SitesBLAST
Comparing GFF2590 FitnessBrowser__WCS417:GFF2590 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)
P0AEJ2 Isochorismate synthase EntC; Isochorismate mutase; EC 5.4.4.2 from Escherichia coli (strain K12) (see paper)
33% identity, 79% coverage: 85:444/455 of query aligns to 59:384/391 of P0AEJ2
- T140 (≠ I201) binding
- T142 (≠ A203) binding
- V145 (≠ L206) binding
- D146 (≠ N207) binding
- G214 (= G274) binding
- S215 (= S275) binding
- E241 (= E301) binding ; binding
- A303 (= A363) binding ; mutation to T: Loss of mutase activity.
- L304 (≠ V364) mutation to A: Loss of mutase activity.
- F327 (≠ Y387) mutation to Y: Loss of mutase activity.
- I346 (≠ L406) mutation to L: Loss of mutase activity.
- R347 (= R407) binding
- F359 (= F419) mutation to Q: Loss of mutase activity.
- G361 (= G421) binding
- E376 (= E436) binding
- K380 (= K440) binding
3hwoA Crystal structure of escherichia coli enterobactin-specific isochorismate synthase entc in complex with isochorismate (see paper)
33% identity, 79% coverage: 85:444/455 of query aligns to 47:372/379 of 3hwoA
- active site: K135 (= K208), E185 (= E257), A201 (= A273), E229 (= E301), H264 (= H336), A291 (= A363), F315 (≠ Y387), R335 (= R407), G351 (= G423), E364 (= E436), K368 (= K440)
- binding (5S,6S)-5-[(1-carboxyethenyl)oxy]-6-hydroxycyclohexa-1,3-diene-1-carboxylic acid: G202 (= G274), S203 (= S275), E229 (= E301), H264 (= H336), I334 (≠ L406), R335 (= R407), A348 (= A420), G349 (= G421), E364 (= E436), K368 (= K440)
- binding magnesium ion: T128 (≠ I201), T130 (≠ A203), V133 (≠ L206), D134 (≠ N207), E229 (= E301), E364 (= E436)
5jy8A An iron-bound structure of the isochorismate synthase entc (see paper)
34% identity, 79% coverage: 85:444/455 of query aligns to 44:362/368 of 5jy8A
- active site: K125 (= K208), E175 (= E257), A191 (= A273), E219 (= E301), H254 (= H336), A281 (= A363), F305 (≠ Y387), R325 (= R407), G341 (= G423), E354 (= E436), K358 (= K440)
- binding fe (iii) ion: E219 (= E301), E237 (≠ D319), H239 (≠ Q321), E354 (= E436)
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: E175 (= E257), L190 (= L272), A191 (= A273), G192 (= G274), E219 (= E301), L282 (≠ V364), I324 (≠ L406), F337 (= F419), A338 (= A420), G339 (= G421), E354 (= E436), K358 (= K440)
5jxzA A low magnesium structure of the isochorismate synthase, entc (see paper)
34% identity, 79% coverage: 85:444/455 of query aligns to 45:367/373 of 5jxzA
- active site: K130 (= K208), E180 (= E257), A196 (= A273), E224 (= E301), H259 (= H336), A286 (= A363), F310 (≠ Y387), R330 (= R407), G346 (= G423), E359 (= E436), K363 (= K440)
- binding (5S,6S)-5-[(1-carboxyethenyl)oxy]-6-hydroxycyclohexa-1,3-diene-1-carboxylic acid: L195 (= L272), G197 (= G274), S198 (= S275), E224 (= E301), A286 (= A363), I329 (≠ L406), R330 (= R407), A343 (= A420), G344 (= G421), E359 (= E436), K363 (= K440)
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: E180 (= E257), L195 (= L272), A196 (= A273), G197 (= G274), E224 (= E301), A286 (= A363), I329 (≠ L406), R330 (= R407), G344 (= G421), A345 (≠ C422), E359 (= E436), K363 (= K440)
- binding magnesium ion: E224 (= E301), E359 (= E436)
3bznA Crystal structure of open form of menaquinone-specific isochorismate synthase, menf (see paper)
38% identity, 57% coverage: 190:448/455 of query aligns to 172:428/430 of 3bznA
- active site: K190 (= K208), E240 (= E257), A256 (= A273), E284 (= E301), H318 (= H336), A344 (= A363), Y368 (= Y387), R387 (= R407), G403 (= G423), E416 (= E436), K420 (= K440)
- binding magnesium ion: E284 (= E301), E416 (= E436)
P38051 Isochorismate synthase MenF; Isochorismate hydroxymutase; Isochorismate mutase; EC 5.4.4.2 from Escherichia coli (strain K12) (see 2 papers)
38% identity, 57% coverage: 190:448/455 of query aligns to 172:428/431 of P38051
- K190 (= K208) active site, Proton acceptor; mutation to A: Lack of activity.
- E240 (= E257) active site, Proton donor; mutation to Q: Lack of activity.
- L255 (= L272) mutation to A: Decrease in activity.
- E284 (= E301) binding
- A344 (= A363) mutation to T: Lack of activity.
- R387 (= R407) mutation to A: Lack of activity.
- E416 (= E436) binding
P45744 Isochorismate synthase DhbC; Isochorismate mutase; EC 5.4.4.2 from Bacillus subtilis (strain 168) (see paper)
33% identity, 57% coverage: 190:448/455 of query aligns to 127:393/398 of P45744
- S271 (≠ H327) modified: Phosphoserine
A0QX93 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
31% identity, 61% coverage: 162:440/455 of query aligns to 223:507/524 of A0QX93
- K355 (≠ E290) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
30% identity, 62% coverage: 161:440/455 of query aligns to 201:486/505 of 5cwaA
- active site: Q248 (≠ K208), E301 (= E257), A317 (= A273), E345 (= E301), H382 (= H336), T409 (≠ A363), Y433 (= Y387), R453 (= R407), G469 (= G423), E482 (= E436), K486 (= K440)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y387), I452 (≠ L406), A466 (= A420), G467 (= G421), K486 (= K440)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
30% identity, 61% coverage: 162:440/455 of query aligns to 202:482/499 of 7bvdA
- active site: Q248 (≠ K208), E301 (= E257), A317 (= A273), E341 (= E301), H378 (= H336), T405 (≠ A363), Y429 (= Y387), R449 (= R407), G465 (= G423), E478 (= E436), K482 (= K440)
Sites not aligning to the query:
O94582 Probable anthranilate synthase component 1; Anthranilate synthase component I; EC 4.1.3.27 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
30% identity, 57% coverage: 190:448/455 of query aligns to 215:474/489 of O94582
- S390 (≠ G365) modified: Phosphoserine
- S392 (≠ L367) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
7pi1DDD Aminodeoxychorismate synthase component 1
27% identity, 56% coverage: 194:450/455 of query aligns to 199:455/459 of 7pi1DDD
Sites not aligning to the query:
P28820 Aminodeoxychorismate synthase component 1; ADC synthase; ADCS; 4-amino-4-deoxychorismate synthase component 1; EC 2.6.1.85 from Bacillus subtilis (strain 168) (see paper)
26% identity, 63% coverage: 166:450/455 of query aligns to 174:462/470 of P28820
- A283 (= A273) mutation to I: Complete loss of aminodeoxychorismate synthase activity.; mutation to K: Absence of covalent intermediate.; mutation to V: Complete loss of aminodeoxychorismate synthase activity.
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
27% identity, 60% coverage: 180:450/455 of query aligns to 281:569/577 of Q94GF1
- D323 (= D224) mutation to N: Insensitive to feedback inhibition by tryptophan.
P32068 Anthranilate synthase alpha subunit 1, chloroplastic; Anthranilate synthase component 1-1; Anthranilate synthase component I-1; Protein A-METHYL TRYPTOPHAN RESISTANT 1; Protein JASMONATE-INDUCED DEFECTIVE LATERAL ROOT 1; Protein TRYPTOPHAN BIOSYNTHESIS 5; Protein WEAK ETHYLENE INSENSITIVE 2; EC 4.1.3.27 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
25% identity, 64% coverage: 158:450/455 of query aligns to 269:587/595 of P32068
- D341 (= D224) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
2fn1A Crystal structures of yersinia enterocolitica salicylate synthase (irp9) in complex with the reaction products salicylate and pyruvate (see paper)
28% identity, 61% coverage: 174:450/455 of query aligns to 134:408/408 of 2fn1A
- active site: K167 (= K208), E214 (= E257), A230 (= A273), E258 (= E301), H295 (= H336), T322 (≠ A363), Y346 (= Y387), R365 (= R407), G381 (= G423), E394 (= E436), K398 (= K440)
- binding magnesium ion: E258 (= E301), E394 (= E436)
- binding pyruvic acid: Y346 (= Y387), L364 (= L406), R365 (= R407), A378 (= A420), G379 (= G421), K398 (= K440)
2fn0A Crystal structure of yersinia enterocolitica salicylate synthase (irp9) (see paper)
28% identity, 61% coverage: 174:450/455 of query aligns to 134:408/408 of 2fn0A
- active site: K167 (= K208), E214 (= E257), A230 (= A273), E258 (= E301), H295 (= H336), T322 (≠ A363), Y346 (= Y387), R365 (= R407), G381 (= G423), E394 (= E436), K398 (= K440)
- binding acetate ion: Y346 (= Y387), L364 (= L406), R365 (= R407), A378 (= A420), G379 (= G421)
- binding magnesium ion: E258 (= E301), E394 (= E436)
- binding phosphate ion: A230 (= A273), G231 (= G274), T232 (≠ S275), E258 (= E301), G381 (= G423), E394 (= E436), K398 (= K440)
5jy9B An iron-bound structure of the salicylate synthase irp9 (see paper)
28% identity, 59% coverage: 184:450/455 of query aligns to 159:424/424 of 5jy9B
- active site: K183 (= K208), E230 (= E257), A246 (= A273), E274 (= E301), H311 (= H336), T338 (≠ A363), Y362 (= Y387), R381 (= R407), G397 (= G423), E410 (= E436), K414 (= K440)
- binding fe (ii) ion: E274 (= E301), E410 (= E436)
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
27% identity, 72% coverage: 121:448/455 of query aligns to 172:510/520 of P00898
- C174 (≠ S123) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N237) mutation to D: Decrease in feedback control by tryptophan.
- P289 (≠ A238) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ L241) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F242) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G253) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ P340) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G398) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ L403) mutation to Y: Complete loss of feedback control by tryptophan. 4-fold decrease of affinity binding for chorismate.
Sites not aligning to the query:
- 39 E→K: Complete loss of feedback control by tryptophan.
- 40 binding ; S→F: Complete loss of feedback control by tryptophan.
- 41 A→V: Decrease in feedback control by tryptophan.
- 50 binding
- 128 R→H: Almost no change in feedback control by tryptophan.
- 515 H→Y: Almost no change in feedback control by tryptophan.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
27% identity, 72% coverage: 121:448/455 of query aligns to 168:506/512 of 1i1qA
- active site: Q259 (≠ K208), E305 (= E257), A323 (= A273), E357 (= E301), H394 (= H336), T421 (vs. gap), Y445 (= Y387), R465 (= R407), G481 (= G423), E494 (= E436), K498 (= K440)
- binding tryptophan: P287 (vs. gap), Y288 (≠ H240), M289 (≠ L241), G450 (= G392), C461 (≠ L403)
Sites not aligning to the query:
Query Sequence
>GFF2590 FitnessBrowser__WCS417:GFF2590
MNENALLKVFQTAHQRAVAYQRPVMAVSSYAAPTLEALALYEAHRQGFFWCTHSPDLALF
GLGCAWQIEASGPRRMLDVDRQWFALCADAVIVGSKAPLLLGGMRFDEQRPCAPHWAAFA
DASFHLAHWLLSEDAHGRWLRCQRVVGPDSDPQALARDSLAAYAQLLNPPAATATAPDVI
ERIALPSRQWQGKVDRALQAISAGDLNKVVLARHIEYQLDASLDSGAVMQRLHARSNASH
LFALHRGEHCFMGATPERLLSCQEGRLTTHALAGSARRGMTANEDHAIGERLLADPKEQH
EHRLVVQTITQALDGKVSDLQAASSPHLLKLANVQHLSTPIMAQLNSDKRLLDGIHALHP
TPAVGGLPTATAMDFIRRHEGFDRGWYAAPVGWLDSQGNGDFLVALRSALIAPRHCHLFA
GCGIVEGSQPAEEYEETQIKLASMEQALLLVPPRP
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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