SitesBLAST
Comparing WP_010964213.1 NCBI__GCF_000008765.1:WP_010964213.1 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)
2pq9A E. Coli epsps liganded with (r)-difluoromethyl tetrahedral reaction intermediate analog (see paper)
32% identity, 97% coverage: 1:417/428 of query aligns to 1:423/427 of 2pq9A
- active site: K22 (= K21), S23 (= S22), D49 (= D48), N94 (≠ E92), P119 (≠ G117), R124 (= R122), D313 (= D306), E341 (= E334), H385 (= H378), R386 (= R379), K411 (= K405)
- 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 (= K21), S23 (= S22), R27 (= R26), G96 (= G94), T97 (≠ S95), R124 (= R122), S169 (= S166), S170 (= S167), Q171 (= Q168), S197 (= S194), Y200 (= Y197), D313 (= D306), N336 (≠ R329), K340 (= K333), R344 (= R337), H385 (= H378), R386 (= R379), K411 (= K405)
2aa9A Epsp synthase liganded with shikimate (see paper)
32% identity, 97% coverage: 1:417/428 of query aligns to 1:423/427 of 2aa9A
- active site: K22 (= K21), S23 (= S22), D49 (= D48), N94 (≠ E92), P119 (≠ G117), R124 (= R122), D313 (= D306), E341 (= E334), H385 (= H378), R386 (= R379), K411 (= K405)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: K22 (= K21), S23 (= S22), R27 (= R26), T97 (≠ S95), Q171 (= Q168), Y200 (= Y197), D313 (= D306), K340 (= K333)
1x8tA Epsps liganded with the (r)-phosphonate analog of the tetrahedral reaction intermediate (see paper)
32% identity, 97% coverage: 1:417/428 of query aligns to 1:423/427 of 1x8tA
- active site: K22 (= K21), S23 (= S22), D49 (= D48), N94 (≠ E92), P119 (≠ G117), R124 (= R122), D313 (= D306), E341 (= E334), H385 (= H378), R386 (= R379), K411 (= K405)
- binding [3r-[3a,4a,5b(r*)]]-5-(1-carboxy-1-phosphonoethoxy)-4-hydroxy-3-(phosphonooxy)-1-cyclohexene-1-carboxylic acid: K22 (= K21), S23 (= S22), R27 (= R26), T97 (≠ S95), S169 (= S166), S170 (= S167), Q171 (= Q168), S197 (= S194), Y200 (= Y197), D313 (= D306), N336 (≠ R329), K340 (= K333), R344 (= R337), H385 (= H378), R386 (= R379)
1x8rA Epsps liganded with the (s)-phosphonate analog of the tetrahedral reaction intermediate (see paper)
32% identity, 97% coverage: 1:417/428 of query aligns to 1:423/427 of 1x8rA
- active site: K22 (= K21), S23 (= S22), D49 (= D48), N94 (≠ E92), P119 (≠ G117), R124 (= R122), D313 (= D306), E341 (= E334), H385 (= H378), R386 (= R379), K411 (= K405)
- binding [3r-[3a,4a,5b(s*)]]-5-(1-carboxy-1-phosphonoethoxy)-4-hydroxy-3-(phosphonooxy)-1-cyclohexene-1-carboxylic acid: K22 (= K21), S23 (= S22), R27 (= R26), G96 (= G94), T97 (≠ S95), R124 (= R122), S169 (= S166), S170 (= S167), Q171 (= Q168), S197 (= S194), Y200 (= Y197), D313 (= D306), N336 (≠ R329), K340 (= K333), E341 (= E334), H385 (= H378), K411 (= K405)
1g6tA Structure of epsp synthase liganded with shikimate-3-phosphate (see paper)
32% identity, 97% coverage: 1:417/428 of query aligns to 1:423/427 of 1g6tA
- active site: K22 (= K21), S23 (= S22), D49 (= D48), N94 (≠ E92), P119 (≠ G117), R124 (= R122), D313 (= D306), E341 (= E334), H385 (= H378), R386 (= R379), K411 (= K405)
- binding phosphate ion: K22 (= K21), G96 (= G94), T97 (≠ S95), R124 (= R122), Q171 (= Q168), E341 (= E334), K411 (= K405)
- binding shikimate-3-phosphate: K22 (= K21), S23 (= S22), R27 (= R26), T97 (≠ S95), S169 (= S166), S170 (= S167), Q171 (= Q168), S197 (= S194), Y200 (= Y197), D313 (= D306), N336 (≠ R329), K340 (= K333)
1g6sA Structure of epsp synthase liganded with shikimate-3-phosphate and glyphosate (see paper)
32% identity, 97% coverage: 1:417/428 of query aligns to 1:423/427 of 1g6sA
- active site: K22 (= K21), S23 (= S22), D49 (= D48), N94 (≠ E92), P119 (≠ G117), R124 (= R122), D313 (= D306), E341 (= E334), H385 (= H378), R386 (= R379), K411 (= K405)
- binding glyphosate: K22 (= K21), G96 (= G94), R124 (= R122), Q171 (= Q168), D313 (= D306), E341 (= E334), R344 (= R337), H385 (= H378), R386 (= R379)
- binding shikimate-3-phosphate: K22 (= K21), S23 (= S22), R27 (= R26), T97 (≠ S95), S169 (= S166), S170 (= S167), Q171 (= Q168), S197 (= S194), Y200 (= Y197), D313 (= D306), N336 (≠ R329), K340 (= K333)
P0A6D3 3-phosphoshikimate 1-carboxyvinyltransferase; 5-enolpyruvylshikimate-3-phosphate synthase; EPSP synthase; EPSPS; EC 2.5.1.19 from Escherichia coli (strain K12) (see 5 papers)
32% identity, 97% coverage: 1:417/428 of query aligns to 1:423/427 of P0A6D3
- K22 (= K21) binding 3-phosphoshikimate
- S23 (= S22) binding 3-phosphoshikimate
- R27 (= R26) binding 3-phosphoshikimate
- G96 (= G94) 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 (≠ S95) mutation to I: This mutant is sensitive to glyphosate and causes a substantial decrease in the affinity for PEP. Is insensitive to glyphosate but maintains high affinity for PEP; when associated with S-101.
- P101 (≠ F99) 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. Is insensitive to glyphosate but maintains high affinity for PEP; when associated with I-97.
- S169 (= S166) binding 3-phosphoshikimate
- S170 (= S167) binding 3-phosphoshikimate
- Q171 (= Q168) binding 3-phosphoshikimate
- S197 (= S194) binding 3-phosphoshikimate
- D313 (= D306) binding 3-phosphoshikimate; mutation to A: The enolpyruvyl transfer reaction is halted after formation of the tetrahedral adduct of the substrates.
- N336 (≠ R329) binding 3-phosphoshikimate
- K340 (= K333) binding 3-phosphoshikimate
- C408 (= C402) Modified by bromopyruvate
- K411 (= K405) Modified by bromopyruvate
3fjzA E. Coli epsp synthase (t97i) liganded with s3p and glyphosate (see paper)
32% identity, 97% coverage: 1:417/428 of query aligns to 1:423/427 of 3fjzA
- active site: K22 (= K21), S23 (= S22), D49 (= D48), N94 (≠ E92), P119 (≠ G117), R124 (= R122), D313 (= D306), E341 (= E334), H385 (= H378), R386 (= R379), K411 (= K405)
- binding N-(phosphonomethyl)glycine: K22 (= K21), G96 (= G94), R124 (= R122), Q171 (= Q168), D313 (= D306), E341 (= E334), R344 (= R337), H385 (= H378), R386 (= R379)
- binding shikimate-3-phosphate: K22 (= K21), S23 (= S22), R27 (= R26), I97 (≠ S95), S169 (= S166), S170 (= S167), Q171 (= Q168), S197 (= S194), Y200 (= Y197), D313 (= D306), N336 (≠ R329), K340 (= K333)
- binding serine: I265 (≠ L260), G266 (≠ N261), S269 (= S264)
7tm5B Crystal structure of shikimate-3-phosphate bound 3-phosphoshikimate 1- carboxyvinyltransferase from klebsiella pneumoniae
30% identity, 97% coverage: 1:417/428 of query aligns to 1:423/427 of 7tm5B
- binding shikimate-3-phosphate: K22 (= K21), S23 (= S22), R27 (= R26), S169 (= S166), S170 (= S167), Q171 (= Q168), S197 (= S194), Y200 (= Y197), D313 (= D306), N336 (≠ R329), K340 (= K333)
7tm6A Crystal structure of shikimate-3-phosphate and glyphosate bound 3- phosphoshikimate 1-carboxyvinyltransferase from klebsiella pneumoniae
30% identity, 95% coverage: 11:417/428 of query aligns to 11:422/426 of 7tm6A
- binding glyphosate: K21 (= K21), G95 (= G94), R123 (= R122), Q170 (= Q168), D312 (= D306), E340 (= E334), R343 (= R337), H384 (= H378), R385 (= R379)
- binding shikimate-3-phosphate: S22 (= S22), R26 (= R26), T96 (≠ S95), S168 (= S166), S169 (= S167), Q170 (= Q168), S196 (= S194), Y199 (= Y197), D312 (= D306), N335 (≠ R329), K339 (= K333)
1q36A Epsp synthase (asp313ala) liganded with tetrahedral reaction intermediate (see paper)
31% identity, 97% coverage: 1:417/428 of query aligns to 1:423/427 of 1q36A
- active site: K22 (= K21), S23 (= S22), D49 (= D48), N94 (≠ E92), P119 (≠ G117), R124 (= R122), A313 (≠ D306), E341 (= E334), H385 (= H378), R386 (= R379), K411 (= K405)
- binding 5-(1-carboxy-1-phosphonooxy-ethoxyl)-4-hydroxy-3-phosphonooxy-cyclohex-1-enecarboxylic acid: K22 (= K21), S23 (= S22), R27 (= R26), G96 (= G94), T97 (≠ S95), R124 (= R122), S169 (= S166), S170 (= S167), Q171 (= Q168), S197 (= S194), Y200 (= Y197), N336 (≠ R329), K340 (= K333), E341 (= E334), R344 (= R337), R386 (= R379), K411 (= K405)
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
30% identity, 97% coverage: 1:417/428 of query aligns to 1:424/426 of 3nvsA
- active site: K22 (= K21), S23 (= S22), D49 (= D48), N94 (≠ E92), P119 (≠ G117), R124 (= R122), H128 (≠ S126), Q135 (≠ E133), Y142 (= Y138), E144 (≠ H140), A247 (= A242), A255 (vs. gap), D314 (= D306), E342 (= E334), H386 (= H378), R387 (= R379), K412 (= K405)
- binding glyphosate: K22 (= K21), G96 (= G94), R124 (= R122), Q172 (= Q168), D314 (= D306), E342 (= E334), R345 (= R337), H386 (= H378), R387 (= R379)
- binding magnesium ion: E123 (≠ Y121), Q145 (≠ P141)
- binding shikimate-3-phosphate: K22 (= K21), S23 (= S22), R27 (= R26), T97 (≠ S95), S170 (= S166), S171 (= S167), Q172 (= Q168), S198 (= S194), Y201 (= Y197), D314 (= D306), N337 (≠ R329), K341 (= K333)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (= S22), R27 (= R26), Q172 (= Q168), Y201 (= Y197), D314 (= D306), K341 (= K333)
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)
30% identity, 97% coverage: 1:417/428 of query aligns to 1:424/426 of Q9KRB0
- K22 (= K21) binding 3-phosphoshikimate
- S23 (= S22) binding 3-phosphoshikimate
- R27 (= R26) binding 3-phosphoshikimate
- S170 (= S166) binding 3-phosphoshikimate
- S171 (= S167) binding 3-phosphoshikimate
- S198 (= S194) binding 3-phosphoshikimate
- D314 (= D306) binding 3-phosphoshikimate
- N337 (≠ R329) binding 3-phosphoshikimate
- K341 (= K333) binding 3-phosphoshikimate
P11043 3-phosphoshikimate 1-carboxyvinyltransferase, chloroplastic; 5-enolpyruvylshikimate-3-phosphate synthase; EPSP synthase; EC 2.5.1.19 from Petunia hybrida (Petunia) (see paper)
33% identity, 95% coverage: 11:416/428 of query aligns to 85:512/516 of P11043
- G173 (= G94) mutation to A: This mutant becomes resistant to glyphosate due to a lower affinity. Shows a slight reduction in EPSP synthase activity.
Q9S400 3-phosphoshikimate 1-carboxyvinyltransferase; 5-enolpyruvylshikimate-3-phosphate synthase; EPSP synthase; EPSPS; EC 2.5.1.19 from Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) (see paper)
31% identity, 97% coverage: 4:417/428 of query aligns to 3:424/427 of Q9S400
- S21 (= S22) binding 3-phosphoshikimate
- R25 (= R26) binding 3-phosphoshikimate
- S166 (= S166) binding 3-phosphoshikimate
- A167 (≠ S167) binding 3-phosphoshikimate
- Q168 (= Q168) binding 3-phosphoshikimate
- D312 (vs. gap) binding 3-phosphoshikimate
- K339 (= K333) binding 3-phosphoshikimate
1rf6A Structural studies of streptococcus pneumoniae epsp synthase in s3p- glp bound state (see paper)
30% identity, 97% coverage: 4:417/428 of query aligns to 3:424/427 of 1rf6A
- active site: K20 (= K21), S21 (= S22), D47 (= D48), N90 (≠ E92), D115 (≠ G117), R120 (= R122), D312 (vs. gap), E340 (= E334), H384 (= H378), R385 (= R379), T412 (≠ K405)
- binding glyphosate: K20 (= K21), G92 (= G94), T93 (≠ S95), R120 (= R122), Q168 (= Q168), D312 (vs. gap), E340 (= E334), R343 (= R337), H384 (= H378), R385 (= R379)
- binding shikimate-3-phosphate: S21 (= S22), R25 (= R26), S166 (= S166), Q168 (= Q168), R193 (≠ V198), I311 (≠ V308), D312 (vs. gap), K339 (= K333)
1rf4A Structural studies of streptococcus pneumoniae epsp synthase, tetrahedral intermediate bound state (see paper)
30% identity, 97% coverage: 4:417/428 of query aligns to 3:424/427 of 1rf4A
- active site: K20 (= K21), S21 (= S22), D47 (= D48), N90 (≠ E92), D115 (≠ G117), R120 (= R122), D312 (vs. gap), E340 (= E334), H384 (= H378), R385 (= R379), T412 (≠ K405)
- binding (3r,4s,5r)-5-{[(1r)-1-carboxy-2-fluoro-1-(phosphonooxy)ethyl]oxy}-4-hydroxy-3-(phosphonooxy)cyclohex-1-ene-1-carboxylic acid: K20 (= K21), S21 (= S22), R25 (= R26), G92 (= G94), T93 (≠ S95), R120 (= R122), S166 (= S166), A167 (≠ S167), Q168 (= Q168), R193 (≠ V198), D312 (vs. gap), K339 (= K333), E340 (= E334), R343 (= R337), H384 (= H378), R385 (= R379)
4egrA 2.50 angstrom resolution structure of 3-phosphoshikimate 1- carboxyvinyltransferase (aroa) from coxiella burnetii in complex with phosphoenolpyruvate
29% identity, 96% coverage: 11:421/428 of query aligns to 13:427/434 of 4egrA
- active site: K23 (= K21), S24 (= S22), D50 (= D48), N95 (≠ E92), R125 (= R122), D313 (= D306), E341 (= E334), H384 (= H378), R385 (= R379), T411 (≠ K405)
- binding phosphoenolpyruvate: K23 (= K21), G97 (= G94), T98 (≠ S95), R125 (= R122), D313 (= D306), E341 (= E334), R344 (= R337), R385 (= R379)
3slhD 1.70 angstrom resolution structure of 3-phosphoshikimate 1- carboxyvinyltransferase (aroa) from coxiella burnetii in complex with shikimate-3-phosphate and glyphosate
29% identity, 96% coverage: 11:421/428 of query aligns to 13:431/440 of 3slhD
- active site: K23 (= K21), S24 (= S22), D50 (= D48), N95 (≠ E92), R125 (= R122), D317 (= D306), E345 (= E334), H388 (= H378), R389 (= R379), T415 (≠ K405)
- binding glyphosate: K23 (= K21), G97 (= G94), T98 (≠ S95), R125 (= R122), Q171 (= Q168), D317 (= D306), E345 (= E334), R348 (= R337), H388 (= H378), R389 (= R379)
- binding shikimate-3-phosphate: S24 (= S22), R28 (= R26), S169 (= S166), Q171 (= Q168), R196 (≠ V198), D317 (= D306), K344 (= K333)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S24 (= S22), R28 (= R26), T98 (≠ S95), Q171 (= Q168), R196 (≠ V198), D317 (= D306), K344 (= K333)
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)
29% identity, 96% coverage: 11:421/428 of query aligns to 11:429/438 of Q83E11
- K21 (= K21) binding phosphoenolpyruvate
- S22 (= S22) binding 3-phosphoshikimate
- R26 (= R26) binding 3-phosphoshikimate
- NSGT 93:96 (≠ ESGS 92:95) Phosphoenolpyruvate
- G95 (= G94) binding phosphoenolpyruvate
- T96 (≠ S95) binding phosphoenolpyruvate
- R123 (= R122) binding phosphoenolpyruvate
- S167 (= S166) binding 3-phosphoshikimate
- A168 (≠ S167) binding 3-phosphoshikimate
- Q169 (= Q168) binding 3-phosphoshikimate; binding phosphoenolpyruvate
- D315 (= D306) binding 3-phosphoshikimate
- K342 (= K333) binding 3-phosphoshikimate
- R346 (= R337) binding phosphoenolpyruvate
- R387 (= R379) binding phosphoenolpyruvate
Query Sequence
>WP_010964213.1 NCBI__GCF_000008765.1:WP_010964213.1
MNCVKINPCCLKGDIKIPPSKSLGHRAIICAALSEEESTIENISYSKDIKATCIGMSKLG
ALIIEDAKDNSTLKIKKQKLVSKEKVYIDCSESGSTVRFLIPISLIEERNVVFDGQGKLS
YRPLDSYFNIFDEKEIAYSHPEGKVLPLQIKGRLKAGMFNLPGNISSQFISGLMFSLPFL
EGDSIINITTNLESVGYVDMTIDMLKKFGIEIENKAYKSFFIKGNQKCKGTKYKVEGDFS
QAAFWLSAGILNGNINCKDLNISSLQGDKVILDILKKMGGAIDEKSFSSKKSHTHGIVID
ASQCPDLVPILSVVAALSEGTTKIVNAARLRIKESDRLKAMATELNKLGAEVVELEDGLL
IEGKEKLKGGEVESWNDHRIAMALGIAALRCEESVTINGSECVSKSYPQFWSDLKQLGGD
VHEWSLGE
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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