SitesBLAST
Comparing 209297 MicrobesOnline__882:209297 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)
P05041 Aminodeoxychorismate synthase component 1; ADC synthase; ADCS; 4-amino-4-deoxychorismate synthase component 1; EC 2.6.1.85 from Escherichia coli (strain K12) (see 4 papers)
39% identity, 85% coverage: 48:332/334 of query aligns to 173:450/453 of P05041
- E258 (= E135) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (= K151) mutation to A: Absence of covalent intermediate. Addition of ammonia allows the formation of the covalent intermediate and shows that ammonia can replace the function of K-274. Reduced catalytic efficiency.; mutation to R: Absence of covalent intermediate.; mutation to R: Reduced catalytic efficiency.
- G275 (= G152) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R191) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (≠ A196) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S202) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (≠ Q219) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
Sites not aligning to the query:
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
38% identity, 85% coverage: 48:332/334 of query aligns to 171:434/437 of 1k0eA
- active site: E256 (= E135), K272 (= K151), E286 (= E182), H323 (≠ Q219), S350 (= S246), W374 (≠ Y270), R394 (= R290), G410 (= G308), E423 (= E321), K427 (= K325)
- binding tryptophan: P238 (= P117), F239 (= F118), S240 (≠ A119)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
36% identity, 85% coverage: 48:332/334 of query aligns to 173:417/420 of 1k0gA
- active site: E258 (= E135), K274 (= K151), E278 (= E182), S333 (= S246), W357 (≠ Y270), R377 (= R290), G393 (= G308), E406 (= E321), K410 (= K325)
- binding phosphate ion: D347 (≠ E260), R353 (≠ P266)
- binding tryptophan: P240 (= P117), F241 (= F118), S242 (≠ A119)
Sites not aligning to the query:
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
36% identity, 85% coverage: 48:332/334 of query aligns to 173:414/415 of 1k0gB
- active site: E258 (= E135), K274 (= K151), E277 (= E182), S330 (= S246), W354 (≠ Y270), R374 (= R290), G390 (= G308), E403 (= E321), K407 (= K325)
- binding phosphate ion: D344 (≠ E260), R350 (≠ P266)
- binding tryptophan: P240 (= P117), F241 (= F118)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
40% identity, 79% coverage: 65:329/334 of query aligns to 407:666/673 of 8hx8A
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
40% identity, 79% coverage: 65:329/334 of query aligns to 368:627/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I150), K454 (= K151), G455 (= G152), T456 (= T153), M547 (≠ V247), Y570 (= Y270), R590 (= R290), V603 (≠ A305), G604 (= G306), G605 (≠ S307), A606 (≠ G308), E619 (= E321), K623 (= K325)
- binding tryptophan: P419 (= P117), Y420 (≠ F118), G421 (≠ A119), L574 (= L274), G575 (≠ V275)
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)
34% identity, 79% coverage: 69:331/334 of query aligns to 202:458/470 of P28820
- A283 (≠ K151) 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.
7pi1DDD Aminodeoxychorismate synthase component 1
34% identity, 79% coverage: 69:331/334 of query aligns to 195:451/459 of 7pi1DDD
Sites not aligning to the query:
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)
32% identity, 83% coverage: 52:327/334 of query aligns to 287:579/595 of P32068
- D341 (= D102) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
33% identity, 80% coverage: 63:329/334 of query aligns to 285:563/577 of Q94GF1
- D323 (= D102) mutation to N: Insensitive to feedback inhibition by tryptophan.
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)
34% identity, 77% coverage: 69:325/334 of query aligns to 215:466/489 of O94582
- S390 (≠ T248) modified: Phosphoserine
- S392 (≠ C250) modified: Phosphoserine
Sites not aligning to the query:
- 488 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)
33% identity, 78% coverage: 69:328/334 of query aligns to 251:510/524 of A0QX93
- K355 (≠ A171) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
33% identity, 78% coverage: 69:328/334 of query aligns to 230:485/499 of 7bvdA
- active site: Q248 (= Q87), E301 (= E135), A317 (≠ K151), E341 (= E182), H378 (≠ Q219), T405 (≠ S246), Y429 (= Y270), R449 (= R290), G465 (= G308), E478 (= E321), K482 (= K325)
Sites not aligning to the query:
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
33% identity, 77% coverage: 73:328/334 of query aligns to 234:489/505 of 5cwaA
- active site: Q248 (= Q87), E301 (= E135), A317 (≠ K151), E345 (= E182), H382 (≠ Q219), T409 (≠ S246), Y433 (= Y270), R453 (= R290), G469 (= G308), E482 (= E321), K486 (= K325)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y270), I452 (= I289), A466 (= A305), G467 (= G306), K486 (= K325)
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
30% identity, 78% coverage: 73:334/334 of query aligns to 245:507/512 of 1i1qA
- active site: Q259 (= Q87), E305 (= E135), A323 (≠ K151), E357 (= E182), H394 (≠ Q219), T421 (≠ S246), Y445 (= Y270), R465 (= R290), G481 (= G308), E494 (= E321), K498 (= K325)
- binding tryptophan: P287 (= P117), Y288 (≠ F118), M289 (≠ A119), G450 (≠ V275), C461 (≠ S286)
Sites not aligning to the query:
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
30% identity, 78% coverage: 73:334/334 of query aligns to 249:511/520 of P00898
- N288 (≠ R114) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P115) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ A119) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ A120) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S131) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ D223) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (≠ R281) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ S286) 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.
- 174 C→Y: Almost no change in feedback control by tryptophan.
- 515 H→Y: Almost no change in feedback control by tryptophan.
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
30% identity, 80% coverage: 69:334/334 of query aligns to 236:502/511 of 1i7sA
- active site: Q254 (= Q87), E300 (= E135), A318 (≠ K151), E352 (= E182), H389 (≠ Q219), T416 (≠ S246), Y440 (= Y270), R460 (= R290), G476 (= G308), E489 (= E321), K493 (= K325)
- binding tryptophan: P282 (= P117), Y283 (≠ F118), M284 (≠ A119), V444 (≠ L274), G445 (≠ V275), D454 (= D284), C456 (≠ S286)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
30% identity, 78% coverage: 73:334/334 of query aligns to 246:508/517 of 1i7qA
- active site: Q260 (= Q87), E306 (= E135), A324 (≠ K151), E358 (= E182), H395 (≠ Q219), T422 (≠ S246), Y446 (= Y270), R466 (= R290), G482 (= G308), E495 (= E321), K499 (= K325)
- binding magnesium ion: E358 (= E182), E495 (= E321)
- binding pyruvic acid: Y446 (= Y270), I465 (= I289), R466 (= R290), A479 (= A305), G480 (= G306), K499 (= K325)
2fn1A Crystal structures of yersinia enterocolitica salicylate synthase (irp9) in complex with the reaction products salicylate and pyruvate (see paper)
28% identity, 83% coverage: 52:329/334 of query aligns to 135:402/408 of 2fn1A
- active site: K167 (≠ Q87), E214 (= E135), A230 (≠ K151), E258 (= E182), H295 (≠ Q219), T322 (≠ S246), Y346 (= Y270), R365 (= R290), G381 (= G308), E394 (= E321), K398 (= K325)
- binding magnesium ion: E258 (= E182), E394 (= E321)
- binding pyruvic acid: Y346 (= Y270), L364 (≠ I289), R365 (= R290), A378 (= A305), G379 (= G306), K398 (= K325)
2fn0A Crystal structure of yersinia enterocolitica salicylate synthase (irp9) (see paper)
28% identity, 83% coverage: 52:329/334 of query aligns to 135:402/408 of 2fn0A
- active site: K167 (≠ Q87), E214 (= E135), A230 (≠ K151), E258 (= E182), H295 (≠ Q219), T322 (≠ S246), Y346 (= Y270), R365 (= R290), G381 (= G308), E394 (= E321), K398 (= K325)
- binding acetate ion: Y346 (= Y270), L364 (≠ I289), R365 (= R290), A378 (= A305), G379 (= G306)
- binding magnesium ion: E258 (= E182), E394 (= E321)
- binding phosphate ion: A230 (≠ K151), G231 (= G152), T232 (= T153), E258 (= E182), G381 (= G308), E394 (= E321), K398 (= K325)
Query Sequence
>209297 MicrobesOnline__882:209297
MRQEKQGAPRAAATGKGSGGDGGDNPYGDVRNHGEGRGLSAAPRDGTAPGDDLALALDEL
VPSLDATTYPDGVRQVLAAIRRGDTYQLNLTSRFTARRPGMDAAAFLLRLWQQRPTPFAA
YLHAGRHRILSLSPERFLRVGGGEVLAQPIKGTRSFDPATTSPGERARLEAALRADPKEH
AELSMVVDLLRNDISATCAYDSVRVPRHCATFAVGPLIQMCSDVTGTLRDGTTCLDLLRH
AFPGGSVTGCPKPRTMSLIERIEPHPRDVYCGSLVAVAGPRDMDSSIAIRTAMYDTTTGL
LHLYAGSGLTVDSDPEGEYRETVDKTSAFRKETA
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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