SitesBLAST
Comparing WP_010936240.1 NCBI__GCF_000011905.1:WP_010936240.1 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)
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
32% identity, 96% coverage: 9:412/420 of query aligns to 11:424/426 of 3nvsA
- active site: K22 (= K20), S23 (= S21), D49 (= D47), N94 (≠ E89), P119 (≠ S115), R124 (= R119), H128 (≠ P123), Q135 (= Q130), Y142 (≠ T137), E144 (≠ G139), A247 (= A237), A255 (= A245), D314 (= D303), E342 (= E331), H386 (= H374), R387 (= R375), K412 (= K400)
- binding glyphosate: K22 (= K20), G96 (≠ A91), R124 (= R119), Q172 (= Q163), D314 (= D303), E342 (= E331), R345 (= R334), H386 (= H374), R387 (= R375)
- binding magnesium ion: E123 (vs. gap), Q145 (≠ N140)
- binding shikimate-3-phosphate: K22 (= K20), S23 (= S21), R27 (= R25), T97 (≠ A92), S170 (= S161), S171 (= S162), Q172 (= Q163), S198 (= S189), Y201 (= Y192), D314 (= D303), N337 (≠ Q326), K341 (= K330)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (= S21), R27 (= R25), Q172 (= Q163), Y201 (= Y192), D314 (= D303), K341 (= K330)
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)
32% identity, 96% coverage: 9:412/420 of query aligns to 11:424/426 of Q9KRB0
7m0oA Dgt-28 epsps (see paper)
31% identity, 95% coverage: 15:412/420 of query aligns to 1:397/400 of 7m0oA
7tm6A Crystal structure of shikimate-3-phosphate and glyphosate bound 3- phosphoshikimate 1-carboxyvinyltransferase from klebsiella pneumoniae
29% identity, 95% coverage: 12:409/420 of query aligns to 13:419/426 of 7tm6A
- binding glyphosate: K21 (= K20), G95 (≠ A91), R123 (= R119), Q170 (= Q163), D312 (= D303), E340 (= E331), R343 (= R334), H384 (= H374), R385 (= R375)
- binding shikimate-3-phosphate: S22 (= S21), R26 (= R25), T96 (≠ A92), S168 (= S161), S169 (= S162), Q170 (= Q163), S196 (= S189), Y199 (= Y192), D312 (= D303), N335 (≠ Q326), K339 (= K330)
7tm5B Crystal structure of shikimate-3-phosphate bound 3-phosphoshikimate 1- carboxyvinyltransferase from klebsiella pneumoniae
29% identity, 95% coverage: 12:409/420 of query aligns to 14:420/427 of 7tm5B
- binding shikimate-3-phosphate: K22 (= K20), S23 (= S21), R27 (= R25), S169 (= S161), S170 (= S162), Q171 (= Q163), S197 (= S189), Y200 (= Y192), D313 (= D303), N336 (≠ Q326), K340 (= K330)
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)
31% identity, 95% coverage: 15:412/420 of query aligns to 410:839/1583 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
P11043 3-phosphoshikimate 1-carboxyvinyltransferase, chloroplastic; 5-enolpyruvylshikimate-3-phosphate synthase; EPSP synthase; EC 2.5.1.19 from Petunia hybrida (Petunia) (see paper)
31% identity, 95% coverage: 12:410/420 of query aligns to 87:511/516 of P11043
- G173 (≠ A91) mutation to A: Resistance to glyphosate due to a lower affinity. Slight reduction in EPSP synthase activity.
2pq9A E. Coli epsps liganded with (r)-difluoromethyl tetrahedral reaction intermediate analog (see paper)
29% identity, 95% coverage: 12:409/420 of query aligns to 14:420/427 of 2pq9A
- active site: K22 (= K20), S23 (= S21), D49 (= D47), N94 (≠ E89), P119 (≠ H114), R124 (= R119), D313 (= D303), E341 (= E331), H385 (= H374), R386 (= R375), K411 (= K400)
- 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 (≠ A91), T97 (≠ A92), R124 (= R119), S169 (= S161), S170 (= S162), Q171 (= Q163), S197 (= S189), Y200 (= Y192), D313 (= D303), N336 (≠ Q326), K340 (= K330), R344 (= R334), H385 (= H374), R386 (= R375), K411 (= K400)
2aa9A Epsp synthase liganded with shikimate (see paper)
29% identity, 95% coverage: 12:409/420 of query aligns to 14:420/427 of 2aa9A
- active site: K22 (= K20), S23 (= S21), D49 (= D47), N94 (≠ E89), P119 (≠ H114), R124 (= R119), D313 (= D303), E341 (= E331), H385 (= H374), R386 (= R375), K411 (= K400)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: K22 (= K20), S23 (= S21), R27 (= R25), T97 (≠ A92), Q171 (= Q163), Y200 (= Y192), D313 (= D303), K340 (= K330)
1x8tA Epsps liganded with the (r)-phosphonate analog of the tetrahedral reaction intermediate (see paper)
29% identity, 95% coverage: 12:409/420 of query aligns to 14:420/427 of 1x8tA
- active site: K22 (= K20), S23 (= S21), D49 (= D47), N94 (≠ E89), P119 (≠ H114), R124 (= R119), D313 (= D303), E341 (= E331), H385 (= H374), R386 (= R375), K411 (= K400)
- 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 (≠ A92), S169 (= S161), S170 (= S162), Q171 (= Q163), S197 (= S189), Y200 (= Y192), D313 (= D303), N336 (≠ Q326), K340 (= K330), R344 (= R334), H385 (= H374), R386 (= R375)
1x8rA Epsps liganded with the (s)-phosphonate analog of the tetrahedral reaction intermediate (see paper)
29% identity, 95% coverage: 12:409/420 of query aligns to 14:420/427 of 1x8rA
- active site: K22 (= K20), S23 (= S21), D49 (= D47), N94 (≠ E89), P119 (≠ H114), R124 (= R119), D313 (= D303), E341 (= E331), H385 (= H374), R386 (= R375), K411 (= K400)
- 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 (≠ A91), T97 (≠ A92), R124 (= R119), S169 (= S161), S170 (= S162), Q171 (= Q163), S197 (= S189), Y200 (= Y192), D313 (= D303), N336 (≠ Q326), K340 (= K330), E341 (= E331), H385 (= H374), K411 (= K400)
1g6tA Structure of epsp synthase liganded with shikimate-3-phosphate (see paper)
29% identity, 95% coverage: 12:409/420 of query aligns to 14:420/427 of 1g6tA
- active site: K22 (= K20), S23 (= S21), D49 (= D47), N94 (≠ E89), P119 (≠ H114), R124 (= R119), D313 (= D303), E341 (= E331), H385 (= H374), R386 (= R375), K411 (= K400)
- binding phosphate ion: K22 (= K20), G96 (≠ A91), T97 (≠ A92), R124 (= R119), Q171 (= Q163), E341 (= E331), K411 (= K400)
- binding shikimate-3-phosphate: K22 (= K20), S23 (= S21), R27 (= R25), T97 (≠ A92), S169 (= S161), S170 (= S162), Q171 (= Q163), S197 (= S189), Y200 (= Y192), D313 (= D303), N336 (≠ Q326), K340 (= K330)
1g6sA Structure of epsp synthase liganded with shikimate-3-phosphate and glyphosate (see paper)
29% identity, 95% coverage: 12:409/420 of query aligns to 14:420/427 of 1g6sA
- active site: K22 (= K20), S23 (= S21), D49 (= D47), N94 (≠ E89), P119 (≠ H114), R124 (= R119), D313 (= D303), E341 (= E331), H385 (= H374), R386 (= R375), K411 (= K400)
- binding glyphosate: K22 (= K20), G96 (≠ A91), R124 (= R119), Q171 (= Q163), D313 (= D303), E341 (= E331), R344 (= R334), H385 (= H374), R386 (= R375)
- binding shikimate-3-phosphate: K22 (= K20), S23 (= S21), R27 (= R25), T97 (≠ A92), S169 (= S161), S170 (= S162), Q171 (= Q163), S197 (= S189), Y200 (= Y192), D313 (= D303), N336 (≠ Q326), K340 (= K330)
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)
29% identity, 95% coverage: 12:409/420 of query aligns to 14:420/427 of P0A6D3
- KS 22:23 (= KS 20:21) binding
- R27 (= R25) binding
- NAGT 94:97 (≠ ESAA 89:92) Phosphoenolpyruvate
- G96 (≠ A91) 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 (≠ A92) 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 (≠ F96) 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 (= R119) binding
- SSQ 169:171 (= SSQ 161:163) binding
- S197 (= S189) binding
- D313 (= D303) active site, Proton acceptor; mutation to A: The enolpyruvyl transfer reaction is halted after formation of the tetrahedral adduct of the substrates.
- N336 (≠ Q326) binding
- K340 (= K330) binding
- E341 (= E331) active site, Proton donor
- R344 (= R334) binding
- R386 (= R375) binding
- C408 (= C397) Modified by bromopyruvate
- K411 (= K400) Modified by bromopyruvate; binding
3fjzA E. Coli epsp synthase (t97i) liganded with s3p and glyphosate (see paper)
29% identity, 95% coverage: 12:409/420 of query aligns to 14:420/427 of 3fjzA
- active site: K22 (= K20), S23 (= S21), D49 (= D47), N94 (≠ E89), P119 (≠ H114), R124 (= R119), D313 (= D303), E341 (= E331), H385 (= H374), R386 (= R375), K411 (= K400)
- binding N-(phosphonomethyl)glycine: K22 (= K20), G96 (≠ A91), R124 (= R119), Q171 (= Q163), D313 (= D303), E341 (= E331), R344 (= R334), H385 (= H374), R386 (= R375)
- binding shikimate-3-phosphate: K22 (= K20), S23 (= S21), R27 (= R25), I97 (≠ A92), S169 (= S161), S170 (= S162), Q171 (= Q163), S197 (= S189), Y200 (= Y192), D313 (= D303), N336 (≠ Q326), K340 (= K330)
- binding serine: I265 (≠ L255), G266 (≠ D256), S269 (= S259)
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)
29% identity, 98% coverage: 1:412/420 of query aligns to 1:424/427 of Q9S400
1rf6A Structural studies of streptococcus pneumoniae epsp synthase in s3p- glp bound state (see paper)
29% identity, 98% coverage: 1:412/420 of query aligns to 1:424/427 of 1rf6A
- active site: K20 (= K20), S21 (= S21), D47 (= D47), N90 (≠ E89), D115 (≠ H114), R120 (= R119), D312 (= D303), E340 (= E331), H384 (= H374), R385 (= R375), T412 (≠ K400)
- binding glyphosate: K20 (= K20), G92 (≠ A91), T93 (≠ A92), R120 (= R119), Q168 (= Q163), D312 (= D303), E340 (= E331), R343 (= R334), H384 (= H374), R385 (= R375)
- binding shikimate-3-phosphate: S21 (= S21), R25 (= R25), S166 (= S161), Q168 (= Q163), R193 (≠ K194), I311 (= I302), D312 (= D303), K339 (= K330)
1rf4A Structural studies of streptococcus pneumoniae epsp synthase, tetrahedral intermediate bound state (see paper)
29% identity, 98% coverage: 1:412/420 of query aligns to 1:424/427 of 1rf4A
- active site: K20 (= K20), S21 (= S21), D47 (= D47), N90 (≠ E89), D115 (≠ H114), R120 (= R119), D312 (= D303), E340 (= E331), H384 (= H374), R385 (= R375), T412 (≠ K400)
- 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 (= K20), S21 (= S21), R25 (= R25), G92 (≠ A91), T93 (≠ A92), R120 (= R119), S166 (= S161), A167 (≠ S162), Q168 (= Q163), R193 (≠ K194), D312 (= D303), K339 (= K330), E340 (= E331), R343 (= R334), H384 (= H374), R385 (= R375)
1q36A Epsp synthase (asp313ala) liganded with tetrahedral reaction intermediate (see paper)
29% identity, 95% coverage: 12:409/420 of query aligns to 14:420/427 of 1q36A
- active site: K22 (= K20), S23 (= S21), D49 (= D47), N94 (≠ E89), P119 (≠ H114), R124 (= R119), A313 (≠ D303), E341 (= E331), H385 (= H374), R386 (= R375), K411 (= K400)
- binding 5-(1-carboxy-1-phosphonooxy-ethoxyl)-4-hydroxy-3-phosphonooxy-cyclohex-1-enecarboxylic acid: K22 (= K20), S23 (= S21), R27 (= R25), G96 (≠ A91), T97 (≠ A92), R124 (= R119), S169 (= S161), S170 (= S162), Q171 (= Q163), S197 (= S189), Y200 (= Y192), N336 (≠ Q326), K340 (= K330), E341 (= E331), R344 (= R334), R386 (= R375), K411 (= K400)
4egrA 2.50 angstrom resolution structure of 3-phosphoshikimate 1- carboxyvinyltransferase (aroa) from coxiella burnetii in complex with phosphoenolpyruvate
30% identity, 96% coverage: 12:416/420 of query aligns to 15:427/434 of 4egrA
- active site: K23 (= K20), S24 (= S21), D50 (= D47), N95 (≠ E89), R125 (= R119), D313 (= D303), E341 (= E331), H384 (= H374), R385 (= R375), T411 (≠ K400)
- binding phosphoenolpyruvate: K23 (= K20), G97 (≠ A91), T98 (≠ A92), R125 (= R119), D313 (= D303), E341 (= E331), R344 (= R334), R385 (= R375)
Query Sequence
>WP_010936240.1 NCBI__GCF_000011905.1:WP_010936240.1
MKIRLDKSLPGGEIAVPSSKSYTIRGLIAAAQANGQSRIISPLAADDTLASRQVLSGLGI
DINTDAEAESWQLTGNTFKKPAGNLFCRESAATLRFMSAVCARLPFECRLLAGHSLMRRP
MLPLIQALHQLGIEIETRGNTTVIKGGEITRSKVSLPGNISSQYVSALMLMAPACKSGLE
IHLATPPASLPYLKMTKQTLESFGIKAYTSIDWQEISIPPQPYLPARYRVEGDWSSASSF
LALGAIAAPLFISNLDTESFQADRIMIKFLSEMGAEVESGQNWVKVSPKPLTAIQADLTH
SIDLLPALAITAACAKGQSILSGVRQARIKESNRIRAVSQGLSAMGINVTEEDDRLIIEG
GMPRGAEIDSLGDHRIAMAFGALGAVTGETCISEAECVSKTYPDFWQKLESLGGKVIKDV
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