SitesBLAST
Comparing 8501011 FitnessBrowser__Miya:8501011 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)
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
37% identity, 98% coverage: 10:448/450 of query aligns to 16:424/426 of 3nvsA
- active site: K22 (= K16), S23 (= S17), D49 (= D43), N94 (≠ E89), P119 (= P114), R124 (= R119), H128 (≠ E123), Q135 (≠ G130), Y142 (= Y137), E144 (≠ G139), A247 (= A262), A255 (= A270), D314 (= D329), E342 (= E357), H386 (= H410), R387 (= R411), K412 (= K436)
- binding glyphosate: K22 (= K16), G96 (= G91), R124 (= R119), Q172 (= Q167), D314 (= D329), E342 (= E357), R345 (= R360), H386 (= H410), R387 (= R411)
- binding magnesium ion: E123 (= E118), Q145 (≠ R140)
- binding shikimate-3-phosphate: K22 (= K16), S23 (= S17), R27 (= R21), T97 (= T92), S170 (= S165), S171 (= S166), Q172 (= Q167), S198 (= S193), Y201 (= Y196), D314 (= D329), N337 (≠ H352), K341 (= K356)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: S23 (= S17), R27 (= R21), Q172 (= Q167), Y201 (= Y196), D314 (= D329), K341 (= K356)
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)
37% identity, 98% coverage: 10:448/450 of query aligns to 16:424/426 of Q9KRB0
7tm6A Crystal structure of shikimate-3-phosphate and glyphosate bound 3- phosphoshikimate 1-carboxyvinyltransferase from klebsiella pneumoniae
38% identity, 98% coverage: 9:448/450 of query aligns to 14:422/426 of 7tm6A
- binding glyphosate: K21 (= K16), G95 (= G91), R123 (= R119), Q170 (= Q167), D312 (= D329), E340 (= E357), R343 (= R360), H384 (= H410), R385 (= R411)
- binding shikimate-3-phosphate: S22 (= S17), R26 (= R21), T96 (= T92), S168 (= S165), S169 (= S166), Q170 (= Q167), S196 (= S193), Y199 (= Y196), D312 (= D329), N335 (≠ H352), K339 (= K356)
7tm5B Crystal structure of shikimate-3-phosphate bound 3-phosphoshikimate 1- carboxyvinyltransferase from klebsiella pneumoniae
38% identity, 98% coverage: 9:448/450 of query aligns to 15:423/427 of 7tm5B
- binding shikimate-3-phosphate: K22 (= K16), S23 (= S17), R27 (= R21), S169 (= S165), S170 (= S166), Q171 (= Q167), S197 (= S193), Y200 (= Y196), D313 (= D329), N336 (≠ H352), K340 (= K356)
2pq9A E. Coli epsps liganded with (r)-difluoromethyl tetrahedral reaction intermediate analog (see paper)
37% identity, 98% coverage: 9:448/450 of query aligns to 15:423/427 of 2pq9A
- active site: K22 (= K16), S23 (= S17), D49 (= D43), N94 (≠ E89), P119 (= P114), R124 (= R119), D313 (= D329), E341 (= E357), H385 (= H410), R386 (= R411), K411 (= K436)
- 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 (= K16), S23 (= S17), R27 (= R21), G96 (= G91), T97 (= T92), R124 (= R119), S169 (= S165), S170 (= S166), Q171 (= Q167), S197 (= S193), Y200 (= Y196), D313 (= D329), N336 (≠ H352), K340 (= K356), R344 (= R360), H385 (= H410), R386 (= R411), K411 (= K436)
2aa9A Epsp synthase liganded with shikimate (see paper)
37% identity, 98% coverage: 9:448/450 of query aligns to 15:423/427 of 2aa9A
- active site: K22 (= K16), S23 (= S17), D49 (= D43), N94 (≠ E89), P119 (= P114), R124 (= R119), D313 (= D329), E341 (= E357), H385 (= H410), R386 (= R411), K411 (= K436)
- binding (3r,4s,5r)-3,4,5-trihydroxycyclohex-1-ene-1-carboxylic acid: K22 (= K16), S23 (= S17), R27 (= R21), T97 (= T92), Q171 (= Q167), Y200 (= Y196), D313 (= D329), K340 (= K356)
1x8tA Epsps liganded with the (r)-phosphonate analog of the tetrahedral reaction intermediate (see paper)
37% identity, 98% coverage: 9:448/450 of query aligns to 15:423/427 of 1x8tA
- active site: K22 (= K16), S23 (= S17), D49 (= D43), N94 (≠ E89), P119 (= P114), R124 (= R119), D313 (= D329), E341 (= E357), H385 (= H410), R386 (= R411), K411 (= K436)
- binding [3r-[3a,4a,5b(r*)]]-5-(1-carboxy-1-phosphonoethoxy)-4-hydroxy-3-(phosphonooxy)-1-cyclohexene-1-carboxylic acid: K22 (= K16), S23 (= S17), R27 (= R21), T97 (= T92), S169 (= S165), S170 (= S166), Q171 (= Q167), S197 (= S193), Y200 (= Y196), D313 (= D329), N336 (≠ H352), K340 (= K356), R344 (= R360), H385 (= H410), R386 (= R411)
1x8rA Epsps liganded with the (s)-phosphonate analog of the tetrahedral reaction intermediate (see paper)
37% identity, 98% coverage: 9:448/450 of query aligns to 15:423/427 of 1x8rA
- active site: K22 (= K16), S23 (= S17), D49 (= D43), N94 (≠ E89), P119 (= P114), R124 (= R119), D313 (= D329), E341 (= E357), H385 (= H410), R386 (= R411), K411 (= K436)
- binding [3r-[3a,4a,5b(s*)]]-5-(1-carboxy-1-phosphonoethoxy)-4-hydroxy-3-(phosphonooxy)-1-cyclohexene-1-carboxylic acid: K22 (= K16), S23 (= S17), R27 (= R21), G96 (= G91), T97 (= T92), R124 (= R119), S169 (= S165), S170 (= S166), Q171 (= Q167), S197 (= S193), Y200 (= Y196), D313 (= D329), N336 (≠ H352), K340 (= K356), E341 (= E357), H385 (= H410), K411 (= K436)
1g6tA Structure of epsp synthase liganded with shikimate-3-phosphate (see paper)
37% identity, 98% coverage: 9:448/450 of query aligns to 15:423/427 of 1g6tA
- active site: K22 (= K16), S23 (= S17), D49 (= D43), N94 (≠ E89), P119 (= P114), R124 (= R119), D313 (= D329), E341 (= E357), H385 (= H410), R386 (= R411), K411 (= K436)
- binding phosphate ion: K22 (= K16), G96 (= G91), T97 (= T92), R124 (= R119), Q171 (= Q167), E341 (= E357), K411 (= K436)
- binding shikimate-3-phosphate: K22 (= K16), S23 (= S17), R27 (= R21), T97 (= T92), S169 (= S165), S170 (= S166), Q171 (= Q167), S197 (= S193), Y200 (= Y196), D313 (= D329), N336 (≠ H352), K340 (= K356)
1g6sA Structure of epsp synthase liganded with shikimate-3-phosphate and glyphosate (see paper)
37% identity, 98% coverage: 9:448/450 of query aligns to 15:423/427 of 1g6sA
- active site: K22 (= K16), S23 (= S17), D49 (= D43), N94 (≠ E89), P119 (= P114), R124 (= R119), D313 (= D329), E341 (= E357), H385 (= H410), R386 (= R411), K411 (= K436)
- binding glyphosate: K22 (= K16), G96 (= G91), R124 (= R119), Q171 (= Q167), D313 (= D329), E341 (= E357), R344 (= R360), H385 (= H410), R386 (= R411)
- binding shikimate-3-phosphate: K22 (= K16), S23 (= S17), R27 (= R21), T97 (= T92), S169 (= S165), S170 (= S166), Q171 (= Q167), S197 (= S193), Y200 (= Y196), D313 (= D329), N336 (≠ H352), K340 (= K356)
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)
37% identity, 98% coverage: 9:448/450 of query aligns to 15:423/427 of P0A6D3
- KS 22:23 (= KS 16:17) binding
- R27 (= R21) binding
- NAGT 94:97 (≠ ESGT 89:92) Phosphoenolpyruvate
- G96 (= G91) 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 (= T92) 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 (≠ L96) 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 165:167) binding
- S197 (= S193) binding
- D313 (= D329) active site, Proton acceptor; mutation to A: The enolpyruvyl transfer reaction is halted after formation of the tetrahedral adduct of the substrates.
- N336 (≠ H352) binding
- K340 (= K356) binding
- E341 (= E357) active site, Proton donor
- R344 (= R360) binding
- R386 (= R411) binding
- C408 (= C433) Modified by bromopyruvate
- K411 (= K436) Modified by bromopyruvate; binding
3fjzA E. Coli epsp synthase (t97i) liganded with s3p and glyphosate (see paper)
36% identity, 98% coverage: 9:448/450 of query aligns to 15:423/427 of 3fjzA
- active site: K22 (= K16), S23 (= S17), D49 (= D43), N94 (≠ E89), P119 (= P114), R124 (= R119), D313 (= D329), E341 (= E357), H385 (= H410), R386 (= R411), K411 (= K436)
- binding N-(phosphonomethyl)glycine: K22 (= K16), G96 (= G91), R124 (= R119), Q171 (= Q167), D313 (= D329), E341 (= E357), R344 (= R360), H385 (= H410), R386 (= R411)
- binding shikimate-3-phosphate: K22 (= K16), S23 (= S17), R27 (= R21), I97 (≠ T92), S169 (= S165), S170 (= S166), Q171 (= Q167), S197 (= S193), Y200 (= Y196), D313 (= D329), N336 (≠ H352), K340 (= K356)
- binding serine: I265 (≠ L281), G266 (≠ R282), S269 (= S285)
1q36A Epsp synthase (asp313ala) liganded with tetrahedral reaction intermediate (see paper)
36% identity, 98% coverage: 9:448/450 of query aligns to 15:423/427 of 1q36A
- active site: K22 (= K16), S23 (= S17), D49 (= D43), N94 (≠ E89), P119 (= P114), R124 (= R119), A313 (≠ D329), E341 (= E357), H385 (= H410), R386 (= R411), K411 (= K436)
- binding 5-(1-carboxy-1-phosphonooxy-ethoxyl)-4-hydroxy-3-phosphonooxy-cyclohex-1-enecarboxylic acid: K22 (= K16), S23 (= S17), R27 (= R21), G96 (= G91), T97 (= T92), R124 (= R119), S169 (= S165), S170 (= S166), Q171 (= Q167), S197 (= S193), Y200 (= Y196), N336 (≠ H352), K340 (= K356), E341 (= E357), R344 (= R360), R386 (= R411), K411 (= K436)
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, 98% coverage: 9:447/450 of query aligns to 88:512/516 of P11043
- G173 (= G91) mutation to A: Resistance to glyphosate due to a lower affinity. Slight reduction in EPSP synthase activity.
7m0oA Dgt-28 epsps (see paper)
38% identity, 97% coverage: 13:449/450 of query aligns to 3:398/400 of 7m0oA
6hqvA Pentafunctional arom complex from chaetomium thermophilum (see paper)
33% identity, 97% coverage: 7:443/450 of query aligns to 399:822/1555 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
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, 98% coverage: 4:443/450 of query aligns to 403:834/1583 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
7tbuA Crystal structure of the 5-enolpyruvate-shikimate-3-phosphate synthase (epsps) domain of aro1 from candida albicans in complex with shikimate-3-phosphate (see paper)
31% identity, 98% coverage: 5:443/450 of query aligns to 14:439/450 of 7tbuA
2o0zA Mycobacterium tuberculosis epsp synthase in complex with product (eps)
34% identity, 99% coverage: 5:448/450 of query aligns to 14:422/424 of 2o0zA
- active site: D54 (= D43), L94 (≠ V87), E311 (≠ D329), E341 (= E357), H384 (= H410), R385 (= R411), K410 (= K436)
- binding 5-[(1-carboxyvinyl)oxy]-4-hydroxy-3-(phosphonooxy)cyclohex-1-ene-1-carboxylic acid: K23 (= K16), S24 (= S17), R28 (= R21), S167 (= S165), S168 (= S166), Q169 (= Q167), S196 (= S193), E311 (≠ D329), H336 (= H352), H340 (≠ K356), R344 (= R360), H384 (= H410), R385 (= R411)
2o0xA Mycobacterium tuberculosis epsp synthase in complex with intermediate
34% identity, 99% coverage: 5:448/450 of query aligns to 14:422/424 of 2o0xA
- active site: D54 (= D43), L94 (≠ V87), E311 (≠ D329), E341 (= E357), H384 (= H410), R385 (= R411), K410 (= K436)
- binding 5-(1-carboxy-1-phosphonooxy-ethoxyl)-4-hydroxy-3-phosphonooxy-cyclohex-1-enecarboxylic acid: K23 (= K16), S24 (= S17), R28 (= R21), G96 (= G91), R124 (= R119), S167 (= S165), S168 (= S166), Q169 (= Q167), S196 (= S193), H199 (≠ Y196), E311 (≠ D329), H340 (≠ K356), E341 (= E357), R344 (= R360), R385 (= R411), K410 (= K436)
Query Sequence
>8501011 FitnessBrowser__Miya:8501011
METKRETVTVAAPPSKSVSHRMLIGAALAAGDSVVEHVLESRDIERTADILRAAGARIER
QGDGRFAVSGVAGTPAGGFDAPVSCDVHESGTTCRLLTAVLAAGKGQFRIHGAPRMHERP
IGELVDVLRGRGVRVTYEGREGCPPLLIDSDGMSGGSTAIGLGESSQYLSGLLLAAPLTS
GLTIEVSGDKVVSWPYVALTLQALEDFGIGFRVETRETPRGKWQADDWRMLREVRPGLVR
FVVSPGVYRAGNYRVEGDWSNASYFLAAGAVGPRPVRVAGLRVDSLQGDRAMLDILGRMG
ARFERADNGVVVAPSSLTGVEVDMGHCPDLVPTVAATAAFAQGVTTIRNVAHLRIKECDR
LSAPAAELRKAGVRVEELDDGLIVHGSLRSGGPAPVIDEKVMPFLSYGDHRMAMSLALLG
FAGVHVVLDDPACVAKSFPHFWNEWEKVRA
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