SitesBLAST
Comparing WP_089300784.1 NCBI__GCF_900188115.1:WP_089300784.1 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)
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)
68% identity, 89% coverage: 15:502/546 of query aligns to 28:512/524 of A0QX93
- K355 (= K345) 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)
68% identity, 89% coverage: 15:502/546 of query aligns to 8:491/505 of 5cwaA
- active site: Q248 (= Q256), E301 (= E312), A317 (= A328), E345 (= E356), H382 (= H393), T409 (= T420), Y433 (= Y444), R453 (= R464), G469 (= G480), E482 (= E493), K486 (= K497)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y444), I452 (= I463), A466 (= A477), G467 (= G478), K486 (= K497)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
68% identity, 89% coverage: 15:502/546 of query aligns to 8:487/499 of 7bvdA
- active site: Q248 (= Q256), E301 (= E312), A317 (= A328), E341 (= E356), H378 (= H393), T405 (= T420), Y429 (= Y444), R449 (= R464), G465 (= G480), E478 (= E493), K482 (= K497)
- binding pyruvic acid: S93 (= S101), G94 (= G102), A100 (= A108)
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)
38% identity, 92% coverage: 11:511/546 of query aligns to 2:480/489 of O94582
- S390 (≠ T422) modified: Phosphoserine
- S392 (≠ A424) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
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)
39% identity, 89% coverage: 23:510/546 of query aligns to 74:590/595 of P32068
- D341 (= D270) 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)
39% identity, 92% coverage: 11:510/546 of query aligns to 45:572/577 of Q94GF1
- D323 (= D270) mutation to N: Insensitive to feedback inhibition by tryptophan.
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)
38% identity, 89% coverage: 30:515/546 of query aligns to 6:470/470 of P28820
- A283 (= A328) 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
38% identity, 88% coverage: 30:509/546 of query aligns to 4:457/459 of 7pi1DDD
- binding magnesium ion: G428 (= G480), E438 (= E490)
- binding tryptophan: L33 (≠ F59), E34 (= E60), S35 (= S61), G39 (= G65), Y41 (≠ W71), P242 (= P285), Y243 (= Y286), M244 (= M287), Q406 (≠ D458), N408 (≠ A460)
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
37% identity, 88% coverage: 30:508/546 of query aligns to 2:509/512 of 1i1qA
- active site: Q259 (= Q256), E305 (= E312), A323 (= A328), E357 (= E356), H394 (= H393), T421 (= T420), Y445 (= Y444), R465 (= R464), G481 (= G480), E494 (= E493), K498 (= K497)
- binding tryptophan: L34 (≠ F59), E35 (= E60), S36 (= S61), K46 (≠ W71), P287 (= P285), Y288 (= Y286), M289 (= M287), G450 (= G449), C461 (≠ A460)
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
37% identity, 88% coverage: 30:508/546 of query aligns to 6:513/520 of P00898
- E39 (= E60) mutation to K: Complete loss of feedback control by tryptophan.
- S40 (= S61) binding ; mutation to F: Complete loss of feedback control by tryptophan.
- A41 (= A62) mutation to V: Decrease in feedback control by tryptophan.
- K50 (≠ W71) binding
- R128 (≠ P126) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (≠ I160) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N282) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P283) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M287) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ Y288) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G308) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ T397) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G455) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ A460) mutation to Y: Complete loss of feedback control by tryptophan. 4-fold decrease of affinity binding for chorismate.
Sites not aligning to the query:
- 515 H→Y: Almost no change in feedback control by tryptophan.
1i7qA Anthranilate synthase from s. Marcescens (see paper)
37% identity, 86% coverage: 42:508/546 of query aligns to 18:510/517 of 1i7qA
- active site: Q260 (= Q256), E306 (= E312), A324 (= A328), E358 (= E356), H395 (= H393), T422 (= T420), Y446 (= Y444), R466 (= R464), G482 (= G480), E495 (= E493), K499 (= K497)
- binding magnesium ion: E358 (= E356), E495 (= E493)
- binding pyruvic acid: Y446 (= Y444), I465 (= I463), R466 (= R464), A479 (= A477), G480 (= G478), K499 (= K497)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
42% identity, 69% coverage: 133:508/546 of query aligns to 139:504/511 of 1i7sA
- active site: Q254 (= Q256), E300 (= E312), A318 (= A328), E352 (= E356), H389 (= H393), T416 (= T420), Y440 (= Y444), R460 (= R464), G476 (= G480), E489 (= E493), K493 (= K497)
- binding tryptophan: P282 (= P285), Y283 (= Y286), M284 (= M287), V444 (= V448), G445 (= G449), D454 (= D458), C456 (≠ A460)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
36% identity, 86% coverage: 42:508/546 of query aligns to 20:512/519 of P00897
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)
33% identity, 87% coverage: 30:505/546 of query aligns to 6:451/453 of P05041
- S36 (= S61) binding
- E258 (= E312) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A328) 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 (= G329) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R365) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R370) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T376) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H393) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
32% identity, 87% coverage: 30:505/546 of query aligns to 4:435/437 of 1k0eA
- active site: E256 (= E312), K272 (≠ A328), E286 (= E356), H323 (= H393), S350 (≠ T420), W374 (≠ Y444), R394 (= R464), G410 (= G480), E423 (= E493), K427 (= K497)
- binding tryptophan: L32 (≠ F59), H33 (≠ E60), S34 (= S61), Y41 (≠ W68), F44 (≠ W71), P238 (= P285), F239 (≠ Y286), S240 (≠ M287)
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
34% identity, 86% coverage: 35:505/546 of query aligns to 210:670/673 of 8hx8A
- binding magnesium ion: E521 (= E356), E655 (= E490), E658 (= E493)
- binding tryptophan: L231 (≠ F59), D232 (≠ E60), S233 (= S61), S241 (= S69), F243 (≠ W71), P458 (= P285), Y459 (= Y286), G460 (≠ M287), G614 (= G449)
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
35% identity, 82% coverage: 56:505/546 of query aligns to 186:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I327), K454 (≠ A328), G455 (= G329), T456 (= T330), M547 (≠ L421), Y570 (= Y444), R590 (= R464), V603 (≠ A477), G604 (= G478), G605 (= G479), A606 (≠ G480), E619 (= E493), K623 (= K497)
- binding tryptophan: L189 (≠ F59), D190 (≠ E60), S191 (= S61), S199 (= S69), F201 (≠ W71), P419 (= P285), Y420 (= Y286), G421 (≠ M287), L574 (≠ V448), G575 (= G449)
Sites not aligning to the query:
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
31% identity, 87% coverage: 30:505/546 of query aligns to 6:418/420 of 1k0gA
- active site: E258 (= E312), K274 (= K352), E278 (= E356), S333 (≠ T420), W357 (≠ Y444), R377 (= R464), G393 (= G480), E406 (= E493), K410 (= K497)
- binding phosphate ion: D113 (= D138), R116 (= R141), D347 (= D434), R353 (= R440)
- binding tryptophan: L34 (≠ F59), H35 (≠ E60), S36 (= S61), Y43 (≠ W68), S44 (= S69), F46 (≠ W71), P240 (= P285), F241 (≠ Y286), S242 (≠ M287)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 87% coverage: 30:505/546 of query aligns to 6:415/415 of 1k0gB
- active site: E258 (= E312), K274 (≠ A328), E277 (= E356), S330 (≠ T420), W354 (≠ Y444), R374 (= R464), G390 (= G480), E403 (= E493), K407 (= K497)
- binding phosphate ion: Y112 (= Y137), D113 (= D138), R116 (= R141), D344 (= D434), R350 (= R440)
- binding tryptophan: L34 (≠ F59), H35 (≠ E60), S36 (= S61), Y43 (≠ W68), S44 (= S69), R45 (= R70), F46 (≠ W71), P240 (= P285), F241 (≠ Y286)
2fn1A Crystal structures of yersinia enterocolitica salicylate synthase (irp9) in complex with the reaction products salicylate and pyruvate (see paper)
31% identity, 50% coverage: 236:506/546 of query aligns to 147:403/408 of 2fn1A
- active site: K167 (≠ Q256), E214 (= E312), A230 (= A328), E258 (= E356), H295 (= H393), T322 (= T420), Y346 (= Y444), R365 (= R464), G381 (= G480), E394 (≠ K497), K398 (≠ V501)
- binding magnesium ion: E258 (= E356), E394 (≠ K497)
- binding pyruvic acid: Y346 (= Y444), L364 (≠ I463), R365 (= R464), A378 (= A477), G379 (= G478), K398 (≠ V501)
Query Sequence
>WP_089300784.1 NCBI__GCF_900188115.1:WP_089300784.1
MVHSGRAGLGSVRPSREEFRALARERRVIPVVRTVLADAETPIGLYRKLAADRPGTFLFE
SAEHGESWSRWSFVGVRSPAALTVHDGEATWLGHPPVGLPSGGNPLSALREAVEELHSEP
LPDMPPLTGGMVGYIGYDAVRWLERLPEHARDDLRIPELIMLLATDLAAYDHHEGTVTLI
ANAVNWDASPERVDAAYDDSVARLDEMSAALAQPTPPTAATFDRPAPQFHRRRTPEDYHD
AIRRAVEAVHAGEAFQIVPSQRFEMATGADALDVYRVLRTSNPSPYMYLLRLDGFDSNGD
QIAFDIVGSSPESLVTVRDGRATTHPIAGTRWRAEDPDEDAMLAKDLLADDKERAEHLML
VDLGRNDLGRVCKPGTVHVVDSFSIERYSHVMHIVSTVTGELDAGATAVDAVAACFPAGT
LTGAPKVRAMELIDELEPTRRGLYGGVVGYLDFAGDADTAIAIRTALMRDGVAYVQAGGG
VVADSSPEYEDNESLNKARTVLAAVAAAETMSPPRPYGQGGHGEPADAAAPAEPAVADTA
RGGSRA
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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