SitesBLAST
Comparing WP_018123679.1 NCBI__GCF_000375485.1:WP_018123679.1 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)
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, 89% coverage: 34:455/474 of query aligns to 33:453/470 of P28820
- A283 (= A282) 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
39% identity, 91% coverage: 34:462/474 of query aligns to 31:453/459 of 7pi1DDD
- binding magnesium ion: G428 (= G437), E438 (= E447)
- binding tryptophan: L33 (= L36), E34 (= E37), S35 (= S38), G39 (= G46), Y41 (= Y48), P242 (= P246), Y243 (≠ F247), M244 (= M248), Q406 (≠ D415), N408 (≠ G417)
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)
39% identity, 94% coverage: 15:459/474 of query aligns to 50:512/524 of A0QX93
- K355 (≠ D299) 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)
39% identity, 94% coverage: 15:460/474 of query aligns to 30:492/505 of 5cwaA
- active site: Q248 (= Q217), E301 (= E266), A317 (= A282), E345 (= E310), H382 (= H347), T409 (= T374), Y433 (= Y398), R453 (= R421), G469 (= G437), E482 (= E450), K486 (= K454)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y398), I452 (= I420), A466 (= A434), G467 (= G435), K486 (= K454)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
38% identity, 94% coverage: 15:459/474 of query aligns to 30:487/499 of 7bvdA
- active site: Q248 (= Q217), E301 (= E266), A317 (= A282), E341 (= E310), H378 (= H347), T405 (= T374), Y429 (= Y398), R449 (= R421), G465 (= G437), E478 (= E450), K482 (= K454)
- binding pyruvic acid: S93 (= S82), G94 (= G83), A100 (≠ G89)
Q94GF1 Anthranilate synthase alpha subunit 1, chloroplastic; OsASA1; EC 4.1.3.27 from Oryza sativa subsp. japonica (Rice) (see paper)
36% identity, 95% coverage: 15:463/474 of query aligns to 72:568/577 of Q94GF1
- D323 (= D231) 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)
37% identity, 95% coverage: 15:463/474 of query aligns to 88:586/595 of P32068
- D341 (= D231) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
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)
36% identity, 94% coverage: 13:456/474 of query aligns to 28:468/489 of O94582
- S390 (= S376) modified: Phosphoserine
- S392 (≠ A378) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
P00898 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
48% identity, 56% coverage: 197:462/474 of query aligns to 243:510/520 of P00898
- N288 (= N243) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P244) mutation to L: Decrease in feedback control by tryptophan.
- M293 (= M248) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (= F249) mutation to L: Decrease in feedback control by tryptophan.
- G305 (= G262) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ Y351) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (≠ S409) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ G417) 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)
48% identity, 56% coverage: 197:462/474 of query aligns to 239:506/512 of 1i1qA
- active site: Q259 (= Q217), E305 (= E266), A323 (= A282), E357 (= E310), H394 (= H347), T421 (= T374), Y445 (= Y398), R465 (= R421), G481 (= G437), E494 (= E450), K498 (= K454)
- binding tryptophan: P287 (= P246), Y288 (≠ F247), M289 (= M248), G450 (= G403), C461 (≠ G417)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
33% identity, 95% coverage: 20:471/474 of query aligns to 18:517/517 of 1i7qA
- active site: Q260 (= Q217), E306 (= E266), A324 (= A282), E358 (= E310), H395 (= H347), T422 (= T374), Y446 (= Y398), R466 (= R421), G482 (= G437), E495 (= E450), K499 (= K454)
- binding magnesium ion: E358 (= E310), E495 (= E450)
- binding pyruvic acid: Y446 (= Y398), I465 (= I420), R466 (= R421), A479 (= A434), G480 (= G435), K499 (= K454)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
37% identity, 85% coverage: 67:471/474 of query aligns to 101:511/511 of 1i7sA
- active site: Q254 (= Q217), E300 (= E266), A318 (= A282), E352 (= E310), H389 (= H347), T416 (= T374), Y440 (= Y398), R460 (= R421), G476 (= G437), E489 (= E450), K493 (= K454)
- binding tryptophan: P282 (= P246), Y283 (≠ F247), M284 (= M248), V444 (≠ I402), G445 (= G403), D454 (= D415), C456 (≠ G417)
Sites not aligning to the query:
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, 94% coverage: 18:461/474 of query aligns to 15:451/453 of P05041
- S36 (= S38) binding L-tryptophan
- E258 (= E266) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (≠ A282) 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 (= G283) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R319) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (= R324) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (≠ T330) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H347) mutation to W: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
32% identity, 95% coverage: 20:471/474 of query aligns to 20:519/519 of P00897
- S39 (= S38) binding L-tryptophan
- PYM 290:292 (≠ PFM 246:248) binding L-tryptophan
- E360 (= E310) binding Mg(2+)
- E497 (= E450) binding Mg(2+)
1k0eA The crystal structure of aminodeoxychorismate synthase from formate grown crystals (see paper)
32% identity, 94% coverage: 18:461/474 of query aligns to 13:435/437 of 1k0eA
- active site: E256 (= E266), K272 (≠ A282), E286 (= E310), H323 (= H347), S350 (≠ T374), W374 (≠ Y398), R394 (= R421), G410 (= G437), E423 (= E450), K427 (= K454)
- binding tryptophan: L32 (= L36), H33 (≠ E37), S34 (= S38), Y41 (≠ L45), F44 (≠ Y48), P238 (= P246), F239 (= F247), S240 (≠ M248)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 94% coverage: 18:461/474 of query aligns to 15:418/420 of 1k0gA
- active site: E258 (= E266), K274 (= K306), E278 (= E310), S333 (≠ T374), W357 (≠ Y398), R377 (= R421), G393 (= G437), E406 (= E450), K410 (= K454)
- binding phosphate ion: D113 (vs. gap), R116 (≠ Y121), D347 (≠ S388), R353 (≠ E394)
- binding tryptophan: L34 (= L36), H35 (≠ E37), S36 (= S38), Y43 (≠ L45), S44 (≠ G46), F46 (≠ Y48), P240 (= P246), F241 (= F247), S242 (≠ M248)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
30% identity, 94% coverage: 18:461/474 of query aligns to 15:415/415 of 1k0gB
- active site: E258 (= E266), K274 (≠ A282), E277 (= E310), S330 (≠ T374), W354 (≠ Y398), R374 (= R421), G390 (= G437), E403 (= E450), K407 (= K454)
- binding phosphate ion: Y112 (= Y118), D113 (vs. gap), R116 (≠ Y121), D344 (≠ S388), R350 (≠ E394)
- binding tryptophan: L34 (= L36), H35 (≠ E37), S36 (= S38), Y43 (≠ L45), S44 (≠ G46), R45 (= R47), F46 (≠ Y48), P240 (= P246), F241 (= F247)
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
33% identity, 74% coverage: 114:464/474 of query aligns to 308:672/673 of 8hx8A
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
32% identity, 74% coverage: 114:463/474 of query aligns to 266:632/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I281), K454 (≠ A282), G455 (= G283), T456 (= T284), M547 (≠ L375), Y570 (= Y398), R590 (= R421), V603 (≠ A434), G604 (= G435), G605 (≠ A436), A606 (≠ G437), E619 (= E450), K623 (= K454)
- binding tryptophan: P419 (= P246), Y420 (≠ F247), G421 (≠ M248), L574 (≠ I402), G575 (= G403)
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)
34% identity, 54% coverage: 197:454/474 of query aligns to 147:398/408 of 2fn1A
- active site: K167 (≠ Q217), E214 (= E266), A230 (= A282), E258 (= E310), H295 (= H347), T322 (= T374), Y346 (= Y398), R365 (= R421), G381 (= G437), E394 (= E450), K398 (= K454)
- binding magnesium ion: E258 (= E310), E394 (= E450)
- binding pyruvic acid: Y346 (= Y398), L364 (≠ I420), R365 (= R421), A378 (= A434), G379 (= G435), K398 (= K454)
Query Sequence
>WP_018123679.1 NCBI__GCF_000375485.1:WP_018123679.1
MKPIQLKQYGKWLPADVQTPISLYLGLVGDAPGILLESAEVDGRLGRYTLIAWDFRLSLR
PENGKLAVEATDERLKPLEKFSGMNFLDGLRRVLRAVAVEQETDDGPLPALTRGLYGYLG
YGIAGMLEPKLAESVKPEDAEACLNLPGQMVLFDHLRHSCCYLSLDKGSVPRPVAAEWGT
DLAAPEASEPQMYPERDDYLRAVEKTKELIADGECIQAVLSTRFTVPLPDDPFRIYRRLR
QANPSPFMFYMKLPGCDGTLLGSSPEMMVRCEEGRLEVRPIAGTRPRGGNESEDLALADE
LLADPKERAEHVMLVDLGRNDLGRISNPGTVEVKRFMNVERFSHVMHLTSYVEGELQDGL
DAVDVLRATFPAGTLSGAPKVRAMEIISEMEPQERGPYGGCIGFLGLDSDSVSLDTGITI
RSLWVRNGQCHWQAGAGIVHDSVPEKEWEECRNKARVLMEVINGRGGTDVFAHR
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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