SitesBLAST
Comparing WP_232226739.1 NCBI__GCF_000733765.1:WP_232226739.1 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)
7pi1DDD Aminodeoxychorismate synthase component 1
41% identity, 81% coverage: 85:441/443 of query aligns to 92:453/459 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)
40% identity, 81% coverage: 85:441/443 of query aligns to 94:460/470 of P28820
- A283 (= A264) 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.
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)
37% identity, 93% coverage: 31:441/443 of query aligns to 33:451/453 of P05041
- S36 (= S34) binding L-tryptophan
- E258 (= E248) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A264) 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 (= G265) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R301) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R306) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S312) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H329) 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)
36% identity, 93% coverage: 31:441/443 of query aligns to 31:435/437 of 1k0eA
- active site: E256 (= E248), K272 (≠ A264), E286 (= E292), H323 (= H329), S350 (≠ T356), W374 (≠ Y380), R394 (= R400), G410 (= G416), E423 (= E429), K427 (= K433)
- binding tryptophan: L32 (= L32), H33 (≠ N33), S34 (= S34), Y41 (≠ T41), F44 (≠ Y44), P238 (= P230), F239 (= F231), S240 (= S232)
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)
38% identity, 87% coverage: 54:438/443 of query aligns to 105:512/524 of A0QX93
- K355 (≠ G281) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
38% identity, 87% coverage: 54:438/443 of query aligns to 84:487/499 of 7bvdA
- active site: Q248 (= Q199), E301 (= E248), A317 (= A264), E341 (= E292), H378 (= H329), T405 (= T356), Y429 (= Y380), R449 (= R400), G465 (= G416), E478 (= E429), K482 (= K433)
- binding pyruvic acid: S93 (≠ E63), G94 (≠ A64), A100 (= A66)
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
37% identity, 86% coverage: 62:441/443 of query aligns to 281:670/673 of 8hx8A
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
36% identity, 86% coverage: 62:441/443 of query aligns to 239:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I263), K454 (≠ A264), G455 (= G265), T456 (= T266), M547 (≠ I357), Y570 (= Y380), R590 (= R400), V603 (≠ A413), G604 (= G414), G605 (≠ A415), A606 (≠ G416), E619 (= E429), K623 (= K433)
- binding tryptophan: P419 (= P230), Y420 (≠ F231), G421 (≠ S232), L574 (= L384), G575 (= G385)
Sites not aligning to the query:
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
38% identity, 81% coverage: 78:438/443 of query aligns to 112:491/505 of 5cwaA
- active site: Q248 (= Q199), E301 (= E248), A317 (= A264), E345 (= E292), H382 (= H329), T409 (= T356), Y433 (= Y380), R453 (= R400), G469 (= G416), E482 (= E429), K486 (= K433)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y380), I452 (= I399), A466 (= A413), G467 (= G414), K486 (= K433)
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)
29% identity, 99% coverage: 3:441/443 of query aligns to 23:474/489 of O94582
- S390 (≠ T358) modified: Phosphoserine
- S392 (≠ C360) 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)
33% identity, 81% coverage: 80:437/443 of query aligns to 179:581/595 of P32068
- D341 (≠ S215) 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)
32% identity, 93% coverage: 25:437/443 of query aligns to 93:563/577 of Q94GF1
- D323 (≠ S215) mutation to N: Insensitive to feedback inhibition by tryptophan.
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
34% identity, 93% coverage: 31:441/443 of query aligns to 33:418/420 of 1k0gA
- active site: E258 (= E248), K274 (= K288), E278 (= E292), S333 (≠ T356), W357 (≠ Y380), R377 (= R400), G393 (= G416), E406 (= E429), K410 (= K433)
- binding phosphate ion: D113 (≠ E99), R116 (≠ A102), D347 (≠ A370), R353 (≠ G376)
- binding tryptophan: L34 (= L32), H35 (≠ N33), S36 (= S34), Y43 (≠ T41), S44 (≠ G42), F46 (≠ Y44), P240 (= P230), F241 (= F231), S242 (= S232)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
34% identity, 93% coverage: 31:441/443 of query aligns to 33:415/415 of 1k0gB
- active site: E258 (= E248), K274 (≠ A264), E277 (= E292), S330 (≠ T356), W354 (≠ Y380), R374 (= R400), G390 (= G416), E403 (= E429), K407 (= K433)
- binding phosphate ion: Y112 (= Y98), D113 (≠ E99), R116 (≠ A102), D344 (≠ A370), R350 (≠ G376)
- binding tryptophan: L34 (= L32), H35 (≠ N33), S36 (= S34), Y43 (≠ T41), S44 (≠ G42), R45 (= R43), F46 (≠ Y44), P240 (= P230), F241 (= F231)
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
40% identity, 57% coverage: 192:443/443 of query aligns to 256:512/520 of P00898
- N288 (= N227) mutation to D: Decrease in feedback control by tryptophan.
- P289 (≠ A228) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ S232) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ A233) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S244) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ N333) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G391) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ S396) 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 L-tryptophan; S→F: Complete loss of feedback control by tryptophan.
- 41 A→V: Decrease in feedback control by tryptophan.
- 50 binding L-tryptophan
- 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.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
40% identity, 57% coverage: 192:443/443 of query aligns to 252:508/512 of 1i1qA
- active site: Q259 (= Q199), E305 (= E248), A323 (= A264), E357 (= E292), H394 (= H329), T421 (= T356), Y445 (= Y380), R465 (= R400), G481 (= G416), E494 (= E429), K498 (= K433)
- binding tryptophan: P287 (= P230), Y288 (≠ F231), M289 (≠ S232), G450 (= G385), C461 (≠ S396)
Sites not aligning to the query:
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
32% identity, 83% coverage: 75:443/443 of query aligns to 123:503/511 of 1i7sA
- active site: Q254 (= Q199), E300 (= E248), A318 (= A264), E352 (= E292), H389 (= H329), T416 (= T356), Y440 (= Y380), R460 (= R400), G476 (= G416), E489 (= E429), K493 (= K433)
- binding tryptophan: P282 (= P230), Y283 (≠ F231), M284 (≠ S232), V444 (≠ L384), G445 (= G385), D454 (= D394), C456 (≠ S396)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
32% identity, 83% coverage: 75:443/443 of query aligns to 129:509/517 of 1i7qA
- active site: Q260 (= Q199), E306 (= E248), A324 (= A264), E358 (= E292), H395 (= H329), T422 (= T356), Y446 (= Y380), R466 (= R400), G482 (= G416), E495 (= E429), K499 (= K433)
- binding magnesium ion: E358 (= E292), E495 (= E429)
- binding pyruvic acid: Y446 (= Y380), I465 (= I399), R466 (= R400), A479 (= A413), G480 (= G414), K499 (= K433)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
32% identity, 83% coverage: 75:443/443 of query aligns to 131:511/519 of P00897
- PYM 290:292 (≠ PFS 230:232) binding L-tryptophan
- E360 (= E292) binding Mg(2+)
- E497 (= E429) binding Mg(2+)
Sites not aligning to the query:
2fn1A Crystal structures of yersinia enterocolitica salicylate synthase (irp9) in complex with the reaction products salicylate and pyruvate (see paper)
30% identity, 62% coverage: 160:433/443 of query aligns to 127:398/408 of 2fn1A
- active site: K167 (≠ Q199), E214 (= E248), A230 (= A264), E258 (= E292), H295 (= H329), T322 (= T356), Y346 (= Y380), R365 (= R400), G381 (= G416), E394 (= E429), K398 (= K433)
- binding magnesium ion: E258 (= E292), E394 (= E429)
- binding pyruvic acid: Y346 (= Y380), L364 (≠ I399), R365 (= R400), A378 (= A413), G379 (= G414), K398 (= K433)
Query Sequence
>WP_232226739.1 NCBI__GCF_000733765.1:WP_232226739.1
MAPAAPVIQPLAAAPDLLALHAADPQRFFCLLNSGAHAERTGRYDILFAEPRRLGSAAAG
TPEADALLARLDAYSLHAAPGMPSELPFVGGYVFHIGYEAAACFEPKLRLPRPGPEALPD
ITVWAVDQAIVVDAVTGQAWCVAPDQATAAALARETGQPRAAVHPYAEGLASSEAEAPQH
YRDGVAAVLDYLHAGDAFQVNLSRGWRLRLAESASGAALHAAMRLHNAAPFSALLHQDGA
SLVSASPERLVRVVDGVVETRPIAGTRRRGRDADEDAALCGELSRNPKERAEHVMLIDLE
RNDLGRICRPGSVCVDELLALEHYASVHHLVSNIRGELSPDVGAARVLRAVFPGGTITGC
PKVRVMEIIAELETVGRGSYTGSLGYVSRNGRMDSSILIRSLLARDDELVFRAGAGIVAD
SDPDAELAETEAKARGLLAGLGA
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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