SitesBLAST
Comparing WP_020561754.1 NCBI__GCF_000372865.1:WP_020561754.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
48% identity, 99% coverage: 1:454/458 of query aligns to 1:453/453 of P05041
- S36 (= S35) binding L-tryptophan
- E258 (= E259) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (= K275) 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 (= G276) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R312) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (≠ K317) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S323) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H340) 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)
48% identity, 97% coverage: 11:454/458 of query aligns to 9:437/437 of 1k0eA
- active site: E256 (= E259), K272 (= K275), E286 (= E303), H323 (= H340), S350 (= S367), W374 (≠ Y391), R394 (= R411), G410 (= G427), E423 (= E440), K427 (= K444)
- binding tryptophan: L32 (= L33), H33 (≠ D34), S34 (= S35), Y41 (≠ Q42), F44 (≠ Y45), P238 (= P241), F239 (= F242), S240 (= S243)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
45% identity, 99% coverage: 1:454/458 of query aligns to 1:420/420 of 1k0gA
- active site: E258 (= E259), K274 (= K275), E278 (= E303), S333 (= S367), W357 (≠ Y391), R377 (= R411), G393 (= G427), E406 (= E440), K410 (= K444)
- binding phosphate ion: D113 (= D109), R116 (= R112), D347 (≠ E381), R353 (= R387)
- binding tryptophan: L34 (= L33), H35 (≠ D34), S36 (= S35), Y43 (≠ Q42), S44 (≠ G43), F46 (≠ Y45), P240 (= P241), F241 (= F242), S242 (= S243)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
45% identity, 99% coverage: 1:452/458 of query aligns to 1:415/415 of 1k0gB
- active site: E258 (= E259), K274 (= K275), E277 (= E303), S330 (= S367), W354 (≠ Y391), R374 (= R411), G390 (= G427), E403 (= E440), K407 (= K444)
- binding phosphate ion: Y112 (= Y108), D113 (= D109), R116 (= R112), D344 (≠ E381), R350 (= R387)
- binding tryptophan: L34 (= L33), H35 (≠ D34), S36 (= S35), Y43 (≠ Q42), S44 (≠ G43), R45 (= R44), F46 (≠ Y45), P240 (= P241), F241 (= F242)
7pi1DDD Aminodeoxychorismate synthase component 1
37% identity, 90% coverage: 43:453/458 of query aligns to 39:454/459 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)
37% identity, 90% coverage: 43:453/458 of query aligns to 41:461/470 of P28820
- A283 (≠ K275) 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.
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)
36% identity, 95% coverage: 14:450/458 of query aligns to 49:513/524 of A0QX93
- K355 (≠ E292) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
36% identity, 95% coverage: 14:450/458 of query aligns to 29:488/499 of 7bvdA
- active site: Q248 (= Q212), E301 (= E259), A317 (≠ K275), E341 (= E303), H378 (= H340), T405 (≠ S367), Y429 (= Y391), R449 (= R411), G465 (= G427), E478 (= E440), K482 (= K444)
- binding pyruvic acid: S93 (= S74), G94 (≠ K75), A100 (≠ L81)
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
36% identity, 94% coverage: 24:452/458 of query aligns to 180:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I274), K454 (= K275), G455 (= G276), T456 (= T277), M547 (≠ I368), Y570 (= Y391), R590 (= R411), V603 (≠ A424), G604 (= G425), G605 (= G426), A606 (≠ G427), E619 (= E440), K623 (= K444)
- binding tryptophan: L189 (= L33), D190 (= D34), S191 (= S35), S199 (≠ G43), F201 (≠ Y45), P419 (= P241), Y420 (≠ F242), G421 (≠ S243), L574 (≠ I395), G575 (= G396)
Sites not aligning to the query:
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
36% identity, 94% coverage: 24:452/458 of query aligns to 222:670/673 of 8hx8A
- binding magnesium ion: E521 (= E303), E655 (= E437), E658 (= E440)
- binding tryptophan: L231 (= L33), D232 (= D34), S233 (= S35), S241 (≠ G43), F243 (≠ Y45), P458 (= P241), Y459 (≠ F242), G460 (≠ S243), G614 (= G396)
Sites not aligning to the query:
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
35% identity, 95% coverage: 14:450/458 of query aligns to 29:492/505 of 5cwaA
- active site: Q248 (= Q212), E301 (= E259), A317 (≠ K275), E345 (= E303), H382 (= H340), T409 (≠ S367), Y433 (= Y391), R453 (= R411), G469 (= G427), E482 (= E440), K486 (= K444)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y391), I452 (= I410), A466 (= A424), G467 (= G425), K486 (= K444)
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)
31% identity, 91% coverage: 33:448/458 of query aligns to 116:581/595 of P32068
- D341 (= D226) 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, 91% coverage: 33:448/458 of query aligns to 100:563/577 of Q94GF1
- D323 (= D226) 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)
32% identity, 91% coverage: 26:444/458 of query aligns to 45:466/489 of O94582
- S390 (≠ T369) modified: Phosphoserine
- S392 (≠ A371) 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)
32% identity, 76% coverage: 104:449/458 of query aligns to 148:507/520 of P00898
- C174 (≠ A131) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N238) mutation to D: Decrease in feedback control by tryptophan.
- P289 (≠ A239) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ S243) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ C244) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S255) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ T344) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G402) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ N407) 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.
- 515 H→Y: Almost no change in feedback control by tryptophan.
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
32% identity, 76% coverage: 104:449/458 of query aligns to 144:503/512 of 1i1qA
- active site: Q259 (= Q212), E305 (= E259), A323 (≠ K275), E357 (= E303), H394 (= H340), T421 (≠ S367), Y445 (= Y391), R465 (= R411), G481 (= G427), E494 (= E440), K498 (= K444)
- binding tryptophan: P287 (= P241), Y288 (≠ F242), M289 (≠ S243), G450 (= G396), C461 (≠ N407)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
32% identity, 76% coverage: 104:449/458 of query aligns to 145:504/517 of 1i7qA
- active site: Q260 (= Q212), E306 (= E259), A324 (≠ K275), E358 (= E303), H395 (= H340), T422 (≠ S367), Y446 (= Y391), R466 (= R411), G482 (= G427), E495 (= E440), K499 (= K444)
- binding magnesium ion: E358 (= E303), E495 (= E440)
- binding pyruvic acid: Y446 (= Y391), I465 (= I410), R466 (= R411), A479 (= A424), G480 (= G425), K499 (= K444)
1i7sA Anthranilate synthase from serratia marcescens in complex with its end product inhibitor l-tryptophan (see paper)
32% identity, 76% coverage: 104:449/458 of query aligns to 139:498/511 of 1i7sA
- active site: Q254 (= Q212), E300 (= E259), A318 (≠ K275), E352 (= E303), H389 (= H340), T416 (≠ S367), Y440 (= Y391), R460 (= R411), G476 (= G427), E489 (= E440), K493 (= K444)
- binding tryptophan: P282 (= P241), Y283 (≠ F242), M284 (≠ S243), V444 (≠ I395), G445 (= G396), D454 (= D405), C456 (≠ N407)
Sites not aligning to the query:
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
31% identity, 76% coverage: 104:449/458 of query aligns to 147:506/519 of P00897
- PYM 290:292 (≠ PFS 241:243) binding L-tryptophan
- E360 (= E303) binding Mg(2+)
- E497 (= E440) binding Mg(2+)
Sites not aligning to the query:
8qc4A Salicylate synthase (see paper)
31% identity, 48% coverage: 210:429/458 of query aligns to 199:411/438 of 8qc4A
Sites not aligning to the query:
Query Sequence
>WP_020561754.1 NCBI__GCF_000372865.1:WP_020561754.1
MSPLNQFMSPLPYFADSADLFSAIAGMPWSVFLDSGYPYSQQGRYDIIAADPVCILVTHG
DETVITRGGKSVISKDDPFDLVKQQLLPAHCQGDTLPFKGGAIGYFSYDLVRRLEHLSEI
AVDAEHIPEMAVGIYDWAVVVDHHCRKSYLVGQNCDMQKWLKLIEQFSVLPVEERRGPFR
IVGDIRSNMDKAFYTRAFDRIKQYLKEGDCYQVNFSQRFVADCEGDPWTAYKALRELNAA
PFSCYLNLPEVQILSTSPERFLKLTDGLVETKPIKGTRPRKRDQAEDRQQIEILEHSPKD
RAENLMIVDLLRNDISKTCKKGSVKVPRIFAVETYATVHHLVSTITGWLADDRHALDLLK
HCFPGGSITGAPKIRAMEVIEELEPNRRGIYCGSIGYIGFDGNMDSNIAIRTLVHSGGTI
RFWAGGGIVNDSEVDDEYQECFDKAAAMLDLLQRFRVG
Or try a new SitesBLAST search
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