SitesBLAST
Comparing WP_022948598.1 NCBI__GCF_000421465.1:WP_022948598.1 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)
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, 97% coverage: 3:455/466 of query aligns to 5:453/453 of P05041
- S36 (= S34) binding L-tryptophan
- E258 (= E260) mutation to A: The reaction is extremely slow.; mutation to D: The reaction is extremely slow.
- K274 (= K276) 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 (= G277) mutation to S: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- R311 (= R313) mutation to K: Catalytically active in the NH3-dependent, but inactive for the glutamine-dependent reactions and fails to complex with PabA.
- R316 (≠ K318) mutation to H: Catalytically inactive for both the glutamine-dependent and ammonia-dependent reactions and fails to interact with PabA.
- S322 (= S324) mutation to T: Complete loss of aminodeoxychorismate synthase activity.
- H339 (= H341) 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)
47% identity, 97% coverage: 3:455/466 of query aligns to 3:437/437 of 1k0eA
- active site: E256 (= E260), K272 (= K276), E286 (= E304), H323 (= H341), S350 (= S368), W374 (≠ Y392), R394 (= R412), G410 (= G428), E423 (= E441), K427 (= K445)
- binding tryptophan: L32 (= L32), H33 (≠ D33), S34 (= S34), Y41 (≠ Q41), F44 (≠ Y44), P238 (= P242), F239 (= F243), S240 (≠ G244)
1k0gA The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
44% identity, 97% coverage: 3:455/466 of query aligns to 5:420/420 of 1k0gA
- active site: E258 (= E260), K274 (= K276), E278 (= E304), S333 (= S368), W357 (≠ Y392), R377 (= R412), G393 (= G428), E406 (= E441), K410 (= K445)
- binding phosphate ion: D113 (= D108), R116 (= R111), D347 (≠ E382), R353 (= R388)
- binding tryptophan: L34 (= L32), H35 (≠ D33), S36 (= S34), Y43 (≠ Q41), S44 (≠ G42), F46 (≠ Y44), P240 (= P242), F241 (= F243), S242 (≠ G244)
1k0gB The crystal structure of aminodeoxychorismate synthase from phosphate grown crystals (see paper)
44% identity, 97% coverage: 3:453/466 of query aligns to 5:415/415 of 1k0gB
- active site: E258 (= E260), K274 (= K276), E277 (= E304), S330 (= S368), W354 (≠ Y392), R374 (= R412), G390 (= G428), E403 (= E441), K407 (= K445)
- binding phosphate ion: Y112 (= Y107), D113 (= D108), R116 (= R111), D344 (≠ E382), R350 (= R388)
- binding tryptophan: L34 (= L32), H35 (≠ D33), S36 (= S34), Y43 (≠ Q41), S44 (≠ G42), R45 (= R43), F46 (≠ Y44), P240 (= P242), F241 (= F243)
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)
35% identity, 95% coverage: 9:453/466 of query aligns to 10:460/470 of P28820
- A283 (≠ K276) 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
36% identity, 95% coverage: 9:453/466 of query aligns to 8:453/459 of 7pi1DDD
- binding magnesium ion: G428 (= G428), E438 (= E438)
- binding tryptophan: L33 (= L32), E34 (≠ D33), S35 (= S34), G39 (= G42), Y41 (= Y44), P242 (= P242), Y243 (≠ F243), M244 (≠ G244), Q406 (≠ D406), N408 (= N408)
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, 92% coverage: 24:451/466 of query aligns to 64:513/524 of A0QX93
- K355 (≠ G293) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
7bvdA Anthranilate synthase component i (trpe)[mycolicibacterium smegmatis]
36% identity, 92% coverage: 24:451/466 of query aligns to 44:488/499 of 7bvdA
- active site: Q248 (= Q213), E301 (= E260), A317 (≠ K276), E341 (= E304), H378 (= H341), T405 (≠ S368), Y429 (= Y392), R449 (= R412), G465 (= G428), E478 (= E441), K482 (= K445)
- binding pyruvic acid: S93 (vs. gap), G94 (vs. gap), A100 (≠ L80)
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, 88% coverage: 42:453/466 of query aligns to 126:585/595 of P32068
- D341 (= D227) mutation to N: In trp5-1; insensitive to feedback inhibition by tryptophan and resistance to the herbicide 6-methylanthranilate.
5cwaA Structure of anthranilate synthase component i (trpe) from mycobacterium tuberculosis with inhibitor bound (see paper)
35% identity, 92% coverage: 24:451/466 of query aligns to 44:492/505 of 5cwaA
- active site: Q248 (= Q213), E301 (= E260), A317 (≠ K276), E345 (= E304), H382 (= H341), T409 (≠ S368), Y433 (= Y392), R453 (= R412), G469 (= G428), E482 (= E441), K486 (= K445)
- binding 3-{[(1Z)-1-carboxyprop-1-en-1-yl]oxy}-2-hydroxybenzoic acid: Y433 (= Y392), I452 (= I411), A466 (= A425), G467 (= G426), K486 (= K445)
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: 32:453/466 of query aligns to 100:567/577 of Q94GF1
- D323 (= D227) mutation to N: Insensitive to feedback inhibition by tryptophan.
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
37% identity, 85% coverage: 60:453/466 of query aligns to 264:670/673 of 8hx8A
Sites not aligning to the query:
8hx9A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae with chorismate (see paper)
37% identity, 85% coverage: 60:453/466 of query aligns to 222:631/632 of 8hx9A
- binding (3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid: I453 (= I275), K454 (= K276), G455 (= G277), T456 (= T278), M547 (≠ I369), Y570 (= Y392), R590 (= R412), V603 (≠ A425), G604 (= G426), G605 (= G427), A606 (≠ G428), E619 (= E441), K623 (= K445)
- binding tryptophan: P419 (= P242), Y420 (≠ F243), G421 (= G244), L574 (≠ I396), G575 (= G397)
Sites not aligning to the query:
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)
35% identity, 78% coverage: 81:445/466 of query aligns to 90:466/489 of O94582
- S390 (≠ T370) modified: Phosphoserine
- S392 (≠ A372) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
1i1qA Structure of the cooperative allosteric anthranilate synthase from salmonella typhimurium (see paper)
32% identity, 83% coverage: 66:454/466 of query aligns to 111:507/512 of 1i1qA
- active site: Q259 (= Q213), E305 (= E260), A323 (≠ K276), E357 (= E304), H394 (= H341), T421 (≠ S368), Y445 (= Y392), R465 (= R412), G481 (= G428), E494 (= E441), K498 (= K445)
- binding tryptophan: P287 (= P242), Y288 (≠ F243), M289 (≠ G244), G450 (= G397), C461 (≠ N408)
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)
32% identity, 82% coverage: 72:454/466 of query aligns to 121:511/520 of P00898
- R128 (≠ K79) mutation to H: Almost no change in feedback control by tryptophan.
- C174 (≠ A130) mutation to Y: Almost no change in feedback control by tryptophan.
- N288 (= N239) mutation to D: Decrease in feedback control by tryptophan.
- P289 (= P240) mutation to L: Decrease in feedback control by tryptophan.
- M293 (≠ G244) mutation to T: Complete loss of feedback control by tryptophan.
- F294 (≠ S245) mutation to L: Decrease in feedback control by tryptophan.
- G305 (≠ S256) mutation to S: Decrease in feedback control by tryptophan.
- R402 (≠ T345) mutation to W: Almost no change in feedback control by tryptophan.
- G460 (= G403) mutation to D: Almost no change in feedback control by tryptophan.
- C465 (≠ N408) 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
- 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)
31% identity, 87% coverage: 49:454/466 of query aligns to 87:502/511 of 1i7sA
- active site: Q254 (= Q213), E300 (= E260), A318 (≠ K276), E352 (= E304), H389 (= H341), T416 (≠ S368), Y440 (= Y392), R460 (= R412), G476 (= G428), E489 (= E441), K493 (= K445)
- binding tryptophan: P282 (= P242), Y283 (≠ F243), M284 (≠ G244), V444 (≠ I396), G445 (= G397), D454 (= D406), C456 (≠ N408)
Sites not aligning to the query:
1i7qA Anthranilate synthase from s. Marcescens (see paper)
31% identity, 87% coverage: 49:454/466 of query aligns to 93:508/517 of 1i7qA
- active site: Q260 (= Q213), E306 (= E260), A324 (≠ K276), E358 (= E304), H395 (= H341), T422 (≠ S368), Y446 (= Y392), R466 (= R412), G482 (= G428), E495 (= E441), K499 (= K445)
- binding magnesium ion: E358 (= E304), E495 (= E441)
- binding pyruvic acid: Y446 (= Y392), I465 (= I411), R466 (= R412), A479 (= A425), G480 (= G426), K499 (= K445)
P00897 Anthranilate synthase component 1; AS; ASI; EC 4.1.3.27 from Serratia marcescens (see paper)
31% identity, 87% coverage: 49:454/466 of query aligns to 95:510/519 of P00897
- PYM 290:292 (≠ PFG 242:244) binding L-tryptophan
- E360 (= E304) binding Mg(2+)
- E497 (= E441) 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)
32% identity, 46% coverage: 237:449/466 of query aligns to 190:402/408 of 2fn1A
- active site: E214 (= E260), A230 (≠ K276), E258 (= E304), H295 (= H341), T322 (≠ S368), Y346 (= Y392), R365 (= R412), G381 (= G428), E394 (= E441), K398 (= K445)
- binding magnesium ion: E258 (= E304), E394 (= E441)
- binding pyruvic acid: Y346 (= Y392), L364 (≠ I411), R365 (= R412), A378 (= A425), G379 (= G426), K398 (= K445)
Sites not aligning to the query:
Query Sequence
>WP_022948598.1 NCBI__GCF_000421465.1:WP_022948598.1
MDSPYLISELPYLEDSSELFAQWAQEPWAIFLDSGRPRIEQGRYDILAARPSATLVTRGN
LTEIRNSDGIRLSPEDPFKLLREILGEPAEGMPDLPFCGGALGYFSYDLARRLENLPQTT
LDPGNIPEMAVGIYDWAVVVDHRERQTYLVARSTPATRKIWPELQQSLRHPFPRISRTGF
CLQSPIRSNLSWDAYAHAFAKIQHYIQEGDCYQVNFAQRFEAKAAGDPWRVYQDLRRENP
APFGSFLRLPQLGILSSSPERFLRVREGKVETKPIKGTRARRLSPEENLFQIGALTESAK
DRAENLMIVDLLRNDLSKTCQLGSVKVPELFQVESFATVHHLVSTVVGELKEDCHSLDLL
RGCFPGGSITGAPKIRAMEIIEELESIRRGIYCGAIGYIGFDGNMDTNIAIRTLVHADRS
IHFWAGGGIVADSDAKREYQESFDKASALIQVLSRFGITSADHVGG
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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