-3-phosphate (see paper)
35% identity, 96% coverage: 8:420/430 of query aligns to 10:423/427 of 1g6tA
- active site: K22 (= K20), S23 (= S21), D49 (vs. gap), N94 (= N88), P119 (≠ S113), R124 (= R118), D313 (= D311), E341 (= E339), H385 (= H382), R386 (= R383), K411 (≠ I408)
- binding phosphate ion: K22 (= K20), G96 (= G90), T97 (= T91), R124 (= R118), Q171 (= Q165), E341 (= E339), K411 (≠ I408)
- binding shikimate-3-phosphate: K22 (= K20), S23 (= S21), R27 (= R25), T97 (= T91), S169 (= S163), S170 (= S164), Q171 (= Q165), S197 (= S191), Y200 (= Y194), D313 (= D311), N336 (≠ H334), K340 (= K338)
1g6sA Structure of epsp synthase liganded with shikimate-3-phosphate and glyphosate (see paper)
35% identity, 96% coverage: 8:420/430 of query aligns to 10:423/427 of 1g6sA
- active site: K22 (= K20), S23 (= S21), D49 (vs. gap), N94 (= N88), P119 (≠ S113), R124 (= R118), D313 (= D311), E341 (= E339), H385 (= H382), R386 (= R383), K411 (≠ I408)
- binding glyphosate: K22 (= K20), G96 (= G90), R124 (= R118), Q171 (= Q165), D313 (= D311), E341 (= E339), R344 (= R342), H385 (= H382), R386 (= R383)
- binding shikimate-3-phosphate: K22 (= K20), S23 (= S21), R27 (= R25), T97 (= T91), S169 (= S163), S170 (= S164), Q171 (= Q165), S197 (= S191), Y200 (= Y194), D313 (= D311), N336 (≠ H334), K340 (= K338)
P0A6D3 3-phosphoshikimate 1-carboxyvinyltransferase; 5-enolpyruvylshikimate-3-phosphate synthase; EPSP synthase; EPSPS; EC 2.5.1.19 from Escherichia coli (strain K12) (see 8 papers)
35% identity, 96% coverage: 8:420/430 of query aligns to 10:423/427 of P0A6D3
- KS 22:23 (= KS 20:21) binding
- R27 (= R25) binding
- NAGT 94:97 (≠ NSGT 88:91) Phosphoenolpyruvate
- G96 (= G90) mutation to A: Insensitive to glyphosate with unaltered affinity for its first substrate S3P, but displays a 30-fold lower affinity for its second substrate PEP.
- T97 (= T91) mutation to I: This mutant is sensitive to glyphosate and causes a substantial decrease in the affinity for PEP. Insensitive to glyphosate but maintains high affinity for PEP. It causes a shift of residue G96 toward the glyphosate binding site, impairing efficient binding of glyphosate, while the side chain of I97 points away from the substrate binding site, facilitating PEP utilization; when associated with S-101.
- P101 (≠ L95) mutation to A: Displays a slight decrease of the affinity binding for both S3P and PEP. Decreases the binding affinity of glyphosate, reducing the potency of this inhibitor.; mutation to G: Displays a slight decrease of the affinity binding for both S3P and PEP. Decreases the binding affinity of glyphosate, reducing the potency of this inhibitor.; mutation to L: Displays a 2-fold lower affinity binding for both S3P and PEP. Decreases the binding affinity of glyphosate, reducing the potency of this inhibitor.; mutation to S: Displays a slight decrease of the affinity binding for both S3P and PEP. Decreases the binding affinity of glyphosate, reducing the potency of this inhibitor. Insensitive to glyphosate but maintains high affinity for PEP. It causes a shift of residue G96 toward the glyphosate binding site, impairing efficient binding of glyphosate, while the side chain of I97 points away from the substrate-binding site, facilitating PEP utilization; when associated with I-97.
- R124 (= R118) binding
- SSQ 169:171 (= SSQ 163:165) binding
- S197 (= S191) binding
- D313 (= D311) active site, Proton acceptor; mutation to A: The enolpyruvyl transfer reaction is halted after formation of the tetrahedral adduct of the substrates.
- N336 (≠ H334) binding
- K340 (= K338) binding
- E341 (= E339) active site, Proton donor
- R344 (= R342) binding
- R386 (= R383) binding
- C408 (≠ S405) Modified by bromopyruvate
- K411 (≠ I408) Modified by bromopyruvate; binding
3fjzA E. Coli epsp synthase (t97i) liganded with s3p and glyphosate (see paper)
35% identity, 96% coverage: 8:420/430 of query aligns to 10:423/427 of 3fjzA
- active site: K22 (= K20), S23 (= S21), D49 (vs. gap), N94 (= N88), P119 (≠ S113), R124 (= R118), D313 (= D311), E341 (= E339), H385 (= H382), R386 (= R383), K411 (≠ I408)
- binding N-(phosphonomethyl)glycine: K22 (= K20), G96 (= G90), R124 (= R118), Q171 (= Q165), D313 (= D311), E341 (= E339), R344 (= R342), H385 (= H382), R386 (= R383)
- binding shikimate-3-phosphate: K22 (= K20), S23 (= S21), R27 (= R25), I97 (≠ T91), S169 (= S163), S170 (= S164), Q171 (= Q165), S197 (= S191), Y200 (= Y194), D313 (= D311), N336 (≠ H334), K340 (= K338)
- binding serine: I265 (≠ N260), G266 (≠ L261), S269 (= S264)
1q36A Epsp synthase (asp313ala) liganded with tetrahedral reaction intermediate (see paper)
35% identity, 96% coverage: 8:420/430 of query aligns to 10:423/427 of 1q36A
- active site: K22 (= K20), S23 (= S21), D49 (vs. gap), N94 (= N88), P119 (≠ S113), R124 (= R118), A313 (≠ D311), E341 (= E339), H385 (= H382), R386 (= R383), K411 (≠ I408)
- binding 5-(1-carboxy-1-phosphonooxy-ethoxyl)-4-hydroxy-3-phosphonooxy-cyclohex-1-enecarboxylic acid: K22 (= K20), S23 (= S21), R27 (= R25), G96 (= G90), T97 (= T91), R124 (= R118), S169 (= S163), S170 (= S164), Q171 (= Q165), S197 (= S191), Y200 (= Y194), N336 (≠ H334), K340 (= K338), E341 (= E339), R344 (= R342), R386 (= R383), K411 (≠ I408)
3slhD 1.70 angstrom resolution structure of 3-phosphoshikimate 1- carboxyvinyltransferase (aroa) from coxiella burnetii in complex with shikimate-3-phosphate and glyphosate
34% identity, 99% coverage: 4:427/430 of query aligns to 7:434/440 of 3slhD
- active site: K23 (= K20), S24 (= S21), D50 (= D46), N95 (= N88), R125 (= R118), D317 (= D311), E345 (= E339), H388 (= H382), R389 (= R383), T415 (≠ I408)
- binding glyphosate: K23 (= K20), G97 (= G90), T98 (= T91), R125 (= R118), Q171 (= Q165), D317 (= D311), E345 (= E339), R348 (= R342), H388 (= H382), R389 (= R383)
- binding shikimate-3-phosphate: S24 (= S21), R28 (= R25), S169 (= S163), Q171 (= Q165), R196 (≠ V195), D317 (= D311), K344 (= K338)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S24 (= S21), R28 (= R25), T98 (= T91), Q171 (= Q165), R196 (≠ V195), D317 (= D311), K344 (= K338)
Q83E11 3-phosphoshikimate 1-carboxyvinyltransferase; 5-enolpyruvylshikimate-3-phosphate synthase; EPSP synthase; EPSPS; EC 2.5.1.19 from Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
34% identity, 99% coverage: 4:427/430 of query aligns to 5:432/438 of Q83E11
- KS 21:22 (= KS 20:21) binding
- R26 (= R25) binding
- NSGT 93:96 (= NSGT 88:91) Phosphoenolpyruvate
- R123 (= R118) binding
- D315 (= D311) active site, Proton acceptor
- K342 (= K338) binding
- R346 (= R342) binding
- R387 (= R383) binding
P11043 3-phosphoshikimate 1-carboxyvinyltransferase, chloroplastic; 5-enolpyruvylshikimate-3-phosphate synthase; EPSP synthase; EC 2.5.1.19 from Petunia hybrida (Petunia) (see paper)
36% identity, 94% coverage: 10:415/430 of query aligns to 85:508/516 of P11043
- G173 (= G90) mutation to A: Resistance to glyphosate due to a lower affinity. Slight reduction in EPSP synthase activity.
4egrA 2.50 angstrom resolution structure of 3-phosphoshikimate 1- carboxyvinyltransferase (aroa) from coxiella burnetii in complex with phosphoenolpyruvate
34% identity, 99% coverage: 4:427/430 of query aligns to 7:430/434 of 4egrA
- active site: K23 (= K20), S24 (= S21), D50 (= D46), N95 (= N88), R125 (= R118), D313 (= D311), E341 (= E339), H384 (= H382), R385 (= R383), T411 (≠ I408)
- binding phosphoenolpyruvate: K23 (= K20), G97 (= G90), T98 (= T91), R125 (= R118), D313 (= D311), E341 (= E339), R344 (= R342), R385 (= R383)
P07547 Pentafunctional AROM polypeptide; EC 4.2.3.4; EC 2.5.1.19; EC 2.7.1.71; EC 4.2.1.10; EC 1.1.1.25 from Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) (see 2 papers)
32% identity, 94% coverage: 17:420/430 of query aligns to 412:839/1583 of P07547
Sites not aligning to the query:
- 44:46 binding
- 81:84 binding
- 114:116 binding
- 119 binding
- 139:140 binding
- 161 binding
- 179:182 binding
- 190 binding
- 194 binding
- 271 binding
- 287 binding
7m0oA Dgt-28 epsps (see paper)
32% identity, 89% coverage: 40:420/430 of query aligns to 27:397/400 of 7m0oA
6hqvA Pentafunctional arom complex from chaetomium thermophilum (see paper)
32% identity, 97% coverage: 14:430/430 of query aligns to 402:836/1555 of 6hqvA
Sites not aligning to the query:
- active site: 123, 145, 187, 243, 253, 257, 261, 264, 268, 280
- binding (4S,5R)-4,5-dihydroxy-3-oxocyclohex-1-ene-1-carboxylic acid: 1060, 1062, 1181, 1224, 1232, 1242, 1243
- binding glutamic acid: 139, 145, 187, 243, 257, 264, 280
- binding nicotinamide-adenine-dinucleotide: 42, 44, 45, 76, 79, 107, 108, 109, 112, 132, 133, 135, 139, 140, 145, 154, 175, 176, 177, 180, 280
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: 874, 923, 924, 979, 1277, 1279, 1323, 1327, 1348, 1368, 1526
- binding zinc ion: 187, 264, 280
Query Sequence
>WP_011024417.1 NCBI__GCF_000007345.1:WP_011024417.1
MRVSISKSSVKGEVFAPSSKSYTHRAITLAALSNESIVRRPLLSADTLATIRASEMFGAS
VKREEENLIIHGFNGKPNVPDDVIDAANSGTTLRLMTAIAGLTDGITVLTGDSSLRTRPN
GPLLKTLNQLGASACSTRGNEKAPLVVKGGLEGKKVSIEGSISSQFISALLIACPLAENS
TTLSIIGKLKSRPYVDVTIEMLELAGVKIHTDENNGTKFIIPGKQKYDLKEYTIPGDFSS
ASYLLAAAAMTEGSEITVKNLFPSKQGDKLIIETLKQMGADITWDREAGIVTVRGGRKLK
AVTFDAGATPDLVPTVAVLAAVAEGTSRIENAEHVRYKETDRLSALATELPKLGVKLKEE
KDSLTITGGELKGAEVHGWDDHRIVMSLALAGMVAGNTTIDTTESVAISYPDFFEDMSNL
GVKIKQISEE
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